PDS5A_MOUSE
ID PDS5A_MOUSE Reviewed; 1332 AA.
AC Q6A026; E9Q656;
DT 24-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 3.
DT 25-MAY-2022, entry version 116.
DE RecName: Full=Sister chromatid cohesion protein PDS5 homolog A;
GN Name=Pds5a; Synonyms=Kiaa0648 {ECO:0000312|EMBL:BAD32270.1};
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [2] {ECO:0000305, ECO:0000312|EMBL:BAD32270.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-1112.
RC TISSUE=Embryonic intestine {ECO:0000312|EMBL:BAD32270.1};
RX PubMed=15368895; DOI=10.1093/dnares/11.3.205;
RA Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA Saga Y., Seino S., Nishimura M., Kaisho T., Hoshino K., Kitamura H.,
RA Nagase T., Ohara O., Koga H.;
RT "Prediction of the coding sequences of mouse homologues of KIAA gene: IV.
RT The complete nucleotide sequences of 500 mouse KIAA-homologous cDNAs
RT identified by screening of terminal sequences of cDNA clones randomly
RT sampled from size-fractionated libraries.";
RL DNA Res. 11:205-218(2004).
RN [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1174, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [4]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-1145 AND LYS-1210, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic fibroblast;
RX PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001;
RA Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y.,
RA Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.;
RT "SIRT5-mediated lysine desuccinylation impacts diverse metabolic
RT pathways.";
RL Mol. Cell 50:919-930(2013).
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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAD32270.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AC112263; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AK172992; BAD32270.1; ALT_INIT; Transcribed_RNA.
DR AlphaFoldDB; Q6A026; -.
DR SMR; Q6A026; -.
DR IntAct; Q6A026; 13.
DR MINT; Q6A026; -.
DR STRING; 10090.ENSMUSP00000031104; -.
DR iPTMnet; Q6A026; -.
DR PhosphoSitePlus; Q6A026; -.
DR SwissPalm; Q6A026; -.
DR EPD; Q6A026; -.
DR jPOST; Q6A026; -.
DR MaxQB; Q6A026; -.
DR PaxDb; Q6A026; -.
DR PRIDE; Q6A026; -.
DR ProteomicsDB; 288025; -.
DR MGI; MGI:1918771; Pds5a.
DR eggNOG; KOG1525; Eukaryota.
DR InParanoid; Q6A026; -.
DR Reactome; R-MMU-2467813; Separation of Sister Chromatids.
DR Reactome; R-MMU-2468052; Establishment of Sister Chromatid Cohesion.
DR Reactome; R-MMU-2470946; Cohesin Loading onto Chromatin.
DR Reactome; R-MMU-2500257; Resolution of Sister Chromatid Cohesion.
DR ChiTaRS; Pds5a; mouse.
DR PRO; PR:Q6A026; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; Q6A026; protein.
DR GO; GO:0000785; C:chromatin; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR GO; GO:0009952; P:anterior/posterior pattern specification; IMP:MGI.
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; IMP:MGI.
DR GO; GO:0002088; P:lens development in camera-type eye; IMP:MGI.
DR GO; GO:0001656; P:metanephros development; IMP:MGI.
DR GO; GO:0007064; P:mitotic sister chromatid cohesion; ISO:MGI.
DR GO; GO:0008156; P:negative regulation of DNA replication; ISS:UniProtKB.
DR GO; GO:0097402; P:neuroblast migration; IMP:MGI.
DR GO; GO:0060021; P:roof of mouth development; IMP:MGI.
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..1332
FT /note="Sister chromatid cohesion protein PDS5 homolog A"
FT /id="PRO_0000296342"
FT REPEAT 392..428
FT /note="HEAT"
FT /evidence="ECO:0000255"
FT REGION 1138..1332
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 1249..1278
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:0007744|PubMed:23806337"
FT MOD_RES 1174
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
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:0007744|PubMed:23806337"
FT MOD_RES 1288
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q29RF7"
FT MOD_RES 1303
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q29RF7"
FT CONFLICT 557
FT /note="K -> E (in Ref. 2; BAD32270)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1332 AA; 150327 MW; 0D6473650AC9D89B CRC64;
MDFTQPKPAT ALCGVVSADG KIAYPPGVKE ITDKITTDEM IKRLKMVVKT FMDMDQDSED
EKQQYLPLAL HLASEFFLRN PNKDVRLLVA CCLADIFRIY APEAPYTSHD KLKDIFLFIT
RQLKGLEDTK SPQFNRYFYL LENLAWVKSY NICFELEDCN EIFIQLFRTL FSVINNSHNT
KVQMHMLDLM SSIIMEGDGV TQELLDSILI NLIPAHKNLN KQSFDLAKVL LKRTVQTIEA
CIANFFNQVL VLGRSSVSDL SEHVFDLIQE LFAIDPQLLL 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 SCKQADVCVR EIARKLANPK
QPTNPFLEMV KFLLERIAPV HIDSEAISAL VKLMNKSIEG TADDEEEGVS PDSAIRSGLE
LLKVLSFTHP TSFHSAETYE SLLQCLRMED DKVAEAAIQI FRNTGHKIET DLPQIRSTLI
PILHQKAKRG TPHQAKQAVH CIHAIFSNKE VQLAQIFEPL SRSLNADVPE QLITPLVSLG
HISMLAPDQF ASPMKSVVAN FIVKDLLMND RSTGEKNGKL WSPDEEVSPE VLAKVYLLRL
LVRWLLGMKN NQSKSANSTL RLLSAMLVSE GDLTEQKRIS KSDMSRLRLA AGSAIMKLAQ
EPCYHEIITP EQFQLCALVI NDECYQVRQI FAQKLHKALV KLLLPLEYMA IFALCAKDPV
KERRAHARQC LLKNISIRRE YIKQNPMATE KLLSLLPEYV VPYMIHLLAH DPDFTRSQDV
DQLRDIKECL WFMLEVLMTK NENNSHAFMK KMAENIKLTR DAQSPDESKT NEKLYTVCDV
ALCVINSKSA LCNADSPKDP VLPMKFFTQP EKDFCNDKSY ISEETRVLLL TGKPKPTGVL
GTVNKPLSAT GRKPYVRSAG TETGSNINAN SELSPSAGSR SREQSSEASE TGVSENEENP
VRIISVTPVK NIDTVKNKEI NSDQSTQGNI SSDRGKKRIV TAAGAENIQK PDEKVDESGP
PAPSKPRRGR RPKSESQGNA TKNDDLNKPV SKGRKRAAGS QESLEAGNAK APKLQDGAKK
AVPAERQIDL QR
