PDS5_YEAST
ID PDS5_YEAST Reviewed; 1277 AA.
AC Q04264; D6VZQ0; Q04780;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 1.
DT 03-AUG-2022, entry version 169.
DE RecName: Full=Sister chromatid cohesion protein PDS5;
DE AltName: Full=Precocious dissociation of sisters protein 5;
GN Name=PDS5; OrderedLocusNames=YMR076C; ORFNames=YM9582.01C, YM9916.15C;
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169872;
RA Bowman S., Churcher C.M., Badcock K., Brown D., Chillingworth T.,
RA Connor R., Dedman K., Devlin K., Gentles S., Hamlin N., Hunt S., Jagels K.,
RA Lye G., Moule S., Odell C., Pearson D., Rajandream M.A., Rice P.,
RA Skelton J., Walsh S.V., Whitehead S., Barrell B.G.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XIII.";
RL Nature 387:90-93(1997).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=24374639; DOI=10.1534/g3.113.008995;
RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [3]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=11062262; DOI=10.1083/jcb.151.3.613;
RA Hartman T., Stead K., Koshland D., Guacci V.;
RT "Pds5p is an essential chromosomal protein required for both sister
RT chromatid cohesion and condensation in Saccharomyces cerevisiae.";
RL J. Cell Biol. 151:613-626(2000).
RN [4]
RP FUNCTION.
RX PubMed=11137006; DOI=10.1016/s0960-9822(00)00854-x;
RA Panizza S., Tanaka T., Hochwagen A., Eisenhaber F., Nasmyth K.;
RT "Pds5 cooperates with cohesin in maintaining sister chromatid cohesion.";
RL Curr. Biol. 10:1557-1564(2000).
RN [5]
RP ACETYLATION.
RX PubMed=11864574; DOI=10.1016/s0960-9822(02)00681-4;
RA Ivanov D., Schleiffer A., Eisenhaber F., Mechtler K., Haering C.H.,
RA Nasmyth K.;
RT "Eco1 is a novel acetyltransferase that can acetylate proteins involved in
RT cohesion.";
RL Curr. Biol. 12:323-328(2002).
RN [6]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=14562095; DOI=10.1038/nature02026;
RA Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W.,
RA Weissman J.S., O'Shea E.K.;
RT "Global analysis of protein localization in budding yeast.";
RL Nature 425:686-691(2003).
RN [7]
RP LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX PubMed=14562106; DOI=10.1038/nature02046;
RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA O'Shea E.K., Weissman J.S.;
RT "Global analysis of protein expression in yeast.";
RL Nature 425:737-741(2003).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1231 AND SER-1233, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=18407956; DOI=10.1074/mcp.m700468-mcp200;
RA Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
RT "A multidimensional chromatography technology for in-depth phosphoproteome
RT analysis.";
RL Mol. Cell. Proteomics 7:1389-1396(2008).
CC -!- FUNCTION: Essential for the establishment and maintenance of sister
CC chromatid cohesion at centromere proximal and distal regions during S
CC phase. Also required for chromosomal condensation.
CC {ECO:0000269|PubMed:11062262, ECO:0000269|PubMed:11137006}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:11062262,
CC ECO:0000269|PubMed:14562095}.
CC -!- PTM: Acetylated by ECO1. {ECO:0000269|PubMed:11864574}.
CC -!- MISCELLANEOUS: Present with 7720 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the PDS5 family. {ECO:0000305}.
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DR EMBL; Z49259; CAA89222.1; -; Genomic_DNA.
DR EMBL; Z48952; CAA88801.1; -; Genomic_DNA.
DR EMBL; BK006946; DAA09974.1; -; Genomic_DNA.
DR PIR; S54451; S54451.
DR RefSeq; NP_013793.1; NM_001182575.1.
DR PDB; 5FRP; X-ray; 2.90 A; A/B=1-701.
DR PDB; 5FRR; X-ray; 5.80 A; A/B=1-701.
DR PDB; 5FRS; X-ray; 4.07 A; A=1-701.
DR PDBsum; 5FRP; -.
DR PDBsum; 5FRR; -.
DR PDBsum; 5FRS; -.
DR AlphaFoldDB; Q04264; -.
DR SMR; Q04264; -.
DR BioGRID; 35251; 392.
DR DIP; DIP-6799N; -.
DR IntAct; Q04264; 13.
DR MINT; Q04264; -.
DR STRING; 4932.YMR076C; -.
DR iPTMnet; Q04264; -.
DR MaxQB; Q04264; -.
DR PaxDb; Q04264; -.
DR PRIDE; Q04264; -.
DR EnsemblFungi; YMR076C_mRNA; YMR076C; YMR076C.
DR GeneID; 855099; -.
DR KEGG; sce:YMR076C; -.
DR SGD; S000004681; PDS5.
DR VEuPathDB; FungiDB:YMR076C; -.
DR eggNOG; KOG1525; Eukaryota.
DR GeneTree; ENSGT00940000168106; -.
DR HOGENOM; CLU_002562_1_0_1; -.
DR InParanoid; Q04264; -.
DR OMA; CFDIVSG; -.
DR BioCyc; YEAST:G3O-32778-MON; -.
DR Reactome; R-SCE-2468052; Establishment of Sister Chromatid Cohesion.
DR Reactome; R-SCE-2500257; Resolution of Sister Chromatid Cohesion.
DR PRO; PR:Q04264; -.
DR Proteomes; UP000002311; Chromosome XIII.
DR RNAct; Q04264; protein.
DR GO; GO:0000785; C:chromatin; IBA:GO_Central.
DR GO; GO:0000794; C:condensed nuclear chromosome; IDA:SGD.
DR GO; GO:0005829; C:cytosol; IDA:SGD.
DR GO; GO:0035808; C:meiotic recombination initiation complex; IDA:SGD.
DR GO; GO:0005634; C:nucleus; IDA:SGD.
DR GO; GO:0005198; F:structural molecule activity; IMP:SGD.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0140588; P:chromatin looping; IMP:SGD.
DR GO; GO:0006281; P:DNA repair; IBA:GO_Central.
DR GO; GO:0006302; P:double-strand break repair; IMP:SGD.
DR GO; GO:0007129; P:homologous chromosome pairing at meiosis; IMP:SGD.
DR GO; GO:0051321; P:meiotic cell cycle; IMP:SGD.
DR GO; GO:0042138; P:meiotic DNA double-strand break formation; IMP:SGD.
DR GO; GO:0007076; P:mitotic chromosome condensation; IMP:SGD.
DR GO; GO:0007064; P:mitotic sister chromatid cohesion; IMP:SGD.
DR Gene3D; 1.25.10.10; -; 1.
DR InterPro; IPR011989; ARM-like.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR032682; Cnd1_C.
DR InterPro; IPR039776; Pds5.
DR PANTHER; PTHR12663; PTHR12663; 1.
DR Pfam; PF12717; Cnd1; 1.
DR SUPFAM; SSF48371; SSF48371; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Cell cycle; Cell division; Mitosis; Nucleus;
KW Phosphoprotein; Reference proteome.
FT CHAIN 1..1277
FT /note="Sister chromatid cohesion protein PDS5"
FT /id="PRO_0000058280"
FT REPEAT 393..429
FT /note="HEAT"
FT REGION 1201..1277
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1234..1267
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 1231
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956"
FT MOD_RES 1233
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956"
FT STRAND 19..21
FT /evidence="ECO:0007829|PDB:5FRP"
FT HELIX 25..41
FT /evidence="ECO:0007829|PDB:5FRP"
FT STRAND 44..47
FT /evidence="ECO:0007829|PDB:5FRP"
FT HELIX 53..58
FT /evidence="ECO:0007829|PDB:5FRP"
FT HELIX 62..65
FT /evidence="ECO:0007829|PDB:5FRP"
FT HELIX 70..87
FT /evidence="ECO:0007829|PDB:5FRP"
FT HELIX 95..113
FT /evidence="ECO:0007829|PDB:5FRP"
FT HELIX 120..132
FT /evidence="ECO:0007829|PDB:5FRP"
FT HELIX 136..141
FT /evidence="ECO:0007829|PDB:5FRP"
FT HELIX 145..157
FT /evidence="ECO:0007829|PDB:5FRP"
FT HELIX 165..167
FT /evidence="ECO:0007829|PDB:5FRP"
FT HELIX 168..180
FT /evidence="ECO:0007829|PDB:5FRP"
FT HELIX 187..199
FT /evidence="ECO:0007829|PDB:5FRP"
FT HELIX 215..226
FT /evidence="ECO:0007829|PDB:5FRP"
FT HELIX 228..247
FT /evidence="ECO:0007829|PDB:5FRP"
FT HELIX 254..272
FT /evidence="ECO:0007829|PDB:5FRP"
FT HELIX 274..279
FT /evidence="ECO:0007829|PDB:5FRP"
FT HELIX 281..288
FT /evidence="ECO:0007829|PDB:5FRP"
FT HELIX 293..306
FT /evidence="ECO:0007829|PDB:5FRP"
FT HELIX 315..318
FT /evidence="ECO:0007829|PDB:5FRP"
FT HELIX 320..327
FT /evidence="ECO:0007829|PDB:5FRP"
FT HELIX 328..331
FT /evidence="ECO:0007829|PDB:5FRP"
FT HELIX 335..343
FT /evidence="ECO:0007829|PDB:5FRP"
FT HELIX 345..351
FT /evidence="ECO:0007829|PDB:5FRP"
FT HELIX 358..366
FT /evidence="ECO:0007829|PDB:5FRP"
FT HELIX 372..384
FT /evidence="ECO:0007829|PDB:5FRP"
FT HELIX 387..393
FT /evidence="ECO:0007829|PDB:5FRP"
FT HELIX 397..405
FT /evidence="ECO:0007829|PDB:5FRP"
FT HELIX 406..408
FT /evidence="ECO:0007829|PDB:5FRP"
FT HELIX 412..431
FT /evidence="ECO:0007829|PDB:5FRP"
FT STRAND 437..439
FT /evidence="ECO:0007829|PDB:5FRP"
FT HELIX 440..446
FT /evidence="ECO:0007829|PDB:5FRP"
FT HELIX 449..455
FT /evidence="ECO:0007829|PDB:5FRP"
FT HELIX 456..459
FT /evidence="ECO:0007829|PDB:5FRP"
FT HELIX 462..475
FT /evidence="ECO:0007829|PDB:5FRP"
FT HELIX 483..495
FT /evidence="ECO:0007829|PDB:5FRP"
FT HELIX 499..526
FT /evidence="ECO:0007829|PDB:5FRP"
FT HELIX 527..529
FT /evidence="ECO:0007829|PDB:5FRP"
FT TURN 530..532
FT /evidence="ECO:0007829|PDB:5FRP"
FT STRAND 535..539
FT /evidence="ECO:0007829|PDB:5FRP"
FT HELIX 540..555
FT /evidence="ECO:0007829|PDB:5FRP"
FT HELIX 561..574
FT /evidence="ECO:0007829|PDB:5FRP"
FT HELIX 577..587
FT /evidence="ECO:0007829|PDB:5FRP"
FT HELIX 593..607
FT /evidence="ECO:0007829|PDB:5FRP"
FT HELIX 626..640
FT /evidence="ECO:0007829|PDB:5FRP"
FT STRAND 643..646
FT /evidence="ECO:0007829|PDB:5FRP"
FT HELIX 648..653
FT /evidence="ECO:0007829|PDB:5FRP"
FT HELIX 662..678
FT /evidence="ECO:0007829|PDB:5FRP"
FT TURN 680..682
FT /evidence="ECO:0007829|PDB:5FRP"
FT HELIX 683..690
FT /evidence="ECO:0007829|PDB:5FRP"
FT HELIX 692..696
FT /evidence="ECO:0007829|PDB:5FRP"
SQ SEQUENCE 1277 AA; 147041 MW; 9DF40A5274FD9623 CRC64;
MAKGAVTKLK FNSPIISTSD QLISTNELLD RLKALHEELA SLDQDNTDLT GLDKYRDALV
SRKLLKHKDV GIRAFTACCL SDILRLYAPD APYTDAQLTD IFKLVLSQFE QLGDQENGYH
IQQTYLITKL LEYRSIVLLA DLPSSNNLLI ELFHIFYDPN KSFPARLFNV IGGILGEVIS
EFDSVPLEVL RLIFNKFLTY NPNEIPEGLN VTSDCGYEVS LILCDTYSNR MSRHLTKYYS
EIIHEATNDD NNSRLLTVVV KLHKLVLRLW ETVPELINAV IGFIYHELSS ENELFRKEAT
KLIGQILTSY SDLNFVSTHS DTFKAWISKI ADISPDVRVE WTESIPQIIA TREDISKELN
QALAKTFIDS DPRVRRTSVM IFNKVPVTEI WKNITNKAIY TSLLHLAREK HKEVRELCIN
TMAKFYSNSL NEIERTYQNK EIWEIIDTIP STLYNLYYIN DLNINEQVDS VIFEYLLPFE
PDNDKRVHRL LTVLSHFDKK AFTSFFAFNA RQIKISFAIS KYIDFSKFLN NQESMSSSQG
PIVMNKYNQT LQWLASGLSD STKAIDALET IKQFNDERIF YLLNACVTND IPFLTFKNCY
NELVSKLQTP GLFKKYNIST GASIMPRDIA KVIQILLFRA SPIIYNVSNI SVLLNLSNNS
DAKQLDLKRR ILDDISKVNP TLFKDQIRTL KTIIKDLDDP DAEKNDNLSL EEALKTLYKA
SKTLKDQVDF DDTFFFTKLY DFAVESKPEI TKYATKLIAL SPKAEETLKK IKIRILPLDL
QKDKYFTSHI IVLMEIFKKF PHVLNDDSTD IISYLIKEVL LSNQVVGDSK KEIDWVEDSL
LSDTKYSAIG NKVFTLKLFT NKLRSIAPDV PRDELAESFT EKTMKLFFYL IASGGELISE
FNKEFYPTPS NYQTKLRCVA GIQVLKLARI SNLNNFIKPS DIIKLINLVE DESLPVRKTF
LEQLKDYVAN ELISIKFLPL VFFTAYEPDV ELKTTTKIWI NFTFGLKSFK KGTIFERALP
RLIHAIAHHP DIVGGLDSEG DAYLNALTTA IDYLLFYFDS IAAQENFSLL YYLSERVKNY
QDKLVEDEID EEEGPQKEEA PKKHRPYGQK MYIIGELSQM ILLNLKEKKN WQHSAYPGKL
NLPSDLFKPF ATVQEAQLSF KTYIPESLTE KIQNNIKAKI GRILHTSQTQ RQRLQKRLLA
HENNESQKKK KKVHHARSQA DDEEGDGDRE SDSDDDSYSP SNKNETKKGH ENIVMKKLRV
RKEVDYKDDE DDDIEMT
