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 08-NOV-2023, entry version 158. 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}. 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; 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 iPTMnet; O13816; -. DR MaxQB; O13816; -. DR PaxDb; 4896-SPAC17H9-20-1; -. 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-2467813; Separation of Sister Chromatids. 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:0000794; C:condensed nuclear chromosome; IC:PomBase. DR GO; GO:0031934; C:mating-type region heterochromatin; IDA:PomBase. DR GO; GO:0030892; C: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:0007059; P:chromosome segregation; IEA:UniProtKB-KW. DR GO; GO:0007064; P:mitotic sister chromatid cohesion; IDA:PomBase. DR GO; GO:0007062; P:sister chromatid cohesion; IBA:GO_Central. DR Gene3D; 1.25.10.10; Leucine-rich Repeat Variant; 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:SF0; LD34181P-RELATED; 1. DR PANTHER; PTHR11199; STROMAL ANTIGEN; 1. DR Pfam; PF08514; STAG; 1. DR SUPFAM; SSF48371; ARM repeat; 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 //