ARPC4_YEAST
ID ARPC4_YEAST Reviewed; 171 AA.
AC P33204; D6VXS3;
DT 01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1994, sequence version 2.
DT 03-AUG-2022, entry version 157.
DE RecName: Full=Actin-related protein 2/3 complex subunit 4;
DE AltName: Full=Arp2/3 complex 20 kDa;
DE Short=p20-ARC;
GN Name=ARC19; OrderedLocusNames=YKL013C; ORFNames=YKL166;
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].
RX PubMed=8154185; DOI=10.1002/yea.320091208;
RA Wiemann S., Voss H., Schwager C., Rupp T., Stegemann J., Zimmermann J.,
RA Grothues D., Sensen C., Erfle H., Hewitt N., Banrevi A., Ansorge W.;
RT "Sequencing and analysis of 51.6 kilobases on the left arm of chromosome XI
RT from Saccharomyces cerevisiae reveals 23 open reading frames including the
RT FAS1 gene.";
RL Yeast 9:1343-1348(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=8196765; DOI=10.1038/369371a0;
RA Dujon B., Alexandraki D., Andre B., Ansorge W., Baladron V.,
RA Ballesta J.P.G., Banrevi A., Bolle P.-A., Bolotin-Fukuhara M., Bossier P.,
RA Bou G., Boyer J., Buitrago M.J., Cheret G., Colleaux L.,
RA Daignan-Fornier B., del Rey F., Dion C., Domdey H., Duesterhoeft A.,
RA Duesterhus S., Entian K.-D., Erfle H., Esteban P.F., Feldmann H.,
RA Fernandes L., Fobo G.M., Fritz C., Fukuhara H., Gabel C., Gaillon L.,
RA Garcia-Cantalejo J.M., Garcia-Ramirez J.J., Gent M.E., Ghazvini M.,
RA Goffeau A., Gonzalez A., Grothues D., Guerreiro P., Hegemann J.H.,
RA Hewitt N., Hilger F., Hollenberg C.P., Horaitis O., Indge K.J.,
RA Jacquier A., James C.M., Jauniaux J.-C., Jimenez A., Keuchel H.,
RA Kirchrath L., Kleine K., Koetter P., Legrain P., Liebl S., Louis E.J.,
RA Maia e Silva A., Marck C., Monnier A.-L., Moestl D., Mueller S.,
RA Obermaier B., Oliver S.G., Pallier C., Pascolo S., Pfeiffer F.,
RA Philippsen P., Planta R.J., Pohl F.M., Pohl T.M., Poehlmann R.,
RA Portetelle D., Purnelle B., Puzos V., Ramezani Rad M., Rasmussen S.W.,
RA Remacha M.A., Revuelta J.L., Richard G.-F., Rieger M.,
RA Rodrigues-Pousada C., Rose M., Rupp T., Santos M.A., Schwager C.,
RA Sensen C., Skala J., Soares H., Sor F., Stegemann J., Tettelin H.,
RA Thierry A., Tzermia M., Urrestarazu L.A., van Dyck L.,
RA van Vliet-Reedijk J.C., Valens M., Vandenbol M., Vilela C., Vissers S.,
RA von Wettstein D., Voss H., Wiemann S., Xu G., Zimmermann J., Haasemann M.,
RA Becker I., Mewes H.-W.;
RT "Complete DNA sequence of yeast chromosome XI.";
RL Nature 369:371-378(1994).
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 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 [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-130.
RX PubMed=1481574; DOI=10.1002/yea.320081109;
RA Pascolo S., Ghazvini M., Boyer J., Colleaux L., Thierry A., Dujon B.;
RT "The sequence of a 9.3 kb segment located on the left arm of the yeast
RT chromosome XI reveals five open reading frames including the CCE1 gene and
RT putative products related to MYO2 and to the ribosomal protein L10.";
RL Yeast 8:987-995(1992).
RN [6]
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 [7]
RP ERRATUM OF PUBMED:9210376.
RA Winter D., Podtelejnikov A.V., Mann M., Li R.;
RL Curr. Biol. 7:R593-R593(1997).
RN [8]
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).
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 P33204; Q05933: ARC18; NbExp=3; IntAct=EBI-2757, EBI-2764;
CC P33204; P53731: ARC35; NbExp=3; IntAct=EBI-2757, EBI-2770;
CC P33204; P38328: ARC40; NbExp=4; IntAct=EBI-2757, EBI-2777;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, actin patch.
CC -!- MISCELLANEOUS: Present with 9020 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the ARPC4 family. {ECO:0000305}.
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DR EMBL; X74152; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; S53418; AAB24905.1; ALT_TERM; Genomic_DNA.
DR EMBL; Z28013; CAA81848.1; -; Genomic_DNA.
DR EMBL; AY558348; AAS56674.1; -; Genomic_DNA.
DR EMBL; BK006944; DAA09143.1; -; Genomic_DNA.
DR PIR; S37826; S37826.
DR RefSeq; NP_012912.1; NM_001179579.1.
DR AlphaFoldDB; P33204; -.
DR SMR; P33204; -.
DR BioGRID; 34119; 27.
DR ComplexPortal; CPX-607; Arp2/3 complex.
DR DIP; DIP-1819N; -.
DR IntAct; P33204; 14.
DR MINT; P33204; -.
DR STRING; 4932.YKL013C; -.
DR MaxQB; P33204; -.
DR PaxDb; P33204; -.
DR PRIDE; P33204; -.
DR EnsemblFungi; YKL013C_mRNA; YKL013C; YKL013C.
DR GeneID; 853856; -.
DR KEGG; sce:YKL013C; -.
DR SGD; S000001496; ARC19.
DR VEuPathDB; FungiDB:YKL013C; -.
DR eggNOG; KOG1876; Eukaryota.
DR GeneTree; ENSGT00390000016233; -.
DR HOGENOM; CLU_084855_1_0_1; -.
DR InParanoid; P33204; -.
DR OMA; EAYLGEF; -.
DR BioCyc; YEAST:G3O-31822-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:P33204; -.
DR Proteomes; UP000002311; Chromosome XI.
DR RNAct; P33204; 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:0051015; F:actin filament binding; IBA:GO_Central.
DR GO; GO:0060090; F:molecular adaptor activity; IMP:SGD.
DR GO; GO:0044396; P:actin cortical patch 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:0030833; P:regulation of actin filament polymerization; IEA:InterPro.
DR Gene3D; 3.30.1460.20; -; 1.
DR InterPro; IPR034666; ARPC2/4.
DR InterPro; IPR008384; ARPC4.
DR PANTHER; PTHR22629; PTHR22629; 1.
DR Pfam; PF05856; ARPC4; 1.
DR PIRSF; PIRSF039100; ARPC4; 1.
DR SUPFAM; SSF69645; SSF69645; 1.
PE 1: Evidence at protein level;
KW Actin-binding; Cytoplasm; Cytoskeleton; Reference proteome.
FT CHAIN 1..171
FT /note="Actin-related protein 2/3 complex subunit 4"
FT /id="PRO_0000124053"
SQ SEQUENCE 171 AA; 19916 MW; B80CBD6642E39C1C CRC64;
MSQSLRPYLT AVRYSLEAAL TLSNFSSQEV ERHNRPEVEV PNTSAELLLQ PMHISRNENE
QVLIEPSVNS VRMSLMVKQA DEIEQILVHK FTRFLEQRAE AFYILRRVPI PGYSISFLIT
NKHTESMKTG KLVDFIIEFM EDVDKEISEI KLFLNARARF VAEAYLDEFV Y
