CCA5B_XENLA
ID CCA5B_XENLA Reviewed; 275 AA.
AC Q5XG21;
DT 05-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT 23-NOV-2004, sequence version 1.
DT 03-AUG-2022, entry version 54.
DE RecName: Full=Sororin-B;
DE AltName: Full=Cell division cycle-associated protein 5-B;
GN Name=cdca5-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]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Spleen;
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases.
RN [2]
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).
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:21111234}.
CC -!- SUBUNIT: Interacts with the APC/C complex (By similarity). Interacts
CC with the chromatin-bound cohesin complex; the interaction is indirect,
CC occurs after DNA replication and requires acetylation of the cohesin
CC component 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:0000250, ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}. Chromosome {ECO:0000305}.
CC Cytoplasm {ECO:0000305}. Note=Associates with nuclear chromatin from S
CC phase until metaphase and is released in the cytoplasm upon nuclear
CC envelope breakdown. {ECO:0000305}.
CC -!- DOMAIN: The KEN box is required for the association with the APC/C
CC complex. {ECO:0000250}.
CC -!- PTM: Ubiquitinated by the APC/C complex in G1, leading to its
CC degradation. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the sororin family. {ECO:0000305}.
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DR EMBL; BC084650; AAH84650.1; -; mRNA.
DR RefSeq; NP_001088380.1; NM_001094911.1.
DR AlphaFoldDB; Q5XG21; -.
DR DNASU; 495231; -.
DR GeneID; 495231; -.
DR KEGG; xla:495231; -.
DR CTD; 495231; -.
DR Xenbase; XB-GENE-6254116; cdca5.L.
DR OrthoDB; 1454872at2759; -.
DR Proteomes; UP000186698; Chromosome 4L.
DR Bgee; 495231; Expressed in gastrula and 14 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:0006302; P:double-strand break repair; ISS:UniProtKB.
DR GO; GO:0007064; P:mitotic sister chromatid cohesion; ISS: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..275
FT /note="Sororin-B"
FT /id="PRO_0000089391"
FT REGION 1..42
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 63..117
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 91..93
FT /note="KEN box"
FT MOTIF 186..188
FT /note="FGF motif"
FT COMPBIAS 63..115
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 275 AA; 30654 MW; AF9DE0394BE5D12E CRC64;
MSERKKRGSS DADSRRGVAI ISPPKRRSQR KSASDSPIPA PIMKRSITVK KIMPRKTLAA
IANTGSQFTP KVSNVTAAPR RSSRISPKIQ KENAFSEQSQ MDPKDVTSQS SAPEIDVLSP
IPVNIQLSPK LDNRDMIMSQ KVRRSYSRLE MSLNSSAFLY SPTRKTDSSD TSTPNAVLKS
SRISLFGFDK LLNSEMPEGE LKKSSAVTRE KTANERNLQT VLPEEPDHNI PGVVLAKQKR
RKRKVPVLEK SDVDEWAAIM NAEFDEAEKF DLTVE