SMC3_YEAST
ID SMC3_YEAST Reviewed; 1230 AA.
AC P47037; D6VWA9;
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1996, sequence version 1.
DT 03-AUG-2022, entry version 194.
DE RecName: Full=Structural maintenance of chromosomes protein 3;
DE AltName: Full=DA-box protein SMC3;
GN Name=SMC3; OrderedLocusNames=YJL074C; ORFNames=J1049;
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].
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 [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=8641269; DOI=10.1002/j.1460-2075.1996.tb00557.x;
RA Galibert F., Alexandraki D., Baur A., Boles E., Chalwatzis N., Chuat J.-C.,
RA Coster F., Cziepluch C., de Haan M., Domdey H., Durand P., Entian K.-D.,
RA Gatius M., Goffeau A., Grivell L.A., Hennemann A., Herbert C.J.,
RA Heumann K., Hilger F., Hollenberg C.P., Huang M.-E., Jacq C.,
RA Jauniaux J.-C., Katsoulou C., Kirchrath L., Kleine K., Kordes E.,
RA Koetter P., Liebl S., Louis E.J., Manus V., Mewes H.-W., Miosga T.,
RA Obermaier B., Perea J., Pohl T.M., Portetelle D., Pujol A., Purnelle B.,
RA Ramezani Rad M., Rasmussen S.W., Rose M., Rossau R.,
RA Schaaff-Gerstenschlaeger I., Smits P.H.M., Scarcez T., Soriano N.,
RA To Van D., Tzermia M., Van Broekhoven A., Vandenbol M., Wedler H.,
RA von Wettstein D., Wambutt R., Zagulski M., Zollner A., Karpfinger-Hartl L.;
RT "Complete nucleotide sequence of Saccharomyces cerevisiae chromosome X.";
RL EMBO J. 15:2031-2049(1996).
RN [3]
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 [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=S288c / FY1678;
RA Sor F.J.;
RL Submitted (JUN-1995) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP IDENTIFICATION IN A COHESIN COMPLEX WITH SMC1; IRR1 AND MCD1, AND
RP INTERACTION OF THE COHESIN COMPLEX 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 [6]
RP IDENTIFICATION IN A COHESIN COMPLEX WITH SMC3; MCD1 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 [7]
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 [8]
RP ACETYLATION AT LYS-112 AND LYS-113.
RX PubMed=18614053; DOI=10.1016/j.molcel.2008.06.006;
RA Zhang J., Shi X., Li Y., Kim B.J., Jia J., Huang Z., Yang T., Fu X.,
RA Jung S.Y., Wang Y., Zhang P., Kim S.T., Pan X., Qin J.;
RT "Acetylation of Smc3 by Eco1 is required for S phase sister chromatid
RT cohesion in both human and yeast.";
RL Mol. Cell 31:143-151(2008).
CC -!- FUNCTION: Involved in chromosome cohesion during cell cycle and in DNA
CC repair. Central component of cohesin complex. The cohesin complex is
CC required for the cohesion of sister chromatids after DNA replication.
CC The cohesin complex apparently forms a large proteinaceous ring within
CC which sister chromatids can be trapped. At anaphase, the complex is
CC cleaved and dissociates from chromatin, allowing sister chromatids to
CC segregate.
CC -!- SUBUNIT: Cohesin complexes are composed of the SMC1 and SMC3
CC heterodimer attached via their SMC hinge domain, MCD1/SCC1 which link
CC them, and IRR1/SCC3, which interacts with MCD1. The cohesin complex
CC also interacts with SCC2, which is required for its association with
CC chromosomes. {ECO:0000269|PubMed:11983169, ECO:0000269|PubMed:9990856}.
CC -!- INTERACTION:
CC P47037; Q12158: MCD1; NbExp=13; IntAct=EBI-17423, EBI-16655;
CC P47037; Q99359: RAD61; NbExp=9; IntAct=EBI-17423, EBI-2082336;
CC P47037; P32908: SMC1; NbExp=19; IntAct=EBI-17423, EBI-17402;
CC P47037; P47037: SMC3; NbExp=4; IntAct=EBI-17423, EBI-17423;
CC -!- SUBCELLULAR LOCATION: Nucleus. Chromosome. Note=Associates with
CC chromatin. Before prophase it is scattered along chromosome arms. At
CC anaphase, the MCD1 subunit of the cohesin complex is cleaved, leading
CC to the dissociation of the complex from chromosomes, allowing
CC chromosome separation.
CC -!- DOMAIN: The flexible SMC hinge domain, which separates the large
CC intramolecular coiled coil regions, allows the heterotypic interaction
CC with the corresponding domain of SMC1, forming a V-shaped heterodimer.
CC The two heads of the heterodimer are then connected by different ends
CC of the cleavable MCD1 protein, forming a ring structure (By
CC similarity). {ECO:0000250}.
CC -!- PTM: Acetylation at Lys-112 and Lys-113 by ECO1 is important for genome
CC stability and S phase sister chromatid cohesion.
CC {ECO:0000269|PubMed:18614053}.
CC -!- MISCELLANEOUS: Present with 2660 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the SMC family. SMC3 subfamily. {ECO:0000305}.
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DR EMBL; Y14278; CAA74655.1; -; Genomic_DNA.
DR EMBL; Z49349; CAA89366.1; -; Genomic_DNA.
DR EMBL; X88851; CAA61313.1; -; Genomic_DNA.
DR EMBL; BK006943; DAA08725.1; -; Genomic_DNA.
DR PIR; S56850; S56850.
DR RefSeq; NP_012461.1; NM_001181507.1.
DR PDB; 4UX3; X-ray; 3.30 A; A=2-261, A=970-1230.
DR PDB; 6QPW; EM; 3.30 A; C=2-261, C=970-1230.
DR PDB; 6ZZ6; EM; 3.40 A; B=2-1222.
DR PDB; 7OGT; EM; 5.50 A; B=1-1230.
DR PDBsum; 4UX3; -.
DR PDBsum; 6QPW; -.
DR PDBsum; 6ZZ6; -.
DR PDBsum; 7OGT; -.
DR AlphaFoldDB; P47037; -.
DR SMR; P47037; -.
DR BioGRID; 33681; 512.
DR ComplexPortal; CPX-1408; Nuclear meiotic cohesin complex.
DR ComplexPortal; CPX-1867; Nuclear mitotic cohesin complex.
DR DIP; DIP-2991N; -.
DR IntAct; P47037; 57.
DR MINT; P47037; -.
DR STRING; 4932.YJL074C; -.
DR iPTMnet; P47037; -.
DR MaxQB; P47037; -.
DR PaxDb; P47037; -.
DR PRIDE; P47037; -.
DR EnsemblFungi; YJL074C_mRNA; YJL074C; YJL074C.
DR GeneID; 853371; -.
DR KEGG; sce:YJL074C; -.
DR SGD; S000003610; SMC3.
DR VEuPathDB; FungiDB:YJL074C; -.
DR eggNOG; KOG0964; Eukaryota.
DR GeneTree; ENSGT00940000169262; -.
DR HOGENOM; CLU_001042_5_0_1; -.
DR InParanoid; P47037; -.
DR OMA; DQHQSMR; -.
DR BioCyc; YEAST:G3O-31532-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 PRO; PR:P47037; -.
DR Proteomes; UP000002311; Chromosome X.
DR RNAct; P47037; protein.
DR GO; GO:0034991; C:nuclear meiotic cohesin complex; IC:ComplexPortal.
DR GO; GO:0034990; C:nuclear mitotic cohesin complex; IDA:SGD.
DR GO; GO:0005634; C:nucleus; IDA:SGD.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0061775; F:cohesin loading activity; IBA:GO_Central.
DR GO; GO:0003690; F:double-stranded DNA binding; IBA:GO_Central.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0019901; F:protein kinase binding; IPI:SGD.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0034089; P:establishment of meiotic sister chromatid cohesion; IC:ComplexPortal.
DR GO; GO:0034087; P:establishment of mitotic sister chromatid cohesion; IC:ComplexPortal.
DR GO; GO:0051177; P:meiotic sister chromatid cohesion; IMP:SGD.
DR GO; GO:0007064; P:mitotic sister chromatid cohesion; IGI:SGD.
DR GO; GO:0007131; P:reciprocal meiotic recombination; IMP:SGD.
DR GO; GO:1990414; P:replication-born double-strand break repair via sister chromatid exchange; IMP:SGD.
DR GO; GO:0007130; P:synaptonemal complex assembly; IMP:SGD.
DR CDD; cd03272; ABC_SMC3_euk; 1.
DR Gene3D; 3.40.50.300; -; 2.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR003395; RecF/RecN/SMC_N.
DR InterPro; IPR024704; SMC.
DR InterPro; IPR041741; SMC3_ABC_euk.
DR InterPro; IPR010935; SMC_hinge.
DR InterPro; IPR036277; SMC_hinge_sf.
DR Pfam; PF06470; SMC_hinge; 1.
DR Pfam; PF02463; SMC_N; 1.
DR PIRSF; PIRSF005719; SMC; 1.
DR SMART; SM00968; SMC_hinge; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR SUPFAM; SSF75553; SSF75553; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; ATP-binding; Cell cycle; Cell division;
KW Chromosome; Coiled coil; Mitosis; Nucleotide-binding; Nucleus;
KW Reference proteome.
FT CHAIN 1..1230
FT /note="Structural maintenance of chromosomes protein 3"
FT /id="PRO_0000119015"
FT DOMAIN 535..651
FT /note="SMC hinge"
FT REGION 1078..1097
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 172..482
FT /evidence="ECO:0000255"
FT COILED 685..1041
FT /evidence="ECO:0000255"
FT BINDING 32..39
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
FT MOD_RES 112
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000269|PubMed:18614053"
FT MOD_RES 113
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000269|PubMed:18614053"
FT STRAND 6..11
FT /evidence="ECO:0007829|PDB:4UX3"
FT STRAND 14..17
FT /evidence="ECO:0007829|PDB:4UX3"
FT STRAND 18..20
FT /evidence="ECO:0007829|PDB:6QPW"
FT STRAND 25..33
FT /evidence="ECO:0007829|PDB:4UX3"
FT HELIX 38..49
FT /evidence="ECO:0007829|PDB:4UX3"
FT STRAND 53..55
FT /evidence="ECO:0007829|PDB:4UX3"
FT HELIX 58..64
FT /evidence="ECO:0007829|PDB:4UX3"
FT STRAND 68..72
FT /evidence="ECO:0007829|PDB:4UX3"
FT STRAND 77..80
FT /evidence="ECO:0007829|PDB:4UX3"
FT STRAND 102..104
FT /evidence="ECO:0007829|PDB:6QPW"
FT TURN 111..113
FT /evidence="ECO:0007829|PDB:4UX3"
FT STRAND 114..117
FT /evidence="ECO:0007829|PDB:6ZZ6"
FT TURN 118..121
FT /evidence="ECO:0007829|PDB:4UX3"
FT HELIX 125..133
FT /evidence="ECO:0007829|PDB:4UX3"
FT TURN 134..136
FT /evidence="ECO:0007829|PDB:6QPW"
FT STRAND 142..146
FT /evidence="ECO:0007829|PDB:4UX3"
FT HELIX 152..154
FT /evidence="ECO:0007829|PDB:4UX3"
FT HELIX 159..167
FT /evidence="ECO:0007829|PDB:4UX3"
FT HELIX 172..237
FT /evidence="ECO:0007829|PDB:4UX3"
FT HELIX 239..244
FT /evidence="ECO:0007829|PDB:4UX3"
FT HELIX 265..288
FT /evidence="ECO:0007829|PDB:6ZZ6"
FT STRAND 306..308
FT /evidence="ECO:0007829|PDB:6ZZ6"
FT STRAND 312..315
FT /evidence="ECO:0007829|PDB:6ZZ6"
FT STRAND 320..323
FT /evidence="ECO:0007829|PDB:6ZZ6"
FT HELIX 333..345
FT /evidence="ECO:0007829|PDB:6ZZ6"
FT HELIX 976..980
FT /evidence="ECO:0007829|PDB:4UX3"
FT HELIX 982..988
FT /evidence="ECO:0007829|PDB:4UX3"
FT HELIX 998..1059
FT /evidence="ECO:0007829|PDB:4UX3"
FT STRAND 1065..1069
FT /evidence="ECO:0007829|PDB:4UX3"
FT STRAND 1109..1113
FT /evidence="ECO:0007829|PDB:4UX3"
FT STRAND 1115..1117
FT /evidence="ECO:0007829|PDB:6QPW"
FT STRAND 1121..1123
FT /evidence="ECO:0007829|PDB:4UX3"
FT HELIX 1128..1143
FT /evidence="ECO:0007829|PDB:4UX3"
FT STRAND 1149..1153
FT /evidence="ECO:0007829|PDB:4UX3"
FT TURN 1154..1159
FT /evidence="ECO:0007829|PDB:4UX3"
FT HELIX 1162..1176
FT /evidence="ECO:0007829|PDB:4UX3"
FT STRAND 1179..1184
FT /evidence="ECO:0007829|PDB:4UX3"
FT HELIX 1188..1190
FT /evidence="ECO:0007829|PDB:4UX3"
FT TURN 1191..1193
FT /evidence="ECO:0007829|PDB:4UX3"
FT STRAND 1198..1203
FT /evidence="ECO:0007829|PDB:4UX3"
FT STRAND 1206..1210
FT /evidence="ECO:0007829|PDB:4UX3"
FT HELIX 1214..1221
FT /evidence="ECO:0007829|PDB:4UX3"
SQ SEQUENCE 1230 AA; 141336 MW; B152D88F7780341F CRC64;
MYIKRVIIKG FKTYRNETII DNFSPHQNVI IGSNGSGKSN FFAAIRFVLS DDYSNLKREE
RQGLIHQGSG GSVMSASVEI VFHDPDHSMI LPSGVLSRGD DEVTIRRTVG LKKDDYQLND
RNVTKGDIVR MLETAGFSMN NPYNIVPQGK IVALTNAKDK ERLQLLEDVV GAKSFEVKLK
ASLKKMEETE QKKIQINKEM GELNSKLSEM EQERKELEKY NELERNRKIY QFTLYDRELN
EVINQMERLD GDYNNTVYSS EQYIQELDKR EDMIDQVSKK LSSIEASLKI KNATDLQQAK
LRESEISQKL TNVNVKIKDV QQQIESNEEQ RNLDSATLKE IKSIIEQRKQ KLSKILPRYQ
ELTKEEAMYK LQLASLQQKQ RDLILKKGEY ARFKSKDERD TWIHSEIEEL KSSIQNLNEL
ESQLQMDRTS LRKQYSAIDE EIEELIDSIN GPDTKGQLED FDSELIHLKQ KLSESLDTRK
ELWRKEQKLQ TVLETLLSDV NQNQRNVNET MSRSLANGII NVKEITEKLK ISPESVFGTL
GELIKVNDKY KTCAEVIGGN SLFHIVVDTE ETATLIMNEL YRMKGGRVTF IPLNRLSLDS
DVKFPSNTTT QIQFTPLIKK IKYEPRFEKA VKHVFGKTIV VKDLGQGLKL AKKHKLNAIT
LDGDRADKRG VLTGGYLDQH KRTRLESLKN LNESRSQHKK ILEELDFVRN ELNDIDTKID
QVNGNIRKVS NDRESVLTNI EVYRTSLNTK KNEKLILEES LNAIILKLEK LNTNRTFAQE
KLNTFENDLL QEFDSELSKE EKERLESLTK EISAAHNKLN ITSDALEGIT TTIDSLNAEL
ESKLIPQEND LESKMSEVGD AFIFGLQDEL KELQLEKESV EKQHENAVLE LGTVQREIES
LIAEETNNKK LLEKANNQQR LLLKKLDNFQ KSVEKTMIKK TTLVTRREEL QQRIREIGLL
PEDALVNDFS DITSDQLLQR LNDMNTEISG LKNVNKRAFE NFKKFNERRK DLAERASELD
ESKDSIQDLI VKLKQQKVNA VDSTFQKVSE NFEAVFERLV PRGTAKLIIH RKNDNANDHD
ESIDVDMDAE SNESQNGKDS EIMYTGVSIS VSFNSKQNEQ LHVEQLSGGQ KTVCAIALIL
AIQMVDPASF YLFDEIDAAL DKQYRTAVAT LLKELSKNAQ FICTTFRTDM LQVADKFFRV
KYENKISTVI EVNREEAIGF IRGSNKFAEV
