ARPC3_SCHPO
ID ARPC3_SCHPO Reviewed; 174 AA.
AC Q9Y7J4;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 1.
DT 25-MAY-2022, entry version 128.
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=arc3; Synonyms=arc21; ORFNames=SPBC1778.08c;
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 [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 [2]
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 ARPC3 family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CU329671; CAB39803.1; -; Genomic_DNA.
DR PIR; T39690; T39690.
DR RefSeq; NP_596291.1; NM_001022213.2.
DR PDB; 3DWL; X-ray; 3.78 A; E/J=1-174.
DR PDB; 6W17; EM; 3.90 A; E=1-174.
DR PDB; 6W18; EM; 4.20 A; E=1-174.
DR PDBsum; 3DWL; -.
DR PDBsum; 6W17; -.
DR PDBsum; 6W18; -.
DR AlphaFoldDB; Q9Y7J4; -.
DR SMR; Q9Y7J4; -.
DR BioGRID; 276681; 12.
DR IntAct; Q9Y7J4; 3.
DR STRING; 4896.SPBC1778.08c.1; -.
DR MaxQB; Q9Y7J4; -.
DR PaxDb; Q9Y7J4; -.
DR EnsemblFungi; SPBC1778.08c.1; SPBC1778.08c.1:pep; SPBC1778.08c.
DR GeneID; 2540144; -.
DR KEGG; spo:SPBC1778.08c; -.
DR PomBase; SPBC1778.08c; arc3.
DR VEuPathDB; FungiDB:SPBC1778.08c; -.
DR eggNOG; KOG3155; Eukaryota.
DR HOGENOM; CLU_094365_2_0_1; -.
DR InParanoid; Q9Y7J4; -.
DR OMA; TPSKWWL; -.
DR PhylomeDB; Q9Y7J4; -.
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; Q9Y7J4; -.
DR PRO; PR:Q9Y7J4; -.
DR Proteomes; UP000002485; Chromosome II.
DR GO; GO:0030479; C:actin cortical patch; IDA: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:0005829; C:cytosol; HDA:PomBase.
DR GO; GO:0005634; C:nucleus; 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:0044396; P:actin cortical patch organization; IMP:PomBase.
DR GO; GO:0034314; P:Arp2/3 complex-mediated actin nucleation; IDA:PomBase.
DR GO; GO:0006897; P:endocytosis; IMP:PomBase.
DR GO; GO:0071963; P:establishment or maintenance of cell polarity regulating cell shape; IMP:PomBase.
DR GO; GO:0030833; P:regulation of actin filament polymerization; IEA:InterPro.
DR Gene3D; 1.10.1760.10; -; 1.
DR InterPro; IPR007204; ARPC3.
DR InterPro; IPR036753; ARPC3_sf.
DR PANTHER; PTHR12391; PTHR12391; 1.
DR Pfam; PF04062; P21-Arc; 1.
DR PIRSF; PIRSF016315; ARP2/3_P21-Arc; 1.
DR SUPFAM; SSF69060; SSF69060; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Actin-binding; Cytoplasm; Cytoskeleton; Reference proteome.
FT CHAIN 1..174
FT /note="Actin-related protein 2/3 complex subunit 3"
FT /id="PRO_0000124047"
SQ SEQUENCE 174 AA; 19844 MW; 0948C5EF7089CB79 CRC64;
MPAYHSSFLS LTDVPTTGNI AMLPLKTKFR GPAYPADESQ MDIIDECIGL FRANCFFRNF
EIKGPADRTL IYGTLFISEC LGRVNGLNYR DAERQLNSLA LENFSIPGSA GFPLNALYAP
PLSPQDAEIM RTYLTQFRQE LAYRLLSHVY ATEKDHPSKW WTCFSKRRFM NKAL
