CCA5A_XENLA
ID CCA5A_XENLA Reviewed; 269 AA.
AC Q563C3;
DT 05-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT 10-MAY-2005, sequence version 1.
DT 03-AUG-2022, entry version 54.
DE RecName: Full=Sororin;
DE AltName: Full=Cell division cycle-associated protein 5-A;
DE AltName: Full=Xp35;
GN Name=cdca5-a;
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]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, UBIQUITINATION, INTERACTION WITH THE
RP APC/C COMPLEX, AND MUTAGENESIS OF 85-LYS--ASN-87.
RX PubMed=15837422; DOI=10.1016/j.molcel.2005.03.017;
RA Rankin S., Ayad N.G., Kirschner M.W.;
RT "Sororin, a substrate of the anaphase-promoting complex, is required for
RT sister chromatid cohesion in vertebrates.";
RL Mol. Cell 18:185-200(2005).
RN [2]
RP ERRATUM OF PUBMED:15837422.
RA Rankin S., Ayad N.G., Kirschner M.W.;
RL Mol. Cell 18:609-609(2005).
RN [3]
RP FUNCTION, AND INTERACTION WITH PDS5A AND PDS5B.
RX PubMed=21111234; DOI=10.1016/j.cell.2010.10.031;
RA Nishiyama T., Ladurner R., Schmitz J., Kreidl E., Schleiffer A.,
RA Bhaskara V., Bando M., Shirahige K., Hyman A.A., Mechtler K., Peters J.M.;
RT "Sororin mediates sister chromatid cohesion by antagonizing wapl.";
RL Cell 143:737-749(2010).
RN [4]
RP SUBCELLULAR LOCATION.
RX PubMed=21059905; DOI=10.1073/pnas.1011069107;
RA Lafont A.L., Song J., Rankin S.;
RT "Sororin cooperates with the acetyltransferase Eco2 to ensure DNA
RT replication-dependent sister chromatid cohesion.";
RL Proc. Natl. Acad. Sci. U.S.A. 107:20364-20369(2010).
CC -!- FUNCTION: Regulator of sister chromatid cohesion in mitosis stabilizing
CC cohesin complex association with chromatin. May antagonize the action
CC of wapl which stimulates cohesin dissociation from chromatin. Cohesion
CC ensures that chromosome partitioning is accurate in both meiotic and
CC mitotic cells and plays an important role in DNA repair. Required for
CC efficient DNA double-stranded break repair (Probable).
CC {ECO:0000305|PubMed:15837422, ECO:0000305|PubMed:21111234}.
CC -!- SUBUNIT: Interacts with the APC/C complex. Interacts with the
CC chromatin-bound cohesin complex; the interaction is indirect, occurs
CC after DNA replication and requires acetylation of the cohesin component
CC smc3. Interacts (via the FGF motif) with pds5a and pds5b; the
CC interaction is direct and prevents the interaction of pds5a with wapl
CC (Probable). {ECO:0000305|PubMed:15837422, ECO:0000305|PubMed:21111234}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:21059905}. Chromosome
CC {ECO:0000269|PubMed:21059905}. Cytoplasm {ECO:0000269|PubMed:21059905}.
CC Note=Associates with nuclear chromatin from S phase until metaphase and
CC is released in the cytoplasm upon nuclear envelope breakdown.
CC -!- DOMAIN: The KEN box is required for the association with the APC/C
CC complex.
CC -!- PTM: Ubiquitinated by the APC/C complex in G1, leading to its
CC degradation. {ECO:0000269|PubMed:15837422}.
CC -!- SIMILARITY: Belongs to the sororin family. {ECO:0000305}.
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DR EMBL; AY962466; AAX73201.1; -; mRNA.
DR RefSeq; NP_001089079.1; NM_001095610.2.
DR AlphaFoldDB; Q563C3; -.
DR GeneID; 733230; -.
DR KEGG; xla:733230; -.
DR CTD; 733230; -.
DR Xenbase; XB-GENE-5908158; cdca5.S.
DR OrthoDB; 1454872at2759; -.
DR Proteomes; UP000186698; Chromosome 4S.
DR Bgee; 733230; Expressed in gastrula and 15 other tissues.
DR GO; GO:0000785; C:chromatin; ISS:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0007059; P:chromosome segregation; IMP:UniProtKB.
DR GO; GO:0006302; P:double-strand break repair; ISS:UniProtKB.
DR GO; GO:0007064; P:mitotic sister chromatid cohesion; IMP:UniProtKB.
DR GO; GO:0045876; P:positive regulation of sister chromatid cohesion; IMP:UniProtKB.
DR GO; GO:0071922; P:regulation of cohesin loading; ISS:UniProtKB.
DR InterPro; IPR018605; Sororin.
DR PANTHER; PTHR31092; PTHR31092; 1.
DR Pfam; PF09666; Sororin; 1.
PE 1: Evidence at protein level;
KW Cell cycle; Cell division; Chromosome; Cytoplasm; Mitosis; Nucleus;
KW Reference proteome; Ubl conjugation.
FT CHAIN 1..269
FT /note="Sororin"
FT /id="PRO_0000089390"
FT REGION 1..39
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 56..110
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 146..169
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 85..87
FT /note="KEN box"
FT MOTIF 180..182
FT /note="FGF motif"
FT COMPBIAS 56..74
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 82..110
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MUTAGEN 85..87
FT /note="KEN->AAA: Prevents ubiquitination and subsequent
FT degradation."
FT /evidence="ECO:0000269|PubMed:15837422"
SQ SEQUENCE 269 AA; 29942 MW; 1701AFBA71E27C8D CRC64;
MSEGKKRSRG GLAIISPPKR RSQRKSTSDS PIPEPIMKRS ITVKKIMPRK TLAAIVNTGS
QSTPKVSNVP PAPRRSSRIS PKIQKENAFS EQSQIVHKDV PGQSSAPKIN VLSPIPVNIQ
LSPKQDNRDI IMSQKVRRSY SRLEMSLNSS SSLYSPTRKT DSSDTSTPNV VLKSGRSSLF
GFDKLLNSEM PDGELKKSNG VTRKKNTKER ILGTVLPEQP DHNIPGVVLA KQKRRKRKVA
IIEKSDLDEW AAFMNAEFEE AEKFDLTVE
