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 01-MAY-2007, entry version 52. DE Cohesin subunit psc3 (SCC3 homolog). GN Name=psc3; ORFNames=SPAC17H9.20, SPAC607.01; OS Schizosaccharomyces pombe (Fission yeast). OC Eukaryota; Fungi; Ascomycota; Schizosaccharomycetes; OC Schizosaccharomycetales; Schizosaccharomycetaceae; OC Schizosaccharomyces. OX NCBI_TaxID=4896; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND SUBCELLULAR LOCATION. RX MEDLINE=20523814; PubMed=11069892; DOI=10.1101/gad.832000; RA Tomonaga T., Nagao K., Kawasaki Y., Furuya K., Murakami A., RA Morishita J., Yuasa T., Sutani T., Kearsey S.E., Uhlmann F., RA Nasmyth K., Yanagida M.; RT "Characterization of fission yeast cohesin: essential anaphase RT proteolysis 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=ATCC 38366 / 972; RX MEDLINE=21848401; 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., RA Collins M., Connor R., Cronin A., Davis P., Feltwell T., Fraser A., RA Gentles S., Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., RA Holroyd S., Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., RA James K.D., Jones L., Jones M., Leather S., McDonald S., McLean J., RA Mooney P., Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., RA Oliver K., O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., RA Rutherford K.M., Rutter S., Saunders D., Seeger K., Sharp S., RA Skelton J., Simmonds M.N., Squares R., Squares S., Stevens K., RA Taylor K., Taylor R.G., Tivey A., Walsh S.V., Warren T., Whitehead S., RA Woodward J.R., Volckaert G., Aert R., Robben J., Grymonprez B., RA Weltjens I., Vanstreels E., Rieger M., Schaefer M., Mueller-Auer S., RA Gabel C., Fuchs M., Duesterhoeft A., Fritzc C., Holzer E., Moestl D., RA Hilbert H., Borzym K., Langer I., Beck A., Lehrach H., Reinhardt R., RA Pohl T.M., Eger P., Zimmermann W., Wedler H., Wambutt R., Purnelle B., RA Goffeau A., Cadieu E., Dreano S., Gloux S., Lelaure V., Mottier S., RA Galibert F., Aves S.J., Xiang Z., Hunt C., Moore K., Hurst S.M., RA Lucas M., Rochet M., Gaillardin C., Tallada V.A., Garzon A., Thode G., RA Daga R.R., Cruzado L., Jimenez J., Sanchez M., del Rey F., Benito J., RA Dominguez A., Revuelta J.L., Moreno S., Armstrong J., Forsburg S.L., RA Cerutti L., Lowe T., McCombie W.R., Paulsen I., Potashkin J., RA Shpakovski G.V., Ussery D., Barrell B.G., 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 MEDLINE=21638697; 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 RT fission 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 CC sister chromatids can be trapped. At anaphase, the rad21 subunit CC of the cohesin complex is cleaved and dissociates from chromatin, CC allowing sister chromatids to segregate. The cohesin complex may CC also play a role in spindle pole assembly during mitosis. CC -!- SUBUNIT: Cohesin complexes are composed of the psm1/smc1 and CC psm3/smc3 heterodimer attached via their hinge domain, rad21/scc1 CC which link them, and psc3/scc3, which interacts with rad21. CC Interacts with swi6 (By similarity). The interaction with swi6 may CC contribute to recruit cohesin complex to heterochromatin. CC -!- SUBCELLULAR LOCATION: Nucleus. Note=Associates with chromatin. CC Cohesin complex mainly associates with broad centromere region. CC Also associates with mating-type heterochromatic region. CC -!- SIMILARITY: Belongs to the SCC3 family. CC -!- SIMILARITY: Contains 1 SCD (stromalin conservative) domain. 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; Z98597; CAJ41421.1; -; Genomic_DNA. DR EMBL; AL135751; CAB63788.1; -; Genomic_DNA. DR PIR; T37885; T50221. DR IntAct; O13816; -. DR KEGG; spo:SPAC17H9.20-1; -. DR KEGG; spo:SPAC17H9.20-2; -. DR GeneDB_Spombe; SPAC17H9.20; -. DR BioCyc; SPOM-XXX-01:SPOM-XXX-01-001943-MONOMER; -. DR ArrayExpress; O13816; -. DR GO; GO:0030892; C:mitotic cohesin complex; IDA:GeneDB_SPombe. DR GO; GO:0005634; C:nucleus; IDA:GeneDB_SPombe. DR GO; GO:0007064; P:mitotic sister chromatid cohesion; IMP:GeneDB_SPombe. DR InterPro; IPR013721; STAG. DR Pfam; PF08514; STAG; 1. KW Cell cycle; Cell division; Chromosome partition; Coiled coil; KW Complete proteome; Mitosis; Nuclear protein. FT CHAIN 1 962 Cohesin subunit psc3. FT /FTId=PRO_0000120192. FT DOMAIN 300 379 SCD. FT COILED 236 275 Potential. FT COMPBIAS 31 38 Poly-Ser. 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 //