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