SCC3_SCHPO
ID SCC3_SCHPO Reviewed; 962 AA.
AC O13816; Q38G50; Q9US16;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 16-MAY-2006, sequence version 3.
DT 25-MAY-2022, entry version 153.
DE RecName: Full=Cohesin subunit psc3;
DE AltName: Full=SCC3 homolog;
GN Name=psc3; ORFNames=SPAC17H9.20, SPAC607.01;
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], FUNCTION, AND SUBCELLULAR LOCATION.
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 [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 SEQUENCE REVISION.
RA Skelton J., Churcher C.M., Barrell B.G., Rajandream M.A., Wood V.;
RL Submitted (OCT-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP INTERACTION WITH SWI6.
RX PubMed=11780129; DOI=10.1038/ncb739;
RA Nonaka N., Kitajima T., Yokobayashi S., Xiao G., Yamamoto M.,
RA Grewal S.I.S., Watanabe Y.;
RT "Recruitment of cohesin to heterochromatic regions by Swi6/HP1 in fission
RT yeast.";
RL Nat. Cell Biol. 4:89-93(2002).
RN [5]
RP IDENTIFICATION OF INTRON.
RX PubMed=16207082; DOI=10.1515/bc.2005.072;
RA Ilyushik E., Pryce D.W., Walerych D., Riddell T., Wakeman J.A.,
RA McInerny C.J., McFarlane R.J.;
RT "Psc3 cohesin of Schizosaccharomyces pombe: cell cycle analysis and
RT identification of three distinct isoforms.";
RL Biol. Chem. 386:613-621(2005).
CC -!- FUNCTION: Component of cohesin complex, a complex required for the
CC cohesion of sister chromatids after DNA replication. The cohesin
CC complex apparently forms a large proteinaceous ring within which sister
CC chromatids can be trapped. At anaphase, the rad21 subunit of the
CC cohesin complex is cleaved and dissociates from chromatin, allowing
CC sister chromatids to segregate. The cohesin complex may also play a
CC role in spindle pole assembly during mitosis.
CC {ECO:0000269|PubMed:11069892}.
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 swi6
CC (By similarity). The interaction with swi6 may contribute to recruit
CC cohesin complex to heterochromatin. {ECO:0000250,
CC ECO:0000269|PubMed:11780129}.
CC -!- INTERACTION:
CC O13816; Q09725: mis4; NbExp=2; IntAct=EBI-1131314, EBI-16083239;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00750,
CC ECO:0000269|PubMed:11069892}. Chromosome, centromere
CC {ECO:0000269|PubMed:11069892}. Note=Associates with chromatin. Cohesin
CC complex mainly associates with broad centromere region. Also associates
CC with mating-type heterochromatic region.
CC -!- SIMILARITY: Belongs to the SCC3 family. {ECO:0000305}.
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DR EMBL; CU329670; CAJ41421.1; -; Genomic_DNA.
DR PIR; T37885; T50221.
DR RefSeq; XP_001713063.1; XM_001713011.2.
DR AlphaFoldDB; O13816; -.
DR SMR; O13816; -.
DR BioGRID; 278851; 14.
DR DIP; DIP-37866N; -.
DR IntAct; O13816; 3.
DR STRING; 4896.SPAC17H9.20.1; -.
DR MaxQB; O13816; -.
DR PaxDb; O13816; -.
DR EnsemblFungi; SPAC17H9.20.1; SPAC17H9.20.1:pep; SPAC17H9.20.
DR PomBase; SPAC17H9.20; psc3.
DR VEuPathDB; FungiDB:SPAC17H9.20; -.
DR eggNOG; KOG2011; Eukaryota.
DR HOGENOM; CLU_309524_0_0_1; -.
DR InParanoid; O13816; -.
DR OMA; TMRPIRH; -.
DR PhylomeDB; O13816; -.
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:O13816; -.
DR Proteomes; UP000002485; Chromosome I.
DR GO; GO:0000785; C:chromatin; IBA:GO_Central.
DR GO; GO:0099115; C:chromosome, subtelomeric region; IDA:PomBase.
DR GO; GO:0008278; C:cohesin complex; IBA:GO_Central.
DR GO; GO:0031934; C:mating-type region heterochromatin; 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; HDA:PomBase.
DR GO; GO:0005721; C:pericentric heterochromatin; IDA:PomBase.
DR GO; GO:0003682; F:chromatin binding; IBA:GO_Central.
DR GO; GO:0003677; F:DNA binding; IDA:PomBase.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0140588; P:chromatin looping; IDA:PomBase.
DR GO; GO:0061780; P:mitotic cohesin loading; IDA:PomBase.
DR GO; GO:0007064; P:mitotic sister chromatid cohesion; IMP:PomBase.
DR GO; GO:0007062; P:sister chromatid cohesion; IBA:GO_Central.
DR Gene3D; 1.25.10.10; -; 1.
DR InterPro; IPR011989; ARM-like.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR039662; Cohesin_Scc3/SA.
DR InterPro; IPR020839; SCD.
DR InterPro; IPR013721; STAG.
DR PANTHER; PTHR11199; PTHR11199; 1.
DR Pfam; PF08514; STAG; 1.
DR SUPFAM; SSF48371; SSF48371; 1.
DR PROSITE; PS51425; SCD; 1.
PE 1: Evidence at protein level;
KW Cell cycle; Cell division; Centromere; Chromosome; Chromosome partition;
KW Coiled coil; Mitosis; Nucleus; Reference proteome.
FT CHAIN 1..962
FT /note="Cohesin subunit psc3"
FT /id="PRO_0000120192"
FT DOMAIN 297..382
FT /note="SCD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00750"
FT REGION 1..72
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 236..275
FT /evidence="ECO:0000255"
FT COMPBIAS 19..39
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 962 AA; 110652 MW; F45C2C2A2E0443CC CRC64;
MSESVTTGSD DDGGDRESSP VMLSQSFDPM SSSSNSSSEE NSDDDYEKTI SSKKRHPRPN
SKGVNVKRSR RNAIVEEDPQ EEIFNNLFAF LLDQKVDTMD IAVSWFADYA KDNQSALANL
INFILKCCGC NRAINVFDVQ DQDSASATLS QIQLSVERTS TRDYPLNSKN LKFRNFRKRL
TGLLSNFVSQ LSIRNYLYNS TVFEDIMSWV VAMSSSTMRP IRHTATVFCL NIMTFLCEKS
KELLNEHAIA TKQLEKEEKR SRVNRNRINE LNNSLGEIVK QQDTLTTYLN DYFDSVFVHR
YRDVEPKIRV DCLQELGVWI NTVPSIFFSG SYLRYLGWML SDINTTVRLT VVKVLRKFFE
TDSFIGGLRH FSSRFKERIL EMSCVDADIG VRVASIRLCN AMRTCGFLEN SEILKVLKLI
LDINPRVQRE AVLFLCKVVD ESVNEKIDLW GEEDYILKAF SQTSLTTFSV HWIKFSQMCK
LLEEVRLSYQ SSFDYDTLLR IFQKNGNFIT PITQALLNAC EIDSIYQSWE DISNFVLFDN
YTSTLKDPID SILSFCKLND FQESILLQLL SASIQTVCNN NFITPKTVHN KQAAETTNDQ
NKDKDLLYLN LLPYINSITE RNSASPTLLH DSLRLLFSMD LTEMTDPQLS RHFELLINNL
KKFFLTNNDL QIIQGCTILF LRLDSIPALK EDLKLLVTDI CDQTVTEFLK NFGSFNIQDA
VITKDEFVIF EACLTRIEGC TSLKDFSDYP EFDIIYERLV SLLSRVPNSY EDTLKFSAIN
TLQSLLFWFF LRKDNPADEE KKKDDETKVF NCLINIMNND SSKILQLQAA RTFLETVIMK
EGVKASHYND DNRVSEEHNF LKPQFLDALL KILEGWLYTY AKVGQFPFKR LTQASSPHTQ
ISLDKNPLNR RLLEHVCCDL TSKLLIVVSL SNTITPEFSQ QFCELRGHYG PKLSAIVDEF
LN
