ARP3_DROME
ID ARP3_DROME Reviewed; 418 AA.
AC P32392; M9PEY5; Q9VSD5;
DT 01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
DT 09-MAY-2003, sequence version 3.
DT 03-AUG-2022, entry version 180.
DE RecName: Full=Actin-related protein 3;
DE AltName: Full=Actin-2;
DE AltName: Full=Actin-like protein 3;
DE AltName: Full=Actin-like protein 66B;
GN Name=Arp3 {ECO:0000312|FlyBase:FBgn0262716};
GN Synonyms=Actr66B, Arp66B {ECO:0000312|FlyBase:FBgn0262716};
GN ORFNames=CG7558 {ECO:0000312|FlyBase:FBgn0262716};
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 [GENOMIC DNA].
RX PubMed=8274139; DOI=10.1007/bf00553175;
RA Fyrberg C., Fyrberg E.A.;
RT "A Drosophila homologue of the Schizosaccharomyces pombe act2 gene.";
RL Biochem. Genet. 31:329-341(1993).
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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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 FUNCTION.
RX PubMed=25739458; DOI=10.1091/mbc.e14-08-1266;
RA Verboon J.M., Rahe T.K., Rodriguez-Mesa E., Parkhurst S.M.;
RT "Wash functions downstream of Rho1 GTPase in a subset of Drosophila immune
RT cell developmental migrations.";
RL Mol. Biol. Cell 26:1665-1674(2015).
CC -!- FUNCTION: Functions as ATP-binding component of the Arp2/3 complex
CC which is involved in regulation of actin polymerization and together
CC with an activating nucleation-promoting factor (NPF) mediates the
CC formation of branched actin networks (By similarity). Seems to contact
CC the pointed end of the daughter actin filament (By similarity).
CC Required during embryogenesis for the developmental migration of tail
CC hemocytes anteriorly, along the ventral midline (PubMed:25739458).
CC {ECO:0000250|UniProtKB:P61158, ECO:0000269|PubMed:25739458}.
CC -!- SUBUNIT: Component of the Arp2/3 complex.
CC {ECO:0000250|UniProtKB:P61158}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton
CC {ECO:0000250|UniProtKB:P61158}.
CC -!- SIMILARITY: Belongs to the actin family. ARP3 subfamily. {ECO:0000305}.
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DR EMBL; X71789; CAA50674.1; -; Genomic_DNA.
DR EMBL; AE014296; AAF50488.1; -; Genomic_DNA.
DR EMBL; AE014296; AGB94254.1; -; Genomic_DNA.
DR EMBL; AY051859; AAK93283.1; -; mRNA.
DR RefSeq; NP_001261559.1; NM_001274630.1.
DR RefSeq; NP_523968.1; NM_079244.3.
DR AlphaFoldDB; P32392; -.
DR SMR; P32392; -.
DR BioGRID; 64322; 25.
DR DIP; DIP-20563N; -.
DR IntAct; P32392; 3.
DR STRING; 7227.FBpp0076460; -.
DR PaxDb; P32392; -.
DR PRIDE; P32392; -.
DR DNASU; 38898; -.
DR EnsemblMetazoa; FBtr0076737; FBpp0076460; FBgn0262716.
DR EnsemblMetazoa; FBtr0334087; FBpp0306212; FBgn0262716.
DR GeneID; 38898; -.
DR KEGG; dme:Dmel_CG7558; -.
DR CTD; 38898; -.
DR FlyBase; FBgn0262716; Arp3.
DR VEuPathDB; VectorBase:FBgn0262716; -.
DR eggNOG; KOG0678; Eukaryota.
DR GeneTree; ENSGT00940000155065; -.
DR HOGENOM; CLU_027965_3_0_1; -.
DR InParanoid; P32392; -.
DR OMA; TAEFKSY; -.
DR OrthoDB; 649708at2759; -.
DR PhylomeDB; P32392; -.
DR Reactome; R-DME-2029482; Regulation of actin dynamics for phagocytic cup formation.
DR Reactome; R-DME-5663213; RHO GTPases Activate WASPs and WAVEs.
DR Reactome; R-DME-8856828; Clathrin-mediated endocytosis.
DR BioGRID-ORCS; 38898; 1 hit in 3 CRISPR screens.
DR GenomeRNAi; 38898; -.
DR PRO; PR:P32392; -.
DR Proteomes; UP000000803; Chromosome 3L.
DR Bgee; FBgn0262716; Expressed in embryonic/larval hemocyte (Drosophila) and 24 other tissues.
DR Genevisible; P32392; DM.
DR GO; GO:0005885; C:Arp2/3 protein complex; ISS:FlyBase.
DR GO; GO:0005829; C:cytosol; IDA:FlyBase.
DR GO; GO:0030027; C:lamellipodium; IDA:FlyBase.
DR GO; GO:0005652; C:nuclear lamina; IDA:FlyBase.
DR GO; GO:0003779; F:actin binding; IEA:UniProtKB-KW.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0005200; F:structural constituent of cytoskeleton; ISS:FlyBase.
DR GO; GO:0030036; P:actin cytoskeleton organization; IMP:FlyBase.
DR GO; GO:0030037; P:actin filament reorganization involved in cell cycle; IPI:FlyBase.
DR GO; GO:0034314; P:Arp2/3 complex-mediated actin nucleation; ISS:FlyBase.
DR GO; GO:0007413; P:axonal fasciculation; IMP:FlyBase.
DR GO; GO:0000902; P:cell morphogenesis; IMP:FlyBase.
DR GO; GO:0022416; P:chaeta development; IMP:FlyBase.
DR GO; GO:0006886; P:intracellular protein transport; IMP:FlyBase.
DR GO; GO:0007520; P:myoblast fusion; IMP:FlyBase.
DR GO; GO:0140591; P:nuclear envelope budding; IMP:FlyBase.
DR GO; GO:0097320; P:plasma membrane tubulation; IMP:FlyBase.
DR GO; GO:0051491; P:positive regulation of filopodium assembly; IMP:FlyBase.
DR GO; GO:0010592; P:positive regulation of lamellipodium assembly; IMP:FlyBase.
DR GO; GO:0045887; P:positive regulation of synaptic assembly at neuromuscular junction; IMP:FlyBase.
DR GO; GO:0030589; P:pseudocleavage involved in syncytial blastoderm formation; IPI:FlyBase.
DR GO; GO:0072553; P:terminal button organization; IMP:FlyBase.
DR InterPro; IPR004000; Actin.
DR InterPro; IPR020902; Actin/actin-like_CS.
DR InterPro; IPR015623; Arp3.
DR InterPro; IPR043129; ATPase_NBD.
DR PANTHER; PTHR11937; PTHR11937; 1.
DR PANTHER; PTHR11937:SF175; PTHR11937:SF175; 1.
DR Pfam; PF00022; Actin; 1.
DR SMART; SM00268; ACTIN; 1.
DR SUPFAM; SSF53067; SSF53067; 2.
DR PROSITE; PS01132; ACTINS_ACT_LIKE; 1.
PE 2: Evidence at transcript level;
KW Actin-binding; ATP-binding; Cytoplasm; Cytoskeleton; Nucleotide-binding;
KW Reference proteome.
FT CHAIN 1..418
FT /note="Actin-related protein 3"
FT /id="PRO_0000089087"
FT CONFLICT 69
FT /note="A -> R (in Ref. 1; CAA50674)"
FT /evidence="ECO:0000305"
FT CONFLICT 176
FT /note="H -> D (in Ref. 1; CAA50674)"
FT /evidence="ECO:0000305"
FT CONFLICT 203
FT /note="F -> L (in Ref. 1; CAA50674)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 418 AA; 47033 MW; D8EAA080ED81513A CRC64;
MAGRLPACVI DVGTGYSKLG FAGNKEPQFI IPSAIAIKES ARVGDTNTRR ITKGIEDLDF
FIGDEAFDAT GYSIKYPVRH GLVEDWDLME RFLEQCVFKY LRAEPEDHYF LLTEPPLNTP
ENREYTAEIM FETFNVPGLY IAVQAVLALA ASWASRSAEE RTLTGIVVDS GDGVTHVIPV
AEGYVIGSCI KHIPIAGRNI TSFIQSLLRE REVGIPPEQS LETAKAIKEK HCYICPDIAK
EFAKYDTEPG KWIRNFSGVN TVTKAPFNVD VGYERFLGPE IFFHPEFSNP DFTIPLSEIV
DNVIQNCPID VRRPLYNNIV LSGGSTMFKD FGRRLQRDIK RSVDTRLRIS ENLSEGRIKP
KPIDVQVITH HMQRYAVWFG GSMLASTPEF YQVCHTKAAY EEYGPSICRH NPVFGTMT
