ID   ARPC2_YEAST             Reviewed;         342 AA.
AC   P53731; D6W1L1;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   04-NOV-2026, entry version 181.
DE   RecName: Full=Actin-related protein 2/3 complex subunit 2;
DE   AltName: Full=Arp2/3 complex 34 kDa subunit;
DE            Short=p34-ARC;
GN   Name=ARC35; OrderedLocusNames=YNR035C; ORFNames=N3296;
OS   Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX   NCBI_TaxID=559292;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=9169873; DOI=10.1038/387s093;
RA   Philippsen P., Kleine K., Poehlmann R., Duesterhoeft A., Hamberg K.,
RA   Hegemann J.H., Obermaier B., Urrestarazu L.A., Aert R., Albermann K.,
RA   Altmann R., Andre B., Baladron V., Ballesta J.P.G., Becam A.-M.,
RA   Beinhauer J.D., Boskovic J., Buitrago M.J., Bussereau F., Coster F.,
RA   Crouzet M., D'Angelo M., Dal Pero F., De Antoni A., del Rey F., Doignon F.,
RA   Domdey H., Dubois E., Fiedler T.A., Fleig U., Floeth M., Fritz C.,
RA   Gaillardin C., Garcia-Cantalejo J.M., Glansdorff N., Goffeau A.,
RA   Gueldener U., Herbert C.J., Heumann K., Heuss-Neitzel D., Hilbert H.,
RA   Hinni K., Iraqui Houssaini I., Jacquet M., Jimenez A., Jonniaux J.-L.,
RA   Karpfinger-Hartl L., Lanfranchi G., Lepingle A., Levesque H., Lyck R.,
RA   Maftahi M., Mallet L., Maurer C.T.C., Messenguy F., Mewes H.-W., Moestl D.,
RA   Nasr F., Nicaud J.-M., Niedenthal R.K., Pandolfo D., Pierard A.,
RA   Piravandi E., Planta R.J., Pohl T.M., Purnelle B., Rebischung C.,
RA   Remacha M.A., Revuelta J.L., Rinke M., Saiz J.E., Sartorello F.,
RA   Scherens B., Sen-Gupta M., Soler-Mira A., Urbanus J.H.M., Valle G.,
RA   Van Dyck L., Verhasselt P., Vierendeels F., Vissers S., Voet M.,
RA   Volckaert G., Wach A., Wambutt R., Wedler H., Zollner A., Hani J.;
RT   "The nucleotide sequence of Saccharomyces cerevisiae chromosome XIV and its
RT   evolutionary implications.";
RL   Nature 387:93-98(1997).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=24374639; DOI=10.1534/g3.113.008995;
RA   Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA   Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA   Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT   "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL   G3 (Bethesda) 4:389-398(2014).
RN   [3]
RP   IDENTIFICATION IN THE ARP2/3 COMPLEX.
RX   PubMed=9210376; DOI=10.1016/s0960-9822(06)00223-5;
RA   Winter D., Podtelejnikov A.V., Mann M., Li R.;
RT   "The complex containing actin-related proteins Arp2 and Arp3 is required
RT   for the motility and integrity of yeast actin patches.";
RL   Curr. Biol. 7:519-529(1997).
RN   [4]
RP   ERRATUM OF PUBMED:9210376.
RA   Winter D., Podtelejnikov A.V., Mann M., Li R.;
RL   Curr. Biol. 7:R593-R593(1997).
RN   [5]
RP   LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX   PubMed=14562106; DOI=10.1038/nature02046;
RA   Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA   O'Shea E.K., Weissman J.S.;
RT   "Global analysis of protein expression in yeast.";
RL   Nature 425:737-741(2003).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-155 AND SER-324, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=18407956; DOI=10.1074/mcp.m700468-mcp200;
RA   Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
RT   "A multidimensional chromatography technology for in-depth phosphoproteome
RT   analysis.";
RL   Mol. Cell. Proteomics 7:1389-1396(2008).
CC   -!- FUNCTION: Functions as actin-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 mother actin
CC       filament (By similarity). {ECO:0000250}.
CC   -!- SUBUNIT: Component of the Arp2/3 complex composed of ARP2, ARP3,
CC       ARC40/p41-ARC, ARC35/p34-ARC, ARC18/p21-ARC, ARC19/p20-ARC and
CC       ARC16/p16-ARC. {ECO:0000269|PubMed:9210376}.
CC   -!- INTERACTION:
CC       P53731; Q05933: ARC18; NbExp=5; IntAct=EBI-2770, EBI-2764;
CC       P53731; P33204: ARC19; NbExp=4; IntAct=EBI-2770, EBI-2757;
CC       P53731; P38328: ARC40; NbExp=7; IntAct=EBI-2770, EBI-2777;
CC       P53731; P32381: ARP2; NbExp=7; IntAct=EBI-2770, EBI-2927;
CC       P53731; P37370: VRP1; NbExp=3; IntAct=EBI-2770, EBI-20502;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, actin patch.
CC   -!- MISCELLANEOUS: Present with 13400 molecules/cell in log phase SD
CC       medium. {ECO:0000269|PubMed:14562106}.
CC   -!- SIMILARITY: Belongs to the ARPC2 family. {ECO:0000305}.
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DR   EMBL; Z71650; CAA96315.1; -; Genomic_DNA.
DR   EMBL; BK006947; DAA10577.1; -; Genomic_DNA.
DR   PIR; S63366; S63366.
DR   RefSeq; NP_014433.1; NM_001183212.1.
DR   AlphaFoldDB; P53731; -.
DR   SMR; P53731; -.
DR   BioGRID; 35861; 485.
DR   ComplexPortal; CPX-607; Actin-related protein 2/3 complex.
DR   DIP; DIP-2304N; -.
DR   FunCoup; P53731; 955.
DR   IntAct; P53731; 28.
DR   STRING; 4932.YNR035C; -.
DR   iPTMnet; P53731; -.
DR   PaxDb; 4932-YNR035C; -.
DR   PeptideAtlas; P53731; -.
DR   EnsemblFungi; YNR035C_mRNA; YNR035C; YNR035C.
DR   GeneID; 855771; -.
DR   KEGG; sce:YNR035C; -.
DR   AGR; SGD:S000005318; -.
DR   SGD; S000005318; ARC35.
DR   VEuPathDB; FungiDB:YNR035C; -.
DR   eggNOG; KOG2826; Eukaryota.
DR   HOGENOM; CLU_059439_1_0_1; -.
DR   InParanoid; P53731; -.
DR   OMA; AAPNMNF; -.
DR   OrthoDB; 148331at2759; -.
DR   BioCyc; YEAST:G3O-33345-MONOMER; -.
DR   Reactome; R-SCE-2029482; Regulation of actin dynamics for phagocytic cup formation.
DR   Reactome; R-SCE-5663213; RHO GTPases Activate WASPs and WAVEs.
DR   BioGRID-ORCS; 855771; 6 hits in 10 CRISPR screens.
DR   PRO; PR:P53731; -.
DR   Proteomes; UP000002311; Chromosome XIV.
DR   RNAct; P53731; protein.
DR   GO; GO:0030479; C:actin cortical patch; IEA:UniProtKB-SubCell.
DR   GO; GO:0015629; C:actin cytoskeleton; NAS:ComplexPortal.
DR   GO; GO:0005885; C:Arp2/3 protein complex; IDA:SGD.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0005829; C:cytosol; IDA:SGD.
DR   GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR   GO; GO:0051015; F:actin filament binding; IBA:GO_Central.
DR   GO; GO:0005516; F:calmodulin binding; IPI:SGD.
DR   GO; GO:0140378; F:protein complex scaffold activity; IMP:SGD.
DR   GO; GO:0044396; P:actin cortical patch organization; IMP:SGD.
DR   GO; GO:0030036; P:actin cytoskeleton organization; IMP:SGD.
DR   GO; GO:0030041; P:actin filament polymerization; IBA:GO_Central.
DR   GO; GO:0045010; P:actin nucleation; NAS:ComplexPortal.
DR   GO; GO:0034314; P:Arp2/3 complex-mediated actin nucleation; IBA:GO_Central.
DR   GO; GO:0000226; P:microtubule cytoskeleton organization; IMP:SGD.
DR   GO; GO:0072697; P:protein localization to cell cortex; IMP:SGD.
DR   GO; GO:0006898; P:receptor-mediated endocytosis; IMP:SGD.
DR   FunFam; 3.30.1460.20:FF:000009; Arp2/3 complex 34 kDa subunit; 1.
DR   FunFam; 3.30.1460.20:FF:000010; Arp2/3 complex 34 kDa subunit; 1.
DR   Gene3D; 3.30.1460.20; -; 2.
DR   InterPro; IPR007188; ARPC2.
DR   InterPro; IPR034666; ARPC2/4.
DR   PANTHER; PTHR12058:SF0; ACTIN-RELATED PROTEIN 2_3 COMPLEX SUBUNIT 2; 1.
DR   PANTHER; PTHR12058; ARP2/3 COMPLEX 34 KDA SUBUNIT; 1.
DR   Pfam; PF04045; P34-Arc; 1.
DR   SUPFAM; SSF69645; Arp2/3 complex subunits; 2.
PE   1: Evidence at protein level;
KW   Actin-binding; Cytoplasm; Cytoskeleton; Phosphoprotein; Reference proteome.
FT   CHAIN           1..342
FT                   /note="Actin-related protein 2/3 complex subunit 2"
FT                   /id="PRO_0000124041"
FT   MOD_RES         155
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0007744|PubMed:18407956"
FT   MOD_RES         324
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:18407956"
SQ   SEQUENCE   342 AA;  39566 MW;  9AF71A93688729F6 CRC64;
     MLHLQPQNLL IQKTLNEAIE ALRKGSPLTM DRIVSDFDYT TYHISNTAED KSILLLSVKT
     KAWVSVSECQ LDGSLTLLKF LADHYSSLGG VTIPSEVEPG YDYTLQITLA ELVQESILQL
     SVLKTIILSF PFELAISKFI ELSQQQPAPV EAEITGGEVA ANGDNTLFTI KYRDEENIFI
     KPSNDRVTII FETIFQDETD KIFGKVFLQE FVDARKRNRQ IQSAPQVLYS HEPPLELKRL
     YQPPKVAEQS RRFITFVLFP RHFQTKELQF HSICQLTLFR NYFHYHIKCS KAYMHSRMRF
     RVDSFIKVLN RAKVDEDDEN DELSAEGRQQ ARRTFTGRKI VY
//