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   24-JAN-2024, entry version 123.
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,
RC   Pancreas, 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; 14.
DR   MINT; Q6A026; -.
DR   STRING; 10090.ENSMUSP00000144171; -.
DR   GlyGen; Q6A026; 2 sites, 1 O-linked glycan (2 sites).
DR   iPTMnet; Q6A026; -.
DR   PhosphoSitePlus; Q6A026; -.
DR   SwissPalm; Q6A026; -.
DR   EPD; Q6A026; -.
DR   jPOST; Q6A026; -.
DR   MaxQB; Q6A026; -.
DR   PaxDb; 10090-ENSMUSP00000031104; -.
DR   ProteomicsDB; 288025; -.
DR   Pumba; Q6A026; -.
DR   AGR; MGI:1918771; -.
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: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   CDD; cd19953; PDS5; 1.
DR   Gene3D; 1.25.10.10; Leucine-rich Repeat Variant; 2.
DR   InterPro; IPR011989; ARM-like.
DR   InterPro; IPR016024; ARM-type_fold.
DR   InterPro; IPR039776; Pds5.
DR   PANTHER; PTHR12663; ANDROGEN INDUCED INHIBITOR OF PROLIFERATION AS3 / PDS5-RELATED; 1.
DR   PANTHER; PTHR12663:SF2; SISTER CHROMATID COHESION PROTEIN PDS5 HOMOLOG A; 1.
DR   Pfam; PF20168; PDS5; 1.
DR   SUPFAM; SSF48371; ARM repeat; 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
//