ID SCC3_SCHPO STANDARD; PRT; 978 AA. AC O13816; Q9US16; DT 15-JUL-1998 (Rel. 36, Created) DT 16-OCT-2001 (Rel. 40, Last sequence update) DT 15-SEP-2003 (Rel. 42, Last annotation update) DE Cohesin subunit psc3 (SCC3 homolog). GN PSC3 OR SPAC17H9.20 OR SPAC607.01. OS Schizosaccharomyces pombe (Fission yeast). OC Eukaryota; Fungi; Ascomycota; Schizosaccharomycetes; OC Schizosaccharomycetales; Schizosaccharomycetaceae; OC Schizosaccharomyces. OX NCBI_TaxID=4896; RN [1] RP SEQUENCE FROM N.A., FUNCTION, AND SUBCELLULAR LOCATION. RX MEDLINE=20523814; PubMed=11069892; 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 SEQUENCE FROM N.A. RC STRAIN=972; RX MEDLINE=21848401; PubMed=11859360; RA Wood V., Gwilliam R., Rajandream M.A., Lyne M., Lyne R., Stewart A., RA Sgouros J., Peat N., Hayles J., Baker S., 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., Hidalgo J., Hodgson G., RA Holroyd S., Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., RA James K., Jones L., Jones M., Leather S., McDonald S., McLean J., RA Mooney P., Moule S., Mungall K., Murphy L., Niblett D., Odell C., RA Oliver K., O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., RA Rutherford K., Rutter S., Saunders D., Seeger K., Sharp S., RA Skelton J., Simmonds M., Squares R., Squares S., Stevens K., RA Taylor K., Taylor R.G., Tivey A., Walsh S.V., Warren T., Whitehead S., RA Woodward J., 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., Fritzc C., Holzer E., Moestl D., Hilbert H., RA Borzym K., Langer I., Beck A., Lehrach H., Reinhardt R., Pohl T.M., RA 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 Cerrutti 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 INTERACTION WITH SWI6. RX MEDLINE=21638697; PubMed=11780129; 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). 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: Nuclear protein. 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; CAB11229.1; -. DR EMBL; AL135751; CAB63788.1; -. DR PIR; T37885; T50221. DR GeneDB_SPombe; SPAC17H9.20; -. DR InterPro; IPR005032; STAG. DR Pfam; PF03365; STAG; 1. KW Mitosis; Cell cycle; Chromosome partition; Coiled coil; KW Nuclear protein. FT DOMAIN 313 398 SCD. FT DOMAIN 249 294 COILED COIL (POTENTIAL). FT DOMAIN 31 38 POLY-SER. SQ SEQUENCE 978 AA; 112537 MW; 2B0800281763A7D4 CRC64; MSESVTTGSD DDGGDRESSP VMLSQSFDPM SSSSNSSSEE NSDDDYEKTI SSKKRHPRPN SKGVNVKRSR RNAIVEEDPQ EEIFNNLFAF LLDQKVDTMD IAVSWFADYA KDNQSALANL INFILKCCGC NRAINVFDVQ DQDSASATLS QIQLSVERVS AFAKILYLYI NNFKTSTRDY PLNSKNLKFR NFRKRLTGLL SNFVSQLSIR NYLYNSTVFE DIMSWVVAMS SSTMRPIRHT ATVFCLNIMT FLCEKSKELL NEHAIATKQL EKEEKRSRVN RNRINELNNS LGEIVKQQDT LTTYLNDYFD SVFVHRYRDV EPKIRVDCLQ ELGVWINTVP SIFFSGSYLR YLGWMLSDIN TTVRLTVVKV LRKFFETDSF IGGLRHFSSR FKERILEMSC VDADIGVRVA SIRLCNAMRT CGFLENSEIL KVLKLILDIN PRVQREAVLF LCKVVDESVN EKIDLWGEED YILKAFSQTS LTTFSVHWIK FSQMCKLLEE VRLSYQSSFD YDTLLRIFQK NGNFITPITQ ALLNACEIDS IYQSWEDISN FVLFDNYTST LKDPIDSILS FCKLNDFQES ILLQLLSASI QTVCNNNFIT PKTVHNKQAA ETTNDQNKDK DLLYLNLLPY INSITERNSA SPTLLHDSLR LLFSMDLTEM TDPQLSRHFE LLINNLKKFF LTNNDLQIIQ GCTILFLRLD SIPALKEDLK LLVTDICDQT VTEFLKNFGS FNIQDAVITK DEFVIFEACL TRIEGCTSLK DFSDYPEFDI IYERLVSLLS RVPNSYEDTL KFSAINTLQS LLFWFFLRKD NPADEEKKKD DETKVFNCLI NIMNNDSSKI LQLQAARTFL ETVIMKEGVK ASHYNDDNRV SEEHNFLKPQ FLDALLKILE GWLYTYAKVG QFPFKRLTQA SSPHTQISLD KNPLNRRLLE HVCCDLTSKL LIVVSLSNTI TPEFSQQFCE LRGHYGPKLS AIVDEFLN //