ARPC1_SCHPO
ID ARPC1_SCHPO Reviewed; 377 AA.
AC P78774; O60088;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 11-JAN-2001, sequence version 3.
DT 03-AUG-2022, entry version 160.
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=arc1; Synonyms=sop2; ORFNames=SPBC14C8.06;
OS Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC Schizosaccharomyces.
OX NCBI_TaxID=284812;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=8978670; DOI=10.1002/j.1460-2075.1996.tb01034.x;
RA Balasubramanian M.K., Feoktostiva A., McCollum D., Gould K.L.;
RT "Fission yeast Sop2p: a novel and evolutionarily conserved protein that
RT interacts with Arp3p and modulates profilin function.";
RL EMBO J. 15:6426-6437(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=972 / ATCC 24843;
RX PubMed=11859360; DOI=10.1038/nature724;
RA Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA Nurse P.;
RT "The genome sequence of Schizosaccharomyces pombe.";
RL Nature 415:871-880(2002).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-239.
RC STRAIN=PR745;
RX PubMed=9501991; DOI=10.1093/dnares/4.6.363;
RA Yoshioka S., Kato K., Nakai K., Okayama H., Nojima H.;
RT "Identification of open reading frames in Schizosaccharomyces pombe
RT cDNAs.";
RL DNA Res. 4:363-369(1997).
RN [4]
RP IDENTIFICATION IN THE ARP2/3 COMPLEX.
RX PubMed=10588653; DOI=10.1091/mbc.10.12.4201;
RA Morrell J.L., Morphew M., Gould K.L.;
RT "A mutant of arp2p causes partial disassembly of the Arp2/3 complex and
RT loss of cortical actin function in fission yeast.";
RL Mol. Biol. Cell 10:4201-4215(1999).
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, act2,
CC arc1/p41-ARC, arc2/p34-ARC, arc3/p21-ARC, arc4/p20-ARC and arc5/p16-
CC ARC. {ECO:0000269|PubMed:10588653}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, actin patch.
CC -!- SIMILARITY: Belongs to the WD repeat ARPC1 family. {ECO:0000305}.
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DR EMBL; Y08998; CAA70202.1; -; Genomic_DNA.
DR EMBL; CU329671; CAA18424.1; -; Genomic_DNA.
DR EMBL; D89122; BAA13784.1; -; mRNA.
DR PIR; T39434; T39434.
DR PIR; T42364; T42364.
DR PIR; T45528; T45528.
DR RefSeq; NP_595909.1; NM_001021817.2.
DR PDB; 3DWL; X-ray; 3.78 A; C/H=1-377.
DR PDB; 6W17; EM; 3.90 A; C=1-377.
DR PDB; 6W18; EM; 4.20 A; C=1-377.
DR PDBsum; 3DWL; -.
DR PDBsum; 6W17; -.
DR PDBsum; 6W18; -.
DR AlphaFoldDB; P78774; -.
DR SMR; P78774; -.
DR BioGRID; 276546; 7.
DR IntAct; P78774; 3.
DR STRING; 4896.SPBC14C8.06.1; -.
DR iPTMnet; P78774; -.
DR MaxQB; P78774; -.
DR PaxDb; P78774; -.
DR PRIDE; P78774; -.
DR EnsemblFungi; SPBC14C8.06.1; SPBC14C8.06.1:pep; SPBC14C8.06.
DR GeneID; 2540002; -.
DR KEGG; spo:SPBC14C8.06; -.
DR PomBase; SPBC14C8.06; arc1.
DR VEuPathDB; FungiDB:SPBC14C8.06; -.
DR eggNOG; KOG1523; Eukaryota.
DR HOGENOM; CLU_034396_1_0_1; -.
DR InParanoid; P78774; -.
DR OMA; YVWEPSP; -.
DR PhylomeDB; P78774; -.
DR Reactome; R-SPO-2029482; Regulation of actin dynamics for phagocytic cup formation.
DR Reactome; R-SPO-5663213; RHO GTPases Activate WASPs and WAVEs.
DR Reactome; R-SPO-8856828; Clathrin-mediated endocytosis.
DR EvolutionaryTrace; P78774; -.
DR PRO; PR:P78774; -.
DR Proteomes; UP000002485; Chromosome II.
DR GO; GO:0030479; C:actin cortical patch; IC:PomBase.
DR GO; GO:0005885; C:Arp2/3 protein complex; IDA:PomBase.
DR GO; GO:0032153; C:cell division site; HDA:PomBase.
DR GO; GO:0051286; C:cell tip; HDA:PomBase.
DR GO; GO:0005737; C:cytoplasm; IDA:PomBase.
DR GO; GO:0005829; C:cytosol; HDA:PomBase.
DR GO; GO:0051015; F:actin filament binding; IDA:PomBase.
DR GO; GO:0000147; P:actin cortical patch assembly; IC:PomBase.
DR GO; GO:0034314; P:Arp2/3 complex-mediated actin nucleation; IDA:PomBase.
DR GO; GO:0030866; P:cortical actin cytoskeleton organization; IMP:PomBase.
DR GO; GO:0006897; P:endocytosis; IC:PomBase.
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; 4.
DR SUPFAM; SSF50978; SSF50978; 1.
DR PROSITE; PS50082; WD_REPEATS_2; 1.
DR PROSITE; PS50294; WD_REPEATS_REGION; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Actin-binding; Cytoplasm; Cytoskeleton; Reference proteome;
KW Repeat; WD repeat.
FT CHAIN 1..377
FT /note="Actin-related protein 2/3 complex subunit 1"
FT /id="PRO_0000050858"
FT REPEAT 9..48
FT /note="WD 1"
FT REPEAT 53..92
FT /note="WD 2"
FT REPEAT 98..139
FT /note="WD 3"
FT REPEAT 144..183
FT /note="WD 4"
FT REPEAT 203..242
FT /note="WD 5"
FT REPEAT 342..376
FT /note="WD 6"
FT REGION 293..313
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 100
FT /note="N -> D (in Ref. 3; BAA13784)"
FT /evidence="ECO:0000305"
FT CONFLICT 232
FT /note="A -> G (in Ref. 3; BAA13784)"
FT /evidence="ECO:0000305"
FT CONFLICT 306
FT /note="G -> V (in Ref. 1; CAA70202)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 377 AA; 41597 MW; C7016B4E6BEAA94D CRC64;
MATSQVLHIL PKPSYEHAFN SQRTEFVTTT ATNQVELYEQ DGNGWKHART FSDHDKIVTC
VDWAPKSNRI VTCSQDRNAY VYEKRPDGTW KQTLVLLRLN RAATFVRWSP NEDKFAVGSG
ARVISVCYFE QENDWWVSKH LKRPLRSTIL SLDWHPNNVL LAAGCADRKA YVLSAYVRDV
DAKPEASVWG SRLPFNTVCA EYPSGGWVHA VGFSPSGNAL AYAGHDSSVT IAYPSAPEQP
PRALITVKLS QLPLRSLLWA NESAIVAAGY NYSPILLQGN ESGWAHTRDL DAGTSKTSFT
HTGNTGEGRE EEGPVSFTAL RSTFRNMDLK GSSQSISSLP TVHQNMIATL RPYAGTPGNI
TAFTSSGTDG RVVLWTL
