ID   ARP3_SCHPO              Reviewed;         427 AA.
AC   P32390;
DT   01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1993, sequence version 1.
DT   03-AUG-2022, entry version 152.
DE   RecName: Full=Actin-related protein 3;
DE   AltName: Full=Actin-like protein 3;
GN   Name=act2; ORFNames=SPAC630.03;
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=1729722; DOI=10.1073/pnas.89.1.80;
RA   Lees-Miller J.P., Henry G., Helfman D.M.;
RT   "Identification of act2, an essential gene in the fission yeast
RT   Schizosaccharomyces pombe that encodes a protein related to actin.";
RL   Proc. Natl. Acad. Sci. U.S.A. 89:80-83(1992).
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   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 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). May be involved in
CC       cytokinesis. {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 actin family. ARP3 subfamily. {ECO:0000305}.
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DR   EMBL; M81068; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CU329670; CAB52725.1; -; Genomic_DNA.
DR   PIR; A41790; A41790.
DR   RefSeq; NP_592898.1; NM_001018298.2.
DR   PDB; 3DWL; X-ray; 3.78 A; A/B=1-427.
DR   PDB; 6W17; EM; 3.90 A; A=1-427.
DR   PDB; 6W18; EM; 4.20 A; A=1-427.
DR   PDBsum; 3DWL; -.
DR   PDBsum; 6W17; -.
DR   PDBsum; 6W18; -.
DR   AlphaFoldDB; P32390; -.
DR   SMR; P32390; -.
DR   BioGRID; 279661; 19.
DR   IntAct; P32390; 3.
DR   STRING; 4896.SPAC630.03.1; -.
DR   iPTMnet; P32390; -.
DR   MaxQB; P32390; -.
DR   PaxDb; P32390; -.
DR   PRIDE; P32390; -.
DR   EnsemblFungi; SPAC630.03.1; SPAC630.03.1:pep; SPAC630.03.
DR   GeneID; 2543233; -.
DR   KEGG; spo:SPAC630.03; -.
DR   PomBase; SPAC630.03; -.
DR   VEuPathDB; FungiDB:SPAC630.03; -.
DR   eggNOG; KOG0678; Eukaryota.
DR   HOGENOM; CLU_027965_3_0_1; -.
DR   InParanoid; P32390; -.
DR   OMA; TAEFKSY; -.
DR   PhylomeDB; P32390; -.
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; P32390; -.
DR   PRO; PR:P32390; -.
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:0032153; C:cell division site; IDA:PomBase.
DR   GO; GO:0005737; C:cytoplasm; HDA:PomBase.
DR   GO; GO:0005829; C:cytosol; HDA:PomBase.
DR   GO; GO:0051015; F:actin filament binding; IDA:PomBase.
DR   GO; GO:0005524; F:ATP binding; IDA:PomBase.
DR   GO; GO:0044396; P:actin cortical patch organization; IMP:PomBase.
DR   GO; GO:0030041; P:actin filament polymerization; IMP:PomBase.
DR   GO; GO:0034314; P:Arp2/3 complex-mediated actin nucleation; IDA:PomBase.
DR   GO; GO:0006897; P:endocytosis; IC:PomBase.
DR   GO; GO:0000281; P:mitotic cytokinesis; IMP:PomBase.
DR   InterPro; IPR004000; Actin.
DR   InterPro; IPR020902; Actin/actin-like_CS.
DR   InterPro; IPR015623; Arp3.
DR   InterPro; IPR043129; ATPase_NBD.
DR   PANTHER; PTHR11937; PTHR11937; 1.
DR   PANTHER; PTHR11937:SF175; PTHR11937:SF175; 1.
DR   Pfam; PF00022; Actin; 1.
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..427
FT                   /note="Actin-related protein 3"
FT                   /id="PRO_0000089088"
SQ   SEQUENCE   427 AA;  47373 MW;  C7909FFEE544789B CRC64;
     MASFNVPIIM DNGTGYSKLG YAGNDAPSYV FPTVIATRSA GASSGPAVSS KPSYMASKGS
     GHLSSKRATE DLDFFIGNDA LKKASAGYSL DYPIRHGQIE NWDHMERFWQ QSLFKYLRCE
     PEDHYFLLTE PPLNPPENRE NTAEIMFESF NCAGLYIAVQ AVLALAASWT SSKVTDRSLT
     GTVVDSGDGV THIIPVAEGY VIGSSIKTMP LAGRDVTYFV QSLLRDRNEP DSSLKTAERI
     KEECCYVCPD IVKEFSRFDR EPDRYLKYAS ESITGHSTTI DVGFERFLAP EIFFNPEIAS
     SDFLTPLPEL VDNVVQSSPI DVRKGLYKNI VLSGGSTLFK NFGNRLQRDL KRIVDERIHR
     SEMLSGAKSG GVDVNVISHK RQRNAVWFGG SLLAQTPEFG SYCHTKADYE EYGASIARRY
     QIFGNSL