ID   ARP1_SCHPO              Reviewed;         379 AA.
AC   O94630;
DT   13-NOV-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1999, sequence version 1.
DT   03-AUG-2022, entry version 107.
DE   RecName: Full=Centractin;
DE   AltName: Full=Actin-like protein;
DE   AltName: Full=Actin-related protein 1;
GN   Name=arp1; ORFNames=SPBC1347.12;
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   SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX   PubMed=16823372; DOI=10.1038/nbt1222;
RA   Matsuyama A., Arai R., Yashiroda Y., Shirai A., Kamata A., Sekido S.,
RA   Kobayashi Y., Hashimoto A., Hamamoto M., Hiraoka Y., Horinouchi S.,
RA   Yoshida M.;
RT   "ORFeome cloning and global analysis of protein localization in the fission
RT   yeast Schizosaccharomyces pombe.";
RL   Nat. Biotechnol. 24:841-847(2006).
CC   -!- FUNCTION: Core component of the dynactin complex which assists
CC       cytoplasmic dynein by increasing its processivity and by regulation of
CC       its cargo binding. The dynactin complex is required for the spindle
CC       translocation late in anaphase and is involved in a cell wall synthesis
CC       checkpoint. Arp1 forms the backbone filament of the dynactin rod
CC       structure and serves as the scaffold for the remaining subunits.
CC       Required for proper orientation of the mitotic spindle (By similarity).
CC       {ECO:0000250}.
CC   -!- SUBUNIT: Self-associates to form an actin-like filament of 8-10
CC       monomers. Component of the dynactin complex. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton
CC       {ECO:0000269|PubMed:16823372}.
CC   -!- SIMILARITY: Belongs to the actin family. ARP1 subfamily. {ECO:0000305}.
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DR   EMBL; CU329671; CAB37443.1; -; Genomic_DNA.
DR   PIR; T39400; T39400.
DR   RefSeq; NP_596704.1; NM_001022628.2.
DR   AlphaFoldDB; O94630; -.
DR   SMR; O94630; -.
DR   BioGRID; 276231; 8.
DR   STRING; 4896.SPBC1347.12.1; -.
DR   PaxDb; O94630; -.
DR   PRIDE; O94630; -.
DR   EnsemblFungi; SPBC1347.12.1; SPBC1347.12.1:pep; SPBC1347.12.
DR   GeneID; 2539676; -.
DR   KEGG; spo:SPBC1347.12; -.
DR   PomBase; SPBC1347.12; arp1.
DR   VEuPathDB; FungiDB:SPBC1347.12; -.
DR   eggNOG; KOG0676; Eukaryota.
DR   HOGENOM; CLU_027965_0_2_1; -.
DR   InParanoid; O94630; -.
DR   OMA; CIHSRFM; -.
DR   PhylomeDB; O94630; -.
DR   Reactome; R-SPO-6798695; Neutrophil degranulation.
DR   PRO; PR:O94630; -.
DR   Proteomes; UP000002485; Chromosome II.
DR   GO; GO:0051285; C:cell cortex of cell tip; IPI:PomBase.
DR   GO; GO:0005829; C:cytosol; HDA:PomBase.
DR   GO; GO:0005869; C:dynactin complex; IPI:PomBase.
DR   GO; GO:0030286; C:dynein complex; IEA:UniProtKB-KW.
DR   GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
DR   GO; GO:0030989; P:dynein-driven meiotic oscillatory nuclear movement; IMP:PomBase.
DR   InterPro; IPR004000; Actin.
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.
PE   3: Inferred from homology;
KW   Cytoplasm; Cytoskeleton; Dynein; Microtubule; Reference proteome.
FT   CHAIN           1..379
FT                   /note="Centractin"
FT                   /id="PRO_0000310306"
SQ   SEQUENCE   379 AA;  42793 MW;  99AEF47CF8491D37 CRC64;
     MTVTEIFDNQ PICIDNGSGF IKAGFAGDDI PKCLFPTCVG RIKHERVMPS SIQKDMFVGS
     EAQNLRGLLK IQRPIERGII QNWSDMEEIW SYIYSDQQLN TLPEEHPLLL TEPPLANIRN
     KEKIAEYFYE TLNVPALSFS LQPVLALYAS ARTTGIVLEC GDGLTHSVPI YDGFSIPSAI
     QQEEIGGRDV TDYLQLQLRK SGHELVSSAE KEIVREIKEK CCYVASDFRS EIESWTEHKP
     QIHTYQLPDN QTITLGTECF SAPEVLFNPE MMGSEASGLH IQLFKSILLS DIDLRSTLYS
     NIVLSGGSTL LRGFGERFIS ELRAISGKKN QVKIYASPER MHNAWLGGSI LASLSTFRRL
     LITSEEYKND QNVIFRRRF