RAD21_XENLA
ID RAD21_XENLA Reviewed; 629 AA.
AC O93310;
DT 25-MAR-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1998, sequence version 1.
DT 03-AUG-2022, entry version 97.
DE RecName: Full=Double-strand-break repair protein rad21 homolog;
DE AltName: Full=SCC1 homolog;
DE Contains:
DE RecName: Full=64-kDa C-terminal product;
DE AltName: Full=64-kDa carboxy-terminal product {ECO:0000250|UniProtKB:O60216};
GN Name=rad21;
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], AND IDENTIFICATION IN THE COHESIN COMPLEX.
RC TISSUE=Egg;
RX PubMed=9649503; DOI=10.1101/gad.12.13.1986;
RA Losada A., Hirano M., Hirano T.;
RT "Identification of Xenopus SMC protein complexes required for sister
RT chromatid cohesion.";
RL Genes Dev. 12:1986-1997(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], AND IDENTIFICATION IN THE COHESIN COMPLEX.
RX PubMed=10931856; DOI=10.1083/jcb.150.3.405;
RA Losada A., Yokochi T., Kobayashi R., Hirano T.;
RT "Identification and characterization of SA/Scc3p subunits in the Xenopus
RT and human cohesin complexes.";
RL J. Cell Biol. 150:405-416(2000).
RN [3]
RP PHOSPHORYLATION BY PLK1, AND SUBCELLULAR LOCATION.
RX PubMed=11931760; DOI=10.1016/s1097-2765(02)00473-2;
RA Sumara I., Vorlaufer E., Stukenberg P.T., Kelm O., Redemann N., Nigg E.A.,
RA Peters J.-M.;
RT "The dissociation of cohesin from chromosomes in prophase is regulated by
RT Polo-like kinase.";
RL Mol. Cell 9:515-525(2002).
CC -!- FUNCTION: [Double-strand-break repair protein rad21 homolog]: As a
CC member of the cohesin complex, involved in sister chromatid cohesion
CC from the time of DNA replication in S phase to their segregation in
CC mitosis, a function that is essential for proper chromosome
CC segregation, post-replicative DNA repair, and the prevention of
CC inappropriate recombination between repetitive regions. The cohesin
CC complex may also play a role in spindle pole assembly during mitosis
CC (By similarity). In interphase, cohesins may function in the control of
CC gene expression by binding to numerous sites within the genome (By
CC similarity). May play a role in embryonic gut development, possibly
CC through the regulation of enteric neuron development (By similarity).
CC {ECO:0000250|UniProtKB:O60216, ECO:0000250|UniProtKB:Q61550,
CC ECO:0000250|UniProtKB:Q6TEL1}.
CC -!- FUNCTION: [64-kDa C-terminal product]: May promote apoptosis.
CC {ECO:0000250|UniProtKB:O60216}.
CC -!- SUBUNIT: Component of the cohesin complex, which consists of an SMC1
CC and SMC3 heterodimer core and 2 non-Smc subunits RAD21 and STAG1/SA1,
CC STAG2/SA2 or STAG3/SA3. {ECO:0000269|PubMed:10931856,
CC ECO:0000269|PubMed:9649503}.
CC -!- SUBCELLULAR LOCATION: [Double-strand-break repair protein rad21
CC homolog]: Nucleus {ECO:0000250|UniProtKB:O60216}. Nucleus matrix
CC {ECO:0000250|UniProtKB:O60216}. Chromosome
CC {ECO:0000269|PubMed:11931760}. Chromosome, centromere
CC {ECO:0000250|UniProtKB:O60216}. Cytoplasm, cytoskeleton, spindle pole
CC {ECO:0000250|UniProtKB:O60216}. Note=Associates with chromatin. Before
CC prophase, scattered along chromosome arms. During prophase and
CC prometaphase, most cohesins dissociate from the arms of condensing
CC chromosome, possibly through Polo-like kinase PLK1/PLX1-catalyzed
CC phosphorylation (PubMed:11931760). A small amount of cohesin remains in
CC centromeric regions and is removed from chromosomes only at the onset
CC of anaphase. At anaphase, cleavage by separase/ESPL1 leads to the
CC dissociation of cohesin from chromosomes and chromosome separation (By
CC similarity). {ECO:0000250|UniProtKB:O60216,
CC ECO:0000269|PubMed:11931760}.
CC -!- SUBCELLULAR LOCATION: [64-kDa C-terminal product]: Cytoplasm, cytosol
CC {ECO:0000250|UniProtKB:O60216}. Nucleus {ECO:0000250|UniProtKB:O60216}.
CC -!- DOMAIN: The C-terminal part associates with the head of smc1a, while
CC the N-terminal part binds to the head of smc3. {ECO:0000250}.
CC -!- PTM: Cleaved by separase/ESPL1 at the onset of anaphase; this cleavage
CC is required for sister chromatid separation and cytokinesis (By
CC similarity). Cleaved by caspases at the beginning of apoptosis (By
CC similarity). {ECO:0000250|UniProtKB:O60216}.
CC -!- PTM: Phosphorylated; becomes hyperphosphorylated in M phase of cell
CC cycle. The large dissociation of cohesin from chromosome arms during
CC prophase may be partly due to phosphorylation by PLK1/PLX1.
CC {ECO:0000269|PubMed:11931760}.
CC -!- SIMILARITY: Belongs to the rad21 family. {ECO:0000305}.
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DR EMBL; AF051786; AAC26809.1; -; mRNA.
DR RefSeq; NP_001083807.1; NM_001090338.1.
DR AlphaFoldDB; O93310; -.
DR SMR; O93310; -.
DR BioGRID; 100454; 4.
DR IntAct; O93310; 6.
DR DNASU; 399129; -.
DR GeneID; 399129; -.
DR KEGG; xla:399129; -.
DR CTD; 399129; -.
DR Xenbase; XB-GENE-17340158; rad21.L.
DR OrthoDB; 1253899at2759; -.
DR Proteomes; UP000186698; Chromosome 6L.
DR Bgee; 399129; Expressed in egg cell and 19 other tissues.
DR GO; GO:0000775; C:chromosome, centromeric region; IEA:UniProtKB-SubCell.
DR GO; GO:0008278; C:cohesin complex; IEA:InterPro.
DR GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
DR GO; GO:0016363; C:nuclear matrix; IEA:UniProtKB-SubCell.
DR GO; GO:0000922; C:spindle pole; IEA:UniProtKB-SubCell.
DR GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
DR GO; GO:0071168; P:protein localization to chromatin; ISS:UniProtKB.
DR GO; GO:0007062; P:sister chromatid cohesion; IEA:InterPro.
DR Gene3D; 1.10.10.580; -; 1.
DR InterPro; IPR039781; Rad21/Rec8-like.
DR InterPro; IPR006909; Rad21/Rec8_C_eu.
DR InterPro; IPR006910; Rad21_Rec8_N.
DR InterPro; IPR023093; ScpA-like_C.
DR InterPro; IPR036390; WH_DNA-bd_sf.
DR PANTHER; PTHR12585; PTHR12585; 1.
DR Pfam; PF04824; Rad21_Rec8; 1.
DR Pfam; PF04825; Rad21_Rec8_N; 1.
DR SUPFAM; SSF46785; SSF46785; 1.
PE 1: Evidence at protein level;
KW Activator; Apoptosis; Cell cycle; Cell division; Centromere; Chromosome;
KW Chromosome partition; Cytoplasm; Cytoskeleton; Developmental protein;
KW DNA damage; DNA repair; Mitosis; Nucleus; Phosphoprotein;
KW Reference proteome; Repressor; Transcription; Transcription regulation.
FT CHAIN 1..629
FT /note="Double-strand-break repair protein rad21 homolog"
FT /id="PRO_0000097874"
FT CHAIN 278..629
FT /note="64-kDa C-terminal product"
FT /evidence="ECO:0000250|UniProtKB:O60216"
FT /id="PRO_0000446319"
FT REGION 245..284
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 447..475
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 491..553
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 491..509
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 530..545
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 172..173
FT /note="Cleavage; by ESPL1"
FT /evidence="ECO:0000250"
FT SITE 277..278
FT /note="Cleavage; by caspases"
FT /evidence="ECO:0000250|UniProtKB:O60216"
SQ SEQUENCE 629 AA; 71555 MW; 0FCD268C712FF2C0 CRC64;
MFYAHFVLSK RGPLAKIWLA AHWDKKLTKA HVFECNLESS VESIICPKVK MALRTSGHLL
LGVVRIYHRK AKYLLADCNE AFIKIKMAFR PGVVDLPEEN REAAYNAITL PEEFHDFDQP
LPDLDDIDVA QQFSLNQSRV EEITMREEVS NINILQDNDF GDFGMDDREM MREGSAFEDD
MLTTNASNLK LEPEQSTSQL NEKSNHLEYD DQYKDDNFGE GNEGGILDDK LLSNDAGGIF
DDPPAMPEEG VAMPEQPVHD DLDDDDNVSM GAPDSPDSVD PVEPLPTMTD QTTLVPNEEE
AFALEPIDIT VKETKAKRKR KLIVDSVKEL DSKTIRAQLS DYSDIVTTLD LAPPTKKLMM
WKETGGVEKL FSLPAQPLWN TRLLKLFTRC LTPLVLDDLR KRRKGGEADN LDEFLKEFEN
PEVPREELRP QDVIDQPILE EASHLQESLM EGSRTHLDDT IMPPPPPKQG VKRDSLQMEP
EPMPMMQEAE PQIEMPPPPL PPPLELPPEE PQSISDLIPE LNLLPEKEKE KDEEEEEEEE
DTTGTEQDQE ERRWNKRTQQ MLHGLQRVLA KTGAESISLL DLCRNTNRKQ AAAKFYSFLV
LKKQQAIELT QREPYSDIVA TPGPRFHTV
