ARP2_YEAST
ID ARP2_YEAST Reviewed; 391 AA.
AC P32381; D6VRW3;
DT 01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1993, sequence version 1.
DT 03-AUG-2022, entry version 192.
DE RecName: Full=Actin-related protein 2;
DE AltName: Full=Actin-like protein ARP2;
DE Short=Actin-like protein 2;
GN Name=ARP2; Synonyms=ACT2; OrderedLocusNames=YDL029W; ORFNames=D2778;
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 [GENOMIC DNA].
RC STRAIN=ATCC 26109 / X2180;
RX PubMed=1729653; DOI=10.1038/355179a0;
RA Schwob E., Martin R.P.;
RT "New yeast actin-like gene required late in the cell cycle.";
RL Nature 355:179-182(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169867;
RA Jacq C., Alt-Moerbe J., Andre B., Arnold W., Bahr A., Ballesta J.P.G.,
RA Bargues M., Baron L., Becker A., Biteau N., Bloecker H., Blugeon C.,
RA Boskovic J., Brandt P., Brueckner M., Buitrago M.J., Coster F.,
RA Delaveau T., del Rey F., Dujon B., Eide L.G., Garcia-Cantalejo J.M.,
RA Goffeau A., Gomez-Peris A., Granotier C., Hanemann V., Hankeln T.,
RA Hoheisel J.D., Jaeger W., Jimenez A., Jonniaux J.-L., Kraemer C.,
RA Kuester H., Laamanen P., Legros Y., Louis E.J., Moeller-Rieker S.,
RA Monnet A., Moro M., Mueller-Auer S., Nussbaumer B., Paricio N., Paulin L.,
RA Perea J., Perez-Alonso M., Perez-Ortin J.E., Pohl T.M., Prydz H.,
RA Purnelle B., Rasmussen S.W., Remacha M.A., Revuelta J.L., Rieger M.,
RA Salom D., Saluz H.P., Saiz J.E., Saren A.-M., Schaefer M., Scharfe M.,
RA Schmidt E.R., Schneider C., Scholler P., Schwarz S., Soler-Mira A.,
RA Urrestarazu L.A., Verhasselt P., Vissers S., Voet M., Volckaert G.,
RA Wagner G., Wambutt R., Wedler E., Wedler H., Woelfl S., Harris D.E.,
RA Bowman S., Brown D., Churcher C.M., Connor R., Dedman K., Gentles S.,
RA Hamlin N., Hunt S., Jones L., McDonald S., Murphy L.D., Niblett D.,
RA Odell C., Oliver K., Rajandream M.A., Richards C., Shore L., Walsh S.V.,
RA Barrell B.G., Dietrich F.S., Mulligan J.T., Allen E., Araujo R., Aviles E.,
RA Berno A., Carpenter J., Chen E., Cherry J.M., Chung E., Duncan M.,
RA Hunicke-Smith S., Hyman R.W., Komp C., Lashkari D., Lew H., Lin D.,
RA Mosedale D., Nakahara K., Namath A., Oefner P., Oh C., Petel F.X.,
RA Roberts D., Schramm S., Schroeder M., Shogren T., Shroff N., Winant A.,
RA Yelton M.A., Botstein D., Davis R.W., Johnston M., Andrews S., Brinkman R.,
RA Cooper J., Ding H., Du Z., Favello A., Fulton L., Gattung S., Greco T.,
RA Hallsworth K., Hawkins J., Hillier L.W., Jier M., Johnson D., Johnston L.,
RA Kirsten J., Kucaba T., Langston Y., Latreille P., Le T., Mardis E.,
RA Menezes S., Miller N., Nhan M., Pauley A., Peluso D., Rifkin L., Riles L.,
RA Taich A., Trevaskis E., Vignati D., Wilcox L., Wohldman P., Vaudin M.,
RA Wilson R., Waterston R., Albermann K., Hani J., Heumann K., Kleine K.,
RA Mewes H.-W., Zollner A., Zaccaria P.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome IV.";
RL Nature 387:75-78(1997).
RN [3]
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 [4]
RP IDENTIFICATION IN THE ARP2/3 COMPLEX, AND SUBCELLULAR LOCATION.
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 [5]
RP ERRATUM OF PUBMED:9210376.
RA Winter D., Podtelejnikov A.V., Mann M., Li R.;
RL Curr. Biol. 7:R593-R593(1997).
RN [6]
RP SUBCELLULAR LOCATION.
RX PubMed=11248049; DOI=10.1073/pnas.051494698;
RA Boldogh I.R., Yang H.C., Nowakowski W.D., Karmon S.L., Hays L.G.,
RA Yates J.R. III, Pon L.A.;
RT "Arp2/3 complex and actin dynamics are required for actin-based
RT mitochondrial motility in yeast.";
RL Proc. Natl. Acad. Sci. U.S.A. 98:3162-3167(2001).
RN [7]
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 [8]
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).
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19779198; DOI=10.1126/science.1172867;
RA Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.;
RT "Global analysis of Cdk1 substrate phosphorylation sites provides insights
RT into evolution.";
RL Science 325:1682-1686(2009).
RN [10]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
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 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 P32381; Q05933: ARC18; NbExp=7; IntAct=EBI-2927, EBI-2764;
CC P32381; P53731: ARC35; NbExp=6; IntAct=EBI-2927, EBI-2770;
CC P32381; P38328: ARC40; NbExp=6; IntAct=EBI-2927, EBI-2777;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, actin patch
CC {ECO:0000269|PubMed:11248049, ECO:0000269|PubMed:9210376}.
CC -!- MISCELLANEOUS: Present with 6650 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the actin family. ARP2 subfamily. {ECO:0000305}.
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DR EMBL; X61502; CAA43718.1; -; Genomic_DNA.
DR EMBL; Z71781; CAA96460.1; -; Genomic_DNA.
DR EMBL; Z74077; CAA98588.1; -; Genomic_DNA.
DR EMBL; BK006938; DAA11823.1; -; Genomic_DNA.
DR PIR; S20225; S20225.
DR RefSeq; NP_010255.1; NM_001180088.1.
DR AlphaFoldDB; P32381; -.
DR SMR; P32381; -.
DR BioGRID; 32027; 402.
DR ComplexPortal; CPX-607; Arp2/3 complex.
DR DIP; DIP-2217N; -.
DR IntAct; P32381; 99.
DR MINT; P32381; -.
DR STRING; 4932.YDL029W; -.
DR iPTMnet; P32381; -.
DR MaxQB; P32381; -.
DR PaxDb; P32381; -.
DR PRIDE; P32381; -.
DR EnsemblFungi; YDL029W_mRNA; YDL029W; YDL029W.
DR GeneID; 851532; -.
DR KEGG; sce:YDL029W; -.
DR SGD; S000002187; ARP2.
DR VEuPathDB; FungiDB:YDL029W; -.
DR eggNOG; KOG0677; Eukaryota.
DR HOGENOM; CLU_027965_0_2_1; -.
DR InParanoid; P32381; -.
DR OMA; WEDMQHL; -.
DR BioCyc; YEAST:G3O-29455-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 Reactome; R-SCE-6798695; Neutrophil degranulation.
DR PRO; PR:P32381; -.
DR Proteomes; UP000002311; Chromosome IV.
DR RNAct; P32381; protein.
DR GO; GO:0030479; C:actin cortical patch; IBA:GO_Central.
DR GO; GO:0015629; C:actin cytoskeleton; IC:ComplexPortal.
DR GO; GO:0005885; C:Arp2/3 protein complex; IDA:SGD.
DR GO; GO:0003779; F:actin binding; IEA:UniProtKB-KW.
DR GO; GO:0005524; F:ATP binding; IDA:SGD.
DR GO; GO:0016887; F:ATP hydrolysis activity; IMP:SGD.
DR GO; GO:0044396; P:actin cortical patch organization; IMP:SGD.
DR GO; GO:0045010; P:actin nucleation; IC:ComplexPortal.
DR GO; GO:0034314; P:Arp2/3 complex-mediated actin nucleation; IMP:SGD.
DR GO; GO:0030476; P:ascospore wall assembly; IMP:SGD.
DR GO; GO:0032258; P:cytoplasm to vacuole transport by the Cvt pathway; IMP:SGD.
DR GO; GO:0051654; P:establishment of mitochondrion localization; IMP:SGD.
DR GO; GO:0000001; P:mitochondrion inheritance; IMP:SGD.
DR InterPro; IPR004000; Actin.
DR InterPro; IPR020902; Actin/actin-like_CS.
DR InterPro; IPR043129; ATPase_NBD.
DR PANTHER; PTHR11937; PTHR11937; 1.
DR Pfam; PF00022; Actin; 1.
DR PRINTS; PR00190; ACTIN.
DR SMART; SM00268; ACTIN; 1.
DR SUPFAM; SSF53067; SSF53067; 2.
DR PROSITE; PS01132; ACTINS_ACT_LIKE; 1.
PE 1: Evidence at protein level;
KW Acetylation; Actin-binding; ATP-binding; Cytoplasm; Cytoskeleton;
KW Nucleotide-binding; Reference proteome.
FT CHAIN 1..391
FT /note="Actin-related protein 2"
FT /id="PRO_0000089077"
FT BINDING 159..161
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 213..217
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 304..309
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0007744|PubMed:22814378"
SQ SEQUENCE 391 AA; 44074 MW; 4C9E8952B477A1B9 CRC64;
MDPHNPIVLD QGTGFVKIGR AGENFPDYTF PSIVGRPILR AEERASVATP LKDIMIGDEA
SEVRSYLQIS YPMENGIIKN WTDMELLWDY AFFEQMKLPS TSNGKILLTE PPMNPLKNRE
KMCEVMFEKY DFGGVYVAIQ AVLALYAQGL SSGVVVDSGD GVTHIVPVYE SVVLSHLTRR
LDVAGRDVTR HLIDLLSRRG YAFNRTADFE TVRQIKEKLC YVSYDLDLDT KLARETTALV
ESYELPDGRT IKVGQERFEA PECLFQPGLV DVEQPGVGEL LFNTVQSADV DIRSSLYKAI
VLSGGSSMYP GLPSRLEKEL KQLWFSRVLH NDPSRLDKFK VRIEDPPRRK HMVFIGGAVL
ASIMADKDHM WLSKQEWQES GPSAMTKFGP R
