ID   ARPC3_YEAST             Reviewed;         178 AA.
AC   Q05933; D6VZ07;
DT   15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   04-NOV-2026, entry version 181.
DE   RecName: Full=Actin-related protein 2/3 complex subunit 3;
DE   AltName: Full=Arp2/3 complex 21 kDa subunit;
DE            Short=p21-ARC;
GN   Name=ARC18; OrderedLocusNames=YLR370C; ORFNames=L8039.15;
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=9169871; DOI=10.1038/387s087;
RA   Johnston M., Hillier L.W., Riles L., Albermann K., Andre B., Ansorge W.,
RA   Benes V., Brueckner M., Delius H., Dubois E., Duesterhoeft A.,
RA   Entian K.-D., Floeth M., Goffeau A., Hebling U., Heumann K.,
RA   Heuss-Neitzel D., Hilbert H., Hilger F., Kleine K., Koetter P., Louis E.J.,
RA   Messenguy F., Mewes H.-W., Miosga T., Moestl D., Mueller-Auer S.,
RA   Nentwich U., Obermaier B., Piravandi E., Pohl T.M., Portetelle D.,
RA   Purnelle B., Rechmann S., Rieger M., Rinke M., Rose M., Scharfe M.,
RA   Scherens B., Scholler P., Schwager C., Schwarz S., Underwood A.P.,
RA   Urrestarazu L.A., Vandenbol M., Verhasselt P., Vierendeels F., Voet M.,
RA   Volckaert G., Voss H., Wambutt R., Wedler E., Wedler H., Zimmermann F.K.,
RA   Zollner A., Hani J., Hoheisel J.D.;
RT   "The nucleotide sequence of Saccharomyces cerevisiae chromosome XII.";
RL   Nature 387:87-90(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   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=17322287; DOI=10.1101/gr.6037607;
RA   Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F.,
RA   Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J.,
RA   Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J.,
RA   Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D.,
RA   LaBaer J.;
RT   "Approaching a complete repository of sequence-verified protein-encoding
RT   clones for Saccharomyces cerevisiae.";
RL   Genome Res. 17:536-543(2007).
RN   [4]
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   [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   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   [7]
RP   IDENTIFICATION BY MASS 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).
RN   [8]
RP   UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-29, AND IDENTIFICATION BY MASS
RP   SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=22106047; DOI=10.1002/pmic.201100166;
RA   Starita L.M., Lo R.S., Eng J.K., von Haller P.D., Fields S.;
RT   "Sites of ubiquitin attachment in Saccharomyces cerevisiae.";
RL   Proteomics 12:236-240(2012).
CC   -!- FUNCTION: Functions as a component of the Arp2/3 complex which is
CC       involved in regulation of actin polymerization and together with an
CC       activating nucleation-promoting factor (NPF) mediates the formation of
CC       branched actin networks. {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       Q05933; P33204: ARC19; NbExp=4; IntAct=EBI-2764, EBI-2757;
CC       Q05933; P53731: ARC35; NbExp=5; IntAct=EBI-2764, EBI-2770;
CC       Q05933; P38328: ARC40; NbExp=5; IntAct=EBI-2764, EBI-2777;
CC       Q05933; P32381: ARP2; NbExp=8; IntAct=EBI-2764, EBI-2927;
CC       Q05933; Q12446: LAS17; NbExp=3; IntAct=EBI-2764, EBI-10022;
CC       Q05933; Q04439: MYO5; NbExp=3; IntAct=EBI-2764, EBI-11687;
CC       Q05933; P37370: VRP1; NbExp=3; IntAct=EBI-2764, EBI-20502;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000250}.
CC   -!- MISCELLANEOUS: Present with 1920 molecules/cell in log phase SD medium.
CC       {ECO:0000269|PubMed:14562106}.
CC   -!- SIMILARITY: Belongs to the ARPC3 family. {ECO:0000305}.
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DR   EMBL; U19103; AAB67576.1; -; Genomic_DNA.
DR   EMBL; AY558319; AAS56645.1; -; Genomic_DNA.
DR   EMBL; BK006945; DAA09673.1; -; Genomic_DNA.
DR   PIR; S51388; S51388.
DR   RefSeq; NP_013474.3; NM_001182259.3.
DR   AlphaFoldDB; Q05933; -.
DR   SMR; Q05933; -.
DR   BioGRID; 31630; 419.
DR   ComplexPortal; CPX-607; Actin-related protein 2/3 complex.
DR   DIP; DIP-2218N; -.
DR   FunCoup; Q05933; 1173.
DR   IntAct; Q05933; 22.
DR   STRING; 4932.YLR370C; -.
DR   iPTMnet; Q05933; -.
DR   PaxDb; 4932-YLR370C; -.
DR   PeptideAtlas; Q05933; -.
DR   TopDownProteomics; Q05933; -.
DR   EnsemblFungi; YLR370C_mRNA; YLR370C; YLR370C.
DR   GeneID; 851085; -.
DR   KEGG; sce:YLR370C; -.
DR   AGR; SGD:S000004362; -.
DR   SGD; S000004362; ARC18.
DR   VEuPathDB; FungiDB:YLR370C; -.
DR   eggNOG; KOG3155; Eukaryota.
DR   HOGENOM; CLU_094365_1_0_1; -.
DR   InParanoid; Q05933; -.
DR   OMA; AARPNKW; -.
DR   OrthoDB; 200404at2759; -.
DR   BioCyc; YEAST:G3O-32439-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; 851085; 4 hits in 10 CRISPR screens.
DR   PRO; PR:Q05933; -.
DR   Proteomes; UP000002311; Chromosome XII.
DR   RNAct; Q05933; protein.
DR   GO; GO:0015629; C:actin cytoskeleton; NAS:ComplexPortal.
DR   GO; GO:0005885; C:Arp2/3 protein complex; IDA:SGD.
DR   GO; GO:0005739; C:mitochondrion; IDA:SGD.
DR   GO; GO:0044396; P:actin cortical patch organization; IMP:SGD.
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:0051654; P:establishment of mitochondrion localization; IMP:SGD.
DR   FunFam; 1.10.1760.10:FF:000002; Actin-related protein 2/3 complex subunit 3; 1.
DR   Gene3D; 1.10.1760.10; Actin-related protein 2/3 complex subunit 3; 1.
DR   InterPro; IPR007204; ARPC3.
DR   InterPro; IPR036753; ARPC3_sf.
DR   PANTHER; PTHR12391; ARP2/3 COMPLEX 21 KD SUBUNIT; 1.
DR   Pfam; PF04062; P21-Arc; 1.
DR   PIRSF; PIRSF016315; ARP2/3_P21-Arc; 1.
DR   SUPFAM; SSF69060; Arp2/3 complex 21 kDa subunit ARPC3; 1.
PE   1: Evidence at protein level;
KW   Actin-binding; Cytoplasm; Cytoskeleton; Isopeptide bond;
KW   Reference proteome; Ubl conjugation.
FT   CHAIN           1..178
FT                   /note="Actin-related protein 2/3 complex subunit 3"
FT                   /id="PRO_0000124048"
FT   CROSSLNK        29
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in ubiquitin)"
FT                   /evidence="ECO:0007744|PubMed:22106047"
SQ   SEQUENCE   178 AA;  20579 MW;  456EABC2B9CC4860 CRC64;
     MPAYHSTFPV DPNTDRMVGN FALLPLNTKF RGPAYPSNSD YDIIDECLDL FRANSFFKNF
     EIKSPADRVL IYGILFINDC LAHLKITTSF NEAVKVLTNV ALDNFTLPGT PGFPLNNVYQ
     VPVQDHNSMD LLKTYIQQFR QELAMRLLER VYSSTDSKEY PSKFWLAFTR RRFMNKSL
//