ID   PD5AB_XENLA             Reviewed;        1323 AA.
AC   Q4KLU7;
DT   21-AUG-2007, integrated into UniProtKB/Swiss-Prot.
DT   02-AUG-2005, sequence version 1.
DT   03-AUG-2022, entry version 65.
DE   RecName: Full=Sister chromatid cohesion protein PDS5 homolog A-B;
GN   Name=pds5a-b;
OS   Xenopus laevis (African clawed frog).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX   NCBI_TaxID=8355;
RN   [1] {ECO:0000312|EMBL:AAH98992.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Oocyte {ECO:0000312|EMBL:AAH98992.1};
RG   NIH - Xenopus Gene Collection (XGC) project;
RL   Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000305}
RP   FUNCTION, AND INTERACTION WITH CHROMATIN AND THE COHESIN COMPLEX.
RX   PubMed=15855230; DOI=10.1242/jcs.02355;
RA   Losada A., Yokochi T., Hirano T.;
RT   "Functional contribution of Pds5 to cohesin-mediated cohesion in human
RT   cells and Xenopus egg extracts.";
RL   J. Cell Sci. 118:2133-2141(2005).
CC   -!- FUNCTION: May regulate sister chromatid cohesion during mitosis and
CC       couple it to DNA replication. {ECO:0000269|PubMed:15855230}.
CC   -!- SUBUNIT: Interacts with the cohesin complex. Binds chromatin in a
CC       cohesin-dependent manner. {ECO:0000269|PubMed:15855230}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q29RF7}.
CC   -!- MISCELLANEOUS: Chromosomes assembled in the absence of pds5a and
CC       aprin/pds5b proteins have a mild defect in centromere cohesion in
CC       vitro. {ECO:0000269|PubMed:15855230}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; BC098992; AAH98992.1; -; mRNA.
DR   RefSeq; NP_001090063.1; NM_001096594.1.
DR   AlphaFoldDB; Q4KLU7; -.
DR   SMR; Q4KLU7; -.
DR   BioGRID; 592918; 5.
DR   PRIDE; Q4KLU7; -.
DR   DNASU; 735137; -.
DR   GeneID; 735137; -.
DR   KEGG; xla:735137; -.
DR   CTD; 735137; -.
DR   Xenbase; XB-GENE-5812802; pds5a.S.
DR   OrthoDB; 69768at2759; -.
DR   Proteomes; UP000186698; Chromosome 1S.
DR   Bgee; 735137; Expressed in egg cell and 19 other tissues.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR   GO; GO:0007064; P:mitotic sister chromatid cohesion; IEA:InterPro.
DR   GO; GO:0008156; P:negative regulation of DNA replication; ISS:UniProtKB.
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   Cell cycle; Cell division; Mitosis; Nucleus; Reference proteome; Repeat.
FT   CHAIN           1..1323
FT                   /note="Sister chromatid cohesion protein PDS5 homolog A-B"
FT                   /id="PRO_0000299067"
FT   REPEAT          385..421
FT                   /note="HEAT"
FT                   /evidence="ECO:0000255"
FT   REGION          1138..1323
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1143..1181
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1207..1224
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1227..1248
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1290..1312
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1323 AA;  149527 MW;  CC1C1F80CFD0FFBD CRC64;
     MEFPTQPKLV DVKTIIYPPG VKEITDKISN DEVVKRLKMV VKTFMDMDQD SEEEKQQYLP
     LALHLSSDFF LRNPNKDVRL LVACCLADIF RIYAPEAPYT SHDKLKEIFL FITRQLKGLE
     DTKSPQFNRY FYLLENLAWV KSYNICFELE DCNEIFIQLF KTLFSVINNS HNQKVQMHML
     DLMSSITMEG DGVTQEQLDS ILINLISAHK NLNKQAFDLA KVLLKRTAQT IEPCIANFFN
     QVLVLGKSSV SDLSEHVFDL IQELFAIDPH LLLSVMPQLE FKLKSNDGEE RLAVVRLLAK
     LFGSKDSDLA TQNRPLWQCF LGRFNDIHVP VRLESVKFAS HCLMNHPDLA KDLTEFLKVR
     SHDPEEAIRH DVIVTIITAA KKDLFLVNDQ LLGFVRERTL DKRWRVRKEA MMGLAQLYKK
     YCLHGEGGKD AAEKVSWIKD KLLHIYYQNS IDDKLLVEKI FAQQLVPHNL ETEERMKCLY
     YLYASLDPNA VKALNEMWKC QNMLRSHVRE LLDLHKQPTS EANTTAMFAK LMTVAKNLPD
     PGKAQDFVKK FNQVLGEDEK LRSQLEVLIS PSCSCKQADV CVRDIARKVA NPKQPTNPFL
     EMVKFLLERI APVHIDSEAI SALVKLMNKS IEGTADDEEE GVSPDSAIRA GLELLKVLSF
     THPTSFHSDE TYESLLQCLR MEDDKVAEAA IQIFRNTGHR IETDLPQIRS ALIPILHQKA
     KRGTPHQAKQ AVHCIHSIFS NKEVQLAQIF EPLSRSLNAD VPEQLVTPLV SLGHISMLAP
     DQFASPMKSV VANFIVKDLL MNDRSNGDKN GKLWCPDEEV SPEVLAKGQA IKLLVRWLLG
     MKNNQSKSAN STLRLLSAML VSEGDLTEQK RISKSDMSRL RLAAGAAIMK LAQEPCYHEI
     ITPEQFQLCA LVINDECYQV RQIFAQKLHK ALVKLQLPLE YMAIFALCAK DPVKERRAHA
     RQCLLKNISI RREYIKQNPV SNEKLLSLLP EYVVPYMIHL LAHDPDFTKP QDIDQLRDIK
     ECLWFMLEVL MTKNENNSHA FMKKLCENIK QTRDAQAPDD PKANEKLFTV CDVALCVVYN
     KSAPCHSESS KDPVLPLTFF TQPDKDFSSK SYITDEARNL LLTGKPKPMT VLGMVNKPLN
     ATGRRPYSRS TGSEISNNVS INSESDASVA NRQSSEVPEI GVSENDENPV RLISVPPAKT
     ETVKNKEVNL DQTAPSNTGT ERGKKRSAAS AGAENIRKES EEKKVDNISA TPTPKPRRGR
     PPKSESQGSA AKNDETSKPS GRGRKRAAAN QESSGAQEAA NAKVPKQDST AKKTAQRQID
     LHR