ID   ARP2_CAEEL              Reviewed;         395 AA.
AC   P53489;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   03-AUG-2022, entry version 141.
DE   RecName: Full=Actin-related protein 2;
DE   AltName: Full=Actin-like protein 2;
DE   AltName: Full=Actin-like protein C;
GN   Name=arx-2; Synonyms=actc; ORFNames=K07C5.1;
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. ARP2 subfamily. {ECO:0000305}.
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DR   EMBL; Z71181; CAA94894.1; -; Genomic_DNA.
DR   PIR; T23402; T23402.
DR   RefSeq; NP_505657.1; NM_073256.6.
DR   AlphaFoldDB; P53489; -.
DR   SMR; P53489; -.
DR   BioGRID; 44470; 14.
DR   DIP; DIP-27263N; -.
DR   STRING; 6239.K07C5.1; -.
DR   EPD; P53489; -.
DR   PaxDb; P53489; -.
DR   PeptideAtlas; P53489; -.
DR   EnsemblMetazoa; K07C5.1.1; K07C5.1.1; WBGene00000200.
DR   GeneID; 179440; -.
DR   KEGG; cel:CELE_K07C5.1; -.
DR   UCSC; K07C5.1; c. elegans.
DR   CTD; 179440; -.
DR   WormBase; K07C5.1; CE06111; WBGene00000200; arx-2.
DR   eggNOG; KOG0677; Eukaryota.
DR   GeneTree; ENSGT00940000154556; -.
DR   HOGENOM; CLU_027965_0_0_1; -.
DR   InParanoid; P53489; -.
DR   OMA; WEDMQHL; -.
DR   OrthoDB; 649708at2759; -.
DR   PhylomeDB; P53489; -.
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-6798695; Neutrophil degranulation.
DR   Reactome; R-CEL-8856828; Clathrin-mediated endocytosis.
DR   PRO; PR:P53489; -.
DR   Proteomes; UP000001940; Chromosome V.
DR   Bgee; WBGene00000200; Expressed in germ line (C elegans) and 4 other tissues.
DR   GO; GO:0005885; C:Arp2/3 protein complex; IBA:GO_Central.
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; 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; IPR004001; Actin_CS.
DR   InterPro; IPR027306; Arp2.
DR   InterPro; IPR043129; ATPase_NBD.
DR   PANTHER; PTHR11937; PTHR11937; 1.
DR   PANTHER; PTHR11937:SF149; PTHR11937:SF149; 1.
DR   Pfam; PF00022; Actin; 1.
DR   PRINTS; PR00190; ACTIN.
DR   SMART; SM00268; ACTIN; 1.
DR   SUPFAM; SSF53067; SSF53067; 2.
DR   PROSITE; PS00432; ACTINS_2; 1.
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..395
FT                   /note="Actin-related protein 2"
FT                   /id="PRO_0000089074"
FT   BINDING         160..162
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
FT   BINDING         214..218
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
FT   BINDING         305..310
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   395 AA;  44841 MW;  D13B735000420692 CRC64;
     MDSQGRKVIV VDNGTGFVKC GYAGTNFPAH IFPSMVGRPI VRSTQRVGNI EIKDLMVGEE
     CSQLRQMLDI NYPMDNGIVR NWDDMAHVWD HTFGPEKLDI DPKECKLLLT EPPLNPNSNR
     EKMFQVMFEQ YGFNSIYVAV QAVLTLYAQG LLTGVVVDSG DGVTHICPVY EGFALHHLTR
     RLDIAGRDIT KYLIKLLLQR GYNFNHSADF ETVRQMKEKL CYIAYDVEQE ERLALETTVL
     SQQYTLPDGR VIRLGGERFE APEILFQPHL INVEKAGLSE LLFGCIQASD IDTRLDFYKH
     IVLSGGTTMY PGLPSRLEKE LKQLYLDRVL HGNTDAFQKF KIRIEAPPSR KHMVFLGGAV
     LANLMKDRDQ DFWVSKKEYE EGGIARCMAK LGIKA