ID   ARP3_CAEBR              Reviewed;         426 AA.
AC   Q61WW9; A8WWG4;
DT   26-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT   23-NOV-2004, sequence version 1.
DT   03-AUG-2022, entry version 95.
DE   RecName: Full=Actin-related protein 3;
DE   AltName: Full=Actin-like protein 3;
GN   Name=arx-1; ORFNames=CBG04224;
OS   Caenorhabditis briggsae.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC   Caenorhabditis.
OX   NCBI_TaxID=6238;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AF16;
RX   PubMed=14624247; DOI=10.1371/journal.pbio.0000045;
RA   Stein L.D., Bao Z., Blasiar D., Blumenthal T., Brent M.R., Chen N.,
RA   Chinwalla A., Clarke L., Clee C., Coghlan A., Coulson A., D'Eustachio P.,
RA   Fitch D.H.A., Fulton L.A., Fulton R.E., Griffiths-Jones S., Harris T.W.,
RA   Hillier L.W., Kamath R., Kuwabara P.E., Mardis E.R., Marra M.A.,
RA   Miner T.L., Minx P., Mullikin J.C., Plumb R.W., Rogers J., Schein J.E.,
RA   Sohrmann M., Spieth J., Stajich J.E., Wei C., Willey D., Wilson R.K.,
RA   Durbin R.M., Waterston R.H.;
RT   "The genome sequence of Caenorhabditis briggsae: a platform for comparative
RT   genomics.";
RL   PLoS Biol. 1:166-192(2003).
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. Seems to contact the pointed end
CC       of the daughter actin filament (By similarity). {ECO:0000250}.
CC   -!- SUBUNIT: Component of the Arp2/3 complex. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the actin family. ARP3 subfamily. {ECO:0000305}.
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DR   EMBL; HE600926; CAP24973.1; -; Genomic_DNA.
DR   RefSeq; XP_002639586.1; XM_002639540.1.
DR   AlphaFoldDB; Q61WW9; -.
DR   SMR; Q61WW9; -.
DR   STRING; 6238.CBG04224; -.
DR   EnsemblMetazoa; CBG04224.1; CBG04224.1; WBGene00026942.
DR   GeneID; 8581579; -.
DR   KEGG; cbr:CBG_04224; -.
DR   CTD; 8581579; -.
DR   WormBase; CBG04224; CBP00997; WBGene00026942; Cbr-arx-1.
DR   eggNOG; KOG0678; Eukaryota.
DR   HOGENOM; CLU_027965_3_0_1; -.
DR   InParanoid; Q61WW9; -.
DR   OMA; TAEFKSY; -.
DR   OrthoDB; 649708at2759; -.
DR   Proteomes; UP000008549; Chromosome I.
DR   GO; GO:0005885; C:Arp2/3 protein complex; IBA:GO_Central.
DR   GO; GO:0031252; C:cell leading edge; IEA:EnsemblMetazoa.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR   GO; GO:0003779; F:actin binding; IEA:UniProtKB-KW.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0034314; P:Arp2/3 complex-mediated actin nucleation; IBA:GO_Central.
DR   GO; GO:0010631; P:epithelial cell migration; IEA:EnsemblMetazoa.
DR   GO; GO:0007369; P:gastrulation; IEA:EnsemblMetazoa.
DR   GO; GO:0016331; P:morphogenesis of embryonic epithelium; IEA:EnsemblMetazoa.
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   3: Inferred from homology;
KW   Actin-binding; ATP-binding; Cytoplasm; Cytoskeleton; Nucleotide-binding;
KW   Reference proteome.
FT   CHAIN           1..426
FT                   /note="Actin-related protein 3"
FT                   /id="PRO_0000089084"
SQ   SEQUENCE   426 AA;  48088 MW;  3CC6F374F3384276 CRC64;
     MSSHQLPACV IDNGTGYTKL GYAGNTEPQF IIPSAIAVKD KVASSNAQAL RWNNRVGGAG
     IDDLDFFIGD EALSPAASNY TVKYPIRHGI VEDWDLMERY WEQCIFKYLR AEPEDHFFLL
     TEPPLNTPEN REYTAEIMFE SFNVPGLYIA VQAVLALTAS WQSREASDRS LTGLVIDSGD
     GVTHCIPVAD GYVIGSCIKH IPIAGRDITY FIQNLLRERE HTIPAEQSYE VAKTIKEKFC
     YVCPDVMKEF VKYDTDSSKW LRTYDGINSI TKRPFSVDVG YERFLGPEIF FHPEFCNPDF
     TTPISDTIDT LIQQCPIDVR RGLYENIVLS GGSTMFKDFA RKLQRDVKRL SDARLQMSET
     LSGGRLKPKP IDVQVISHKM QRYAVWFGGS MLASTSEFYQ VSHSKAEYME KGPSICRYNP
     VFGALT