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ACTY_DROME
ID   ACTY_DROME              Reviewed;         376 AA.
AC   P45891; Q9V7T9;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   09-MAY-2003, sequence version 2.
DT   03-AUG-2022, entry version 126.
DE   RecName: Full=Actin-like protein 53D {ECO:0000303|PubMed:8064864};
GN   Name=Arp53D {ECO:0000303|PubMed:8064864, ECO:0000312|FlyBase:FBgn0011743};
GN   Synonyms=Actr53D {ECO:0000312|FlyBase:FBgn0011743};
GN   ORFNames=CG5409 {ECO:0000312|FlyBase:FBgn0011743};
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].
RC   STRAIN=Oregon-R;
RX   PubMed=8064864; DOI=10.1006/jmbi.1994.1526;
RA   Fyrberg C., Ryan L., Kenton M., Fyrberg E.A.;
RT   "Genes encoding actin-related proteins of Drosophila melanogaster.";
RL   J. Mol. Biol. 241:498-503(1994).
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.
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   FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, DISRUPTION PHENOTYPE,
RP   AND MUTAGENESIS OF 1-MET--ILE-40.
RX   PubMed=34282725; DOI=10.7554/elife.71279;
RA   Schroeder C.M., Tomlin S.A., Mejia Natividad I., Valenzuela J.R.,
RA   Young J.M., Malik H.S.;
RT   "An actin-related protein that is most highly expressed in Drosophila
RT   testes is critical for embryonic development.";
RL   Elife 10:0-0(2021).
CC   -!- FUNCTION: Required for optimal embryo development, particularly under
CC       heat stress conditions (PubMed:34282725). Also appears to have a role
CC       in negatively regulating spermatocyte cyst development
CC       (PubMed:34282725). Under heat stress conditions, required for the
CC       correct organization and migration of nuclei during early
CC       embryogenesis, and therefore possibly functions by regulating embryonic
CC       actin networks during the heat stress response (PubMed:34282725).
CC       {ECO:0000269|PubMed:34282725}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton
CC       {ECO:0000269|PubMed:34282725}. Note=In spermatocyte cysts, detected
CC       only during and after meiosis (PubMed:34282725). Localizes to two
CC       germline-specific actin structures: the fusome and actin cones
CC       (PubMed:34282725). First localizes to the fusome during meiosis
CC       (PubMed:34282725). Then once spermatid elongation is complete,
CC       localizes to the leading edge of the forming actin cones where it
CC       remains until the actin cones are destroyed following the completion of
CC       sperm individualization (PubMed:34282725).
CC       {ECO:0000269|PubMed:34282725}.
CC   -!- TISSUE SPECIFICITY: High expression in males whereas expression in
CC       females is very low (PubMed:34282725). In adult males, highest levels
CC       of expression are in the testis (PubMed:34282725). In adult females,
CC       expressed only in the ovaries at very low levels (PubMed:34282725). In
CC       larvae, highly expressed in the imaginal disk whereas in prepupae and
CC       pupae modest levels of expression occur in the fat body
CC       (PubMed:34282725). {ECO:0000269|PubMed:34282725}.
CC   -!- DISRUPTION PHENOTYPE: Increases male fertility but overall population
CC       fitness is decreased (PubMed:34282725). Males develop significantly
CC       more spermatocyte cysts with actin cones per testis, suggesting that
CC       sperm production is accelerated (PubMed:34282725). No effect on female
CC       fertility at 25 degrees Celsius (PubMed:34282725). However at 29
CC       degrees Celsius (heat stress conditions), embryos lacking either
CC       maternal and/or zygotic Arp53D activity display gross nuclear
CC       abnormalities and nuclei appear disorganized and uncompacted
CC       (PubMed:34282725). As a result females produce fewer progeny that reach
CC       the adult stage (PubMed:34282725). No effect on number of eggs laid or
CC       the percent of fertilized eggs (PubMed:34282725).
CC       {ECO:0000269|PubMed:34282725}.
CC   -!- SIMILARITY: Belongs to the actin family. ARP1 subfamily. {ECO:0000305}.
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DR   EMBL; X78487; CAA55239.1; -; mRNA.
DR   EMBL; AE013599; AAF57954.1; -; Genomic_DNA.
DR   PIR; S47986; S47986.
DR   RefSeq; NP_477037.2; NM_057689.4.
DR   AlphaFoldDB; P45891; -.
DR   SMR; P45891; -.
DR   IntAct; P45891; 1.
DR   STRING; 7227.FBpp0086174; -.
DR   PaxDb; P45891; -.
DR   PRIDE; P45891; -.
DR   DNASU; 36879; -.
DR   EnsemblMetazoa; FBtr0340069; FBpp0309075; FBgn0011743.
DR   GeneID; 36879; -.
DR   KEGG; dme:Dmel_CG5409; -.
DR   CTD; 36879; -.
DR   FlyBase; FBgn0011743; Arp53D.
DR   VEuPathDB; VectorBase:FBgn0011743; -.
DR   eggNOG; KOG0676; Eukaryota.
DR   GeneTree; ENSGT00950000182960; -.
DR   HOGENOM; CLU_027965_0_2_1; -.
DR   InParanoid; P45891; -.
DR   OrthoDB; 649708at2759; -.
DR   PhylomeDB; P45891; -.
DR   SignaLink; P45891; -.
DR   BioGRID-ORCS; 36879; 0 hits in 1 CRISPR screen.
DR   GenomeRNAi; 36879; -.
DR   PRO; PR:P45891; -.
DR   Proteomes; UP000000803; Chromosome 2R.
DR   Bgee; FBgn0011743; Expressed in testis and 9 other tissues.
DR   ExpressionAtlas; P45891; baseline and differential.
DR   Genevisible; P45891; DM.
DR   GO; GO:0015629; C:actin cytoskeleton; IDA:UniProtKB.
DR   GO; GO:0045169; C:fusome; IDA:UniProtKB.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0000281; P:mitotic cytokinesis; IBA:GO_Central.
DR   GO; GO:0040019; P:positive regulation of embryonic development; IMP:UniProtKB.
DR   GO; GO:0007286; P:spermatid development; IMP:UniProtKB.
DR   InterPro; IPR004000; Actin.
DR   InterPro; IPR020902; Actin/actin-like_CS.
DR   InterPro; IPR043129; ATPase_NBD.
DR   PANTHER; PTHR11937; PTHR11937; 1.
DR   Pfam; PF00022; Actin; 1.
DR   PRINTS; PR00190; ACTIN.
DR   SMART; SM00268; ACTIN; 1.
DR   SUPFAM; SSF53067; SSF53067; 2.
DR   PROSITE; PS01132; ACTINS_ACT_LIKE; 1.
PE   1: Evidence at protein level;
KW   ATP-binding; Cytoplasm; Cytoskeleton; Nucleotide-binding;
KW   Reference proteome.
FT   CHAIN           1..376
FT                   /note="Actin-like protein 53D"
FT                   /id="PRO_0000089062"
FT   REGION          1..40
FT                   /note="Necessary and sufficient for recruitment to the
FT                   fusome and actin cones of spermatocyte cysts"
FT                   /evidence="ECO:0000269|PubMed:34282725"
FT   MUTAGEN         1..40
FT                   /note="Missing: Detected in spermatocyte cysts during
FT                   meiosis but expression is diffuse. No localization to the
FT                   fusome or actin cones."
FT                   /evidence="ECO:0000269|PubMed:34282725"
FT   CONFLICT        63..66
FT                   /note="AAAR -> RQPE (in Ref. 1; CAA55239)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        148..149
FT                   /note="YA -> CT (in Ref. 1; CAA55239)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   376 AA;  42030 MW;  BD4860016F4E2259 CRC64;
     MSSEVDSNSH HAAVVIDNGS GVCKAGFSPE DTPRAVFPSI VGRPRHLNVL LDSVIGDSVI
     GEAAARKRGI LTLKYPIEHG MVKNWDEMEM VWQHTYELLR ADPMDLPALL TEAPLNPKKN
     REKMTEIMFE HFQVPAFYVA VQAVLSLYAT GRTVGIVVDS GDGVTHTVPI YEGFALPHAC
     VRVDLAGRDL TDYLCKLLLE RGVTMGTSAE REIVREIKEK LCYVSMNYAK EMDLHGKVET
     YELPDGQKIV LGCERFRCPE ALFQPSLLGQ EVMGIHEATH HSITNCDMDL RKDMYANIVL
     SGGTTMFRNI EHRFLQDLTE MAPPSIRIKV NASPDRRFSV WTGGSVLASL TSFQNMWIDS
     LEYEEVGSAI VHRKCF
 
 
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