ID   ARP2_CAEBR              Reviewed;         393 AA.
AC   Q61JZ2; A8X8R1;
DT   26-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT   23-NOV-2004, sequence version 1.
DT   03-AUG-2022, entry version 89.
DE   RecName: Full=Actin-related protein 2;
DE   AltName: Full=Actin-like protein 2;
GN   Name=arx-2; ORFNames=CBG09586;
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. ARP2 subfamily. {ECO:0000305}.
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DR   EMBL; HE600998; CAP29022.3; -; Genomic_DNA.
DR   RefSeq; XP_002637087.1; XM_002637041.1.
DR   AlphaFoldDB; Q61JZ2; -.
DR   SMR; Q61JZ2; -.
DR   STRING; 6238.CBG09586; -.
DR   GeneID; 8579083; -.
DR   KEGG; cbr:CBG_09586; -.
DR   CTD; 8579083; -.
DR   WormBase; CBG09586; CBP38609; WBGene00031147; Cbr-arx-2.
DR   eggNOG; KOG0677; Eukaryota.
DR   HOGENOM; CLU_027965_0_0_1; -.
DR   InParanoid; Q61JZ2; -.
DR   OMA; WEDMQHL; -.
DR   OrthoDB; 649708at2759; -.
DR   Proteomes; UP000008549; Chromosome V.
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; IBA:GO_Central.
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..393
FT                   /note="Actin-related protein 2"
FT                   /id="PRO_0000089073"
FT   BINDING         158..160
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
FT   BINDING         212..216
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
FT   BINDING         303..308
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   393 AA;  44599 MW;  20D7D2943B709463 CRC64;
     MDSQGRKVIV VDNGTGFVKC GYAGTNFPAH IFPSMVGRPI VRSTQRVGNI EIKDLMVGEE
     CSQLRQMLDI NYPMDNGIVR NWDDMGHVWD HTFGPEKLDI DPKECKLLLT EPPLNPNSNR
     EKMFQVMFEQ YGFNSIYVAA VLTLYAQGLL TGVVVDSGDG VTHICPVYEG FALHHLTRRL
     DIAGRDITKY LIKLLLQRGY NFNHSADFET VRQMKEKLCY IAYDVEQEER LALETTVLSQ
     QYTLPDGRVI RLGGERFEAP EILFQPHLIN VEKAGLSELL FGCIQASDID TRLDFYKHIV
     LSGGTTMYPG LPSRLEKELK QLYLDRVLHG NTDAFQKFKI RIEAPPSRKH MVFLGGAVLA
     NLMKDRDQDF WVSKKEYEEG GIARCMAKLG IKA