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SPC7_SCHPO
ID   SPC7_SCHPO              Reviewed;        1364 AA.
AC   O59757;
DT   12-JUN-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1998, sequence version 1.
DT   03-AUG-2022, entry version 129.
DE   RecName: Full=Kinetochore protein spc7;
DE   AltName: Full=NMS complex subunit spc7;
GN   Name=spc7; ORFNames=SPCC1020.02;
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   IDENTIFICATION IN THE NMS COMPLEX.
RX   PubMed=16079914; DOI=10.1038/sj.emboj.7600762;
RA   Liu X., McLeod I., Anderson S., Yates J.R. III, He X.;
RT   "Molecular analysis of kinetochore architecture in fission yeast.";
RL   EMBO J. 24:2919-2930(2005).
RN   [3]
RP   IDENTIFICATION IN THE NMS COMPLEX.
RX   PubMed=17035632; DOI=10.1091/mbc.e06-05-0388;
RA   Hayashi A., Asakawa H., Haraguchi T., Hiraoka Y.;
RT   "Reconstruction of the kinetochore during meiosis in fission yeast
RT   Schizosaccharomyces pombe.";
RL   Mol. Biol. Cell 17:5173-5184(2006).
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   INTERACTION WITH SOS7.
RX   PubMed=22711988; DOI=10.1128/mcb.00212-12;
RA   Jakopec V., Topolski B., Fleig U.;
RT   "Sos7, an essential component of the conserved Schizosaccharomyces pombe
RT   Ndc80-MIND-Spc7 complex, identifies a new family of fungal kinetochore
RT   proteins.";
RL   Mol. Cell. Biol. 32:3308-3320(2012).
CC   -!- FUNCTION: Acts as a component of the NMS (Ndc80-MIND-Spc7) super
CC       complex which has a role in kinetochore function during late meiotic
CC       prophase and throughout the mitotic cell cycle.
CC   -!- SUBUNIT: Component of the NMS super complex which consists of mis12,
CC       mis13, mis14, ndc80, nnf1, nuf2, sos7, spc7, spc24 and spc25. Interacts
CC       (via C-terminus) directly with sos7 (via C-terminus).
CC       {ECO:0000269|PubMed:16079914, ECO:0000269|PubMed:17035632,
CC       ECO:0000269|PubMed:22711988}.
CC   -!- INTERACTION:
CC       O59757; Q10113: mal3; NbExp=2; IntAct=EBI-1002205, EBI-1002268;
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:16823372}.
CC       Chromosome, centromere, kinetochore {ECO:0000269|PubMed:16823372}.
CC       Cytoplasm, cytoskeleton, microtubule organizing center, spindle pole
CC       body {ECO:0000269|PubMed:16823372}.
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DR   EMBL; CU329672; CAA18990.1; -; Genomic_DNA.
DR   PIR; T40839; T40839.
DR   RefSeq; NP_587958.1; NM_001022949.2.
DR   AlphaFoldDB; O59757; -.
DR   SMR; O59757; -.
DR   BioGRID; 275727; 47.
DR   DIP; DIP-35340N; -.
DR   IntAct; O59757; 5.
DR   STRING; 4896.SPCC1020.02.1; -.
DR   iPTMnet; O59757; -.
DR   PaxDb; O59757; -.
DR   PRIDE; O59757; -.
DR   EnsemblFungi; SPCC1020.02.1; SPCC1020.02.1:pep; SPCC1020.02.
DR   GeneID; 2539155; -.
DR   KEGG; spo:SPCC1020.02; -.
DR   PomBase; SPCC1020.02; spc7.
DR   VEuPathDB; FungiDB:SPCC1020.02; -.
DR   eggNOG; ENOG502S20P; Eukaryota.
DR   HOGENOM; CLU_256785_0_0_1; -.
DR   InParanoid; O59757; -.
DR   OMA; RSACHEL; -.
DR   PhylomeDB; O59757; -.
DR   PRO; PR:O59757; -.
DR   Proteomes; UP000002485; Chromosome III.
DR   GO; GO:0032153; C:cell division site; HDA:PomBase.
DR   GO; GO:0000779; C:condensed chromosome, centromeric region; IDA:PomBase.
DR   GO; GO:0005829; C:cytosol; HDA:PomBase.
DR   GO; GO:0000939; C:inner kinetochore; IDA:PomBase.
DR   GO; GO:0000776; C:kinetochore; IDA:PomBase.
DR   GO; GO:0031617; C:NMS complex; IDA:PomBase.
DR   GO; GO:0005634; C:nucleus; HDA:PomBase.
DR   GO; GO:0005816; C:spindle pole body; IEA:UniProtKB-SubCell.
DR   GO; GO:0140483; F:kinetochore adaptor activity; IPI:PomBase.
DR   GO; GO:0051010; F:microtubule plus-end binding; TAS:PomBase.
DR   GO; GO:0051315; P:attachment of mitotic spindle microtubules to kinetochore; IMP:PomBase.
DR   GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR   GO; GO:1902426; P:deactivation of mitotic spindle assembly checkpoint; IMP:PomBase.
DR   GO; GO:1990813; P:meiotic centromeric cohesion protection; IMP:PomBase.
DR   GO; GO:1990758; P:mitotic sister chromatid biorientation; IMP:PomBase.
DR   GO; GO:0007094; P:mitotic spindle assembly checkpoint signaling; IMP:PomBase.
DR   GO; GO:0034501; P:protein localization to kinetochore; IBA:GO_Central.
DR   InterPro; IPR033338; Spc105/Spc7.
DR   InterPro; IPR013253; Spc7_domain.
DR   PANTHER; PTHR28260; PTHR28260; 1.
DR   Pfam; PF08317; Spc7; 1.
DR   SMART; SM00787; Spc7; 1.
PE   1: Evidence at protein level;
KW   Cell cycle; Cell division; Centromere; Chromosome; Coiled coil; Cytoplasm;
KW   Cytoskeleton; Kinetochore; Meiosis; Mitosis; Nucleus; Reference proteome.
FT   CHAIN           1..1364
FT                   /note="Kinetochore protein spc7"
FT                   /id="PRO_0000290644"
FT   REGION          1..36
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          124..190
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          202..223
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          289..334
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          456..503
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          564..643
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          697..837
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          1071..1160
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        1..17
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        124..138
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        139..190
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        289..316
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        317..334
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        456..497
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        567..581
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        582..621
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        734..771
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        801..823
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1364 AA;  153593 MW;  829312F81FFB7502 CRC64;
     MPTSPRRNSI ATTDNVIGRN KSRKRPHSLG GPGALQELKE HTNPAKGILK SYSSFSVDPA
     FTGDEDFNDI HTQINNTVIG ISSNVMAASK RLQMEDLQQL SRETSRKSLN RRVSFASHAR
     VRWYPKDHQS DSEKSTSNHS TPERTFASDA KNHSPKGPTT TSFSRNETQS SPHSHSASII
     SDGSDMDIAS PIRSTESDMV SEALNAGHPP PSLYPENDDL SIQNPTKALP EAEKALDVHD
     ATREQVNDRE ETNMDLTIQF QEADSFLSHS ESIKGLSSSE QGTVYSLKAS HDPSNQTQLS
     SPNKSSSPTS IEISDFSKNN ENHDQSENKE EEEDMMLTRP IEIPQHFSPI ARPLTSQEAI
     VDMDITSNNI NLSPVSHFSN GLDLQNLEEA PMNLTRPINA NPHLTNHSPN DLTNGEEEMD
     TTSAFNIENS HLTLLSPIRP SSRSMEEQIM DLTQPISSTN APTHLNEDDL NQFTSNISSS
     SKPRKDNNKT ANSSKPIPDS EDFMDITRPF NILSPSKEAL SEEQPMELTS TVFPCENSTS
     HLEVEEAAMD ETVAFQIRGN NVELPSADKE NAEREEIPSY SDKSENFNTT SFTNHERSPN
     GNNNLKFSKD PNSSSPSRHV VATPTDKLGT RKRRLRYSTS SFDQSTLRRN RLATIRNARK
     SISTLNDREL LPVNFFEKKV NSGLYKSVER SENYRLGATP LTAEKPFTTE KPLSSLPEEV
     SRQPTDDKGE QVSNADVDSG LSKTERLTIQ QTNEIKHVPT NTTSSVKLPQ QPSNEDEKER
     ITTADYADST SLERLESQEP NRNELVQVGS SNAGNTTSVG MNEHEKSPVK LSKGVSNVDT
     SLGASTINTN ILNQDSGPNE EIPVGNEPEF DTMPTLPNVE PISLSDFLKM TGIEFLDNLT
     IAKRRETLLP NAEENKKCSI QELLESFYIQ FPLLELYKFS CQQLQDYIAE GKDFVTKIEE
     ETLKENPLLF YEYRKASSDM RVLMDSQFLM MKTFARLQAK GDWYEWREGL MQGIKHELNL
     NLTGMQRSLT HLMDVANVIH PYAQEIQERY NGSITTVQTL KKQKEFANQY DSTLLAQAQE
     KLEKLKVEVE RRRRLLSEKE ERRKELAIKI EQVTNSCSDL ELRTNAEQDF YAKNQDFEFD
     EIKRYEEQLL NLKNELGWTI VSLTAGGIKL ATNNTALSPY SAEVTVEILR QNFQVNVDIA
     CKFPNESNAC SSNVLEHVAS SFSKWHSKVF SRNLRLLKKY LNDVSICWEQ IVYLVQDFQR
     LWYHWPFLSV ENDDKSIIIN VELYLRSVSS KVKVVFGLPI DTIYQTTEVG KFYASTSVAV
     KQMYAESEGD SYVSEVLNTL SEVVHCTSTY ALSSACLTVW NKYS
 
 
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