CCQ1_SCHPO
ID CCQ1_SCHPO Reviewed; 735 AA.
AC Q10432;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 124.
DE RecName: Full=Coiled-coil quantitatively-enriched protein 1;
DE AltName: Full=Structural maintenance of chromosomes protein ccq1;
DE Short=SMC protein ccq1;
GN Name=ccq1; ORFNames=SPCC188.07;
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 PROTEIN SEQUENCE OF 57-79, FUNCTION, INTERACTION WITH PCP1 AND TAZ1, AND
RP 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 [3]
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 [4]
RP FUNCTION, INTERACTION WITH CLR3, AND SUBCELLULAR LOCATION.
RX PubMed=17289569; DOI=10.1016/j.cell.2006.12.035;
RA Sugiyama T., Cam H.P., Sugiyama R., Noma K., Zofall M., Kobayashi R.,
RA Grewal S.I.S.;
RT "SHREC, an effector complex for heterochromatic transcriptional
RT silencing.";
RL Cell 128:491-504(2007).
RN [5]
RP FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH POT1 AND TPZ1.
RX PubMed=18535244; DOI=10.1126/science.1154819;
RA Miyoshi T., Kanoh J., Saito M., Ishikawa F.;
RT "Fission yeast Pot1-Tpp1 protects telomeres and regulates telomere
RT length.";
RL Science 320:1341-1344(2008).
CC -!- FUNCTION: Component of the meiotic bouquet that facilitates meiotic
CC nuclear reorganization of the telomeres to the centrosome. Links
CC telomeres to the meiotic centrosome component pcp1. Essential for the
CC formation of normal telomere clusters during meiotic prophase. Required
CC for telomere length regulation and chromosome segregation. Required for
CC proper positioning of nucleosomes at heterochromatic loci and for
CC transcriptional gene silencing (TGS) function of the Snf2/Hdac-
CC containing repressor complex (SHREC). {ECO:0000269|PubMed:15546621,
CC ECO:0000269|PubMed:17289569, ECO:0000269|PubMed:18535244}.
CC -!- SUBUNIT: Interacts (during meiosis) with pcp1. Interacts with clr3,
CC pot1, taz1 and tpz1. {ECO:0000269|PubMed:15546621,
CC ECO:0000269|PubMed:17289569, ECO:0000269|PubMed:18535244}.
CC -!- INTERACTION:
CC Q10432; O74804: est1; NbExp=4; IntAct=EBI-15953947, EBI-1556899;
CC Q10432; O14246: tpz1; NbExp=2; IntAct=EBI-15953947, EBI-8802014;
CC -!- SUBCELLULAR LOCATION: Nucleus, nucleoplasm. Chromosome, telomere.
CC Note=Associates with major heterochromatin, sub-telomeres, rDNA and the
CC mat locus.
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DR EMBL; CU329672; CAB41227.1; -; Genomic_DNA.
DR PIR; T41187; T41187.
DR RefSeq; NP_588210.1; NM_001023200.2.
DR PDB; 7CUJ; X-ray; 2.40 A; A/B=123-439.
DR PDBsum; 7CUJ; -.
DR AlphaFoldDB; Q10432; -.
DR SMR; Q10432; -.
DR BioGRID; 275918; 73.
DR DIP; DIP-59444N; -.
DR IntAct; Q10432; 3.
DR STRING; 4896.SPCC188.07.1; -.
DR iPTMnet; Q10432; -.
DR MaxQB; Q10432; -.
DR PaxDb; Q10432; -.
DR PRIDE; Q10432; -.
DR EnsemblFungi; SPCC188.07.1; SPCC188.07.1:pep; SPCC188.07.
DR GeneID; 2539352; -.
DR KEGG; spo:SPCC188.07; -.
DR PomBase; SPCC188.07; ccq1.
DR VEuPathDB; FungiDB:SPCC188.07; -.
DR HOGENOM; CLU_386440_0_0_1; -.
DR InParanoid; Q10432; -.
DR OMA; YFAFCID; -.
DR PRO; PR:Q10432; -.
DR Proteomes; UP000002485; Chromosome III.
DR GO; GO:0099115; C:chromosome, subtelomeric region; IDA:PomBase.
DR GO; GO:0140445; C:chromosome, telomeric repeat region; IDA:PomBase.
DR GO; GO:0005654; C:nucleoplasm; IDA:PomBase.
DR GO; GO:0005634; C:nucleus; HDA:PomBase.
DR GO; GO:0070187; C:shelterin complex; IDA:PomBase.
DR GO; GO:0000782; C:telomere cap complex; IDA:PomBase.
DR GO; GO:0060090; F:molecular adaptor activity; EXP:PomBase.
DR GO; GO:0045132; P:meiotic chromosome segregation; IMP:PomBase.
DR GO; GO:0045141; P:meiotic telomere clustering; IMP:PomBase.
DR GO; GO:0032211; P:negative regulation of telomere maintenance via telomerase; IMP:PomBase.
DR GO; GO:0032212; P:positive regulation of telomere maintenance via telomerase; IMP:PomBase.
DR GO; GO:0016233; P:telomere capping; IGI:PomBase.
DR GO; GO:0000723; P:telomere maintenance; IMP:PomBase.
DR GO; GO:0007004; P:telomere maintenance via telomerase; IMP:PomBase.
DR GO; GO:1905324; P:telomere-telomerase complex assembly; IMP:PomBase.
PE 1: Evidence at protein level;
KW 3D-structure; Chromosome; Chromosome partition; Coiled coil;
KW Direct protein sequencing; Nucleus; Reference proteome; Telomere.
FT CHAIN 1..735
FT /note="Coiled-coil quantitatively-enriched protein 1"
FT /id="PRO_0000116882"
FT COILED 514..719
FT /evidence="ECO:0000255"
FT STRAND 133..138
FT /evidence="ECO:0007829|PDB:7CUJ"
FT HELIX 142..154
FT /evidence="ECO:0007829|PDB:7CUJ"
FT HELIX 156..163
FT /evidence="ECO:0007829|PDB:7CUJ"
FT HELIX 169..187
FT /evidence="ECO:0007829|PDB:7CUJ"
FT HELIX 189..192
FT /evidence="ECO:0007829|PDB:7CUJ"
FT HELIX 219..221
FT /evidence="ECO:0007829|PDB:7CUJ"
FT HELIX 224..234
FT /evidence="ECO:0007829|PDB:7CUJ"
FT TURN 235..239
FT /evidence="ECO:0007829|PDB:7CUJ"
FT STRAND 243..249
FT /evidence="ECO:0007829|PDB:7CUJ"
FT HELIX 251..263
FT /evidence="ECO:0007829|PDB:7CUJ"
FT STRAND 268..270
FT /evidence="ECO:0007829|PDB:7CUJ"
FT STRAND 283..288
FT /evidence="ECO:0007829|PDB:7CUJ"
FT HELIX 289..291
FT /evidence="ECO:0007829|PDB:7CUJ"
FT HELIX 292..295
FT /evidence="ECO:0007829|PDB:7CUJ"
FT HELIX 296..299
FT /evidence="ECO:0007829|PDB:7CUJ"
FT STRAND 305..312
FT /evidence="ECO:0007829|PDB:7CUJ"
FT HELIX 313..322
FT /evidence="ECO:0007829|PDB:7CUJ"
FT STRAND 330..335
FT /evidence="ECO:0007829|PDB:7CUJ"
FT HELIX 339..345
FT /evidence="ECO:0007829|PDB:7CUJ"
FT TURN 346..349
FT /evidence="ECO:0007829|PDB:7CUJ"
FT HELIX 354..365
FT /evidence="ECO:0007829|PDB:7CUJ"
FT HELIX 397..416
FT /evidence="ECO:0007829|PDB:7CUJ"
FT HELIX 421..423
FT /evidence="ECO:0007829|PDB:7CUJ"
FT HELIX 433..435
FT /evidence="ECO:0007829|PDB:7CUJ"
SQ SEQUENCE 735 AA; 83301 MW; 14193682700A2634 CRC64;
MSEINDFTNS IIINESDTKY EVYSEVNSSN RWIAKEDCPS PLEDVWLLKL AGHKRKLEEP
LSCMRNEEPA SKQREIEKFL RTDLDHSEND FLTQEVDEFP STQQLFPIPL QNDTAFDSSE
ESITKSSKSS FSVLDIGLPM SALQRKMMHR LVQYFAFCID HFCTGPSDSR IQEKIRLFIQ
SAHNIAKHPS LYDTEVRNPS AAESTNSHVS LDASNFSSYA ENSSKFLFLQ ELFKNLSPSY
SKTFFLFISN QFLANTLTQW LKSQNIDAEL WAEEDAKTSQ HPAIWICVSK KAPSASHFLQ
SCPDLSATIF YDIEAYMSVT SSLPSIQSLV LRLIHLGSIE HAIKCFQSSY NASFLVNIVG
VVATLSSSSE ENSEASNLST LFEKSGNFEE ILGSESHSSI TEKTRDIAKN VATWLKNGEN
FSSWPLPPLM DLASLSVAEP RDSQPSVSQV NDTFVKSSDS TFPSSQSMQS PSKLHSLTSN
ATDLLSSSSL KKNFFSQQEA DEVELSNNYD LQGAAVQYLQ RRLRMVEDEL HEAINSKNVQ
QSRSEELEQQ ISKLTDNLQE YRNTVRELKL DLEKSKKKNE DLSKLEVEKV EEIANLKKEL
THLAKQQEFG FKYVQEFSNE DLQGKLIEAN EKNYKLTQLL KTQKEDADFI TNQYQNASTF
AAEQSKEVAK LQAECKRLQA INSKVMEEVK VYNDSRVEAL LAKVSSLEET LKILEQKSLP
KFTPHNQSPR IIDSN
