SCC1_YEAST
ID SCC1_YEAST Reviewed; 566 AA.
AC Q12158; D6VRY5; Q05325;
DT 09-MAY-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 185.
DE RecName: Full=Sister chromatid cohesion protein 1;
GN Name=MCD1; Synonyms=PDS3, RHC21, SCC1; OrderedLocusNames=YDL003W;
GN ORFNames=YD8119.04;
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND SUBCELLULAR LOCATION.
RC STRAIN=ATCC 200060 / W303;
RX PubMed=9335333; DOI=10.1016/s0092-8674(01)80007-6;
RA Michaelis C., Ciosk R., Nasmyth K.;
RT "Cohesins: chromosomal proteins that prevent premature separation of sister
RT chromatids.";
RL Cell 91:35-45(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND SUBCELLULAR LOCATION.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9335334; DOI=10.1016/s0092-8674(01)80008-8;
RA Guacci V., Koshland D., Strunnikov A.V.;
RT "A direct link between sister chromatid cohesion and chromosome
RT condensation revealed through the analysis of MCD1 in S. cerevisiae.";
RL Cell 91:47-57(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169867;
RA Jacq C., Alt-Moerbe J., Andre B., Arnold W., Bahr A., Ballesta J.P.G.,
RA Bargues M., Baron L., Becker A., Biteau N., Bloecker H., Blugeon C.,
RA Boskovic J., Brandt P., Brueckner M., Buitrago M.J., Coster F.,
RA Delaveau T., del Rey F., Dujon B., Eide L.G., Garcia-Cantalejo J.M.,
RA Goffeau A., Gomez-Peris A., Granotier C., Hanemann V., Hankeln T.,
RA Hoheisel J.D., Jaeger W., Jimenez A., Jonniaux J.-L., Kraemer C.,
RA Kuester H., Laamanen P., Legros Y., Louis E.J., Moeller-Rieker S.,
RA Monnet A., Moro M., Mueller-Auer S., Nussbaumer B., Paricio N., Paulin L.,
RA Perea J., Perez-Alonso M., Perez-Ortin J.E., Pohl T.M., Prydz H.,
RA Purnelle B., Rasmussen S.W., Remacha M.A., Revuelta J.L., Rieger M.,
RA Salom D., Saluz H.P., Saiz J.E., Saren A.-M., Schaefer M., Scharfe M.,
RA Schmidt E.R., Schneider C., Scholler P., Schwarz S., Soler-Mira A.,
RA Urrestarazu L.A., Verhasselt P., Vissers S., Voet M., Volckaert G.,
RA Wagner G., Wambutt R., Wedler E., Wedler H., Woelfl S., Harris D.E.,
RA Bowman S., Brown D., Churcher C.M., Connor R., Dedman K., Gentles S.,
RA Hamlin N., Hunt S., Jones L., McDonald S., Murphy L.D., Niblett D.,
RA Odell C., Oliver K., Rajandream M.A., Richards C., Shore L., Walsh S.V.,
RA Barrell B.G., Dietrich F.S., Mulligan J.T., Allen E., Araujo R., Aviles E.,
RA Berno A., Carpenter J., Chen E., Cherry J.M., Chung E., Duncan M.,
RA Hunicke-Smith S., Hyman R.W., Komp C., Lashkari D., Lew H., Lin D.,
RA Mosedale D., Nakahara K., Namath A., Oefner P., Oh C., Petel F.X.,
RA Roberts D., Schramm S., Schroeder M., Shogren T., Shroff N., Winant A.,
RA Yelton M.A., Botstein D., Davis R.W., Johnston M., Andrews S., Brinkman R.,
RA Cooper J., Ding H., Du Z., Favello A., Fulton L., Gattung S., Greco T.,
RA Hallsworth K., Hawkins J., Hillier L.W., Jier M., Johnson D., Johnston L.,
RA Kirsten J., Kucaba T., Langston Y., Latreille P., Le T., Mardis E.,
RA Menezes S., Miller N., Nhan M., Pauley A., Peluso D., Rifkin L., Riles L.,
RA Taich A., Trevaskis E., Vignati D., Wilcox L., Wohldman P., Vaudin M.,
RA Wilson R., Waterston R., Albermann K., Hani J., Heumann K., Kleine K.,
RA Mewes H.-W., Zollner A., Zaccaria P.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome IV.";
RL Nature 387:75-78(1997).
RN [4]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=24374639; DOI=10.1534/g3.113.008995;
RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [5]
RP FUNCTION.
RX PubMed=9491073; DOI=10.1007/s004380050634;
RA Heo S.-J., Tatebayashi K., Kato J., Ikeda H.;
RT "The RHC21 gene of budding yeast, a homologue of the fission yeast rad21+
RT gene, is essential for chromosome segregation.";
RL Mol. Gen. Genet. 257:149-156(1998).
RN [6]
RP SUBCELLULAR LOCATION, INTERACTION WITH IRR1, IDENTIFICATION IN A COHESIN
RP COMPLEX WITH SMC1; SMC3 AND IRR1, AND INTERACTION OF THE COHESIN COMPLEX
RP WITH SCC2.
RX PubMed=9990856; DOI=10.1101/gad.13.3.320;
RA Toth A., Ciosk R., Uhlmann F., Galova M., Schleiffer A., Nasmyth K.;
RT "Yeast cohesin complex requires a conserved protein, Eco1p(Ctf7), to
RT establish cohesion between sister chromatids during DNA replication.";
RL Genes Dev. 13:320-333(1999).
RN [7]
RP CLEAVAGE BY ESP1, FUNCTION, AND MUTAGENESIS OF ARG-180 AND ARG-268.
RX PubMed=10403247; DOI=10.1038/21831;
RA Uhlmann F., Lottspeich F., Nasmyth K.;
RT "Sister-chromatid separation at anaphase onset is promoted by cleavage of
RT the cohesin subunit Scc1.";
RL Nature 400:37-42(1999).
RN [8]
RP PHOSPHORYLATION AT SER-175 AND SER-263 BY CDC5, AND MUTAGENESIS OF SER-175
RP AND SER-263.
RX PubMed=11371343; DOI=10.1016/s0092-8674(01)00362-2;
RA Alexandru G., Uhlmann F., Mechtler K., Poupart M.-A., Nasmyth K.;
RT "Phosphorylation of the cohesin subunit Scc1 by Polo/Cdc5 kinase regulates
RT sister chromatid separation in yeast.";
RL Cell 105:459-472(2001).
RN [9]
RP IDENTIFICATION IN A COHESIN COMPLEX WITH SMC1; SMC3 AND IRR1, AND
RP STRUCTURE.
RX PubMed=11983169; DOI=10.1016/s1097-2765(02)00515-4;
RA Haering C.H., Loewe J., Hochwagen A., Nasmyth K.;
RT "Molecular architecture of SMC proteins and the yeast cohesin complex.";
RL Mol. Cell 9:773-788(2002).
RN [10]
RP ACETYLATION AT LYS-210, AND MUTAGENESIS OF LYS-210; LYS-252; LYS-290;
RP LYS-310; LYS-319 AND LYS-324.
RX PubMed=11864574; DOI=10.1016/s0960-9822(02)00681-4;
RA Ivanov D., Schleiffer A., Eisenhaber F., Mechtler K., Haering C.H.,
RA Nasmyth K.;
RT "Eco1 is a novel acetyltransferase that can acetylate proteins involved in
RT cohesion.";
RL Curr. Biol. 12:323-328(2002).
RN [11]
RP LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX PubMed=14562106; DOI=10.1038/nature02046;
RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA O'Shea E.K., Weissman J.S.;
RT "Global analysis of protein expression in yeast.";
RL Nature 425:737-741(2003).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-161; SER-307 AND THR-354, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=18407956; DOI=10.1074/mcp.m700468-mcp200;
RA Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
RT "A multidimensional chromatography technology for in-depth phosphoproteome
RT analysis.";
RL Mol. Cell. Proteomics 7:1389-1396(2008).
RN [13]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19779198; DOI=10.1126/science.1172867;
RA Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.;
RT "Global analysis of Cdk1 substrate phosphorylation sites provides insights
RT into evolution.";
RL Science 325:1682-1686(2009).
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 ESP1 and dissociates from
CC chromatin, allowing sister chromatids to segregate.
CC {ECO:0000269|PubMed:10403247, ECO:0000269|PubMed:9335333,
CC ECO:0000269|PubMed:9335334, ECO:0000269|PubMed:9491073}.
CC -!- SUBUNIT: Interacts directly with IRR1/SCC3 in cohesin complex. Cohesin
CC complexes are composed of the SMC1 and SMC3 heterodimer attached via
CC their hinge domain, MCD1/SCC1 which link them, and IRR1, which
CC interacts with MCD1. The cohesin complex also interacts with SCC2,
CC which is required for its association with chromosomes.
CC {ECO:0000269|PubMed:11983169, ECO:0000269|PubMed:9990856}.
CC -!- INTERACTION:
CC Q12158; P40541: IRR1; NbExp=7; IntAct=EBI-16655, EBI-16667;
CC Q12158; P32908: SMC1; NbExp=9; IntAct=EBI-16655, EBI-17402;
CC Q12158; P47037: SMC3; NbExp=13; IntAct=EBI-16655, EBI-17423;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:9335333,
CC ECO:0000269|PubMed:9335334, ECO:0000269|PubMed:9990856}. Chromosome
CC {ECO:0000269|PubMed:9335333, ECO:0000269|PubMed:9990856}. Chromosome,
CC centromere {ECO:0000269|PubMed:9990856}. Note=Associates with
CC chromatin. Before prophase it is scattered along chromosome arms.
CC During prophase, most of cohesin complexes dissociate from chromatin
CC except at centromeres, where cohesin complexes remain. At anaphase, it
CC is cleaved by ESP1, leading to the dissociation of the complex from
CC chromosomes, allowing chromosome separation.
CC {ECO:0000269|PubMed:9990856}.
CC -!- DOMAIN: The C-terminal part associates with the head of SMC1, while the
CC N-terminal part binds to the head of SMC3.
CC -!- PTM: Cleaved by ESP1 at the onset of anaphase.
CC -!- PTM: Phosphorylated by CDC5/Polo-like kinase at the onset of anaphase.
CC Phosphorylation takes places at proximity to cleavage sites and is
CC required for an efficient cleavage by ESP1.
CC {ECO:0000269|PubMed:10403247, ECO:0000269|PubMed:11371343}.
CC -!- PTM: Acetylated by ECO1. {ECO:0000269|PubMed:11864574}.
CC -!- MISCELLANEOUS: Present with 1040 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the rad21 family. {ECO:0000305}.
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DR EMBL; Y14280; CAA74657.1; -; Genomic_DNA.
DR EMBL; U23759; AAB38803.1; -; Genomic_DNA.
DR EMBL; Z48008; CAA88058.1; -; Genomic_DNA.
DR EMBL; Z48432; CAA88356.1; -; Genomic_DNA.
DR EMBL; Z74051; CAA98559.1; -; Genomic_DNA.
DR EMBL; BK006938; DAA11845.1; -; Genomic_DNA.
DR PIR; S50979; S50979.
DR RefSeq; NP_010281.1; NM_001180062.1.
DR PDB; 1W1W; X-ray; 2.90 A; E/F/G/H=451-564.
DR PDB; 4UX3; X-ray; 3.30 A; B=1-115.
DR PDB; 5FRP; X-ray; 2.90 A; C/D=116-159.
DR PDB; 5FRS; X-ray; 4.07 A; C=126-142.
DR PDB; 6H8Q; X-ray; 3.63 A; G/H=301-400.
DR PDB; 6QPQ; X-ray; 2.10 A; B/D=1-566.
DR PDB; 6QPW; EM; 3.30 A; B=480-564, E=1-160.
DR PDB; 6ZZ6; EM; 3.40 A; C=67-555.
DR PDBsum; 1W1W; -.
DR PDBsum; 4UX3; -.
DR PDBsum; 5FRP; -.
DR PDBsum; 5FRS; -.
DR PDBsum; 6H8Q; -.
DR PDBsum; 6QPQ; -.
DR PDBsum; 6QPW; -.
DR PDBsum; 6ZZ6; -.
DR AlphaFoldDB; Q12158; -.
DR SMR; Q12158; -.
DR BioGRID; 32051; 359.
DR ComplexPortal; CPX-1867; Nuclear mitotic cohesin complex.
DR DIP; DIP-5812N; -.
DR ELM; Q12158; -.
DR IntAct; Q12158; 48.
DR MINT; Q12158; -.
DR STRING; 4932.YDL003W; -.
DR iPTMnet; Q12158; -.
DR MaxQB; Q12158; -.
DR PaxDb; Q12158; -.
DR PRIDE; Q12158; -.
DR TopDownProteomics; Q12158; -.
DR EnsemblFungi; YDL003W_mRNA; YDL003W; YDL003W.
DR GeneID; 851561; -.
DR KEGG; sce:YDL003W; -.
DR SGD; S000002161; MCD1.
DR VEuPathDB; FungiDB:YDL003W; -.
DR eggNOG; KOG1213; Eukaryota.
DR GeneTree; ENSGT00940000170664; -.
DR HOGENOM; CLU_462364_0_0_1; -.
DR InParanoid; Q12158; -.
DR OMA; QIWLASN; -.
DR BioCyc; YEAST:G3O-29434-MON; -.
DR Reactome; R-SCE-2468052; Establishment of Sister Chromatid Cohesion.
DR Reactome; R-SCE-2500257; Resolution of Sister Chromatid Cohesion.
DR Reactome; R-SCE-3108214; SUMOylation of DNA damage response and repair proteins.
DR EvolutionaryTrace; Q12158; -.
DR PRO; PR:Q12158; -.
DR Proteomes; UP000002311; Chromosome IV.
DR RNAct; Q12158; protein.
DR GO; GO:0000775; C:chromosome, centromeric region; IEA:UniProtKB-SubCell.
DR GO; GO:0008278; C:cohesin complex; IBA:GO_Central.
DR GO; GO:0000794; C:condensed nuclear chromosome; IDA:SGD.
DR GO; GO:0005739; C:mitochondrion; IDA:SGD.
DR GO; GO:0034990; C:nuclear mitotic cohesin complex; IDA:SGD.
DR GO; GO:0005634; C:nucleus; IDA:SGD.
DR GO; GO:0003682; F:chromatin binding; IDA:SGD.
DR GO; GO:0019901; F:protein kinase binding; IPI:SGD.
DR GO; GO:0006915; P:apoptotic process; IMP:SGD.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0006974; P:cellular response to DNA damage stimulus; IMP:SGD.
DR GO; GO:0006302; P:double-strand break repair; IMP:SGD.
DR GO; GO:0034087; P:establishment of mitotic sister chromatid cohesion; IMP:SGD.
DR GO; GO:0007076; P:mitotic chromosome condensation; IMP:SGD.
DR GO; GO:0007064; P:mitotic sister chromatid cohesion; IBA:GO_Central.
DR GO; GO:0006473; P:protein acetylation; IDA:UniProtKB.
DR GO; GO:1990414; P:replication-born double-strand break repair via sister chromatid exchange; IMP:SGD.
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; 2.
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; Acetylation; Cell cycle; Cell division; Centromere;
KW Chromosome; Chromosome partition; Mitosis; Nucleus; Phosphoprotein;
KW Reference proteome.
FT CHAIN 1..566
FT /note="Sister chromatid cohesion protein 1"
FT /id="PRO_0000097881"
FT REGION 325..356
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 180..181
FT /note="Cleavage; by ESP1"
FT SITE 268..269
FT /note="Cleavage; by ESP1"
FT MOD_RES 161
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956"
FT MOD_RES 175
FT /note="Phosphoserine; by CDC5"
FT /evidence="ECO:0000269|PubMed:11371343"
FT MOD_RES 210
FT /note="N6-acetyllysine; by ECO1"
FT /evidence="ECO:0000269|PubMed:11864574"
FT MOD_RES 263
FT /note="Phosphoserine; by CDC5"
FT /evidence="ECO:0000269|PubMed:11371343"
FT MOD_RES 307
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956"
FT MOD_RES 354
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18407956"
FT MUTAGEN 175
FT /note="S->A: Reduces phosphorylation. Abolishes
FT phosphorylation; when associated with A-263."
FT /evidence="ECO:0000269|PubMed:11371343"
FT MUTAGEN 180
FT /note="R->D: Abolishes cleavage by ESP1; when associated
FT with D-268."
FT /evidence="ECO:0000269|PubMed:10403247"
FT MUTAGEN 210
FT /note="K->R: Loss of acetylation by ECO1."
FT /evidence="ECO:0000269|PubMed:11864574"
FT MUTAGEN 252
FT /note="K->R: No effect on acetylation by ECO1."
FT /evidence="ECO:0000269|PubMed:11864574"
FT MUTAGEN 263
FT /note="S->A: Reduces phosphorylation. Abolishes
FT phosphorylation; when associated with A-175."
FT /evidence="ECO:0000269|PubMed:11371343"
FT MUTAGEN 268
FT /note="R->D: Abolishes first cleavage by ESP1. Abolishes
FT all cleavage by ESP1; when associated with D-180."
FT /evidence="ECO:0000269|PubMed:10403247"
FT MUTAGEN 290
FT /note="K->R: No effect on acetylation by ECO1."
FT /evidence="ECO:0000269|PubMed:11864574"
FT MUTAGEN 310
FT /note="K->R: No effect on acetylation by ECO1."
FT /evidence="ECO:0000269|PubMed:11864574"
FT MUTAGEN 319
FT /note="K->R: No effect on acetylation by ECO1."
FT /evidence="ECO:0000269|PubMed:11864574"
FT MUTAGEN 324
FT /note="K->R: No effect on acetylation by ECO1."
FT /evidence="ECO:0000269|PubMed:11864574"
FT HELIX 26..28
FT /evidence="ECO:0007829|PDB:4UX3"
FT HELIX 44..51
FT /evidence="ECO:0007829|PDB:4UX3"
FT TURN 52..54
FT /evidence="ECO:0007829|PDB:4UX3"
FT STRAND 56..58
FT /evidence="ECO:0007829|PDB:4UX3"
FT HELIX 69..100
FT /evidence="ECO:0007829|PDB:4UX3"
FT STRAND 134..138
FT /evidence="ECO:0007829|PDB:5FRP"
FT HELIX 484..498
FT /evidence="ECO:0007829|PDB:6QPQ"
FT STRAND 499..503
FT /evidence="ECO:0007829|PDB:6QPQ"
FT HELIX 504..512
FT /evidence="ECO:0007829|PDB:6QPQ"
FT HELIX 516..518
FT /evidence="ECO:0007829|PDB:6QPQ"
FT HELIX 521..536
FT /evidence="ECO:0007829|PDB:6QPQ"
FT STRAND 539..543
FT /evidence="ECO:0007829|PDB:6QPQ"
FT STRAND 546..548
FT /evidence="ECO:0007829|PDB:6ZZ6"
FT STRAND 552..555
FT /evidence="ECO:0007829|PDB:6QPQ"
FT HELIX 557..560
FT /evidence="ECO:0007829|PDB:6QPQ"
SQ SEQUENCE 566 AA; 63290 MW; EB6C7CA33BAC208F CRC64;
MVTENPQRLT VLRLATNKGP LAQIWLASNM SNIPRGSVIQ THIAESAKEI AKASGCDDES
GDNEYITLRT SGELLQGIVR VYSKQATFLL TDIKDTLTKI SMLFKTSQKM TSTVNRLNTV
TRVHQLMLED AVTEREVLVT PGLEFLDDTT IPVGLMAQEN SMERKVQGAA PWDTSLEVGR
RFSPDEDFEH NNLSSMNLDF DIEEGPITSK SWEEGTRQSS RNFDTHENYI QDDDFPLDDA
GTIGWDLGIT EKNDQNNDDD DNSVEQGRRL GESIMSEEPT DFGFDLDIEK EAPAGNIDTI
TDAMTESQPK QTGTRRNSKL LNTKSIQIDE ETENSESIAS SNTYKEERSN NLLTPQPTNF
TTKRLWSEIT ESMSYLPDPI LKNFLSYESL KKRKIHNGRE GSIEEPELNV SLNLTDDVIS
NAGTNDNSFN ELTDNMSDFV PIDAGLNEAP FPEENIIDAK TRNEQTTIQT EKVRPTPGEV
ASKAIVQMAK ILRKELSEEK EVIFTDVLKS QANTEPENIT KREASRGFFD ILSLATEGCI
GLSQTEAFGN IKIDAKPALF ERFINA
