PDS5A_RAT
ID PDS5A_RAT Reviewed; 1333 AA.
AC A4L9P7;
DT 24-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2007, sequence version 1.
DT 03-AUG-2022, entry version 93.
DE RecName: Full=Sister chromatid cohesion protein PDS5 homolog A;
GN Name=Pds5a;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1] {ECO:0000312|EMBL:ABO47655.1}
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Pheochromocytoma;
RA Hagemann C., Stojic J., Weigelin B., Gerngras S., Roosen K., Vince G.H.;
RL Submitted (FEB-2007) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1174, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
CC -!- FUNCTION: Probable regulator of sister chromatid cohesion in mitosis
CC which may stabilize cohesin complex association with chromatin. May
CC couple sister chromatid cohesion during mitosis to DNA replication.
CC Cohesion ensures that chromosome partitioning is accurate in both
CC meiotic and mitotic cells and plays an important role in DNA repair (By
CC similarity). {ECO:0000250}.
CC -!- SUBUNIT: Interacts with the cohesin complex. Interacts with WAPL (via
CC FGF motifs) or CDCA5 (via the FGF motif); the interaction is direct,
CC cohesin-dependent and competitive. Interacts with SMC3. Interacts with
CC TP63 (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q29RF7}.
CC Note=Associated with chromatin through most of the cell cycle.
CC Dissociates from chromatin in late prophase, reassociates during late
CC telophase (By similarity). {ECO:0000250|UniProtKB:Q29RF7}.
CC -!- SIMILARITY: Belongs to the PDS5 family. {ECO:0000305}.
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DR EMBL; EF460313; ABO47655.1; -; mRNA.
DR RefSeq; NP_001077093.1; NM_001083624.1.
DR AlphaFoldDB; A4L9P7; -.
DR SMR; A4L9P7; -.
DR STRING; 10116.ENSRNOP00000003437; -.
DR CarbonylDB; A4L9P7; -.
DR iPTMnet; A4L9P7; -.
DR PhosphoSitePlus; A4L9P7; -.
DR PaxDb; A4L9P7; -.
DR PeptideAtlas; A4L9P7; -.
DR PRIDE; A4L9P7; -.
DR GeneID; 305343; -.
DR KEGG; rno:305343; -.
DR UCSC; RGD:1307094; rat.
DR CTD; 23244; -.
DR RGD; 1307094; Pds5a.
DR VEuPathDB; HostDB:ENSRNOG00000002541; -.
DR eggNOG; KOG1525; Eukaryota.
DR HOGENOM; CLU_004041_0_0_1; -.
DR InParanoid; A4L9P7; -.
DR OMA; VVACDIM; -.
DR OrthoDB; 69768at2759; -.
DR PhylomeDB; A4L9P7; -.
DR TreeFam; TF106415; -.
DR Reactome; R-RNO-2467813; Separation of Sister Chromatids.
DR Reactome; R-RNO-2468052; Establishment of Sister Chromatid Cohesion.
DR Reactome; R-RNO-2470946; Cohesin Loading onto Chromatin.
DR Reactome; R-RNO-2500257; Resolution of Sister Chromatid Cohesion.
DR PRO; PR:A4L9P7; -.
DR Proteomes; UP000002494; Chromosome 14.
DR Bgee; ENSRNOG00000002541; Expressed in spleen and 18 other tissues.
DR GO; GO:0000785; C:chromatin; ISO:RGD.
DR GO; GO:0005654; C:nucleoplasm; IEA:Ensembl.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; IEA:Ensembl.
DR GO; GO:0009952; P:anterior/posterior pattern specification; ISO:RGD.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0006281; P:DNA repair; IBA:GO_Central.
DR GO; GO:0003007; P:heart morphogenesis; ISO:RGD.
DR GO; GO:0002088; P:lens development in camera-type eye; ISO:RGD.
DR GO; GO:0001656; P:metanephros development; ISO:RGD.
DR GO; GO:0007064; P:mitotic sister chromatid cohesion; ISO:RGD.
DR GO; GO:0008156; P:negative regulation of DNA replication; ISS:UniProtKB.
DR GO; GO:0097402; P:neuroblast migration; ISO:RGD.
DR GO; GO:0060021; P:roof of mouth development; ISO:RGD.
DR Gene3D; 1.25.10.10; -; 2.
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 Acetylation; Cell cycle; Cell division; Mitosis; Nucleus; Phosphoprotein;
KW Reference proteome; Repeat.
FT CHAIN 1..1333
FT /note="Sister chromatid cohesion protein PDS5 homolog A"
FT /id="PRO_0000296343"
FT REPEAT 392..428
FT /note="HEAT"
FT /evidence="ECO:0000255"
FT REGION 1133..1333
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1159..1201
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1210..1234
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1250..1279
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000250|UniProtKB:Q29RF7"
FT MOD_RES 1096
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q29RF7"
FT MOD_RES 1145
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q29RF7"
FT MOD_RES 1174
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 1194
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q29RF7"
FT MOD_RES 1207
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q29RF7"
FT MOD_RES 1210
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q29RF7"
FT MOD_RES 1289
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q29RF7"
FT MOD_RES 1304
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q29RF7"
SQ SEQUENCE 1333 AA; 150286 MW; AC6FC6215E0F7F56 CRC64;
MDFTQPKPAT ALCGVVSADG KIAYPPGVKE ITDKITTDEM IKRLKMVVKT FMDMDQDSED
EKQQYLPLAL HLASEFFLRN PNKDVRLLVA CCLADIFRIY APEAPYTSHD KLKDIFLFIT
RQLKGLEDTK SPQFNRYFYL LENLAWVKSY NICFELEDCN EIFIQLFRTL FSVINNSHNK
KVQMHMLDLM SSIIMEGDGV TQELLDSILI NLIPAHKNLN KQSFDLAKVL LKRTVQTIEA
CIANFFNQVL VLGRSSVSDL SEHVFDLIQE LFAIDPHLLL SVMPQLEFKL KSNDGEERLA
VVRLLAKLFG SKDSDLATQN RPLWQCFLGR FNDIHVPVRL ESVKFASHCL MNHPDLAKDL
TEYLKVRSHD PEEAIRHDVI VTIITAAKRD LALVNDQLLG FVRERTLDKR WRVRKEAMMG
LAQLYKKYCL HGEAGKEAAE KVSWIKDKLL HIYYQNSIDD KLLVEKIFAQ YLVPHNLETE
ERMKCLYYLY ASLDPNAVKA LNEMWKCQNM LRSHVRELLD LHKQPTSEAN CSAMFGKLMT
IAKNLPDPGK AQDFVKKFNQ VLGDDEKLRS QLELLISPTC SCKQADICVR EIARKLANPK
QPTNPFLEMV KFLLERIAPV HIDSEAISAL VKLMNKSIEG TADDEEEGVS PDSAIRSGLE
LLKVLSFTHP TSFHSAETYE SLLQCLRMED DKVAEAAIQI FRNTGHKIET DLPQIRSTLI
PILHQKAKRG TPHQAKQAVH CIHAIFSNKE VQLAQIFEPL SRSLNADVPE QLITPLVSLG
HISMLAPDQF ASPMKSVVAN FIVKDLLMND RSTGEKNGKL WSPDEEVSPE VLAKVQAIKL
LVRWLLGMKN NQSKSANSTL RLLSAMLVSE GDLTEQKRIS KSDMSRLRLA AGSAIMKLAQ
EPCYHEIITP EQFQLCALVI NDECYQVRQI FAQKLHKALV KLLLPLEYMA IFALCAKDPV
KERRAHARQC LLKNISIRRE YIKQNPMATE KLLSLLPEYV VPYMIHLLAH DPDFTRSQDV
DQLRDIKECL WFMLEVLMTK NENNSHAFMK KMAENIKLTR DAQSPDEAKT NEKLYTVCDV
ALCVINSKSA LCNADSPKDP VLPMKFFTQP EKDFSNDKSY ISEETRVLLL TGKPKPTGVL
GTVNKPLSAT GRKPYVRSAG TETGSNINAS SELSPSAGNR SREQSSEASE TGVSENEENP
VRIISVTPVK SIDTVKNKEI NSDQSTQGNI SSDRGKKRIV TAAGAENIQQ KPDEKADESG
PPAPSKPRRG RRPKSESQGN ATKNDDLSKP VSKGRKRAAG SQESLEAGNA KAPKLQDGAK
KAVPAERQID LQR
