RAD21_BOVIN
ID RAD21_BOVIN Reviewed; 630 AA.
AC Q3SWX9;
DT 11-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2005, sequence version 1.
DT 03-AUG-2022, entry version 106.
DE RecName: Full=Double-strand-break repair protein rad21 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; Synonyms=SCC1;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Ascending colon;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
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 control RUNX1 gene expression. Binds to and represses
CC APOB gene promoter (By similarity). May play a role in embryonic gut
CC development, possibly through the regulation of enteric neuron
CC development (By similarity). {ECO:0000250|UniProtKB:O60216,
CC ECO:0000250|UniProtKB:Q61550, 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 SMC1A/B
CC and SMC3 heterodimer core and 2 non-Smc subunits RAD21 and STAG1/SA1,
CC STAG2/SA2 or STAG3/SA3. Interacts (via N-terminus) with SMC1A; the
CC interaction is direct (By similarity). The cohesin complex interacts
CC with NUMA1. The cohesin complex also interacts with CDCA5, PDS5A and
CC PDS5B; this interaction might regulate the ability of the cohesin
CC complex to mediate sister chromatid cohesion. The interaction with
CC PDS5B is direct and is stimulated by STAG1/SA1. The cohesin complex
CC interacts with the cohesin loading complex subunits NIPBL/Scc2 (via
CC HEAT repeats) and MAU2/Scc4. The cohesin complex interacts with
CC DDX11/ChIR1. Directly interacts with WAPL; this interaction is
CC stimulated by STAG1/SA1. Interacts with the ISWI chromatin remodeling
CC complex component SMARCA5; the interaction is direct (By similarity).
CC Interacts with the NuRD complex component CHD4; the interaction is
CC direct (By similarity). {ECO:0000250|UniProtKB:O60216}.
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:0000250|UniProtKB:O60216}. 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 PLK1-mediated phosphorylation (By
CC similarity). A small amount of cohesin remains in centromeric regions
CC and is removed from chromosomes only at the onset of anaphase. At
CC anaphase, cleavage by separase/ESPL1 leads to the dissociation of
CC cohesin from chromosomes and chromosome separation (By similarity).
CC {ECO:0000250|UniProtKB:O60216, ECO:0000250|UniProtKB:O93310}.
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. Cleaved by
CC caspase-3/CASP3 or caspase-7/CASP7 at the beginning of apoptosis.
CC {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 its phosphorylation by PLK1.
CC {ECO:0000250|UniProtKB:O60216}.
CC -!- SIMILARITY: Belongs to the rad21 family. {ECO:0000305}.
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DR EMBL; BC104612; AAI04613.1; -; mRNA.
DR RefSeq; NP_001029889.1; NM_001034717.1.
DR AlphaFoldDB; Q3SWX9; -.
DR SMR; Q3SWX9; -.
DR STRING; 9913.ENSBTAP00000009607; -.
DR PaxDb; Q3SWX9; -.
DR PRIDE; Q3SWX9; -.
DR Ensembl; ENSBTAT00000009607; ENSBTAP00000009607; ENSBTAG00000007303.
DR GeneID; 540966; -.
DR KEGG; bta:540966; -.
DR CTD; 5885; -.
DR VEuPathDB; HostDB:ENSBTAG00000007303; -.
DR VGNC; VGNC:33680; RAD21.
DR eggNOG; KOG1213; Eukaryota.
DR GeneTree; ENSGT00940000154655; -.
DR HOGENOM; CLU_015775_1_1_1; -.
DR InParanoid; Q3SWX9; -.
DR OMA; LKQEEPY; -.
DR OrthoDB; 1253899at2759; -.
DR TreeFam; TF101215; -.
DR Proteomes; UP000009136; Chromosome 14.
DR Bgee; ENSBTAG00000007303; Expressed in occipital lobe and 107 other tissues.
DR GO; GO:0000785; C:chromatin; IEA:Ensembl.
DR GO; GO:0000775; C:chromosome, centromeric region; IEA:UniProtKB-SubCell.
DR GO; GO:0008278; C:cohesin complex; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
DR GO; GO:0030496; C:midbody; IEA:Ensembl.
DR GO; GO:0016363; C:nuclear matrix; IEA:UniProtKB-SubCell.
DR GO; GO:0034991; C:nuclear meiotic cohesin complex; IBA:GO_Central.
DR GO; GO:0005654; C:nucleoplasm; IEA:Ensembl.
DR GO; GO:0000922; C:spindle pole; IEA:UniProtKB-SubCell.
DR GO; GO:0003682; F:chromatin binding; IBA:GO_Central.
DR GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0010972; P:negative regulation of G2/M transition of mitotic cell cycle; IEA:Ensembl.
DR GO; GO:0045841; P:negative regulation of mitotic metaphase/anaphase transition; IEA:Ensembl.
DR GO; GO:0045876; P:positive regulation of sister chromatid cohesion; IEA:Ensembl.
DR GO; GO:0071168; P:protein localization to chromatin; ISS:UniProtKB.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IEA:Ensembl.
DR GO; GO:1990414; P:replication-born double-strand break repair via sister chromatid exchange; IBA:GO_Central.
DR GO; GO:0007062; P:sister chromatid cohesion; IBA:GO_Central.
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 2: Evidence at transcript level;
KW Apoptosis; Cell cycle; Cell division; Centromere; Chromosome;
KW Chromosome partition; Cytoplasm; Cytoskeleton; Developmental protein;
KW DNA damage; DNA repair; Isopeptide bond; Mitosis; Nucleus; Phosphoprotein;
KW Reference proteome; Ubl conjugation.
FT CHAIN 1..630
FT /note="Double-strand-break repair protein rad21 homolog"
FT /id="PRO_0000245487"
FT CHAIN 280..630
FT /note="64-kDa C-terminal product"
FT /evidence="ECO:0000250|UniProtKB:O60216"
FT /id="PRO_0000446316"
FT REGION 1..126
FT /note="Required for interaction with SMCA1"
FT /evidence="ECO:0000250|UniProtKB:O60216"
FT REGION 126..282
FT /note="Required for interaction with SMARCA5"
FT /evidence="ECO:0000250|UniProtKB:O60216"
FT REGION 258..285
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 287..403
FT /note="Interaction with WAPL and PDS5B"
FT /evidence="ECO:0000250"
FT REGION 362..403
FT /note="Interaction with STAG1"
FT /evidence="ECO:0000250"
FT REGION 423..488
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 516..557
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 423..453
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 532..546
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 279..280
FT /note="Cleavage; by caspase-3 or caspase-7"
FT /evidence="ECO:0000250"
FT SITE 450..451
FT /note="Cleavage; by ESPL1"
FT /evidence="ECO:0000250"
FT MOD_RES 46
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O60216"
FT MOD_RES 153
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O60216"
FT MOD_RES 175
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O60216"
FT MOD_RES 249
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O60216"
FT MOD_RES 394
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:O60216"
FT MOD_RES 454
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O60216"
FT MOD_RES 544
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O60216"
FT MOD_RES 622
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:O60216"
FT CROSSLNK 48
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:O60216"
FT CROSSLNK 216
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:O60216"
FT CROSSLNK 418
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:O60216"
SQ SEQUENCE 630 AA; 71514 MW; DC23DA37F757CD27 CRC64;
MFYAHFVLSK RGPLAKIWLA AHWDKKLTKA HVFECNLESS VESIISPKVK MALRTSGHLL
LGVVRIYHRK AKYLLADCNE AFIKIKMAFR PGVVDLPEEN REAAYNAITL PEEFHDFDQP
LPDLDDIDVA QQFSLNQSRV EEITMREEVG NISILQENDF GDFGMDDREI MREGSAFEDD
DMLASTGASN LLLEPEQSTS NLNEKINHLE YEDQYKDDNF GEGNDGGILD DKLISNNDGG
IFDDPPALSE AGVMLPEQPA HDDMDEDDNV SMGGPDSPDS VDPVEPMPTM TDQTTLVPNE
EEAFALEPID ITVKETKAKR KRKLIVDSVK ELDSKTIRAQ LSDYSDIVTT LDLAPPTKKL
MMWKETGGVE KLFSLPAQPL WNNRLLKLFT RCLTPLVPED LRKRRKGGEA DNLDEFLKEF
ENPEVPREDQ QQQHQQRDVI DEPILEEPSR LQESMETSRT NLDESAMPPP PPQGVKRKAG
QIDPEPMIPP QQAEQMEIPP VELPPEEPPN ICQLIPELEL LPEKEKEKEK EKEDDEEEED
EDASGGDQDQ EERRWNKRTQ QMLHGLQRAL AKTGAESISL LELCRNTNRK QAAAKFYSFL
VLKKQQAIEL TQEEPYSDII ATPGPRFHII
