ANLN_DROME
ID ANLN_DROME Reviewed; 1239 AA.
AC Q9V4P1; Q24240; Q8MKN2; Q8T067;
DT 21-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 3.
DT 03-AUG-2022, entry version 155.
DE RecName: Full=Anillin;
DE AltName: Full=Actin-binding protein 8;
DE Short=ABP8;
DE AltName: Full=Protein scraps;
GN Name=scra; Synonyms=ani; ORFNames=CG2092;
OS Drosophila melanogaster (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7227;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM A), INTERACTION WITH ACTIN, SUBCELLULAR
RP LOCATION, AND DEVELOPMENTAL STAGE.
RC TISSUE=Embryo;
RX PubMed=7559773; DOI=10.1083/jcb.131.1.165;
RA Field C.M., Alberts B.M.;
RT "Anillin, a contractile ring protein that cycles from the nucleus to the
RT cell cortex.";
RL J. Cell Biol. 131:165-178(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley;
RX PubMed=10731132; DOI=10.1126/science.287.5461.2185;
RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., Brandon R.C.,
RA Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C.,
RA Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A.,
RA An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A.,
RA Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V.,
RA Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J.,
RA Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E.,
RA Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B.,
RA Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I.,
RA Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C.,
RA Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S.,
RA Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M.,
RA Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D.,
RA Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F.,
RA Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D.,
RA Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A.,
RA Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C.,
RA McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C.,
RA Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L.,
RA Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R.,
RA Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V.,
RA Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F.,
RA Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R.,
RA Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y.,
RA Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T.,
RA Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S.,
RA Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W.,
RA Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M.,
RA Venter J.C.;
RT "The genome sequence of Drosophila melanogaster.";
RL Science 287:2185-2195(2000).
RN [3]
RP GENOME REANNOTATION, AND ALTERNATIVE SPLICING.
RC STRAIN=Berkeley;
RX PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M.,
RA Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.;
RT "Annotation of the Drosophila melanogaster euchromatic genome: a systematic
RT review.";
RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM B).
RC STRAIN=Berkeley; TISSUE=Embryo;
RX PubMed=12537569; DOI=10.1186/gb-2002-3-12-research0080;
RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A.,
RA Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M.,
RA Celniker S.E.;
RT "A Drosophila full-length cDNA resource.";
RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002).
RN [5]
RP SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=9013326; DOI=10.1242/jcs.109.12.2779;
RA Hime G.R., Brill J.A., Fuller M.T.;
RT "Assembly of ring canals in the male germ line from structural components
RT of the contractile ring.";
RL J. Cell Sci. 109:2779-2788(1996).
RN [6]
RP SUBCELLULAR LOCATION.
RX PubMed=9477328; DOI=10.1242/dev.125.7.1295;
RA Rothwell W.F., Fogarty P., Field C.M., Sullivan W.;
RT "Nuclear-fallout, a Drosophila protein that cycles from the cytoplasm to
RT the centrosomes, regulates cortical microfilament organization.";
RL Development 125:1295-1303(1998).
RN [7]
RP SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=9655801; DOI=10.1242/dev.125.15.2781;
RA de Cuevas M., Spradling A.C.;
RT "Morphogenesis of the Drosophila fusome and its implications for oocyte
RT specification.";
RL Development 125:2781-2789(1998).
RN [8]
RP SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=10381388; DOI=10.1242/jcs.112.14.2323;
RA Giansanti M.G., Bonaccorsi S., Gatti M.;
RT "The role of anillin in meiotic cytokinesis of Drosophila males.";
RL J. Cell Sci. 112:2323-2334(1999).
RN [9]
RP SUBCELLULAR LOCATION.
RX PubMed=10444383; DOI=10.1242/jcs.112.17.2885;
RA Rothwell W.F., Zhang C.X., Zelano C., Hsieh T.-S., Sullivan W.;
RT "The Drosophila centrosomal protein Nuf is required for recruiting Dah, a
RT membrane associated protein, to furrows in the early embryo.";
RL J. Cell Sci. 112:2885-2893(1999).
RN [10]
RP DEVELOPMENTAL STAGE.
RX PubMed=10751177; DOI=10.1242/dev.127.9.1887;
RA Afshar K., Stuart B., Wasserman S.A.;
RT "Functional analysis of the Drosophila diaphanous FH protein in early
RT embryonic development.";
RL Development 127:1887-1897(2000).
RN [11]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=12134082; DOI=10.1091/mbc.01-12-0589;
RA Somma M.P., Fasulo B., Cenci G., Cundari E., Gatti M.;
RT "Molecular dissection of cytokinesis by RNA interference in Drosophila
RT cultured cells.";
RL Mol. Biol. Cell 13:2448-2460(2002).
RN [12]
RP SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=12538517; DOI=10.1242/dev.00315;
RA Mathe E., Inoue Y.H., Palframan W., Brown G., Glover D.M.;
RT "Orbit/Mast, the CLASP orthologue of Drosophila, is required for asymmetric
RT stem cell and cystocyte divisions and development of the polarised
RT microtubule network that interconnects oocyte and nurse cells during
RT oogenesis.";
RL Development 130:901-915(2003).
RN [13]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=15380073; DOI=10.1016/j.cub.2004.08.063;
RA Echard A., Hickson G.R.X., Foley E., O'Farrell P.H.;
RT "Terminal cytokinesis events uncovered after an RNAi screen.";
RL Curr. Biol. 14:1685-1693(2004).
RN [14]
RP FUNCTION, SUBCELLULAR LOCATION, AND DEVELOPMENTAL STAGE.
RX PubMed=14736750; DOI=10.1242/dev.00989;
RA Thomas J.H., Wieschaus E.;
RT "src64 and tec29 are required for microfilament contraction during
RT Drosophila cellularization.";
RL Development 131:863-871(2004).
RN [15]
RP SUBCELLULAR LOCATION.
RX PubMed=15240570; DOI=10.1083/jcb.200402157;
RA D'Avino P.P., Savoian M.S., Glover D.M.;
RT "Mutations in sticky lead to defective organization of the contractile ring
RT during cytokinesis and are enhanced by Rho and suppressed by Rac.";
RL J. Cell Biol. 166:61-71(2004).
RN [16]
RP SUBCELLULAR LOCATION.
RX PubMed=15004238; DOI=10.1091/mbc.e03-08-0603;
RA Giansanti M.G., Farkas R.M., Bonaccorsi S., Lindsley D.L., Wakimoto B.T.,
RA Fuller M.T., Gatti M.;
RT "Genetic dissection of meiotic cytokinesis in Drosophila males.";
RL Mol. Biol. Cell 15:2509-2522(2004).
RN [17]
RP SUBCELLULAR LOCATION.
RX PubMed=15371536; DOI=10.1091/mbc.e04-06-0536;
RA Naim V., Imarisio S., Di Cunto F., Gatti M., Bonaccorsi S.;
RT "Drosophila citron kinase is required for the final steps of cytokinesis.";
RL Mol. Biol. Cell 15:5053-5063(2004).
RN [18]
RP FUNCTION, SUBCELLULAR LOCATION, AND CHARACTERIZATION OF MUTANTS ILE-549;
RP SER-1107; ILE-1114; GLU-1121 AND SER-1143.
RX PubMed=15930114; DOI=10.1242/dev.01843;
RA Field C.M., Coughlin M., Doberstein S., Marty T., Sullivan W.;
RT "Characterization of anillin mutants reveals essential roles in septin
RT localization and plasma membrane integrity.";
RL Development 132:2849-2860(2005).
RN [19]
RP SUBCELLULAR LOCATION.
RX PubMed=16280552; DOI=10.1242/jcs.02652;
RA Zavortink M., Contreras N., Addy T., Bejsovec A., Saint R.;
RT "Tum/RacGAP50C provides a critical link between anaphase microtubules and
RT the assembly of the contractile ring in Drosophila melanogaster.";
RL J. Cell Sci. 118:5381-5392(2005).
RN [20]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=15496454; DOI=10.1091/mbc.e04-08-0758;
RA Straight A.F., Field C.M., Mitchison T.J.;
RT "Anillin binds nonmuscle myosin II and regulates the contractile ring.";
RL Mol. Biol. Cell 16:193-201(2005).
RN [21]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-712; THR-740; SER-744;
RP SER-754 AND THR-831, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC TISSUE=Embryo;
RX PubMed=18327897; DOI=10.1021/pr700696a;
RA Zhai B., Villen J., Beausoleil S.A., Mintseris J., Gygi S.P.;
RT "Phosphoproteome analysis of Drosophila melanogaster embryos.";
RL J. Proteome Res. 7:1675-1682(2008).
CC -!- FUNCTION: Required for cytokinesis. Essential for the structural
CC integrity of the cleavage furrow and for completion of cleavage furrow
CC ingression and proper formation of the midbody. Required during
CC cellularization of syncytial embryos for the proper formation and
CC function of the furrow canals, the stable inward folds of the plasma
CC membrane which separate the peripheral nuclei. Also required for the
CC formation of the pole cells, the progenitors of the adult germline
CC which are formed by cytokinesis of the cytoplasmic buds at the
CC posterior pole of the syncytial embryo. Essential for embryonic
CC viability. {ECO:0000269|PubMed:12134082, ECO:0000269|PubMed:14736750,
CC ECO:0000269|PubMed:15380073, ECO:0000269|PubMed:15496454,
CC ECO:0000269|PubMed:15930114}.
CC -!- SUBUNIT: Interacts with and bundles F-actin.
CC {ECO:0000269|PubMed:7559773}.
CC -!- SUBCELLULAR LOCATION: Nucleus. Cytoplasm, cytoskeleton. Cytoplasm, cell
CC cortex. Note=Mainly found in the nucleus during interphase. Colocalizes
CC with cortical F-actin upon nuclear envelope breakdown in mitosis and
CC subsequently concentrates in the area of the prospective contractile
CC ring in anaphase. This pattern persists until telophase, when the
CC protein becomes concentrated in the midbody. Accumulates in the nucleus
CC of newly divided cells in a diffuse staining pattern, thereby
CC restarting the cycle.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=B;
CC IsoId=Q9V4P1-1; Sequence=Displayed;
CC Name=A;
CC IsoId=Q9V4P1-2; Sequence=VSP_017618;
CC -!- TISSUE SPECIFICITY: Accumulates in the ring canals that interconnect
CC cells of the germline cysts in males and the ovarian follicles in
CC females. These structures develop from arrested contractile rings after
CC a specialized cytokinesis in which the closing of the invaginating
CC plasma membrane is incomplete. Also concentrates in the arrested
CC cleavage furrows that initially link the oocyte to its 15 nurse cells
CC in the early egg chamber and is subsequently lost from these furrows as
CC germline cell division is completed. {ECO:0000269|PubMed:10381388,
CC ECO:0000269|PubMed:12538517, ECO:0000269|PubMed:9013326,
CC ECO:0000269|PubMed:9655801}.
CC -!- DEVELOPMENTAL STAGE: Expressed throughout development and at reduced
CC levels late in embryogenesis. Localizes to the embryonic cortex and to
CC the metaphase furrows which separate mitotic nuclei in the syncytial
CC embryo prior to cellularization. Concentrates in the leading edges of
CC the furrow canals at the onset of cellularization.
CC {ECO:0000269|PubMed:10751177, ECO:0000269|PubMed:14736750,
CC ECO:0000269|PubMed:7559773}.
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DR EMBL; X89858; CAA61954.1; -; mRNA.
DR EMBL; AE013599; AAF59225.3; -; Genomic_DNA.
DR EMBL; AE013599; AAM71099.1; -; Genomic_DNA.
DR EMBL; AY069520; AAL39665.1; -; mRNA.
DR PIR; A57369; A57369.
DR RefSeq; NP_724582.1; NM_165543.2. [Q9V4P1-1]
DR RefSeq; NP_724583.1; NM_165544.2. [Q9V4P1-2]
DR AlphaFoldDB; Q9V4P1; -.
DR SMR; Q9V4P1; -.
DR BioGRID; 61572; 50.
DR IntAct; Q9V4P1; 6.
DR STRING; 7227.FBpp0087986; -.
DR iPTMnet; Q9V4P1; -.
DR PaxDb; Q9V4P1; -.
DR PRIDE; Q9V4P1; -.
DR DNASU; 35696; -.
DR EnsemblMetazoa; FBtr0088911; FBpp0087985; FBgn0261385. [Q9V4P1-2]
DR EnsemblMetazoa; FBtr0088912; FBpp0087986; FBgn0261385. [Q9V4P1-1]
DR GeneID; 35696; -.
DR KEGG; dme:Dmel_CG2092; -.
DR CTD; 35696; -.
DR FlyBase; FBgn0261385; scra.
DR VEuPathDB; VectorBase:FBgn0261385; -.
DR eggNOG; KOG3640; Eukaryota.
DR GeneTree; ENSGT00390000008749; -.
DR HOGENOM; CLU_008475_0_0_1; -.
DR InParanoid; Q9V4P1; -.
DR OMA; PHEIKYH; -.
DR PhylomeDB; Q9V4P1; -.
DR Reactome; R-DME-8980692; RHOA GTPase cycle.
DR Reactome; R-DME-9013026; RHOB GTPase cycle.
DR Reactome; R-DME-9013106; RHOC GTPase cycle.
DR SignaLink; Q9V4P1; -.
DR BioGRID-ORCS; 35696; 0 hits in 1 CRISPR screen.
DR GenomeRNAi; 35696; -.
DR PRO; PR:Q9V4P1; -.
DR Proteomes; UP000000803; Chromosome 2R.
DR Bgee; FBgn0261385; Expressed in egg cell and 39 other tissues.
DR ExpressionAtlas; Q9V4P1; baseline and differential.
DR Genevisible; Q9V4P1; DM.
DR GO; GO:0005826; C:actomyosin contractile ring; IDA:UniProtKB.
DR GO; GO:0032154; C:cleavage furrow; IDA:FlyBase.
DR GO; GO:0070938; C:contractile ring; IDA:FlyBase.
DR GO; GO:0005737; C:cytoplasm; IDA:FlyBase.
DR GO; GO:0045172; C:germline ring canal; IDA:UniProtKB.
DR GO; GO:0035323; C:male germline ring canal; IDA:FlyBase.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0003779; F:actin binding; IDA:FlyBase.
DR GO; GO:0051015; F:actin filament binding; IDA:WormBase.
DR GO; GO:0008017; F:microtubule binding; IDA:FlyBase.
DR GO; GO:0017022; F:myosin binding; IDA:UniProtKB.
DR GO; GO:0000915; P:actomyosin contractile ring assembly; IMP:UniProtKB.
DR GO; GO:0008356; P:asymmetric cell division; IMP:FlyBase.
DR GO; GO:0007349; P:cellularization; IMP:FlyBase.
DR GO; GO:0032188; P:establishment of actomyosin contractile ring localization; IMP:FlyBase.
DR GO; GO:0043063; P:intercellular bridge organization; IMP:FlyBase.
DR GO; GO:0030726; P:male germline ring canal formation; IMP:UniProtKB.
DR GO; GO:0007112; P:male meiosis cytokinesis; IMP:FlyBase.
DR GO; GO:0000281; P:mitotic cytokinesis; IMP:UniProtKB.
DR GO; GO:0048477; P:oogenesis; IEA:UniProtKB-KW.
DR GO; GO:0007009; P:plasma membrane organization; IMP:UniProtKB.
DR GO; GO:0007279; P:pole cell formation; IMP:UniProtKB.
DR GO; GO:0008104; P:protein localization; IMP:UniProtKB.
DR GO; GO:0032465; P:regulation of cytokinesis; IMP:FlyBase.
DR GO; GO:0007423; P:sensory organ development; IMP:FlyBase.
DR GO; GO:0045035; P:sensory organ precursor cell division; IMP:FlyBase.
DR GO; GO:0031106; P:septin ring organization; IMP:FlyBase.
DR CDD; cd01263; PH_anillin; 1.
DR Gene3D; 2.30.29.30; -; 1.
DR InterPro; IPR012966; AHD.
DR InterPro; IPR031970; Anillin_N.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR037840; PH_Anillin.
DR InterPro; IPR001849; PH_domain.
DR Pfam; PF08174; Anillin; 1.
DR Pfam; PF16018; Anillin_N; 1.
DR Pfam; PF00169; PH; 1.
DR SMART; SM00233; PH; 1.
DR PROSITE; PS50003; PH_DOMAIN; 1.
PE 1: Evidence at protein level;
KW Actin-binding; Alternative splicing; Cell cycle; Cell division;
KW Coiled coil; Cytoplasm; Cytoskeleton; Developmental protein;
KW Differentiation; Meiosis; Mitosis; Nucleus; Oogenesis; Phosphoprotein;
KW Reference proteome; Spermatogenesis.
FT CHAIN 1..1239
FT /note="Anillin"
FT /id="PRO_0000227968"
FT DOMAIN 1106..1230
FT /note="PH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00145"
FT REGION 32..67
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 126..371
FT /note="Interaction with and bundling of F-actin"
FT REGION 230..265
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 493..621
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 684..716
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 834..861
FT /evidence="ECO:0000255"
FT COMPBIAS 512..531
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 544..565
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 592..610
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 712
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 740
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 744
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 754
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 831
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT VAR_SEQ 272..298
FT /note="Missing (in isoform A)"
FT /evidence="ECO:0000303|PubMed:7559773"
FT /id="VSP_017618"
FT MUTAGEN 549
FT /note="T->I: In allele scra3. Weak maternal effect allele;
FT abrogates separation of pole cells."
FT MUTAGEN 1107
FT /note="V->S: In alleles scra1; scra3; scra4; and scra5."
FT MUTAGEN 1114
FT /note="T->I: In allele scra5. Strong maternal effect
FT allele; abrogates cellularization of syncytial embryos."
FT MUTAGEN 1121
FT /note="G->E: In allele scra1. Strong maternal effect
FT allele; abrogates cellularization of syncytial embryos."
FT MUTAGEN 1143
FT /note="P->S: In allele scra4. Strong maternal effect
FT allele; abrogates cellularization of syncytial embryos."
FT CONFLICT 38..40
FT /note="Missing (in Ref. 1; CAA61954)"
FT /evidence="ECO:0000305"
FT CONFLICT 50..60
FT /note="LAPRSRSPGGQ -> PAP (in Ref. 1; CAA61954)"
FT /evidence="ECO:0000305"
FT CONFLICT 228
FT /note="L -> P (in Ref. 1; CAA61954)"
FT /evidence="ECO:0000305"
FT CONFLICT 394
FT /note="G -> A (in Ref. 1; CAA61954)"
FT /evidence="ECO:0000305"
FT CONFLICT 426
FT /note="M -> V (in Ref. 1; CAA61954)"
FT /evidence="ECO:0000305"
FT CONFLICT 689
FT /note="D -> E (in Ref. 1; CAA61954)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1239 AA; 136033 MW; EAA58335AE139A24 CRC64;
MDPFTQHMLE KAEQRSRALG ISNASKFPLV ECSVPSSSAT SASGGDAGVL APRSRSPGGQ
SAASGGGKVV TLGKATLEAS PAKPLRHYTA VNKENLDMGI EINITTDKPI GVQVEIQEQE
VTDDEEQAEG GALNPLLEAE PVNQPLARLR DTSRSRLQRM GALYSNTDDL SSPIHRTEGQ
FHVTTGEEED CGNRSSRQPK QRLGKLAALA DTINQWEDDT SHHEVHRLLE APPPKPHLSS
RRAEKGPAPL PPKKDEVDEA SRTKQLKWDP KVLSSLEAQG FQRRESSTIK HTYDYAKQEE
AAPASKVEDA VLTAKPPVPQ KSTTVSQVAK NFASSAPAPK PAPAPAVSVK SGLVSGRAAL
FENKGTGGQS QGLRNQKDPC ELSLKERMKL FETGNNKAML PMAPIGSAPS ITQIRAEEVK
QHLAAMHPVT AAAATTVVAA TKPKQENKLR DKVAALVANA QSSAETRIKD IDRQRQEDMQ
IISNRFNKQK ELFDNQPSDS SVAAQARPPA PAPSRVVRPM PPPPPPPIAA LSPGLASSKR
RSPGDAPTTD EDSKRARKSH SDRLYPALSD LDSSGDNCCA AETASATDDS HQQDEEETES
CMDESDDQSQ TEDSSAGMCN GSLGREIMSA VQRNEVEMQQ QQTGKKTVRY ADQDMYYDDS
SLNSSQVSAG IDDYLDEALV EDYGSTQDDQ SDSGDEQNAS RLSLGSKGTT ASNSFSFRKN
PASICTPIEE HHEMEMDLQT PLLSGAQPVK SELSVNQDND NLVTLVHTVS FYRRQQSANS
SNSTPVRKIC REQQVMRSAL AGDCHAKHRL EYDSPQQSDY VAAATDIADQ TDEDDEEMQN
AREVNDASQA QDKIKKLLSE VCKQQQVIGQ ASQALNLCAA TVEFSGSTES VEGERYLLLA
THRRQACLDE VQRLRVENSI RPVGAPKEKG LLTVKDITIP LRQEYVRKMA SNNINGHHLV
CLLKYNEHVL ATKTVPTMPG LLSVKFPDVL QLNNVYADFR ITLEIYGMLA QRDQLPHELK
YHINLNKKGG IKTPKKKGGE NRLVMPPVQS PAGPHVVRTP QLVQYGFAIF SLREIQRTTW
TLTQVLGVSP LEGVVHMKVN CELSVSVEYK GFLTMFEDIS GFGAWHRRWC YLNGSVINYW
KYPDDEKRKT PMGSIDLNSC TSQKVTTAPR DICARLNTML LECERPALET DQESLIIVPN
GRTTTVRHLL SADTKEEREE WCAYLNKALT LLRAWGTTH
