ID   ARP2_SCHPO              Reviewed;         390 AA.
AC   Q9UUJ1; Q9US62; Q9UTP2;
DT   01-JUN-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   03-AUG-2022, entry version 139.
DE   RecName: Full=Actin-related protein 2;
DE   AltName: Full=Actin-like protein 2;
GN   Name=arp2; ORFNames=SPAC11H11.06, SPAC22F8.01;
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], FUNCTION, SUBCELLULAR LOCATION, AND
RP   IDENTIFICATION IN THE ARP2/3 COMPLEX.
RC   STRAIN=972 / ATCC 24843;
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).
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).
CC   -!- FUNCTION: Functions as ATP-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 pointed end
CC       of the daughter actin filament (By similarity). During cytokinesis it
CC       colocalizes to the cortical actin patches until spetation is complete.
CC       Has a role in the mobility of these patches. Essential for viability.
CC       {ECO:0000250, ECO:0000269|PubMed:10588653}.
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       {ECO:0000269|PubMed:10588653}.
CC   -!- SIMILARITY: Belongs to the actin family. ARP2 subfamily. {ECO:0000305}.
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DR   EMBL; AF095900; AAF21808.1; -; Genomic_DNA.
DR   EMBL; CU329670; CAB59802.1; -; Genomic_DNA.
DR   PIR; T38191; T38191.
DR   RefSeq; XP_001713111.1; XM_001713059.2.
DR   PDB; 6W17; EM; 3.90 A; B=1-390.
DR   PDB; 6W18; EM; 4.20 A; B=1-390.
DR   PDBsum; 6W17; -.
DR   PDBsum; 6W18; -.
DR   AlphaFoldDB; Q9UUJ1; -.
DR   SMR; Q9UUJ1; -.
DR   BioGRID; 858103; 18.
DR   IntAct; Q9UUJ1; 9.
DR   STRING; 4896.SPAC11H11.06.1; -.
DR   MaxQB; Q9UUJ1; -.
DR   PaxDb; Q9UUJ1; -.
DR   PRIDE; Q9UUJ1; -.
DR   EnsemblFungi; SPAC11H11.06.1; SPAC11H11.06.1:pep; SPAC11H11.06.
DR   PomBase; SPAC11H11.06; arp2.
DR   VEuPathDB; FungiDB:SPAC11H11.06; -.
DR   eggNOG; KOG0677; Eukaryota.
DR   HOGENOM; CLU_027965_0_2_1; -.
DR   InParanoid; Q9UUJ1; -.
DR   OMA; WEDMQHL; -.
DR   PhylomeDB; Q9UUJ1; -.
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-6798695; Neutrophil degranulation.
DR   Reactome; R-SPO-8856828; Clathrin-mediated endocytosis.
DR   PRO; PR:Q9UUJ1; -.
DR   Proteomes; UP000002485; Chromosome I.
DR   GO; GO:0030479; C:actin cortical patch; IDA:PomBase.
DR   GO; GO:0005885; C:Arp2/3 protein complex; IDA:PomBase.
DR   GO; GO:0051285; C:cell cortex of cell tip; IDA:PomBase.
DR   GO; GO:0031097; C:medial cortex; IDA:PomBase.
DR   GO; GO:0051015; F:actin filament binding; IDA:PomBase.
DR   GO; GO:0005524; F:ATP 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:0006897; P:endocytosis; IMP:PomBase.
DR   InterPro; IPR004000; Actin.
DR   InterPro; IPR020902; Actin/actin-like_CS.
DR   InterPro; IPR043129; ATPase_NBD.
DR   PANTHER; PTHR11937; PTHR11937; 1.
DR   Pfam; PF00022; Actin; 1.
DR   PRINTS; PR00190; ACTIN.
DR   SMART; SM00268; ACTIN; 1.
DR   SUPFAM; SSF53067; SSF53067; 2.
DR   PROSITE; PS01132; ACTINS_ACT_LIKE; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Actin-binding; ATP-binding; Cytoplasm; Cytoskeleton;
KW   Nucleotide-binding; Reference proteome.
FT   CHAIN           1..390
FT                   /note="Actin-related protein 2"
FT                   /id="PRO_0000089076"
FT   BINDING         156..158
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
FT   BINDING         210..214
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
FT   BINDING         301..306
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
FT   CONFLICT        358
FT                   /note="A -> V (in Ref. 1; AAF21808)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   390 AA;  44231 MW;  D1439F6B49E4E306 CRC64;
     MESAPIVLDN GTGFVKVGYA KDNFPRFQFP SIVGRPILRA EEKTGNVQIK DVMVGDEAEA
     VRSLLQVKYP MENGIIRDFE EMNQLWDYTF FEKLKIDPRG RKILLTEPPM NPVANREKMC
     ETMFERYGFG GVYVAIQAVL SLYAQGLSSG VVVDSGDGVT HIVPVYESVV LNHLVGRLDV
     AGRDATRYLI SLLLRKGYAF NRTADFETVR EMKEKLCYVS YDLELDHKLS EETTVLMRNY
     TLPDGRVIKV GSERYECPEC LFQPHLVGSE QPGLSEFIFD TIQAADVDIR KYLYRAIVLS
     GGSSMYAGLP SRLEKEIKQL WFERVLHGDP ARLPNFKVKI EDAPRRRHAV FIGGAVLADI
     MAQNDHMWVS KAEWEEYGVR ALDKLGPRTT