RAD21_SCHPO
ID RAD21_SCHPO Reviewed; 628 AA.
AC P30776;
DT 01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1993, sequence version 1.
DT 03-AUG-2022, entry version 148.
DE RecName: Full=Cohesin subunit rad21;
DE AltName: Full=Double-strand-break repair protein rad21;
DE AltName: Full=SCC1 homolog;
GN Name=rad21; ORFNames=SPCC338.17c;
OS Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC Schizosaccharomyces.
OX NCBI_TaxID=284812;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
RX PubMed=1480481; DOI=10.1093/nar/20.24.6605;
RA Birkenbihl R.P., Subramani S.;
RT "Cloning and characterization of rad21 an essential gene of
RT Schizosaccharomyces pombe involved in DNA double-strand-break repair.";
RL Nucleic Acids Res. 20:6605-6611(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=972 / ATCC 24843;
RX PubMed=11859360; DOI=10.1038/nature724;
RA Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA Nurse P.;
RT "The genome sequence of Schizosaccharomyces pombe.";
RL Nature 415:871-880(2002).
RN [3]
RP FUNCTION, SUBUNIT, SUBCELLULAR LOCATION, POST-TRANSLATIONAL MODIFICATIONS,
RP AND MUTAGENESIS OF ARG-179 AND ARG-231.
RX PubMed=11069892; DOI=10.1101/gad.832000;
RA Tomonaga T., Nagao K., Kawasaki Y., Furuya K., Murakami A., Morishita J.,
RA Yuasa T., Sutani T., Kearsey S.E., Uhlmann F., Nasmyth K., Yanagida M.;
RT "Characterization of fission yeast cohesin: essential anaphase proteolysis
RT of Rad21 phosphorylated in the S phase.";
RL Genes Dev. 14:2757-2770(2000).
RN [4]
RP INTERACTION WITH SSL3.
RX PubMed=16682348; DOI=10.1016/j.cub.2006.03.037;
RA Bernard P., Drogat J., Maure J.-F., Dheur S., Vaur S., Genier S.,
RA Javerzat J.-P.;
RT "A screen for cohesion mutants uncovers ssl3, the fission yeast counterpart
RT of the cohesin loading factor scc4.";
RL Curr. Biol. 16:875-881(2006).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-219; SER-547 AND SER-553, AND
RP IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=18257517; DOI=10.1021/pr7006335;
RA Wilson-Grady J.T., Villen J., Gygi S.P.;
RT "Phosphoproteome analysis of fission yeast.";
RL J. Proteome Res. 7:1088-1097(2008).
CC -!- FUNCTION: Cleavable component of the cohesin complex, involved in
CC chromosome cohesion during cell cycle. The cohesin complex is required
CC for the cohesion of sister chromatids after DNA replication. The
CC cohesin complex apparently forms a large proteinaceous ring within
CC which sister chromatids can be trapped. At metaphase-anaphase
CC transition, this protein is cleaved by cut1 and dissociates from
CC chromatin, allowing sister chromatids to segregate. Also involved in
CC the DNA double-strand-break (DSB) repair system.
CC {ECO:0000269|PubMed:11069892, ECO:0000269|PubMed:1480481}.
CC -!- SUBUNIT: Cohesin complexes are composed of the psm1/smc1 and psm3/smc3
CC heterodimer attached via their hinge domain, rad21/scc1 which link
CC them, and psc3/scc3, which interacts with rad21. Interacts with ssl3.
CC {ECO:0000269|PubMed:11069892, ECO:0000269|PubMed:16682348}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:11069892}.
CC Chromosome, centromere {ECO:0000269|PubMed:11069892}. Note=Associates
CC with chromatin. Cohesin complex mainly associates with broad centromere
CC region. Also associates with mating-type heterochromatic region.
CC -!- PTM: Hyperphosphorylated during S and G2 phases.
CC -!- PTM: Proteolytic cleavage of a fraction of hyperphosphorylated form at
CC the onset of anaphase may be essential for the proper progression of
CC anaphase and sister chromatid separation.
CC -!- SIMILARITY: Belongs to the rad21 family. {ECO:0000305}.
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; M96437; AAA35330.1; -; Genomic_DNA.
DR EMBL; CU329672; CAA19348.1; -; Genomic_DNA.
DR PIR; S35547; S35547.
DR RefSeq; NP_588151.1; NM_001023140.2.
DR PDB; 6YUF; EM; 3.94 A; B=1-628.
DR PDBsum; 6YUF; -.
DR AlphaFoldDB; P30776; -.
DR SMR; P30776; -.
DR BioGRID; 276010; 34.
DR ELM; P30776; -.
DR IntAct; P30776; 3.
DR STRING; 4896.SPCC338.17c.1; -.
DR iPTMnet; P30776; -.
DR MaxQB; P30776; -.
DR PaxDb; P30776; -.
DR PRIDE; P30776; -.
DR EnsemblFungi; SPCC338.17c.1; SPCC338.17c.1:pep; SPCC338.17c.
DR GeneID; 2539447; -.
DR KEGG; spo:SPCC338.17c; -.
DR PomBase; SPCC338.17c; rad21.
DR VEuPathDB; FungiDB:SPCC338.17c; -.
DR eggNOG; KOG1213; Eukaryota.
DR HOGENOM; CLU_015775_0_0_1; -.
DR InParanoid; P30776; -.
DR OMA; PLCLNTN; -.
DR PhylomeDB; P30776; -.
DR Reactome; R-SPO-2470946; Cohesin Loading onto Chromatin.
DR Reactome; R-SPO-2500257; Resolution of Sister Chromatid Cohesion.
DR Reactome; R-SPO-3108214; SUMOylation of DNA damage response and repair proteins.
DR PRO; PR:P30776; -.
DR Proteomes; UP000002485; Chromosome III.
DR GO; GO:0000785; C:chromatin; IDA:PomBase.
DR GO; GO:0034507; C:chromosome, centromeric outer repeat region; IDA:PomBase.
DR GO; GO:0099115; C:chromosome, subtelomeric region; IDA:PomBase.
DR GO; GO:0008278; C:cohesin complex; IBA:GO_Central.
DR GO; GO:0000779; C:condensed chromosome, centromeric region; IDA:PomBase.
DR GO; GO:1990342; C:heterochromatin island; IDA:PomBase.
DR GO; GO:0030892; C:mitotic cohesin complex; IDA:PomBase.
DR GO; GO:0034990; C:nuclear mitotic cohesin complex; IDA:PomBase.
DR GO; GO:0005634; C:nucleus; IDA:PomBase.
DR GO; GO:0110092; C:nucleus leading edge; IDA:PomBase.
DR GO; GO:0005721; C:pericentric heterochromatin; IDA:PomBase.
DR GO; GO:0033553; C:rDNA heterochromatin; IDA:PomBase.
DR GO; GO:0003682; F:chromatin binding; IBA:GO_Central.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0006974; P:cellular response to DNA damage stimulus; IMP:PomBase.
DR GO; GO:0140588; P:chromatin looping; IDA:PomBase.
DR GO; GO:0006302; P:double-strand break repair; IMP:PomBase.
DR GO; GO:0061780; P:mitotic cohesin loading; IDA:PomBase.
DR GO; GO:0062022; P:mitotic cohesin ssDNA (lagging strand) loading; IDA:PomBase.
DR GO; GO:0007064; P:mitotic sister chromatid cohesion; IMP:PomBase.
DR GO; GO:0000070; P:mitotic sister chromatid segregation; IMP:PomBase.
DR GO; GO:0044820; P:mitotic telomere tethering at nuclear periphery; IMP:PomBase.
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 1: Evidence at protein level;
KW 3D-structure; Cell cycle; Cell division; Centromere; Chromosome;
KW Chromosome partition; DNA damage; DNA repair; Mitosis; Nucleus;
KW Phosphoprotein; Reference proteome.
FT CHAIN 1..628
FT /note="Cohesin subunit rad21"
FT /id="PRO_0000097871"
FT REGION 439..466
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 439..460
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 179..180
FT /note="Cleavage"
FT /evidence="ECO:0000305"
FT SITE 231..232
FT /note="Cleavage"
FT /evidence="ECO:0000305"
FT MOD_RES 219
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT MOD_RES 547
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT MOD_RES 553
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT MUTAGEN 179
FT /note="R->E: Sister chromatid separation blocked; when
FT associated with E-231."
FT /evidence="ECO:0000269|PubMed:11069892"
FT MUTAGEN 231
FT /note="R->E: Sister chromatid separation blocked; when
FT associated with E-179."
FT /evidence="ECO:0000269|PubMed:11069892"
SQ SEQUENCE 628 AA; 67854 MW; DB60FF893AE0C9DE CRC64;
MFYSEAILSK KGPLAKVWLA AHWEKKLSKV QTLHTSIEQS VHAIVTEETA PMALRLSGQL
MLGVVRIYSR KARYLLEDCT EALMRLKMSF QPGQVDMIEP ATALQSLKGK DAVTQSANLT
LPETITEFDL LVPDSTFDFQ WSQLLRTPSR SSNTLELHSL PISSSPSFPS SQLSIEAGRN
AQVESGFSLG ESFAHVGNDM QFHLPISNSG AATPRSVHSD NQSQISIEVG RDAPAAAATD
LSGIIGPQMT KSPASSVTHF STPSMLPIGG TSLDDELLAP VDDLNLDLGL DDLLGDEQGA
NAPAIEADEQ AETSSIHLPS DIMEDDSSRP AAAGVEEGQV VESATAPQQE KINPQKTVRR
QRAIIDPVTE LSSKQMKKQL ADTSSITSPL CLNTSSIVFN ATVNFTRNGK FNTSIFSSNL
NPKVNELLQA DFKQAILRKR KNESPEEVEP AKHQRTDTST ENQETAEVLD PEEIAAAELA
NITEAAIATL PQETVVQPEG EAPELGSPMG FPVTALESAD DSLFDAPPVM LDEADLLGSE
RLDSSVSEAL PSSQTAKDSL RNKWDPYTEG EKVSFQTLSA GCNREEAVQL FFDVLVLATK
DVISVKQDVA IQNEITLTAK RGMLLSSL
