ID   PCP1_SCHPO              Reviewed;        1208 AA.
AC   Q92351;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1997, sequence version 1.
DT   25-MAY-2022, entry version 142.
DE   RecName: Full=Spindle pole body protein pcp1;
GN   Name=pcp1; ORFNames=SPAC6G9.06c;
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, AND SUBCELLULAR LOCATION.
RX   PubMed=11864908;
RA   Flory M.R., Morphew M., Joseph J.D., Means A.R., Davis T.N.;
RT   "Pcp1p, a Spc110p-related calmodulin target at the centrosome of the
RT   fission yeast Schizosaccharomyces pombe.";
RL   Cell Growth Differ. 13:47-58(2002).
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   INTERACTION WITH CCQ1, AND SUBCELLULAR LOCATION.
RX   PubMed=15546621; DOI=10.1016/j.molcel.2004.10.027;
RA   Flory M.R., Carson A.R., Muller E.G., Aebersold R.;
RT   "An SMC-domain protein in fission yeast links telomeres to the meiotic
RT   centrosome.";
RL   Mol. Cell 16:619-630(2004).
RN   [4]
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).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-906, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY.
RX   PubMed=18257517; DOI=10.1021/pr7006335;
RA   Wilson-Grady J.T., Villen J., Gygi S.P.;
RT   "Phosphoproteome analysis of fission yeast.";
RL   J. Proteome Res. 7:1088-1097(2008).
CC   -!- FUNCTION: Spindle pole body component that binds calmodulin.
CC       Overexpression of pcp1 causes the formation of supernumerary SPB-like
CC       structures and disrupts both mitotic spindle assembly and chromosome
CC       segregation. {ECO:0000269|PubMed:11864908}.
CC   -!- SUBUNIT: Interacts with ccq1. {ECO:0000269|PubMed:15546621}.
CC   -!- INTERACTION:
CC       Q92351; Q9URY2: alp7; NbExp=3; IntAct=EBI-7633620, EBI-1556697;
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:11864908}. Cytoplasm,
CC       cytoskeleton, microtubule organizing center, spindle pole body
CC       {ECO:0000269|PubMed:11864908, ECO:0000269|PubMed:15546621,
CC       ECO:0000269|PubMed:16823372}.
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DR   EMBL; CU329670; CAB03608.1; -; Genomic_DNA.
DR   EMBL; AF348506; AAK31344.1; -; Genomic_DNA.
DR   PIR; T39068; T39068.
DR   RefSeq; NP_594115.1; NM_001019539.2.
DR   AlphaFoldDB; Q92351; -.
DR   SMR; Q92351; -.
DR   BioGRID; 277958; 16.
DR   IntAct; Q92351; 4.
DR   MINT; Q92351; -.
DR   STRING; 4896.SPAC6G9.06c.1; -.
DR   iPTMnet; Q92351; -.
DR   MaxQB; Q92351; -.
DR   PaxDb; Q92351; -.
DR   PRIDE; Q92351; -.
DR   EnsemblFungi; SPAC6G9.06c.1; SPAC6G9.06c.1:pep; SPAC6G9.06c.
DR   GeneID; 2541455; -.
DR   KEGG; spo:SPAC6G9.06c; -.
DR   PomBase; SPAC6G9.06c; pcp1.
DR   VEuPathDB; FungiDB:SPAC6G9.06c; -.
DR   eggNOG; ENOG502R0AV; Eukaryota.
DR   HOGENOM; CLU_278102_0_0_1; -.
DR   InParanoid; Q92351; -.
DR   OMA; KNEFTPM; -.
DR   PhylomeDB; Q92351; -.
DR   PRO; PR:Q92351; -.
DR   Proteomes; UP000002485; Chromosome I.
DR   GO; GO:0061493; C:central plaque of mitotic spindle pole body; IDA:PomBase.
DR   GO; GO:0005737; C:cytoplasm; IDA:PomBase.
DR   GO; GO:0035974; C:meiotic spindle pole body; IDA:PomBase.
DR   GO; GO:0044732; C:mitotic spindle pole body; IDA:PomBase.
DR   GO; GO:0071958; C:new mitotic spindle pole body; IDA:PomBase.
DR   GO; GO:0110092; C:nucleus leading edge; IDA:PomBase.
DR   GO; GO:0005516; F:calmodulin binding; IEA:UniProtKB-KW.
DR   GO; GO:0140475; F:spindle pole body anchor activity; IPI:PomBase.
DR   GO; GO:0061804; P:mitotic spindle formation (spindle phase one); IMP:PomBase.
DR   InterPro; IPR012943; Cnn_1N.
DR   InterPro; IPR019528; PACT_domain.
DR   Pfam; PF07989; Cnn_1N; 1.
DR   Pfam; PF10495; PACT_coil_coil; 1.
PE   1: Evidence at protein level;
KW   Calmodulin-binding; Coiled coil; Cytoplasm; Cytoskeleton; Nucleus;
KW   Phosphoprotein; Reference proteome.
FT   CHAIN           1..1208
FT                   /note="Spindle pole body protein pcp1"
FT                   /id="PRO_0000058259"
FT   REGION          1..91
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          151..375
FT                   /evidence="ECO:0000255"
FT   COILED          387..803
FT                   /evidence="ECO:0000255"
FT   COILED          874..1091
FT                   /evidence="ECO:0000255"
FT   COILED          1177..1204
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        12..87
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         906
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000269|PubMed:18257517"
SQ   SEQUENCE   1208 AA;  140764 MW;  70264159ADD42424 CRC64;
     MSERDFNTQS PKFKDENANS VISQSDFLGK SLKNNNDDYS DFRGSYLNDK SSFQTPLRNG
     SYQPKGSLEF TPLLQSSNKN SDKYNGSLGD KGSFDPNSYG LSAISKQATQ EALSISQGND
     SYDVSKLTDL SKNSEIDHTD GELPANAALT LREQEKVLEK VSRENFGLRI KIVCLEKRLE
     SMAPEQIKEA VKDNVELHAE RANLQLQLKR TESLLQKSED KNFKLEEKVD YLSKVNDVEQ
     SQNVKVFTER IRFLENALEK VQREKDSLST EMEEDKSNKE VDYEYEIRQL QNRLDELSEE
     LDVAQDLLTE KEDEIATLKR QIEEKENSSS AFENEENSSY VHLQEDYAIL QAKCDEFADR
     IQVLTADLEK EKENQIMHES EASIGLTDSM QVHTLQEQLH KANEEIEFLH DQISRMNEEG
     KNFEDIMLQF RSLEEERDVL ESKLQTLEDD NNSLRLMTSS LGNQIESLRT QNREIDEEKN
     HLRLLASKNS DKALAETNIR LQEVTKELET LRMKNSNDLN EIHDLREENE GLTLKIDSIT
     KEKDRLINEL EQRIKSYEVN VSELNGTIDE YRNKLKDKEE TYNEVMNAFQ YKDNDLRRFH
     ESINKLQDRE KELTSNLEKK NLVISSLRET VAMLEKERES IKKYLSGNAK DLDNTNLMEI
     LNDKISVLQR QLTDVKDELD VSEEEREEAI VAGQKLSASF ELMSNEKQAL ELKYSSLKNE
     LINAQNLLDR REEELSELSK KLFEERKIRS GSNDDIEKNK EINVLNSELA DKLAQIRHLE
     SDKMELDKLV HHLNRGIEEA NIEENAVKKR LCLLMGCDYS SVSILQIVSQ IEHFVNQQIQ
     TIRSLKQELR HDFVQFSGKK EQELSRSFEK FGLGTETKHD ILAQRNRNVS EKMNDLENAA
     QKFFSSPDRK NGYLYPSEHT SKIEYLEKTI EDLKLALQDE LKNRNLLMDD ISSYNKQTTK
     LQEKIKWLER ERSILIDELE SYRSNQFNYQ NNLVQDKNEL EERLKEIQKE LEVYNNHFMK
     QAELMTSNVT DESQLMLKTL REALQSKTNN IDHLSTILER NRKEYKSLLD DYNQLRARYK
     NLQSNTPQST QSGQYESEIK GLSKLTKYLQ SKCRREHSLR LDLAFSKKFI LMQLTGYETC
     NKINLRMLQK IGISPDPDLS KKHIKLKSLI IVVCSIERMK RMKNEWLKQA QLKQSLQRAA
     AKAKTANY