ARPC1_YEAST
ID ARPC1_YEAST Reviewed; 384 AA.
AC P38328; D6VQN0;
DT 01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1994, sequence version 1.
DT 03-AUG-2022, entry version 176.
DE RecName: Full=Actin-related protein 2/3 complex subunit 1;
DE AltName: Full=Arp2/3 complex 41 kDa subunit;
DE AltName: Full=p41-ARC;
GN Name=ARC40; OrderedLocusNames=YBR234C; ORFNames=YBR1532;
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=7813418; DOI=10.1002/j.1460-2075.1994.tb06923.x;
RA Feldmann H., Aigle M., Aljinovic G., Andre B., Baclet M.C., Barthe C.,
RA Baur A., Becam A.-M., Biteau N., Boles E., Brandt T., Brendel M.,
RA Brueckner M., Bussereau F., Christiansen C., Contreras R., Crouzet M.,
RA Cziepluch C., Demolis N., Delaveau T., Doignon F., Domdey H.,
RA Duesterhus S., Dubois E., Dujon B., El Bakkoury M., Entian K.-D.,
RA Feuermann M., Fiers W., Fobo G.M., Fritz C., Gassenhuber J., Glansdorff N.,
RA Goffeau A., Grivell L.A., de Haan M., Hein C., Herbert C.J.,
RA Hollenberg C.P., Holmstroem K., Jacq C., Jacquet M., Jauniaux J.-C.,
RA Jonniaux J.-L., Kallesoee T., Kiesau P., Kirchrath L., Koetter P.,
RA Korol S., Liebl S., Logghe M., Lohan A.J.E., Louis E.J., Li Z.Y.,
RA Maat M.J., Mallet L., Mannhaupt G., Messenguy F., Miosga T., Molemans F.,
RA Mueller S., Nasr F., Obermaier B., Perea J., Pierard A., Piravandi E.,
RA Pohl F.M., Pohl T.M., Potier S., Proft M., Purnelle B., Ramezani Rad M.,
RA Rieger M., Rose M., Schaaff-Gerstenschlaeger I., Scherens B.,
RA Schwarzlose C., Skala J., Slonimski P.P., Smits P.H.M., Souciet J.-L.,
RA Steensma H.Y., Stucka R., Urrestarazu L.A., van der Aart Q.J.M.,
RA Van Dyck L., Vassarotti A., Vetter I., Vierendeels F., Vissers S.,
RA Wagner G., de Wergifosse P., Wolfe K.H., Zagulski M., Zimmermann F.K.,
RA Mewes H.-W., Kleine K.;
RT "Complete DNA sequence of yeast chromosome II.";
RL EMBO J. 13:5795-5809(1994).
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=10377407; DOI=10.1073/pnas.96.13.7288;
RA Winter D.C., Choe E.Y., Li R.;
RT "Genetic dissection of the budding yeast Arp2/3 complex: a comparison of
RT the in vivo and structural roles of individual subunits.";
RL Proc. Natl. Acad. Sci. U.S.A. 96:7288-7293(1999).
RN [5]
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).
CC -!- FUNCTION: Functions as 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:10377407}.
CC -!- INTERACTION:
CC P38328; Q05933: ARC18; NbExp=4; IntAct=EBI-2777, EBI-2764;
CC P38328; P33204: ARC19; NbExp=4; IntAct=EBI-2777, EBI-2757;
CC P38328; P53731: ARC35; NbExp=6; IntAct=EBI-2777, EBI-2770;
CC P38328; P32381: ARP2; NbExp=6; IntAct=EBI-2777, EBI-2927;
CC P38328; P47117: ARP3; NbExp=4; IntAct=EBI-2777, EBI-2933;
CC P38328; Q12446: LAS17; NbExp=2; IntAct=EBI-2777, EBI-10022;
CC P38328; Q04439: MYO5; NbExp=3; IntAct=EBI-2777, EBI-11687;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, actin patch.
CC -!- SIMILARITY: Belongs to the WD repeat ARPC1 family. {ECO:0000305}.
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DR EMBL; Z36103; CAA85197.1; -; Genomic_DNA.
DR EMBL; AY692758; AAT92777.1; -; Genomic_DNA.
DR EMBL; BK006936; DAA07350.1; -; Genomic_DNA.
DR PIR; S46110; S46110.
DR RefSeq; NP_009793.1; NM_001178582.1.
DR AlphaFoldDB; P38328; -.
DR SMR; P38328; -.
DR BioGRID; 32929; 176.
DR ComplexPortal; CPX-607; Arp2/3 complex.
DR DIP; DIP-2219N; -.
DR IntAct; P38328; 48.
DR MINT; P38328; -.
DR STRING; 4932.YBR234C; -.
DR iPTMnet; P38328; -.
DR MaxQB; P38328; -.
DR PaxDb; P38328; -.
DR PRIDE; P38328; -.
DR EnsemblFungi; YBR234C_mRNA; YBR234C; YBR234C.
DR GeneID; 852536; -.
DR KEGG; sce:YBR234C; -.
DR SGD; S000000438; ARC40.
DR VEuPathDB; FungiDB:YBR234C; -.
DR eggNOG; KOG1523; Eukaryota.
DR GeneTree; ENSGT00950000183183; -.
DR HOGENOM; CLU_034396_1_0_1; -.
DR InParanoid; P38328; -.
DR OMA; YVWEPSP; -.
DR BioCyc; YEAST:G3O-29165-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:P38328; -.
DR Proteomes; UP000002311; Chromosome II.
DR RNAct; P38328; 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:0043130; F:ubiquitin binding; IDA: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; IBA:GO_Central.
DR GO; GO:2000601; P:positive regulation of Arp2/3 complex-mediated actin nucleation; IMP:SGD.
DR GO; GO:0030833; P:regulation of actin filament polymerization; IEA:InterPro.
DR Gene3D; 2.130.10.10; -; 1.
DR InterPro; IPR017383; ARPC1.
DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR InterPro; IPR001680; WD40_repeat.
DR InterPro; IPR036322; WD40_repeat_dom_sf.
DR PANTHER; PTHR10709; PTHR10709; 1.
DR Pfam; PF00400; WD40; 2.
DR PIRSF; PIRSF038093; ARP2/3_su1; 1.
DR SMART; SM00320; WD40; 5.
DR SUPFAM; SSF50978; SSF50978; 1.
PE 1: Evidence at protein level;
KW Actin-binding; Cytoplasm; Cytoskeleton; Reference proteome; Repeat;
KW WD repeat.
FT CHAIN 1..384
FT /note="Actin-related protein 2/3 complex subunit 1"
FT /id="PRO_0000050859"
FT REPEAT 61..99
FT /note="WD 1"
FT REPEAT 105..146
FT /note="WD 2"
FT REPEAT 151..190
FT /note="WD 3"
FT REPEAT 212..251
FT /note="WD 4"
FT REPEAT 349..383
FT /note="WD 5"
SQ SEQUENCE 384 AA; 42475 MW; D75C6BB8EC35EEDF CRC64;
MSFSNSKDKS VVAVYKLVKA PIYSHCFSQD KSILAVTCET DCLVYRVSNN TPPVLFATLK
DHDKTITAVD ISIHGRIVTC SQDRNAYVWE PLSDGTYKPT LVLLRINRAA TSVTWAPNGY
KFAVGSSARI IAVCYYEHEN NWWVSKHIKK PIKSTINCLS WHANGVLLAA GGTDGFMRVF
SGFIKGLDSK ESVAGSPWGQ KFPFGCLIRE WYQGSYIHDV EWRSQMERIA YVAHDGTLNV
VDYQSPVQSV NAPEGLPYRS LVWINDHEIV CGGYSCHPVL FSEASEGWKF AKNLDKSDNN
KSSALTASGN TDELSGNNDE SSTFGISALR KFKELDLKGK VSTDVQESAH ENAIVELRPF
AESNGQITQV SSCGLDGKIV IYTI
