ID   ARPC2_SCHPO             Reviewed;         317 AA.
AC   O14241;
DT   15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1998, sequence version 1.
DT   03-AUG-2022, entry version 128.
DE   RecName: Full=Actin-related protein 2/3 complex subunit 2;
DE   AltName: Full=Arp2/3 complex 34 kDa subunit;
DE            Short=p34-ARC;
GN   Name=arc2; Synonyms=arc34; ORFNames=SPAC6F6.10c;
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 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, 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 ARPC2 family. {ECO:0000305}.
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DR   EMBL; CU329670; CAB11733.1; -; Genomic_DNA.
DR   PIR; T39044; T39044.
DR   RefSeq; NP_593903.1; NM_001019333.2.
DR   PDB; 3DWL; X-ray; 3.78 A; D/I=1-317.
DR   PDB; 6W17; EM; 3.90 A; D=1-317.
DR   PDB; 6W18; EM; 4.20 A; D=1-317.
DR   PDBsum; 3DWL; -.
DR   PDBsum; 6W17; -.
DR   PDBsum; 6W18; -.
DR   AlphaFoldDB; O14241; -.
DR   SMR; O14241; -.
DR   BioGRID; 278755; 4.
DR   IntAct; O14241; 3.
DR   STRING; 4896.SPAC6F6.10c.1; -.
DR   iPTMnet; O14241; -.
DR   MaxQB; O14241; -.
DR   PaxDb; O14241; -.
DR   PRIDE; O14241; -.
DR   EnsemblFungi; SPAC6F6.10c.1; SPAC6F6.10c.1:pep; SPAC6F6.10c.
DR   GeneID; 2542287; -.
DR   KEGG; spo:SPAC6F6.10c; -.
DR   PomBase; SPAC6F6.10c; arc2.
DR   VEuPathDB; FungiDB:SPAC6F6.10c; -.
DR   eggNOG; KOG2826; Eukaryota.
DR   HOGENOM; CLU_059439_1_0_1; -.
DR   InParanoid; O14241; -.
DR   OMA; GPYIVSP; -.
DR   PhylomeDB; O14241; -.
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; O14241; -.
DR   PRO; PR:O14241; -.
DR   Proteomes; UP000002485; Chromosome I.
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: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:0005200; F:structural constituent of cytoskeleton; IBA:GO_Central.
DR   GO; GO:0000147; P:actin cortical patch assembly; IC:PomBase.
DR   GO; GO:0030041; P:actin filament polymerization; IEA:InterPro.
DR   GO; GO:0034314; P:Arp2/3 complex-mediated actin nucleation; IDA:PomBase.
DR   GO; GO:0006897; P:endocytosis; IC:PomBase.
DR   GO; GO:0030833; P:regulation of actin filament polymerization; IEA:InterPro.
DR   Gene3D; 3.30.1460.20; -; 2.
DR   InterPro; IPR007188; ARPC2.
DR   InterPro; IPR034666; ARPC2/4.
DR   PANTHER; PTHR12058; PTHR12058; 1.
DR   Pfam; PF04045; P34-Arc; 1.
DR   SUPFAM; SSF69645; SSF69645; 2.
PE   1: Evidence at protein level;
KW   3D-structure; Actin-binding; Cytoplasm; Cytoskeleton; Reference proteome.
FT   CHAIN           1..317
FT                   /note="Actin-related protein 2/3 complex subunit 2"
FT                   /id="PRO_0000124040"
SQ   SEQUENCE   317 AA;  36974 MW;  2B1FD6B3498F0C2A CRC64;
     MLSLDYNNIF IYELLTERFS SENPSSIDQV VTDFDGVTFH ISTPEEKTKI LISLSMKCYP
     ELVNYGTLDL LKQIYGAYVH EPEMGYNFSI LIDLQQLPAT DEEKEQLAMS ISMLKRNVLA
     APFHRAFTKQ AELADLARKD PENAPMLDKQ ATSQELMAIH YRDEETIVLW PEHDRVTVVF
     STKFREETDR IFGKVFLQEF VDARRRPAIQ TAPQVLFSYR DPPLEIRDIQ GIQKGDDFGF
     VTFVLFERHF TPQNREDCIS HIQVFRNTLH FHIKASKAYM HQRMRKRVAD FQKVLNRAKP
     DVELERKTAT GRSFVRA