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PDS5_SCHPO
ID   PDS5_SCHPO              Reviewed;        1205 AA.
AC   Q9HFF5; O94237;
DT   23-MAY-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2001, sequence version 1.
DT   03-AUG-2022, entry version 133.
DE   RecName: Full=Sister chromatid cohesion protein pds5;
DE   AltName: Full=Precocious dissociation of sisters protein 5;
GN   Name=pds5; ORFNames=SPAC110.02;
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 [MRNA], FUNCTION, INTERACTION WITH ESO1, AND
RP   SUBCELLULAR LOCATION.
RC   STRAIN=972 / ATCC 24843;
RX   PubMed=11598020; DOI=10.1093/emboj/20.20.5779;
RA   Tanaka K., Hao Z., Kai M., Okayama H.;
RT   "Establishment and maintenance of sister chromatid cohesion in fission
RT   yeast by a unique mechanism.";
RL   EMBO J. 20:5779-5790(2001).
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   NUCLEOTIDE SEQUENCE [MRNA] OF 816-1205.
RA   Lee M., Yoo H.S., Chung K.S.;
RL   Submitted (FEB-1998) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   FUNCTION.
RX   PubMed=11861765; DOI=10.1242/jcs.115.3.587;
RA   Wang S.-W., Read R.L., Norbury C.J.;
RT   "Fission yeast Pds5 is required for accurate chromosome segregation and for
RT   survival after DNA damage or metaphase arrest.";
RL   J. Cell Sci. 115:587-598(2002).
RN   [5]
RP   SUBCELLULAR LOCATION, AND INTERACTION WITH HRK1.
RX   PubMed=20929775; DOI=10.1126/science.1194498;
RA   Yamagishi Y., Honda T., Tanno Y., Watanabe Y.;
RT   "Two histone marks establish the inner centromere and chromosome bi-
RT   orientation.";
RL   Science 330:239-243(2010).
CC   -!- FUNCTION: Required for the establishment and maintenance of sister
CC       chromatid cohesion during S phase. Prevents their formation until eso1
CC       is present. May also have a role during meiosis.
CC       {ECO:0000269|PubMed:11598020, ECO:0000269|PubMed:11861765}.
CC   -!- SUBUNIT: Interacts with eso1 and hrk1. {ECO:0000269|PubMed:11598020,
CC       ECO:0000269|PubMed:20929775}.
CC   -!- SUBCELLULAR LOCATION: Nucleus. Chromosome, centromere. Note=Localized
CC       to chromatin throughout the cell cycle.
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DR   EMBL; AB067651; BAB71784.1; -; mRNA.
DR   EMBL; CU329670; CAC08560.1; -; Genomic_DNA.
DR   EMBL; AF049529; AAD02493.1; -; mRNA.
DR   PIR; T43647; T43647.
DR   RefSeq; NP_593535.1; NM_001018969.2.
DR   AlphaFoldDB; Q9HFF5; -.
DR   SMR; Q9HFF5; -.
DR   BioGRID; 278124; 120.
DR   IntAct; Q9HFF5; 2.
DR   STRING; 4896.SPAC110.02.1; -.
DR   MaxQB; Q9HFF5; -.
DR   PaxDb; Q9HFF5; -.
DR   PRIDE; Q9HFF5; -.
DR   EnsemblFungi; SPAC110.02.1; SPAC110.02.1:pep; SPAC110.02.
DR   GeneID; 2541628; -.
DR   KEGG; spo:SPAC110.02; -.
DR   PomBase; SPAC110.02; pds5.
DR   VEuPathDB; FungiDB:SPAC110.02; -.
DR   eggNOG; KOG1525; Eukaryota.
DR   HOGENOM; CLU_002562_1_0_1; -.
DR   InParanoid; Q9HFF5; -.
DR   OMA; CFDIVSG; -.
DR   PhylomeDB; Q9HFF5; -.
DR   Reactome; R-SPO-2470946; Cohesin Loading onto Chromatin.
DR   Reactome; R-SPO-2500257; Resolution of Sister Chromatid Cohesion.
DR   PRO; PR:Q9HFF5; -.
DR   Proteomes; UP000002485; Chromosome I.
DR   GO; GO:0000785; C:chromatin; IBA:GO_Central.
DR   GO; GO:0099115; C:chromosome, subtelomeric region; IDA:PomBase.
DR   GO; GO:0031934; C:mating-type region heterochromatin; IDA:PomBase.
DR   GO; GO:0000228; C:nuclear chromosome; IDA:PomBase.
DR   GO; GO:0005634; C:nucleus; IDA:PomBase.
DR   GO; GO:0005721; C:pericentric heterochromatin; IDA:PomBase.
DR   GO; GO:0090695; C:Wpl/Pds5 cohesin loading/unloading complex; EXP:PomBase.
DR   GO; GO:0003677; F:DNA binding; IDA:PomBase.
DR   GO; GO:0051456; P:attachment of spindle microtubules to kinetochore involved in meiotic sister chromatid segregation; IMP:PomBase.
DR   GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR   GO; GO:0006281; P:DNA repair; IBA:GO_Central.
DR   GO; GO:0061780; P:mitotic cohesin loading; IMP:PomBase.
DR   GO; GO:0061781; P:mitotic cohesin unloading; IDA:PomBase.
DR   GO; GO:0007064; P:mitotic sister chromatid cohesion; IMP:PomBase.
DR   GO; GO:1902682; P:protein localization to pericentric heterochromatin; IMP:PomBase.
DR   Gene3D; 1.25.10.10; -; 1.
DR   InterPro; IPR011989; ARM-like.
DR   InterPro; IPR016024; ARM-type_fold.
DR   InterPro; IPR039776; Pds5.
DR   PANTHER; PTHR12663; PTHR12663; 1.
DR   SUPFAM; SSF48371; SSF48371; 1.
PE   1: Evidence at protein level;
KW   Cell cycle; Cell division; Centromere; Chromosome; Mitosis; Nucleus;
KW   Reference proteome.
FT   CHAIN           1..1205
FT                   /note="Sister chromatid cohesion protein pds5"
FT                   /id="PRO_0000058279"
FT   REGION          1111..1205
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1123..1149
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1156..1183
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1184..1205
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CONFLICT        816..818
FT                   /note="TMC -> GTS (in Ref. 3)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        902..908
FT                   /note="QISLLCQ -> SNLLIMP (in Ref. 3; AAD02493)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   1205 AA;  138875 MW;  935DABDE0A5E30FF CRC64;
     MIKLQFQRNI VPTHDNPLTT SEILKRLRDL LGELTSLSQD TIDRDSVLPV ARSLVNNNLL
     HHKDKGIRSY TLCCIVELLR LCAPDAPFTL SQLEDIFQVI LKILSGLMNQ ESTYYPQIYE
     ILESLSNVKS AVLIVDLPNA EEFLVNIFRL FFDLARKGTT KNVEFYMLDI INQLINEINT
     IPAAALNILF AQLISGKGVR QTIGSSDSTN HGPAFQLARN IFHDSADRLQ RYVCQYFSDI
     IFDSRDSLSD SMTTPEFIFS HNLVLQLWKY APTTLLNIIP QFENELQAEQ TSVRLVAIET
     VGLMLQDNAI WSDYPRVWSA FCGRLNDKSV ACRIKCIEVA SNALQNSLAT SEIIENVVQM
     LQSKLADTDE KVRVATLKTI EQLTFETFKM QFSVQALKLM GDRLRDRKLN VRLQAIRTLS
     QIYNRAYQDL IDGVEYSIQM FSWIPSSLLE VFYVNDETTN AAVEICMAEL VLQYLSSDTQ
     TRLNRLFLSI KYFSEKAMRV FILLLQRQVK YSELLNYYIE CCKNYNGGVM DNDEESITNK
     LKKVIDIISS KSSNPTLTEA TFRKFAELND RQSYKMLLQT FSIKSEYQVV LKSIKYLFKR
     VSETLSTASL ECFRIFVYRS ALFAFNKSNV HEIIQLLNEP VKYHNFLKPS EALLQHLPLI
     HPNIYGEVVI EVENIIVSSG IESDPKVIKA LSQFSKRKKN FSIQTTTAEI LRKLCLHGTQ
     EQAKQAATII AITETKEFKL DMITNIVENL EYNGGLPVRL MTLGQLFLYT LEEVEKVADQ
     VTEFLVKKVI QRFPEKYDDT HNDEEWCTYE KLDNLTMCKV LAIRVLVNRL RAAAGGTEAL
     NIGAPIIKLL KVLLMADGEL SPFKNTPKIS RAYLRLTASK YFLKLCSIPF YAEHIDFSSY
     VQISLLCQDE NFDVRNLFLT KLQKQLQLKK LPISYYPLLF LTAVDPEEEI KTKASIWIRS
     QVAFFQKTHD FTMEYVATYL IHLLSHHPDI SSIESENSLD FIAYIRFYVD TVVNSENVPI
     VFHLMQRIKQ SYDVIEDGNN YIYVLSDMAQ KILQVKSQNF GWSLTTYPKQ IKLPYEILRP
     IPSIDEKKRI FNKIFITPKM ESQIEHAIRT PVSSFAKQTT NKHANLKQKK THSSKSDKKS
     SRRRKNEKRR KLNEQNPNIR NVPERSSSRF QGIRINYSEA PSSSEEISEE EEEISEEDFD
     EIEDL
 
 
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