# a: arc location: 2-99.2. discoverer: Bridges, 12e24. references: Bridges and Morgan, 1919, Carnegie Inst. Washington Publ. No. 278: 202 (fig.). Morgan, Bridges, and Sturtevant, 1925, Bibliog. Genet. 2: 212 (fig.). Bridges, 1937, Cytologia (Tokyo), Fujii Jub., Vol. 2: 745-55. phenotype: Wings broader; bent downward in slight, even arc; edges drawn down to diamond shape. Sometimes in stock, wings are bent upward instead of downward. Crossveins closer together. RK2. alleles: a1, aba (see below), *aba1, *aba2, *aba3, *aba4, *abad6, *abadp, *abar, *aBa, *aBaC, *aBap1, *aBap2, *aBaX, *aBay (Goldschmidt, 1945, Univ. Calif. Berkeley Publ. Zool. 49: 351-56, 388-89, 519; CP627), and *aM60 (Meyer, 1963, DIS 37: 50). cytology: Placed between 57F11 and 58E4 on the basis of its inclusion within Df(2R)M-1 = Df(2R)57F11-58A1;58F8-59A1 but not Dp(2;3)P = Dp(2;3)58E3-4;60D14-E2;96B5-C1 (Bridges, 1937). Likely in band 58D6 or 7 based on Df(2R)a-ba2 = Df(2R)58D5- 6;58D7-8. a: arc From Bridges and Morgan, 1919, Carnegie Inst. Washington Publ. No. 278: 148. # aba: arc-broad angular origin: Spontaneous. discoverer: Goldschmidt, 1934. synonym: Referred to as bran: broad angular by Goldschmidt, but shown by him to be an allele of arc. references: 1945, Univ. Calif. Berkeley Publ. Zool. 49: 351- 56, 388-89, 519. phenotype: Wings broader and shorter than wild type, blunt at the tip. Frequently shows upturned posterior scutellar bris- tles. In combination with svrpoi, produces soft blistered wing. Other interactions described by Goldschmidt, 1945, table 74. Wing grows in pupal stage to full length and then retracts, possibly with histolysis [Goldschmidt, 1934, Z. Indukt. Abstamm. Vererbungsl. 69: 38-131 (fig.)]. RK2. cytology: Salivary chromosomes normal (Kodani). other information: Claimed to recur repeatedly in certain lines (Goldschmidt, 1945). # (1: see tyr1 #*A: Abnormal abdomen location: 1-4.5. discoverer: Morgan, 11g. synonym: Abnormal. references: 1915, Am. Naturalist 49: 384-429 (fig.). Morgan and Bridges, 1916, Carnegie Inst. Washington Publ. No. 237: 27 (fig.). phenotype: Tergites and sternites raggedly incomplete, exposing a thin crinkled cuticle; bristles and hairs on abdomen correspondingly eliminated. Highly variable, wild phenotype in old dry cultures. A/+ less extreme than A/A and A male; homozygous female fully viable and fertile. RK2 in well-fed cultures. alleles: *A1 (Morgan and Bridges, 1916), A53g (see below), A70 [allelism conjectural (Gooskov, 1971, DIS 46: 41)]. other information: Lost by reversion to wild type. # A: see bwA # A53g location: 1- (between y and w; may not be allelic to A). origin: Spontaneous. discoverer: Hillman, 53g. references: 1953, DIS 27: 56. 1973, Genet. Res. 22: 37-53. 1977, Amer. Zool. 17: 521-33. Hillman and Barbour, 1963, Proc. Intern. Congr. Genet., 11th, Vol. 1: 170. phenotype: Epidermal foldings of abdomen abnormal. Tergite formation incomplete, ranging from loss of tergites 2-8 in extreme cases to loss of lateral part of tergite in one or more segments. Expression in A53g/A53g females > A53g/Y males > A53g/+ females. Expression maternally influenced (Shafer and Hillman, 1974, J. Insect Physiol. 20: 223-230). Highly variable; sensitive to modifiers on X, 2, and 3, including E(A53g) on 2L. Sensitive to culture conditions; expression reduced in old cultures and under conditions of crowding, low temperature (TSP in late second and early third instar), and low humidity. Also reduced by agents that inhibit RNA or pro- tein synthesis or oxidative phosphorylation (Hillman, Shafer, and Sang, 1973, Genet. Res. 21: 229-38). Supernatents from homogenates of A53g-bearing adults stimulate amino acid incor- poration and aminoacylation of tRNA more than those from wild type (Rose and Hillman, 1969, Biochem. Biophys. Res. Commun. 35: 197-204). Mutant late pupae and adults show increased concentrations of soluble protein. Expression of biochemical phenotype correlated with that of visible phenotype (Rose and Hillman, 1973, Genet. Res. 21: 239-245). RK2 in young cul- tures. cytology: Deficiency analysis places A53g in 3A5 (Hillman), which is at variance with the genetic position of A. # a-3: see a(3)26 #*A-p: Abnormal abdomen-polygenic location: Polygenic. discoverer: Sobels, 49i. references: 1950, DIS 24: 62. 1951, DIS 25: 75-76. 1952, Genetica 26: 117-279 (fig.). 1952, Trans. Intern. Congr. Entomol., 9th, Vol. 1: 225-30. synonym: AA; Asy: Asymmetric. phenotype: Incomplete mediodorsal fusion and onesided reduction of tergites. When more than one tergite is abnormal, spiral segmentation types are most frequent. Expression strongly dependent on environment. Penetrance and expressivity corre- lated (Bezem and Sobels, 1953, Koninkl. Ned. Akad. Weten- schap., Proc. Ser. C. 56: 48-61). In strains selected for penetrance of A-p, mediodorsal fusion or asymmetrical reduc- tion of head and thorax also occur. RK3. #*a(1)48: abnormal abdomen in chromosome 1 location: 1- (not located). origin: Spontaneous. discoverer: Zimmerman, 1948. references: 1952, DIS 26: 69. 1954, Z. Indukt. Abstamm. Vererbungsl. 86: 327-72 (fig.). phenotype: Used to describe three X chromosomes with little or no effect of their own but which increase the incidence of abdominal malformations in crosses with a(2) and a(3). Via- bility and fertility good. RK3. alleles: The three chromosomes designated *a(1)48, *a(1)50, and *a(1)51 (CP627). Genetic relations not worked out. # a(1)HM26 location: 1-(y-cv). origin: Induced by ethyl methanesulfonate. synonym: l(1)HM26. references: Mayoh and Suzuki, 1973, Can. J. Genet. Cytol. 15: 237-54. phenotype: Missing or reduced sternites; missing or angled ter- gites; black specks on ventral surface of abdomen in about one-third of males at 22 and more than half of males at 17. Viability reduced at 17 relative to that at 22. # a(1)HM27 location: 1-(near y). origin: Induced by ethyl methanesulfonate. synonym: l(1)HM26. references: Mayoh and Suzuki, 1973, Can. J. Genet. Cytol. 15: 237-54. phenotype: Same as a(1)HM26; more severe at 17 than at 22. Viability slightly reduced at 17 relative to that at 22. #*a(2)48 location: 2- (not located). origin: Spontaneous. discoverer: Zimmerman, 1948. references: 1952, DIS 26: 69. 1954, Z. Indukt. Abstamm. Vererbungsl. 86: 327-72 (fig.). phenotype: Abdominal irregularities most frequently involve anterior segments. Penetrance 7%. Also shows maternal effect. Viability and fertility good. RK3. alleles: Second chromosomes with some or all of these effects are *a(2)50, *a(2)51, and *A(2)51. Genetic relations not worked out. # a(3)26: see abd #*a(3)48 location: 3- (not located). origin: Spontaneous. discoverer: Zimmerman, 1948. references: 1952, DIS 26: 69. 1954, Z. Indukt. Abstamm. Vererbungsl. 86: 327-72 (fig.). phenotype: Only a maternal effect affecting 2.5% of progeny. Irregularities most frequently involve posterior segments of abdomen. Viability and fertility good. RK3. # A34: see bwV6 # aa: anarista location: 3-0. discoverer: Bridges, 23d10. synonym: al-b: aristaless-b. references: Morgan, Bridges, and Sturtevant, 1925, Bibliog. Genet. 2: 218. phenotype: Aristae bare or tufted. Wings somewhat broader than wild type. Expression variable, overlaps wild type often in female and sometimes in male. RK3. cytology: Placed between 61E2 and 62A6 on basis of its inclu- sion in Df(3L)D = Df(3L)61E2-F1;62A4-6 from T(Y;2;3)D. # Aa: Altered abdomen location: 1- (not located). origin: X ray induced in the In(1)dl-49, y w f component of C(1)DX. discoverer: Cicak, 56f. references: Cicak and Oster, 1957, DIS 31: 80. phenotype: Heavy deposition of melanin in tergites of females and males. Aa detachment-bearing males sterile. RK2A. cytology: Possibly associated with a rearrangement in addition to In(1)dl-49. # AA: see A-p # ab: abrupt location: 2-44.0. origin: Spontaneous. discoverer: Bridges, 16j16. references: Morgan, Bridges, and Sturtevant, 1925, Bibliog. Genet. 2: 218 (fig.). phenotype: Vein L5 usually stops after posterior crossvein. Scutellar bristles usually fewer. Wing effect probably acts during contraction period (Waddington). Overlaps wild type. Expression more severe in females than in males and when pupal stage takes place at 20 than at 25. TSP during the first 10% of pupal stage. (Thompson, Bruni, Carbonaro, and Russo, 1988, DIS 67: 86). RK2. alleles: ab1, ab2 (see below), ab51g, like ab2 in In(2L+2R)Cy; *abl-60h: abrupt lethal (CP627). ab: abrupt Edith M. Wallace, unpublished. # ab2 origin: Spontaneous. discoverer: Bridges, 23g6. synonym: pt: parted. references: Morgan, Bridges, and Sturtevant, 1925, Bibliog. Genet. 2: 232. phenotype: Vein L5 does not reach margin. Scutellar bristles always fewer than wild type. Hairs parted down midline of thorax and abdomen. Supra-alar bristles sometimes absent. Coxae tend to be thickened. Males sterile and have rotated genitalia. ab/ab2 resembles ab/ab but has a stronger bristle effect. RK2. # abb: abbreviated location: 2-105.5. discoverer: Bridges, 28d6. references: 1937, Cytologia (Tokyo), Fujii Jub., Vol. 2: 745- 55. phenotype: Bristles smaller, especially posterior scutellars. Developmental time slightly longer than normal. Viability only slightly reduced. Classification difficult, especially in early eclosions; improves with age of culture. Enhanced by shr (2-2.3), making classification easy. RK3; RK2 with shr. cytology: Placed in region between 59E2 and 60B10 by Bridges (1937) on basis of its being to the right of In(2R)bwVDe1 = In(2R)41B2-C1;59E2-4 and to the left of Df(2R)Px = Df(2R)60B8-10;60D1-2. abb: abbreviated From Bridges and Brehme, 1944, Carnegie Inst. Washington Publ. No. 552: 11. # abd: abdominal location: 3-27 (to the right of se). origin: Spontaneous. discoverer: H. A. and N. W. Timof'eff-Ressovsky. synonym: a-3, a(3)26. references: 1927, Wilhelm Roux's Arch. Entwicklungsmech. Organ. 109: 70-109. Schaffer, 1935, Z. Indukt. Abstamm. Vererbungsl. 68: 336-60 (fig.). phenotype: Irregular reduction of abdominal tergites, ster- nites, pigmentation, and bristles; more marked in females and increased by crowding and dry food (Braun, 1938, Am. Natural- ist 72: 189-92). Schaffer's data (1935) suggest irregular dominance in heterozygote, overlapping of wild type in homozy- gote, and genetic modifiers. RK3. alleles: abd2, spontaneous; recovered by Gottschewski, 1939. Partially complements abd1. Allelism inferred from similarity in genetic location and phenotype and incomplete complementa- tion. cytology: Placed in 66D9-E1 based on its inclusion in Df(3L)h- i22 = Df(3L)66D9-E1 (Ingham, Pinchin, Howard, and Ish- Horowicz, 1985, Genetics 111: 463-86). # abd-A: see BXC # Abd-B: see BXC # abdomen rotatum: see ar # abdominal: see abd # abe: see mit15 # abero: see abr # Abl: Cellular abl oncogene sequence location: 3-{44}. origin: Isolated from genome library using v-abl probe. synonym: Dash. references: Shilo and Weinberg, 1981, Proc. Nat. Acad. Sci. USA 78: 6789-92. Simon, Kornberg, and Bishop, 1983, Nature (London) 302: 837- 39. phenotype: Considered to be the Drosophila sequence homologous to mammalian c-abl based both on its origin and amino acid sequence as inferred from its nucleotide sequence. ABL protein detected at the time of germ-band shortening in the axons of the central nervous system in a bilateral sym- metrical series of points that correspond to the positions of neuromeres; later, protein appears in the axons growing across the midline, but not in the cell bodies of the CNS nor in the PNS. As development proceeds, staining of the longitudinal fascicles and to a lesser extent the commissural fascicles becomes intense; staining also seen in association with axonal outgrowth of neural cells in the eye imaginal disk (Bennett and Hoffmann). Recessive alleles in combination with Df(3L)st-j7 = Df(3L)73A1-2;73B1-2 either die as late pupae or pharate adults with complete cuticle and roughened eyes, Abll1, or as short lived (5-6 days), rough-eyed adults, Abll2 and Abll3. Surviv- ing females lay few eggs, some of which develop into adults; surviving males have motile sperm, but do not mate and produce no progeny. The rough eye is a reflection of some loss of photoreceptor cells plus ommatidial fusion. In combination with a deficiency extending further to the left, e.g., Df(3L)std11 = Df(3L)73A11-B1;73D1-2 to include the locus of Dab, Abll/Abl- genotypes die as late embryos or early first- instar larvae with disrupted axonal organization in the ven- tral nerve cord (Henkemeyer, Gertler, Goodman, and Hoffmann, Cell 51: 821-28). CNS of doubly deficient embryos, i.e., Abl- Dab-, fails to form commissures and is defective in axonal outgrowth, although the PNS develops normally. alleles: Three ethyl-methanesulfonate-induced recessive lethal or semilethal alleles recovered in combination with Df(3L)st4 or Df(3L)st-e5 by Belote, McKeown, and Hoffmann are designated Abll1, Abll2, and Abll3. Phenotypic descriptions given above. cytology: Localized to 73B by in situ hybridization with genomic clone (Simon et al.). molecular biology: Sequence isolated using v-abl probe from murine leukemia virus (Hoffman-Falk, Einat, Shilo, and Hoff- mann, 1983, Cell 35: 393-401). cDNA and genomic sequencing (Telford, Burkhardt, Butler, and Pirrotta, 1985, EMBO J. 4: 2609-15; Henkemeyer, Bennett, Gertler, and Hoffmann, 1988, Mol. Cell Biol. 8: 843-53) reveal a gene of ten exons distri- buted over 26 kb of genomic DNA; the exons encode a protein of 1520 amino acids, whose sequence is more similar to mammalian c-abl sequence than to that of any other gene; between resi- dues 187 and 656, which contains the tyrosine kinase essential domain, the Drosophila sequence is 75-85% similar to that of the human abl gene. 33 bp region beginning at tyrosine-416 84% homologous to mammalian nucleotide sequence and 62% homo- logous to C-src DNA from Drosophila (Hoffmann, Fresco, Hoffman-Falk and Shilo, 1983, Cell 35: 393-401). The polypeptide product as yet unidentified but presumed to be a protein kinase; Drosophila extracts do contain a tyrosine kinase activity (Simon et al.). The carboxy half of the ABL protein is not conserved between flies and mammals. Expres- sion of the kinase essential domain in bacteria leads to excessive phosphorylation of proteins at tyrosine residues. Developmental Northerns probed with 800 base-pair sequence from region of highest homology with v-abl reveal a 6.2 kb polyadenylated transcript in early but not late embryos, lar- vae or adults; most abundant in 0-4 hr embryos; absent after 8 hr (Lev, Liebovitz, Segev, and Shilo, 1984, Mol. Cell. Biol. 4: 982-84); returns in a burst of activity in early pupae. # Abnormal: see A # abnormal abdomen: see a( ) # Abnormal abdomen: see A # abnormal eye: see mit15 # abnormal oocytes: see abo # abnormal tergites: see abt # abnormal wings: see abw # abo: abnormal oocyte location: 2-44.0 (mapped with respect to J, 2-41). origin: Naturally occurring allele recovered near Rome, Italy. references: Sandler, Lindsley, Nicoletti, and Trippa, 1969, Genetics 64: 481-93. Mange and Sandler, 1973, Genetics 73: 73-86. Sandler, 1970, Genetics 64: 481-93. 1975, Israel J. Mol. Sci. 11: 1124-34. 1977, Genetics 86: 567-82. phenotype: Probability of survival of embryos produced by abo/abo mothers reduced; male embryos more severely affected than female embryos. Both preblastoderm and postblastoderm embryonic death observed; partial rescue of postblastoderm mortality effected by paternally inherited abo+ allele; par- tial rescue of preblastoderm mortality by heterochromatic ABO elements located in Xh between 3/4 and 7/8 of the distance from the centromere, in YL region h10-11, in YS region h19, in 2R proximal, and perhaps in other heterochromatic regions (Pimpinelli, Sullivan, Prout, and Sandler, 1985, Genetics 109: 701-24). Gradual loss of phenotype in homozygous abo stocks accompanied by increase in quantity of ribosomal DNA (Krider and Levine, 1975, Genetics 81: 501-13). New restric- tion fragments appear in Hind III/Hae III double digests of such homozygous lines probed with nontranscribed spacer sequences of ribosomal genes (Graziani, Vicari, Boncinelli, Malva, Manzi, and Mariani, 1981, Proc. Nat. Acad. Sci. USA 78: 7662-64). abo phenotype returns with subsequent mainte- nance in heterozygous condition. Homozygous abo females exhi- bit moderate decrease in recombination with concommitant increase in exceptional progeny (Carpenter and Sandler, 1974, Genetics 76: 453-75). cytology: Located in 31F-32E based on its inclusion in Df(2L)J39 = Df(2L)31A-B;32E but not Df(2L)J27 = Df(2L)31B- D;31F or Df(2L)Mdh = Df(2L)30D-F;31F. abo-bearing chromosomes differ from others in having a blood insertion sequence in 32E (Lavorgna, Malva, Manzi, Gigliotti, and Graziani, 1989, Genet- ics 123: 485-94). # ABO A series of heterochromatic elements capable of reducing the level of maternally influenced preblastoderm, but not post- blastoderm, mortality among the progeny of abo/abo mothers; embryos that carry ABO elements survive better than those that do not (Pimpinelli, Sullivan, Prout, and Sandler, 1985, Genet- ics 109: 701-24). Elements identified to date and their heterochromatic locations, where known, are listed in the accompanying table. The rescuing capability of ABO-X approxi- mates that of ABO-YL + ABO-YS. ABO-X apparently defective in In(1)sc4 (Malva, Labella, Manzi, Salzano, Lavorgna, De Ponti, & Graziani, 1985, Genetics 111: 487-94). Effectiveness of ABO-X and ABO-2R appears to be enhanced by maintenance in a homozygous abo stock (Sullivan and Pimpinelli, 1986, Genetics 114: 885-95). element cytology _______________________ ABO-2R ABO-X h26-28 ( ABO-YL h10-11 ABO-YS h19 ( In region that includes proximal half of h26 and distal half of h28 (Pimpinelli, Sullivan, Prout, and Sander, 1985, Genetics 109: 701-24). # abr: abero location: 2-83. origin: Spontaneous. discoverer: Bridges, 33b10. phenotype: Abdominal banding etched and irregular. Wing mar- gins irregular. Eyes rough. Bristles and hairs sparse and disarranged. abr/+ sometimes lacks anterior dorsocentrals. Viability usually poor. RK3. other information: Not allelic to fr or nw. # abrupt: see ab # Abruptex: see Ax, listed under N: Notch #*abt: abnormal tergites location: 1-45.6. origin: Induced by 2-chloroethyl methanesulfonate. discoverer: Fahmy, 1955. references: 1959, DIS 33: 83. phenotype: Abdomen affected to various degrees, from extreme deformation of tergites to slight abnormalities in distribu- tion of pigment and hairs. Eyes also deformed to various degrees from gross alterations in shape to slight derangement of ommatidia. Wings vary from alterations in size, outline, and venation to small incisions of the inner margin. Most- extreme effects not always positively correlated, and all flies show several atypical characters. Males viable; fertil- ity severely reduced. RK3. #*abw: abnormal wings location: 1-60. origin: X ray induced. discoverer: Halfer, 1963. phenotype: Wing size reduced; wings upturned; L5 and crossveins absent. Plexus of veins between L3 and L4. RK1. # abx: see BXC # ac: see ASC # Ac: see CuA # Ac-SD: see Rsp # acc: acclinal wing location: 1-54.5. origin: Induced by triethylenemelamine. discoverer: Fahmy, 1952. references: 1958, DIS 32: 67. phenotype: Wings upheld but slope backward at 45 angle from abdomen. Unable to fly or jump; muscles normal in gross and ultrastructural morphology. Mosaic experiment suggests possi- ble thoracic neural etiology (Deak, 1976, J. Insect Physiol. 22: 1159-65). Viability and fertility good in both sexes. RK1. alleles: One allele each induced by D-p-N,N-di-(2- chloroethyl)amino-phenylalanine and by DL-p-N,N-di-(2- chloroethyl)amino-phenylalanine. # Ace: Acetyl cholinesterase (J.C. Hall) location: 3-52.2. synonym: l(3)26. references: Hall and Kankel, 1976, Genetics 83: 517-35. Greenspan, Finn, and Hall, 1980, J. Comp. Neurol. 189: 741- 74. Hall, Alahiotis, Strumpf, and White, 1980, Genetics 96: 939- 65. phenotype: The structural gene for acetylcholinesterase [AChE, acetylcholine acetyl hydrolase (EC 3.1.1.7)], the enzyme that terminates synaptic transmission by rapidly hydrolyzing the neurotransmitter acetylcholine. Biochemical analysis (e.g., Zingde, Rodrigues, Joshi, and Krishnan, 1983, J. Neurochem. 41: 1243-52; Gnagey, Forte, and Rosenberry, 1987, J. Biol. Chem. 262: 13290-98; Fournier, Bride, Karch, and Berge, 1988, FEBS Lett. 238: 333-37; Haas, Marshall, and Rosenberry, 1988, Biochemistry 27: 6453-57; Toutant, Arpagaus, and Fournier, 1988, J. Neurochem. 50: 209-18; Fournier, Berge, Almeida, and Bordier, 1988, J. Neurochem. 50: 1158-63), indicates that the mature enzyme contains noncovalently associated subunits of 16 and 55 kd, which are processed from a primary translation pro- duct of ca 70 kd such that the 16-kd moiety is from the N ter- minus and the 55-kd moiety is from the C terminus; two such associations are linked via disulfide bonds connecting the 55-kd polypeptides anchored to membrane via a glycoinositol phospholipid anchor covalently linked to the C termini of the 55-kd subunits. Extracts contain amphiphilic dimers and mono- mers as well as hydrophilic dimers and monomers, which lack the glycoinositol phospholipid anchor. Developmental profile studied by Dewhurst, McCaman, and Kaplan (1970, Biochem. Genet. 4: 499-508; see also Arpagaus, Fournier, and Toutant, 1988, Insect Biochem. 18: 539-49); total AChE activity shows a transient peak during first larval instar and rises again to a maximum in the adult. In the developing eye disc, AChE first appears in retinula cells three to four days before they are functional and when it cannot have a synaptic function; levels are reduced in retinula cells midway through pupal development, and the enzyme accumulates rapidly in the neuro- pils of the optic lobes of the brain and the midbrain (Wolf- gang and Forte, 1989, Dev. Biol. 131: 321-30). Putative nulls are lethal at end of embryonic stage; then ultrastructural observations of CNS in such mutants suggest neural- degenerative defects (Chase and Kankel, 1988, Dev. Biol. 125: 361-80). ACE-minus tissues survive in mosaics unless enzyme absent from posterior midbrain; surviving mosaics have defective visual physiology, optomotor behavior or courtship, depending on location of mutant clone. Such clones associated with defective morphology or neuropile of various ganglia in central nervous system (Greenspan et al., 1980). In heat- sensitive combinations of Ace mutations (Greenspan et al., 1980), both membrane-bound and soluble enzyme has reduced activity (Zador, 1989, Mol. Gen. Genet. 218: 487-90). alleles: Unless noted otherwise in comments column alleles are null as is Ace1. allele origin discoverer synonym ref ( comments ____________________________________________________________________________ Ace1 | X ray Schalet l(3)26 4, 8 Ace2 EMS Deland l(3)m15 4 Ace3 EMS Hilliker, Clark l(3)B2-5 4 Ace4 EMS Hilliker, Clark l(3)B4-2 4 Ace5 EMS Hilliker, Clark l(3)B8-2 4 Ace6 EMS Hilliker, Clark l(3)B15-2 4 hypomorphic Ace7 EMS Hilliker, Clark l(3)B22-1 4 Ace8 EMS Hilliker, Clark l(3)B22-2 4 hypomorphic Ace9 EMS Hilliker, Clark l(3)B27-1 4 Ace10 EMS Hilliker, Clark l(3)B29-1 4 Ace11 EMS Hilliker, Clark l(3)B29-2 4 Ace12 EMS Hilliker, Clark l(3)H36 4 Ace13 EMS Hilliker, Clark l(3)H41 4 Ace14 EMS Hilliker, Clark l(3)H89 4 Ace15 EMS Hilliker, Clark l(3)B21-5 4 Ace16 EMS Hilliker, Clark l(3)H15 4 AceHD1 | HD 6 Acej19 EMS 1 Acej21 EMS 1 Acej27 EMS 1 Acej29 | EMS 1, 2 cold sensitive Acej31 EMS 1 Acej32 EMS 1 Acej33 EMS 1 Acej39 EMS 1 Acej40 | EMS 1, 2, 7 few survivors; suppressor of variegation Acej41 EMS 1 Acej43 EMS 1 Acej44 | EMS 1 Acej45 EMS 1 Acej50 EMS 1 Acej51 EMS 1 Acej53 EMS 1 Acej55 EMS 1 Acelm35 | EMS 3 hypomorphic Acelm38 EMS 3 Acelm115 EMS 3 AceG11 EMS Gelbart Acemr | spont 5 ( 1 = Greenspan, Finn, and Hall, 1980, J. Comp. Neurol. 189: 741-74; 2 = Hall, Alahiotis, Strumpf, and White, 1980, Genetics 96: 939-65; 3 = Hall and Kankel, 1976, Genetics 83: 517-35; 4 = Hilliker, Clark, Gelbart, and Chovnick, 1981, DIS 56: 65-72; 5 = Mortan and Singh, 1982, Biochem. Genet. 20: 179-98; 6 = Nagoshi and Gelbart, 1987, Genetics 117: 487-502; 7 = Reuter, Gausz, Gyurkovics, Friede, Bang, Spierer, Hall, and Spierer, 1987, Mol. Gen. Genet. 210: 429-36; 8 = Schalet, Kernaghan, and Chovnick, 1964, Genetics 50: 1261-68. | More detailed description below. cytology: Located in 87E3 based on its location between Df(3R)ry1301 = Df(3R)87D2-4;87E1-2 and Df(3R)GE41 = Df(3R)87E4 (Hall and Spierer 1986, EMBO J. 5: 2949-54). molecular biology: Locus comprises ten exons and nine introns distributed within a 34-kb transcription unit (Fournier, Karch, Bride, Hall, Berge, and Spierer, 1989, J. Mol. Biol. 210: 15-22) extending from approximately coordinates 18 to 52 kb on the molecular map of Bender, Spierer, and Hogness (1983, J. Mol. Biol. 168: 17-33) whose origin is 6.5 kb to the left of the left breakpoint of In(3R)Cbxrv1 with positive values extending to the right. Transcription takes place from right to left. The 5 untranslated region is transcribed from exons I and II; the signal sequence is encoded in exon II, the 16-kd polypeptide by exons II, III, and IV; the 55-kd polypeptide by exons IV, V, VI, VII, VIII, and IX; the hydrophobic peptide exchanged in mature protein with a glycolipid anchor as well as the 3 untranslated region by exon X. The mature tran- scripts are estimated at 4.2 and 4.5 kb (Nagoshi and Gelbart, 1987, Genetics 117: 487-502). cDNA sequencing (Hall and Spierer, 1986; Fournier et al., 1989) indicates mature tran- script of 4291 nucleotides encoding a 650-amino-acid protein product, which displays a high degree of homology with AChE from Torpedo californica; however, the Drosophila protein car- ries a 38-amino-acid signal sequence lacking in Torpedo, and a 41-amino-acid hydrophilic sequence extending from residues 140 to 180 that is not contained in the Torpedo sequence; the latter is encoded by exons III and IV, and contains the site of proteolytic cleavage of the Drosophila AChE primary trans- lation product. # Acel phenotype: Temperature insensitive lethal; lethal in homozy- gotes or in combination with deficiency for Ace+. Lethality at end of embryonic stage. Greatly reduced levels of acetyl- cholinesterase. AChE-minus tissues survive in mosaics unless enzyme absent from posterior midbrain; surviving mosaics have defective visual physiology, optomotor behavior, or courtship depending on location of mutant clone. Such clones associated with defective morphology of neuropile of various ganglia in central nervous system. molecular biology: DNA insert in fifth intron (Fournier et al., 1989) observed at approximately coordinate +30; separable by recombination from the Ace1 mutation (Nagoshi and Gelbart, 1987, Genetics 117: 487-502). # AceHD1 phenotype: Retains some ACE activity (Nagoshi and Gelbart, 1987, Genetics 117: 487-502), but only as soluble enzyme out- side CNS (Zudor et al., 1986). molecular biology: Deleted of promoter region and first (non- coding) exon (Fournier et al., 1989). # Acej29 phenotype: The original allele of this complementation group. Cold sensitive lethal. Maximum survival of Acej29/Df(3R)l26d at 27, no survival at 18. Exposure to 18 does not reduce AChE activity. Acej29 alters Km of enzyme, further implying struc- tural gene locus. # Acej40 phenotype: Nearly completely lethal. Two percent survival in combination with Df(3R)l26d at 18, none at 29. Partial com- plementation of Acej19 and Acej50; heat sensitive; extracts of Acej40 lack the 110 kilodalton molecular species, whereas Acej19 and Acej50 lack the 64 and 75 kilodalton species (Zingde, Rodrigues, Joshi, and Krishnan, 1983, J. Neurochem. 41: 1243-52). Enzyme produced by heteroallelic combinations raised under permissive conditions is thermolabile. Exposure of Acej40/Acej19 or Acej40/Acej50 flies to restrictive tem- perature during late embryonic-early larvae stage lethal; lit- tle effect on mid and late larval stages; pupal exposure causes defects in adult phototaxis and motor activity. Heat treatment of adults causes no decline in ACE activity but decrements in phototaxis (29), and cessation of movement (31) observed. Acej40 produces enzyme with altered Km. molecular biology: Appears to map proximal to a DNA insert located between coordinates +43 and +48 (Nagoshi and Gelbart, 1987). # Acej44 molecular biology: Associated with a molecularly defined struc- tural variation; probably loss of a Bam H1 site around coordi- nate +33 (Gausz, Hall, Spierer, and Spierer, 1986, Genetics 112: 65-78). Structural variant and mutation appear to be inseparable by recombination (Nagoshi and Gelbart, 1987). # Acelm35 phenotype: Hypomorphic allele. Exhibits reduced survival (< 30%) in combination with Df(3R)l26d. Enzyme activity in Acelm35/+ heterozygotes lower than in heterozygotes for more severe alleles. # Acemr: Acetylcholinesterase-malathion resistant origin: Recovered from line selected for malathion resistance. phenotype: Acetylcholinesterase from homozygotes has lower Km, lower activity, and slightly increased electrophoretic mobil- ity compared to wild type. Relation to malathion resistance unclear. # ACE1: Amplification Control Element on chromosome 1 A sequence required for amplification in ovarian follicle cells of the cluster of chorion-protein genes located at 7F1-2 (Cp36 and Cp38); provisionally located between 654 and 266 base pairs upstream from Cp38 (Wakimoto). # ACE3 A sequence required for amplification in ovarian follicle cells of the cluster of chorion-protein genes located at 66D11-15 (Cp15, Cp16, Cp18 and Cp19); located between 615 and 187 base pairs upstream from Cp18 (Kalfayan, Levine, Orr- Weaver, Parks, Wakimoto, deCicco, and Spradling, 1985, Cold Spring Harbor Symp. Quant. Biol. 50: 527-35). # Acetyl choline receptor: see Acr # achaete: see ac under ASC # Ach: see emcD # Acp: Accessory gland protein Genes inferred from bands on SDS polyacrylamide gels. Six polypeptides are highly polymorphic, exhibiting several elec- trophoretic variants; these all map to chromosome 2 and are tabulated below. Codominant expression indicates that vari- ants are in structural genes and not attributable to differ- ences in post-translational modification (Whalen and Wilson, 1986, Genetics 114: 77-92). genetic cytological molecular locus location location mass (kd) ____________________________________________________ AcpA 2- 165-70 AcpB 2-42.8 36D1-E4 130-140 AcpC ( 2-53.0 125-128 Acp-g1 ( 2-13.5 145-163 AcpJ 2- 45 AcpK ( 2-54.1 43 ( variants include a null allele. # Acp70A: Accessory gland peptide location: 3-{40}. references: Chen, Stumm-Zollinger, Aigaki, Balmer, Bienz, and Bohlen, 1986, Cell 54: 291-98). phenotype: Encodes a 36-amino-acid peptide that is synthesized in the accessory gland and is transferred to the female where it represses female sexual receptivity and stimulates oviposi- tion. The peptide contains a high concentration of basic amino acids, tryptophan and hydroxyproline as well as an unique residue of unknown nature that is encoded by a leucine codon. cytology: Placed in 70A by in situ hybridization. molecular biology: Gene cloned and sequenced; conceptual sequence indicates a hydrophobic amino-terminal signal sequence of 19 residues. mRNA for prepeptide accumulates exclusively in the male accessory gland. # Acph-1: Acid phosphatase 1 location: 3-101.1 (between ca and bv). discoverer: MacIntyre, 1964. references: 1966, DIS 41: 61. 1966, Genetics 53: 461-74. phenotype: Structural gene for acid phosphatase 1 [ACPH- 1 (EC3.1.3.2)], the major phosphatase in adults; responsible for approximately 90% of the low-pH nucleotidase activity throughout development. Glycoprotein homodimer with subunit molecular weight of 50,000 daltons. Purification and biochem- ical characterization by Feigen, Mitrick, Johns, Postlethwait, and Sederoff (1980, J. Biol. Chem. 255: 10338-43). Serves as a reliable cytochemical marker in many tissues (Hall, 1979, Genetics 92: 437-57). Enzyme appears to be produced in nurse cells and follicular cells of ovary and transferred to oocyte through the ring canals and by pinocytosis, respectively (Sawicki and MacIntyre, 1977, Dev. Biol. 60: 1-13); mater- nally produced enzyme persists to third instar; paternal gene function detectable in gels after 9-10 hr of embryonic development (Yasbin, Sawicki, and MacIntyre, 1978, Dev. Biol. 63: 35-46); and after 5 hr histochemically (Sawicki and MacIntyre, 1978, Dev. Biol. 63: 47-58). Enzyme found in lar- vae, pupae, and adults; levels increase during adult life (Postlethwait and Gray, 1975, Dev. Biol. 47: 196-205). alleles: In addition to the information tabulated below, pair- wise combinations of Acph-1n2, Acph-1n3, Acph-1n6, and Acph- 1n9 exhibit 20-40% normal levels of cross reacting material (CRM). allele origin derivative of discoverer ref ( comments _____________________________________________________________________ Acph-1A spont MacIntyre 4 slow Acph-1B spont MacIntyre 4 intermediate Acph-1C spont MacIntyre 4 fast Acph-1n1 EMS Acph-1B MacIntyre 1 A-like mobility in heterodimer Acph-1n2 EMS Acph-1A MacIntyre 1 Acph-1n3 EMS Acph-1B MacIntyre 1 Acph-1n4 EMS Acph-1A MacIntyre 1 0-5% normal CRM Acph-1n5 EMS Acph-1A MacIntyre 1 0-5% normal CRM Acph-1n6 EMS Acph-1B MacIntyre 1 A-like mobility in heterodimer Acph-1n7 EMS Acph-1B MacIntyre 1 Acph-1n8 EMS Acph-1A MacIntyre 1 0-5% normal CRM Acph-1n9 EMS Acph-1B MacIntyre 1 Acph-1n10 EMS Acph-1A MacIntyre 1 Acph-1n11 EMS Acph-1B MacIntyre 1 0-5% normal CRM Acph-1n12 EMS Acph-1B MacIntyre 1 Acph-1n13 EMS Acph-1B MacIntyre 1 0-5% normal CRM Acph-1n14 EMS Acph-1A MacIntyre 1 B-like mobility in heterodimer Acph-1n15 EMS Acph-1A MacIntyre 1 0-5% normal CRM Acph-1nGB1 spont Acph-1B 2, 3 B-like mobility in heterodimer Acph-1nGB2 spont Acph-1B 2, 3 Acph-1nNC1 spont Acph-1B 2, 3 ( 1 = Bell, MacIntyre, and Olivieri, 1972, Biochem. Genet. 6: 205-16; 2 = Burkhart, Montgomery, Langley, and Voelker, 1984, Genetics 107: 295-306; 3 = Langley, Voelker, Leigh Brown, Ohnishi, Dickson, and Montgomery, 1981, Genetics 99: 151-56; 4 = MacIntyre, 1968, DIS 3: 60. cytology: Located between 99C5 and 7 based on its deletion by Df(3R)ca-R14 = Df(3R)99A8-9;99D1-2 but not by Df(3R)ca-165P = Df(3R)99B2-4;99C5-6 (Frisardi and MacIntyre, 1984, Mol. Gen. Genet. 197: 403-13). # Acr60C: Acetyl choline receptor in 60C location: 2-{107}. references: Shapiro, Wakimoto, Subers, and Nathanson, 1989, Proc. Nat. Acad. Sci. USA 86: 9039-43. Onai, FitzGerald, Arakawa, Gocayne, Urquhart, Hall, Fraser, McCombie, and Venter, 1989, FEBS Lett. 255: 219-25. phenotype: The structural gene encoding a Drosophila homologue of vertebrate muscarinic acetylcholine receptor (mAChR). When expressed in Y1 adrenal cells it is physiologically active as measured by agonist dependent stimulation of phosphatidylino- sitol metabolism. cytology: Placed in 60C7-8 by in situ hybridization. molecular biology: Genomic clone isolated from library using a probes from vertebrate muscarinic acetylcholine receptor genes. Nucleotide sequences of cDNA clones reveal a long open reading frame that encodes a 788-amino-acid protein with cal- culated molecular weight of 84,807 (Onai et al.). The amino- acid sequence shows a number of features characteristic of the muscarinic/adrenergic receptor gene superfamily in ver- tebrates: three potential N-linked glycosylation sites (Asn 65, 84, and 87), seven putative membrane-spanning domains. It displays a high degree of amino-acid identity with vertebrate muscarinic acetylcholine receptors, ~60% overall and up to 88% in transmembrane regions; the segment between transmembrane domains 5 and 6 is considerably longer than that of vertebrate sequences; also the gene has three introns in the region. # Acr64B location: 3-{8}. synonym: ard. references: Hermans-Borgmeyer, Zopf, Ryseck, Hovemann, Betz, and Gundelfinger, 1986, EMBO J. 5: 1503-08. Wadsworth, Rosenthal, Kammermeyer, Potter, and Nelson, 1988, Mol. Cell Biol. 8: 778-85. Sawruk, Hermans-Borgmeyer, Betz, and Gundelfinger, 1988, FEBS Lett. 235: 40-46. phenotype: Structural gene encoding a Drosophila homologue of a subunit of vertebrate nicotinic acetylcholine receptors (nAChR). Antibody raised against Acr64B fusion proteins immu- noprecipitate one of two high-affinity (-bungarotoxin-binding sites from detergent extracts of Drosophila head membranes (Schloss, Hermans-Borgmeyer, Betz, and Gundelfinger, 1988, EMBO J. 7: 2889-94). In situ hybridization localizes Acr64B expression to nervous tissue, especially in late embryos, pupae, and newly eclosed adults (Hermans-Borgmeyer, Hoffmeis- ter, Sawruk, Betz, Schmitt, and Gundelfinger, 1989, Neuron. 2: 1147-56). cytology: Placed in 64B by means of in situ hybridization. molecular biology: Genomic clones identified using a Torpedo californica nAChR probe; these hybridize to a 3.2-kb mRNA present at high levels on developmental Northern blots in late embryos and during metamorphosis, periods of neuronal dif- ferentiation. Genomic probes used to isolate overlapping cDNA clones. The gene comprises six exons distributed over approx- imately seven kb of genomic sequence. The predicted mature protein after cleavage of a 24 amino-acid signal sequence, consists of 497 amino acids, has a calculated molecular weight of 57,340 and shows extensive homology to all known nAChR genes of other species along its entire amino acid sequence, conforming most closely to neuronal ( subunits, although it lacks the cysteine doublet at residues 201 and 202 charac- teristic of all other ( subunits. It contains four putative transmembrane domains, a potential amphipathic ( helix, and a canonical N-glycosylation site Asn48; however, the N-linked glycosylation site found at residue 141 in all vertebrate nAChR's is absent in Drosophila. # Acr96A location: 3-{83}. synonym: ALS: Alpha-Like Subunit. references: Bossy, Ballivet, and Spierer, 1988, EMBO J. 7: 611-18. phenotype: Structural gene encoding a Drosophila homologue of a subunit of vertebrate nicotinic acetylcholine receptors (nAChR); inferred to be homologous to neuronal ( subunits based on the cystein doublet at amino-acid residues 201 and 202. cytology: Placed in 96A by in situ hybridization. molecular biology: Genomic clones identified using as a probe a fragment of the chick neuronal nAChR(2 gene; these hybridize to a 10.5 kb mRNA present at high levels on developmental Northern blots from late embryo to pupation, decreasing in late pupae and adults; genomic probes used to isolate overlap- ping cDNA clones. The gene comprises ten exons distributed over 54 kb of genomic sequence; combined nucleotide sequence from the cDNA clones defines a single long open reading frame of 1701 nucleotides bracketed by 1282 5 and 514 3 nucleo- tides. The ORF encodes 567 amino acids, which show 40-44% sequence conservation with mammalian neuronal nAChR ( subunits and with Drosophila Acr64B product. Structural domains homo- logous to those of vertebrate nAChR subunits include a cystein doublet at residues 201 and 202 that characterizes all ( subunits, four transmembrane domains, two potential glycosyla- tion sites (Asn 24 and 212) characteristic of vertebrate neu- ronal ( subunits, and an amphipathic (-helical region in the C-terminal quarter of the polypeptide. In addition, the posi- tions of four Drosophila introns correspond exactly to those of four of seven vertebrate AChR introns. # Activator of SD: see Rsp # act: actidione sensitive location: 3-90 (21 units to the right of H). origin: Naturally occurring allele. references: Marzluf, 1969, Biochem. Genet. 3: 229-38. phenotype: act/act killed by 0.1 the concentration of actidione (cycloheximide) that act+-bearing strains survive. alleles: Recessive allele fixed in Oregon-R and Canton-S strains. Urbana-S and Swedish-b carry act+. # Act5C: Actin in region 5C location: 1-{14}. references: Tobin, Zulauf, S'nchez, Craig, and McCarthy, 1980, Cell 19: 121-31. Fyrberg, Kindle, Davidson, and Sodja, 1980, Cell 19: 365-78. Fyrberg, Bond, Hershey, Mixter, and Davidson, 1981, Cell 24: 107-16. phenotype: Codes for cytoplasmic actin; transcribed throughout development; one of two actin genes transcribed in Kc cells and several other cell lines (Fyrberg, Mahaffy, Bond, and Davidson, 1983, Cell 33: 115-23). One of three actin genes expressed in the wing disc during wing development, each with its characteristic profile. Peak expression at 44h of pupal age, little or no expression at 60h rising again at 80h. 44h peak corresponds to time of maximum change in cell shape (Peterson, Bond, Mitchell, and Davidson, 1985, Dev. Genet. 5: 219-25). Transcripts present in the preblastoderm embryo suggesting maternal transcription; during blastoderm forma- tion, Act5C transcripts accumulate at the periphery of the embryo; local concentrations of transcript observed in ante- rior and posterior midgut rudiments in stage 13 embryos; hybridization also observed in the developing ventral nervous system. Later in embryogenesis, transcript found in all tis- sues but with dramatic concentrations of transcripts in the anterior and posterior midgut and the proventriculus. Exon specific probes demonstrate that transcripts containing exon 1 tend to be concentrated in anterior portions of early embryos, including the anterior midgut primordium and the proventri- culus, as well as in the posterior midgut primordium; during germ-band extension, small local concentrations of exon 2 transcripts are seen in posterior and ventral regions of the embryo (Burn, Vigoreaux, and Tobin, 1989, Dev. Biol. 131: 345-55). cytology: Localized to 5C2-5 based on failure of Act5 specific probe to hybridize to either Df(1)N73 = Df(1)5C2;5C5-6 or Df(1)C149 = Df(1)5A8-9;5C5-6 (Sodja, Rizki, Rizki and Zafar, 1982, Chromosoma 86: 293-98). molecular biology: Genomic clone restriction mapped (Fyrberg et al., 1980) and partially sequenced (Fyrberg et al., 1981). Comparison with cDNA clones indicates the presence of three exons, two of which are included in any cDNA (Bond and David- son, 1986, Mol. Cell Biol. 6: 2080-88). Partial sequence (Bond and Davidson; Vigoreaux and Tobin, 1987, Genes Dev. 1: 1161-71) indicate that all protein encoding sequences reside in exon 3, that either exon 1 or exon 2 is spliced to exon 3, and that there are three transcription start sites, one in exon 1 and two in exon 2, giving rise to different 5 untranslated regions; also there are indications of at least three polyadenylation sites generating messages with 3 untranslated regions of 375, 655, and 945 nucleotides. Using discriminating 5 and 3 probes, Burn, Vigoreaux, and Tobin (1989) have shown that transcripts differing in 5 untranslated regions display different tissue specificities; no 3 specificities are seen. Exons 1 and 2 are each preceded by a functional promoter (Bond-Matthews and Davidson, 1988, Gene 62: 289-300). # Act42A location: 2-55.4 (inferred from polytene position). references: Tobin, Zulauf, S'nchez, Craig, and McCarthy, 1980, Cell 19: 121-31. Fyrberg, Bond, Hershey, Mixter, and Davidson, 1981, Cell 24: 107-16. phenotype: Codes for cytoplasmic actin; transcribed throughout development; one of two actin genes transcribed in Kc cells and several other cell lines (Fyrberg, Mahaffy, Bond, and Davidson, 1983, Cell 33: 115-23). One of three actin genes expressed in the wing disc during wing development, each with its characteristic profile. Peak expression at 44h of pupal age, little or no expression at 60h rising again at 80h. 44h peak corresponds to time of maximum change in cell shape (Peterson, Bond, Mitchell, and Davidson, 1985, Dev. Genet. 5: 219-25). cytology: Located in 42A by in situ hybridization. molecular biology: Genomic clone = \DmA3. Partial nucleotide sequence in Fyrberg et al. (1981). # Act57A location: 2-{93}. references: Tobin, Zulauf, S'nchez, Craig, and McCarthy, 1980, Cell 19: 121-31. Fyrberg, Kindle, Davidson, and Sodja, 1980, Cell 19: 365-78. Fyrberg, Bond, Hershey, Mixter, and Davidson, 1981, Cell 24: 107-16. phenotype: According to Fyrberg and Davidson, Act57A encodes the actin I protein isoform, which is the major actin species of larval intersegmental muscle; also encodes adult cephalic and abdominal muscle (Fyrberg, Mahaffy, Bond and Davidson, 1983, Cell 33: 115-33). cytology: Localized to 57A by in situ hybridization. molecular biology: Genomic clone = \DmA4; coding region res- triction mapped and partially sequenced (Fyrberg et al., 1981). Intervening sequence of approximately 630 base pairs inserted in the glycine codon at amino acid position 13 (Fyr- berg et al., 1981). # Act79B location: 3-{47.5}. references: Tobin, Zulauf, S'nchez, Craig, and McCarthy, 1980, Cell 19: 121-31. Fyrberg, Kindle, Davidson, and Sodja, 1980, Cell 19: 365-78. Fyrberg, Bond, Hershey, Mixter, and Davidson, 1981, Cell 24: 107-16. Zulauf, S'nchez, Tobin, Rdest, and McCarthy, 1981, Nature 292: 556-58. S'nchez, Tobin, Rdest, Zulauf, and McCarthy, 1983, J. Mol. Biol. 163: 533-51. phenotype: According to Zulauf et al. (1981), Act79B appears to code for actin I, a larval muscle-specific actin. Initial translation product, which migrates as actin II, apparently acetylated to become actin I. Using probe from 3' transcribed-but-not-translated sequences, S'nchez et al. demonstrated two minor peaks of transcription during embryo- genesis and major peaks during first and second instar and to a lesser degree in the pupa. Fyrberg, Mahaffy, Bond, and Davidson, (1983, Cell 33: 115-23) on the other hand, find Act79B to be expressed in adult legs and tubular muscles of thorax, including direct flight muscles, pleurosternal mus- cles, and muscles of various leg segments. In addition, Act79B is expressed in muscles that support the head and abdo- men, in the scutellar pulsatile organ, and in two pairs of abdominal muscles that are present only in male flies (Courchesne-Smith, and Tobin, 1989, Dev. Biol. 133: 313-21). One of three actin genes expressed in wing development each with its characteristic developmental profile; peak activity at 80h of pupal age (Petersen, Bond, Mitchell, and Davidson, 1985, Dev. Genet. 5: 219-25. cytology: Localized to 79B by in situ hybridization. molecular biology: Genomic clone by Zulauf et al. (1981) and as \DmA6 by Fyrberg et al. (1981). Coding region restriction mapped and partially sequenced by Fyrberg et al. (1981). Intervening sequence of 357 nucleotides within a glycine codon at position 307 (Fyrberg et al., 1981). Coding sequences, intervening sequences and flanking sequences completely sequenced (S'nchez et al.). Encodes a 374-amino-acid 43-kd polypeptide which is 95% homologous with the product of Act88F and 91% homologous with rabbit actin. # Act87E location: 3-{52.3}. references: Tobin, Zulauf, S'nchez, Craig, and McCarthy, 1980, Cell 19: 121-31. Fyrberg, Kindle, Davidson, and Sodja, 1980, Cell 19: 365-78. Fyrberg, Bond, Hershey, Mixter, and Davidson, 1981, Cell 24: 107-16. phenotype: Encodes actin found in larval muscle and adult cephalic and abdominal muscle (Fyrberg, Mahaffey, Bond, and Davidson, 1983, Cell 33: 115-23). alleles: No lethal alleles of Act87E recovered in a lethal- saturation study (Manseau, Ganetzky, and Craig, 1988, Genetics 119: 407-20). cytology: Placed in 87E9-12 by in situ hybridization; included in Df(3R)ry619 = Df(3R)87D7-9;87E12-F1, but not in Df(3R)ry1168 = Df(3R)87B15-C1;87E9-12 (Manseau et al., 1988). molecular biology: Genome clone restriction mapped and par- tially sequenced by Fyrberg et al. (1981). Comparison of genomic and cDNA sequence indicates a 556 nucleotide intron in the 5 untranslated region. Conceptual amino-acid sequence shows ~95% identity with other Drosophila actins (Manseau et al., 1988). # Act88F location: 3-57.1 (based on 41 cu-sr and 84 red-e recombinants). references: Tobin, Zulauf, Sanchez, Craig, and McCarthy, 1980, Cell 19: 121-31. Fyrberg, Kindle, Davidson, and Sodja, 1980, Cell 19: 365-78. Fyrberg, Bond, Hershey, Mixter, and Davidson, 1981, Cell 24: 107-16. Sanchez, Tobin, Rdest, Zulauf, and McCarthy, 1983, J. Mol. Biol. 163: 533-51. phenotype: Structural gene encoding actin III; expressed only in the developing thorax, specifically in the indirect flight muscles (Fyrberg, Mahaffey, Bond, and Davidson, 1983, Cell 33: 115-23; Hiromi and Hotta, 1985, EMBO J. 4: 1681-87). The only actin expressed in indirect flight muscle (Fyrberg). Heterozygotes for null mutations or Act88F deficiencies are flightless; flightlessness is apparently caused by imbalance between myosin heavy chains and actin III; whereas hemizygos- ity for either Mhc or Act88F leads to complex myofibrillar defects and flightlessness, double hemizygotes have nearly normal fibrillar structure and are able to fly [Beall, Sepan- ski, and Fyrberg, 1989, Genes Dev. 3: 131-40 (fig.)]. Major peaks of transcription during pupal stage (Sanchez et al., 1983). Heterozygotes and to a greater degree, homozygotes and heteroallelic heterozygotes for antimorphic alleles Act88F4 and Act88F5 show constitutive synthesis of heat-shock pro- teins, with HSP26 and HSP27 less actively synthesized than HSP22, HSP70, and HSP84; response to heat shock normal (Hiromi and Hotta). alleles: allele origin synonym ref ( comments _______________________________________________________________________ Act88F1 EMS Ifm(3)1, Ifm(3)2 3, 4, 7 dominant antimorphic allele weak inducer of HSP arg 28 -> cys Act88F2 EMS Ifm(3)4 3, 4, 7 dominant antimorphic allele weak inducer of HSP ile 76 -> phe Act88F3 EMS Ifm(3)6 1, 7 Act88F4 EMS Ifm(3)7, Act88FKM75 3, 7, 8 dominant antimorphic allele strong inducer of HSP trp 356 -> opal Act88F5 Act88FHH5 2, 8 dominant antimorphic allele strong inducer of HSP gly 366 -> ser Act88F6 Act88FKM88 2, 8 dominant hypomorphic allele trp 75 -> ambera Act88F7 Act88FKM129 2, 8 Act88F8 spont Act88Frsd 5, 6 ( 1 = Ball, Karlik, Beall, Saville, Sparrow, Bullard, and Fyr- berg, 1987, Cell 51: 221-28; 2 = Hiromi and Hotta, 1985, EMBO J. 4: 1681-87; 3 = Karlik, Coutu, and Fyrberg, 1984, Cell 38: 711-19 (fig.); 4 = Karlik, Saville, and Fyrberg, 1987, Mol. Cell Biol. 7: 3084-91; 5 = Lang, Wyss, and Eppenberger, 1981, Nature 291: 506-08; 6 = Mahaffey, Coutu, Fyrberg, and Inwood, 1985, Cell 40: 101-10; 7 = Mogami and Hotta, 1981, Mol. Gen. Genet 183: 409-17; 8 = Okamoto, Hiromi, Ishikawa, Yamada, Isoda, Mackasa, and Hotta, 1986, EMBO J. 5: 589-96. cytology: Placed in 88F by in situ hybridization. molecular biology: Genomic clones isolated by Tobin et al. (1980) and by Fyrberg et al. (1981). Sequence analysis reveals a translated sequence accounting encoding a 374- amino-acid polypeptide of molecular weight 43 kd, which shows 95% homology with the Act79B gene product and 92% homology with rabbit actin. The genomic sequence shows an intron of 60 nucleotides within codon 307 (Sanchez et al., 1983). Deletion analysis of upstream cis-acting regulatory sequences carried out by Geyer and Fyrberg (1986, Mol. Cell Biol. 6: 3388-96). Arthrin, a 55-kd protein found in indirect flight muscle shown to be an uniquinated form of actin III (Ball, Karlik, Beall, Saville, Sparrow, Bullard, and Fyrberg, 1987, Cell 51: 221- 28). # Act88F4 phenotype: Dominant flightless allele; actin III replaced by a truncated polypeptide of 42 kd that is stable and capable of incorporation into myofibrils; actin II reduced in homozygotes (Hiromi and Hotta, 1985). Myofibrils in indirect flight mus- cles of homozygotes severely deranged; sarcomere structure obliterated; indirect-flight-muscle nuclei enlarged. Skeins of morphologically normal but highly disorgainzed thick fila- ments present, but Z discs absent. Thin filaments scarce. Electron dense material of unknown origin seen in sections. Wild-type flies transformed with cloned Act4 sequence produces both the 42-kd and the heat-shock proteins (Hiromi, Okamoto, Gehring, and Hotta, 1986, Cell 44: 293-301). # Act88F5 phenotype: Produces half normal amount of actin isoform III; shows increased synthesis of actin I, normally present in only trace amounts in indirect flight muscle. Indirect-flight- muscle nuclei enlarged and myofibrils disrupted. Heterozy- gotes flightless. # Act88F6 phenotype: Actin III entirely absent from indirect flight mus- cle in homozygotes; levels of actin II also reduced. # Act88F7 phenotype: Actin III replaced by a truncated polypeptide of 38 kd; its low concentrations on gels suggests high instability (Hiromi and Hotta, 1985). # Act88F8 phenotype: Studied only in combination with rsd at 95.4 on chromosome 3; not examined in rsd+ background. Wings of homozygotes held straight up, nearly meeting over thorax; heterozygotes have wings held normally, but are nearly flight- less. Electron microscropy of homozygotes reveals grossly abnormal indirect-flight-muscle structure; lack thin filaments and Z discs (Deak, Bellamy, Bienz, Dubuis, Fenner, Gollin, Rahmi, Ramp, Reinhardt, and Cotton, 1982, J. Embryol. Exp. Morphol. 69: 61-81). Abnormal protein accumulation observed in thoraces. Actin III and its ubiquinated derivative, arth- rin, absent in Act88F8 homozygotes (Lang et al.); six other polypeptides, including an indirect-flight-muscle tropomyosin isoform and two indirect-flight-muscle tropomyosin-related isoforms, markedly reduced. Homozygotes transformed with Act88F+ show restoration to approximately normal levels of the six reduced polypeptides. Accumulation of actin III and arth- rin still negative, however; the latter attributed to the failure of post-translational modification in the presence of homozygous rsd. Viability and fertility normal. molecular biology: a null mutant; Act88F mRNA reduced 10-15 fold; alteration of normal sequence apparently outside the coding region; mRNA level, and to some degree, the phenotype rescuable by germ-line transformation using Act88F normal genomic sequence. Sequence of coding region of DNA including 60-nucleotide intron reveals differences from that of Canton-S that account for five amino-acids substitution (Mahaffey et al.). other information: Conceivable that Act88F9 is a wild-type isoallele with normal phenotype in the absence of rsd. # actidione sensitive: see act # Actin: see Act # Actn: ( Actinin location: 1-1.0. synonym: l(1)2Cb phenotype: The structural gene for ( Actinin (Fyrberg). Both lethal and viable alleles recovered; allelism determined by Homyk and Emerson. Viable alleles unconditionally flightless; wing position normal, but unable to fly or beat wings; jump abnormally short distances. Gynandromorph studies of Actn1 indicate a bilateral pair of submissive foci located mid ven- trally close to the embryonic midline (Homyk and Emerson). ERG normal (Homyk and Pye, 1989, J. Neurogenet. 5: 37-48). Actn4 is a heat sensitive lethal, and when raised at low tem- perature, causes aberrant wing display of courting males; Actn1/Actn4 jumps and flies abnormally when raised at 22 but normally when raised at 29; temperature sensitive period for this effect in first half of pupal stage (Homyk et al.,1980). Trans heterozygotes (i.e., Actn3, Actn4, Actn8, and Actn14) with hdp-a2 also flightless. Lethal alleles die in late larval or early pupal stages; homozygous maternal germline clones produce normal ova. Polyphasic lethality of Actn8 attributed to position effect of the inversion on arm (Perrimon, Engstrom, and Mahowald, l985, Genetics 111: 23-41). alleles: allele origin discoverer synonym ref ( comments __________________________________________________________________________ Actn1 EMS Homyk fliA1 1, 2, 3 Actn2 EMS Homyk fliA2 1, 2, 3 Actn3 EMS Homyk fliA3 1, 2, 3 Actn4 EMS Homyk fliA4 1, 2, 4 heat-sensitive pupal lethal Actn5 X ray Lefevre l(1)A115 6, 8 larval lethal Actn6 X ray Lefevre l(1)C212 6 T(1;3)1A7;2C3;80 Actn7 X ray Lefevre l(1)GA17 6, 8 embryonic lethal (double mutant) Actn8 X ray Lefevre l(1)HC207 1, 6, 8 In(1)2C3;7B1; polyphasic lethal Actn9 X ray Lefevre l(1)HC288 6, 8 larval-pupal lethal Actn10 X ray Lefevre l(1)HF356 6 Actn11 X ray Lefevre l(1)JC111 6 In(1)2C3;9A2-3 Actn12 EMS Lefevre l(1)EA43 7, 8 larval lethal Actn13 EMS Lefevre l(1)EA45 7 Actn14 EMS Lefevre l(1)EA82 1, 7, 8 larval lethal Actn15 EMS Lefevre l(1)EA111 7 Actn16 EMS Lefevre l(1)VE692 7, 8 larval lethal Actn17 spont Schalet l(1)4-3 Actn18 spont Schalet l(1)17-44-1 Actn19 HMS l(1)HM29 5 ( 1 = Homyk and Emerson, 1988, Genetics 119: 105-21; 2 = Homyk and Grigliatti, 1983, Dev. Genet. 4: 77-97; 3 = Homyk and Sheppard, 1977, Genetics 87: 95-104; 4 = Homyk, Szidonya, and Suzuki, 1980, Mol. Gen. Genet. 177: 553-65; 5 = Kramers, Schalet, Paradi, and Huiser- Hoogteyling, 1983, Mutat. Res. 107: 187-201; 6 = Lefevre, 1981, Genetics 99: 461-80; 7 = Lefevre and Watkins, 1986, Genetics 113: 869-95; 8 = Perrimon, Engstrom, and Mahowald, l985, Genetics 111: 23-41. cytology: Placed in 2C3 based on breakpoint common to three rearrangement associated lethal alleles (Lefevre). Covered by Dp(1;3)wvco = Dp(1;3)2B17-C1;3C4-5;77D3-5;81 but not by Dp(1;Y)w+303 = Dp(1;Y)2D1-2;3D3-4 (Perrimon, et al.).