ARPC2_YEAST
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 03-AUG-2022, entry version 165.
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;
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=3; IntAct=EBI-2770, EBI-2757;
CC P53731; P38328: ARC40; NbExp=6; IntAct=EBI-2770, EBI-2777;
CC P53731; P32381: ARP2; NbExp=6; IntAct=EBI-2770, EBI-2927;
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; 462.
DR ComplexPortal; CPX-607; Arp2/3 complex.
DR DIP; DIP-2304N; -.
DR IntAct; P53731; 17.
DR MINT; P53731; -.
DR STRING; 4932.YNR035C; -.
DR iPTMnet; P53731; -.
DR MaxQB; P53731; -.
DR PaxDb; P53731; -.
DR PRIDE; P53731; -.
DR EnsemblFungi; YNR035C_mRNA; YNR035C; YNR035C.
DR GeneID; 855771; -.
DR KEGG; sce:YNR035C; -.
DR SGD; S000005318; ARC35.
DR VEuPathDB; FungiDB:YNR035C; -.
DR eggNOG; KOG2826; Eukaryota.
DR GeneTree; ENSGT00390000016794; -.
DR HOGENOM; CLU_059439_1_0_1; -.
DR InParanoid; P53731; -.
DR OMA; GPYIVSP; -.
DR BioCyc; YEAST:G3O-33345-MON; -.
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 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; IC:ComplexPortal.
DR GO; GO:0005885; C:Arp2/3 protein complex; IDA:SGD.
DR GO; GO:0005829; C:cytosol; IPI:SGD.
DR GO; GO:0051015; F:actin filament binding; IBA:GO_Central.
DR GO; GO:0005516; F:calmodulin binding; IPI:SGD.
DR GO; GO:0060090; F:molecular adaptor activity; IMP:SGD.
DR GO; GO:0005200; F:structural constituent of cytoskeleton; IBA:GO_Central.
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; IEA:InterPro.
DR GO; GO:0045010; P:actin nucleation; IC: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 GO; GO:0030833; P:regulation of actin filament polymerization; IEA:InterPro.
DR Gene3D; 3.30.1460.20; -; 2.
DR InterPro; IPR007188; ARPC2.
DR InterPro; IPR034666; ARPC2/4.
DR PANTHER; PTHR12058; PTHR12058; 1.
DR Pfam; PF04045; P34-Arc; 1.
DR SUPFAM; SSF69645; SSF69645; 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
