SMC1_YEAST
ID SMC1_YEAST Reviewed; 1225 AA.
AC P32908; D6VTM2;
DT 01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1993, sequence version 1.
DT 03-AUG-2022, entry version 200.
DE RecName: Full=Structural maintenance of chromosomes protein 1;
DE AltName: Full=DA-box protein SMC1;
GN Name=SMC1; Synonyms=CHL10; OrderedLocusNames=YFL008W;
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, AND MUTANTS SMC1-1 AND SMC1-2.
RX PubMed=8276886; DOI=10.1083/jcb.123.6.1635;
RA Strunnikov A.V., Larionov V.L., Koshland D.;
RT "SMC1: an essential yeast gene encoding a putative head-rod-tail protein is
RT required for nuclear division and defines a new ubiquitous protein
RT family.";
RL J. Cell Biol. 123:1635-1648(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=7670463; DOI=10.1038/ng0795-261;
RA Murakami Y., Naitou M., Hagiwara H., Shibata T., Ozawa M., Sasanuma S.,
RA Sasanuma M., Tsuchiya Y., Soeda E., Yokoyama K., Yamazaki M., Tashiro H.,
RA Eki T.;
RT "Analysis of the nucleotide sequence of chromosome VI from Saccharomyces
RT cerevisiae.";
RL Nat. Genet. 10:261-268(1995).
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 IDENTIFICATION IN A COHESIN COMPLEX WITH SMC3; 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 [5]
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 [6]
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).
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 P32908; P36022: DYN1; NbExp=3; IntAct=EBI-17402, EBI-6230;
CC P32908; P17119: KAR3; NbExp=4; IntAct=EBI-17402, EBI-9499;
CC P32908; Q12158: MCD1; NbExp=9; IntAct=EBI-17402, EBI-16655;
CC P32908; P47149: NNF1; NbExp=6; IntAct=EBI-17402, EBI-12098;
CC P32908; P53253: NNF2; NbExp=4; IntAct=EBI-17402, EBI-23229;
CC P32908; P32908: SMC1; NbExp=7; IntAct=EBI-17402, EBI-17402;
CC P32908; P38989: SMC2; NbExp=3; IntAct=EBI-17402, EBI-17412;
CC P32908; P47037: SMC3; NbExp=19; IntAct=EBI-17402, EBI-17423;
CC P32908; Q12306: SMT3; NbExp=2; IntAct=EBI-17402, EBI-17490;
CC P32908; P36094: SPC42; NbExp=3; IntAct=EBI-17402, EBI-17777;
CC P32908; P32558: SPT16; NbExp=2; IntAct=EBI-17402, EBI-4334;
CC P32908; Q9UQE7: SMC3; Xeno; NbExp=4; IntAct=EBI-17402, EBI-80718;
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 SMC3, 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.
CC -!- MISCELLANEOUS: Present with 5710 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the SMC family. SMC1 subfamily. {ECO:0000305}.
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DR EMBL; L00602; AAA16595.1; -; Unassigned_DNA.
DR EMBL; D50617; BAA09230.1; -; Genomic_DNA.
DR EMBL; BK006940; DAA12432.1; -; Genomic_DNA.
DR PIR; A49464; A49464.
DR RefSeq; NP_116647.1; NM_001179958.1.
DR PDB; 1W1W; X-ray; 2.90 A; A/B/C/D=1-214, A/B/C/D=1024-1225.
DR PDB; 6ZZ6; EM; 3.40 A; A=1003-1224.
DR PDB; 7OGT; EM; 5.50 A; A=1-1225.
DR PDBsum; 1W1W; -.
DR PDBsum; 6ZZ6; -.
DR PDBsum; 7OGT; -.
DR AlphaFoldDB; P32908; -.
DR SMR; P32908; -.
DR BioGRID; 31139; 453.
DR ComplexPortal; CPX-1408; Nuclear meiotic cohesin complex.
DR ComplexPortal; CPX-1867; Nuclear mitotic cohesin complex.
DR DIP; DIP-2982N; -.
DR IntAct; P32908; 29.
DR MINT; P32908; -.
DR STRING; 4932.YFL008W; -.
DR iPTMnet; P32908; -.
DR MaxQB; P32908; -.
DR PaxDb; P32908; -.
DR PRIDE; P32908; -.
DR EnsemblFungi; YFL008W_mRNA; YFL008W; YFL008W.
DR GeneID; 850540; -.
DR KEGG; sce:YFL008W; -.
DR SGD; S000001886; SMC1.
DR VEuPathDB; FungiDB:YFL008W; -.
DR eggNOG; KOG0018; Eukaryota.
DR GeneTree; ENSGT00940000171089; -.
DR HOGENOM; CLU_001042_0_1_1; -.
DR InParanoid; P32908; -.
DR OMA; YIRDHTT; -.
DR BioCyc; YEAST:G3O-30448-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; P32908; -.
DR PRO; PR:P32908; -.
DR Proteomes; UP000002311; Chromosome VI.
DR RNAct; P32908; protein.
DR GO; GO:0008278; C:cohesin complex; IBA:GO_Central.
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; HDA:SGD.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0003677; F:DNA binding; IBA:GO_Central.
DR GO; GO:0000217; F:DNA secondary structure binding; IDA:SGD.
DR GO; GO:0003690; F:double-stranded DNA binding; IDA:SGD.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0003680; F:minor groove of adenine-thymine-rich DNA binding; IDA:SGD.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0006302; P:double-strand break repair; IMP:SGD.
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:0007064; P:mitotic sister chromatid cohesion; IGI:SGD.
DR GO; GO:0000070; P:mitotic sister chromatid segregation; IMP:SGD.
DR GO; GO:0007062; P:sister chromatid cohesion; IBA:GO_Central.
DR CDD; cd03275; ABC_SMC1_euk; 2.
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; IPR028468; Smc1_ABC.
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; 2.
DR SUPFAM; SSF75553; SSF75553; 1.
PE 1: Evidence at protein level;
KW 3D-structure; ATP-binding; Cell cycle; Cell division; Chromosome;
KW Coiled coil; Mitosis; Nucleotide-binding; Nucleus; Reference proteome.
FT CHAIN 1..1225
FT /note="Structural maintenance of chromosomes protein 1"
FT /id="PRO_0000119011"
FT DOMAIN 527..641
FT /note="SMC hinge"
FT COILED 173..489
FT /evidence="ECO:0000255"
FT COILED 679..1063
FT /evidence="ECO:0000255"
FT MOTIF 1057..1061
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000255"
FT BINDING 33..40
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
FT MUTAGEN 173
FT /note="S->L: In temperature-sensitive mutant SMC1-2."
FT MUTAGEN 458
FT /note="N->D: In temperature-sensitive mutant SMC1-1."
FT STRAND 4..11
FT /evidence="ECO:0007829|PDB:1W1W"
FT STRAND 17..22
FT /evidence="ECO:0007829|PDB:1W1W"
FT STRAND 27..32
FT /evidence="ECO:0007829|PDB:1W1W"
FT HELIX 39..49
FT /evidence="ECO:0007829|PDB:1W1W"
FT HELIX 63..65
FT /evidence="ECO:0007829|PDB:1W1W"
FT STRAND 91..100
FT /evidence="ECO:0007829|PDB:1W1W"
FT STRAND 103..112
FT /evidence="ECO:0007829|PDB:1W1W"
FT STRAND 117..121
FT /evidence="ECO:0007829|PDB:1W1W"
FT STRAND 124..126
FT /evidence="ECO:0007829|PDB:1W1W"
FT HELIX 128..137
FT /evidence="ECO:0007829|PDB:1W1W"
FT TURN 142..144
FT /evidence="ECO:0007829|PDB:1W1W"
FT HELIX 156..159
FT /evidence="ECO:0007829|PDB:1W1W"
FT HELIX 162..167
FT /evidence="ECO:0007829|PDB:1W1W"
FT HELIX 170..173
FT /evidence="ECO:0007829|PDB:1W1W"
FT TURN 175..178
FT /evidence="ECO:0007829|PDB:1W1W"
FT HELIX 179..188
FT /evidence="ECO:0007829|PDB:1W1W"
FT HELIX 240..259
FT /evidence="ECO:0007829|PDB:1W1W"
FT STRAND 269..272
FT /evidence="ECO:0007829|PDB:1W1W"
FT STRAND 274..279
FT /evidence="ECO:0007829|PDB:1W1W"
FT HELIX 280..282
FT /evidence="ECO:0007829|PDB:1W1W"
FT STRAND 287..290
FT /evidence="ECO:0007829|PDB:1W1W"
FT HELIX 298..300
FT /evidence="ECO:0007829|PDB:1W1W"
FT HELIX 304..319
FT /evidence="ECO:0007829|PDB:1W1W"
FT STRAND 325..331
FT /evidence="ECO:0007829|PDB:1W1W"
FT TURN 332..335
FT /evidence="ECO:0007829|PDB:1W1W"
FT HELIX 338..350
FT /evidence="ECO:0007829|PDB:1W1W"
FT STRAND 352..357
FT /evidence="ECO:0007829|PDB:1W1W"
FT HELIX 361..364
FT /evidence="ECO:0007829|PDB:1W1W"
FT HELIX 1005..1016
FT /evidence="ECO:0007829|PDB:6ZZ6"
FT HELIX 1022..1037
FT /evidence="ECO:0007829|PDB:6ZZ6"
FT HELIX 1045..1083
FT /evidence="ECO:0007829|PDB:6ZZ6"
FT STRAND 1086..1088
FT /evidence="ECO:0007829|PDB:6ZZ6"
FT STRAND 1096..1102
FT /evidence="ECO:0007829|PDB:6ZZ6"
FT TURN 1107..1109
FT /evidence="ECO:0007829|PDB:6ZZ6"
FT STRAND 1112..1117
FT /evidence="ECO:0007829|PDB:6ZZ6"
FT HELIX 1131..1147
FT /evidence="ECO:0007829|PDB:6ZZ6"
FT STRAND 1152..1158
FT /evidence="ECO:0007829|PDB:6ZZ6"
FT HELIX 1165..1178
FT /evidence="ECO:0007829|PDB:6ZZ6"
FT STRAND 1181..1188
FT /evidence="ECO:0007829|PDB:6ZZ6"
FT TURN 1192..1194
FT /evidence="ECO:0007829|PDB:6ZZ6"
FT HELIX 1195..1197
FT /evidence="ECO:0007829|PDB:6ZZ6"
FT STRAND 1199..1207
FT /evidence="ECO:0007829|PDB:6ZZ6"
FT TURN 1208..1211
FT /evidence="ECO:0007829|PDB:6ZZ6"
FT STRAND 1212..1217
FT /evidence="ECO:0007829|PDB:6ZZ6"
FT STRAND 1220..1222
FT /evidence="ECO:0007829|PDB:6ZZ6"
SQ SEQUENCE 1225 AA; 141280 MW; B504017AA0ECCA8C CRC64;
MGRLVGLELS NFKSYRGVTK VGFGESNFTS IIGPNGSGKS NMMDAISFVL GVRSNHLRSN
ILKDLIYRGV LNDENSDDYD NEGAASSNPQ SAYVKAFYQK GNKLVELMRI ISRNGDTSYK
IDGKTVSYKD YSIFLENENI LIKAKNFLVF QGDVEQIAAQ SPVELSRMFE EVSGSIQYKK
EYEELKEKIE KLSKSATESI KNRRRIHGEL KTYKEGINKN EEYRKQLDKK NELQKFQALW
QLYHLEQQKE ELTDKLSALN SEISSLKGKI NNEMKSLQRS KSSFVKESAV ISKQKSKLDY
IFKDKEKLVS DLRLIKVPQQ AAGKRISHIE KRIESLQKDL QRQKTYVERF ETQLKVVTRS
KEAFEEEIKQ SARNYDKFKL NENDLKTYNC LHEKYLTEGG SILEEKIAVL NNDKREIQEE
LERFNKRADI SKRRITEELS ITGEKLDTQL NDLRVSLNEK NALHTERLHE LKKLQSDIES
ANNQEYDLNF KLRETLVKID DLSANQRETM KERKLRENIA MLKRFFPGVK GLVHDLCHPK
KEKYGLAVST ILGKNFDSVI VENLTVAQEC IAFLKKQRAG TASFIPLDTI ETELPTLSLP
DSQDYILSIN AIDYEPEYEK AMQYVCGDSI ICNTLNIAKD LKWKKGIRGK LVTIEGALIH
KAGLMTGGIS GDANNRWDKE EYQSLMSLKD KLLIQIDELS NGQRSNSIRA REVENSVSLL
NSDIANLRTQ VTQQKRSLDE NRLEIKYHND LIEKEIQPKI TELKKKLDDL ENTKDNLVKE
KEALQNNIFK EFTSKIGFTI KEYENHSGEL MRQQSKELQQ LQKQILTVEN KLQFETDRLS
TTQRRYEKAQ KDLENAQVEM KSLEEQEYAI EMKIGSIESK LEEHKNHLDE LQKKFVTKQS
ELNSSEDILE DMNSNLQVLK RERDGIKEDI EKFDLERVTA LKNCKISNIN IPISSETTID
DLPISSTDNE AITISNSIDI NYKGLPKKYK ENNTDSARKE LEQKIHEVEE ILNELQPNAR
ALERYDEAEG RFEVINNETE QLKAEEKKIL NQFLKIKKKR KELFEKTFDY VSDHLDAIYR
ELTKNPNSNV ELAGGNASLT IEDEDEPFNA GIKYHATPPL KRFKDMEYLS GGEKTVAALA
LLFAINSYQP SPFFVLDEVD AALDITNVQR IAAYIRRHRN PDLQFIVISL KNTMFEKSDA
LVGVYRQQQE NSSKIITLDL SNYAE
