ID   ARP3_CAEEL              Reviewed;         425 AA.
AC   Q9N4I0;
DT   26-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   03-AUG-2022, entry version 136.
DE   RecName: Full=Actin-related protein 3;
DE   AltName: Full=Actin-like protein 3;
GN   Name=arx-1; ORFNames=Y71F9AL.16;
OS   Caenorhabditis elegans.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC   Caenorhabditis.
OX   NCBI_TaxID=6239;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Bristol N2;
RX   PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG   The C. elegans sequencing consortium;
RT   "Genome sequence of the nematode C. elegans: a platform for investigating
RT   biology.";
RL   Science 282:2012-2018(1998).
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; FO081777; CCD73510.1; -; Genomic_DNA.
DR   RefSeq; NP_491066.1; NM_058665.4.
DR   AlphaFoldDB; Q9N4I0; -.
DR   SMR; Q9N4I0; -.
DR   BioGRID; 37336; 11.
DR   IntAct; Q9N4I0; 2.
DR   STRING; 6239.Y71F9AL.16; -.
DR   EPD; Q9N4I0; -.
DR   PaxDb; Q9N4I0; -.
DR   PeptideAtlas; Q9N4I0; -.
DR   EnsemblMetazoa; Y71F9AL.16.1; Y71F9AL.16.1; WBGene00000199.
DR   GeneID; 171857; -.
DR   KEGG; cel:CELE_Y71F9AL.16; -.
DR   UCSC; Y71F9AL.16; c. elegans.
DR   CTD; 171857; -.
DR   WormBase; Y71F9AL.16; CE25554; WBGene00000199; arx-1.
DR   eggNOG; KOG0678; Eukaryota.
DR   GeneTree; ENSGT00940000155065; -.
DR   HOGENOM; CLU_027965_3_0_1; -.
DR   InParanoid; Q9N4I0; -.
DR   OMA; TAEFKSY; -.
DR   OrthoDB; 649708at2759; -.
DR   PhylomeDB; Q9N4I0; -.
DR   Reactome; R-CEL-2029482; Regulation of actin dynamics for phagocytic cup formation.
DR   Reactome; R-CEL-3928662; EPHB-mediated forward signaling.
DR   Reactome; R-CEL-5663213; RHO GTPases Activate WASPs and WAVEs.
DR   Reactome; R-CEL-8856828; Clathrin-mediated endocytosis.
DR   PRO; PR:Q9N4I0; -.
DR   Proteomes; UP000001940; Chromosome I.
DR   Bgee; WBGene00000199; Expressed in pharyngeal muscle cell (C elegans) and 4 other tissues.
DR   GO; GO:0005885; C:Arp2/3 protein complex; IBA:GO_Central.
DR   GO; GO:0031252; C:cell leading edge; IDA:WormBase.
DR   GO; GO:0005737; C:cytoplasm; IDA:WormBase.
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; IMP:WormBase.
DR   GO; GO:0010631; P:epithelial cell migration; IMP:WormBase.
DR   GO; GO:0007369; P:gastrulation; IMP:WormBase.
DR   GO; GO:0016331; P:morphogenesis of embryonic epithelium; IMP:WormBase.
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..425
FT                   /note="Actin-related protein 3"
FT                   /id="PRO_0000089085"
SQ   SEQUENCE   425 AA;  48088 MW;  5435946CACBECE6C CRC64;
     MSAHQLPACV IDNGTGYTKL GYAGNTEPQF IIPSAIAVKD KVASSNSQAM RWNNRVGAGI
     DDLDFFIGDE ALSPAATNYT VKYPIRHGIV EDWDLMERYW EQCIFKYLRA EPEDHFFLLT
     EPPLNTPENR EYTAEIMFES FNVPGLYIAV QAVLALTASW NSREANERSL TGLVIDSGDG
     VTHCIPVADG YVIGSCIKHI PIAGRDITYF IQSLLRDREH TIPAEQSYEV AKMIKEKFCY
     VCPDVMKEFV KYDTDAAKWL RTYDGINSIT KKPFNVDVGY ERFLGPEIFF HPEFCNPEFT
     TPISDTIDTL IQQCPIDVRR GLYENIVLSG GSTMFKDFAR KLQRDVKRLS DGRLQMSETL
     SGGRLKPKPI DVQVISHKMQ RYAVWFGGSM LASTSEFYQV SHTKAEYMER GPSICRYNPV
     FGALT