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Protein

Structural maintenance of chromosomes protein 3

Gene

SMC3

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Involved in chromosome cohesion during cell cycle and in DNA repair. Central component of cohesin complex. The cohesin complex is required for the cohesion of sister chromatids after DNA replication. The cohesin complex apparently forms a large proteinaceous ring within which sister chromatids can be trapped. At anaphase, the complex is cleaved and dissociates from chromatin, allowing sister chromatids to segregate.

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi32 – 398ATPSequence Analysis

GO - Molecular functioni

  • ATPase activity Source: SGD
  • ATP binding Source: UniProtKB-KW
  • chromatin binding Source: InterPro
  • identical protein binding Source: IntAct

GO - Biological processi

  • ascospore formation Source: SGD
  • cell division Source: UniProtKB-KW
  • meiotic sister chromatid cohesion Source: SGD
  • mitotic sister chromatid cohesion Source: SGD
  • reciprocal meiotic recombination Source: SGD
  • replication-born double-strand break repair via sister chromatid exchange Source: SGD
  • synaptonemal complex assembly Source: SGD
Complete GO annotation...

Keywords - Biological processi

Cell cycle, Cell division, Mitosis

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

BioCyciYEAST:G3O-31532-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Structural maintenance of chromosomes protein 3
Alternative name(s):
DA-box protein SMC3
Gene namesi
Name:SMC3
Ordered Locus Names:YJL074C
ORF Names:J1049
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
ProteomesiUP000002311 Componenti: Chromosome X

Organism-specific databases

CYGDiYJL074c.
EuPathDBiFungiDB:YJL074C.
SGDiS000003610. SMC3.

Subcellular locationi

  • Nucleus
  • Chromosome

  • Note: Associates with chromatin. Before prophase it is scattered along chromosome arms. At anaphase, the MCD1 subunit of the cohesin complex is cleaved, leading to the dissociation of the complex from chromosomes, allowing chromosome separation.

GO - Cellular componenti

  • cohesin core heterodimer Source: InterPro
  • nuclear mitotic cohesin complex Source: SGD
  • nucleus Source: SGD
Complete GO annotation...

Keywords - Cellular componenti

Chromosome, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 12301230Structural maintenance of chromosomes protein 3PRO_0000119015Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei112 – 1121N6-acetyllysine1 Publication
Modified residuei113 – 1131N6-acetyllysine1 Publication

Post-translational modificationi

Acetylation at Lys-112 and Lys-113 by ECO1 is important for genome stability and S phase sister chromatid cohesion.1 Publication

Keywords - PTMi

Acetylation

Proteomic databases

MaxQBiP47037.
PaxDbiP47037.
PeptideAtlasiP47037.

Interactioni

Subunit structurei

Cohesin complexes are composed of the SMC1 and SMC3 heterodimer attached via their hinge domain, MCD1/SCC1 which link them, and IRR1/SCC3, which interacts with MCD1. The cohesin complex also interacts with SCC2, which is required for its association with chromosomes.2 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
itself5EBI-17423,EBI-17423
IRR1P405412EBI-17423,EBI-16667
MCD1Q1215813EBI-17423,EBI-16655
RAD61Q993599EBI-17423,EBI-2082336
SMC1P3290820EBI-17423,EBI-17402

Protein-protein interaction databases

BioGridi33681. 278 interactions.
DIPiDIP-2991N.
IntActiP47037. 55 interactions.
MINTiMINT-435389.
STRINGi4932.YJL074C.

Structurei

Secondary structure

1
1230
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi6 – 116Combined sources
Beta strandi14 – 174Combined sources
Beta strandi25 – 339Combined sources
Helixi38 – 4912Combined sources
Beta strandi53 – 553Combined sources
Helixi58 – 647Combined sources
Beta strandi68 – 725Combined sources
Beta strandi77 – 804Combined sources
Turni111 – 1133Combined sources
Turni118 – 1214Combined sources
Helixi125 – 1339Combined sources
Beta strandi142 – 1465Combined sources
Helixi152 – 1543Combined sources
Helixi159 – 1679Combined sources
Helixi172 – 23766Combined sources
Helixi239 – 2446Combined sources
Helixi976 – 9805Combined sources
Helixi982 – 9887Combined sources
Helixi998 – 105962Combined sources
Beta strandi1065 – 10695Combined sources
Beta strandi1109 – 11135Combined sources
Beta strandi1121 – 11233Combined sources
Helixi1128 – 114316Combined sources
Beta strandi1149 – 11535Combined sources
Turni1154 – 11596Combined sources
Helixi1162 – 117615Combined sources
Beta strandi1179 – 11846Combined sources
Helixi1188 – 11903Combined sources
Turni1191 – 11933Combined sources
Beta strandi1198 – 12036Combined sources
Beta strandi1206 – 12105Combined sources
Helixi1214 – 12218Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4UX3X-ray3.30A2-261[»]
A970-1230[»]
ProteinModelPortaliP47037.
SMRiP47037. Positions 2-250, 458-694, 973-1222.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni483 – 684202Flexible hingeAdd
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili172 – 482311Sequence AnalysisAdd
BLAST
Coiled coili685 – 1041357Sequence AnalysisAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi1126 – 116136Ala/Asp-rich (DA-box)Add
BLAST

Domaini

The flexible hinge domain, which separates the large intramolecular coiled coil regions, allows the heterotypic interaction with the corresponding domain of SMC1, forming a V-shaped heterodimer. The two heads of the heterodimer are then connected by different ends of the cleavable MCD1 protein, forming a ring structure (By similarity).By similarity

Sequence similaritiesi

Belongs to the SMC family. SMC3 subfamily.Curated

Keywords - Domaini

Coiled coil

Phylogenomic databases

eggNOGiCOG1196.
GeneTreeiENSGT00580000081628.
HOGENOMiHOG000166512.
InParanoidiP47037.
KOiK06669.
OMAiKKERDEW.
OrthoDBiEOG7M0P0T.

Family and domain databases

Gene3Di3.40.50.300. 2 hits.
InterProiIPR027417. P-loop_NTPase.
IPR003395. RecF/RecN/SMC_N.
IPR024704. SMC.
IPR029685. SMC3.
IPR010935. SMC_hinge.
[Graphical view]
PANTHERiPTHR18937:SF8. PTHR18937:SF8. 1 hit.
PfamiPF06470. SMC_hinge. 1 hit.
PF02463. SMC_N. 1 hit.
[Graphical view]
PIRSFiPIRSF005719. SMC. 1 hit.
SMARTiSM00968. SMC_hinge. 1 hit.
[Graphical view]
SUPFAMiSSF52540. SSF52540. 2 hits.
SSF75553. SSF75553. 1 hit.

Sequencei

Sequence statusi: Complete.

P47037-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MYIKRVIIKG FKTYRNETII DNFSPHQNVI IGSNGSGKSN FFAAIRFVLS
60 70 80 90 100
DDYSNLKREE RQGLIHQGSG GSVMSASVEI VFHDPDHSMI LPSGVLSRGD
110 120 130 140 150
DEVTIRRTVG LKKDDYQLND RNVTKGDIVR MLETAGFSMN NPYNIVPQGK
160 170 180 190 200
IVALTNAKDK ERLQLLEDVV GAKSFEVKLK ASLKKMEETE QKKIQINKEM
210 220 230 240 250
GELNSKLSEM EQERKELEKY NELERNRKIY QFTLYDRELN EVINQMERLD
260 270 280 290 300
GDYNNTVYSS EQYIQELDKR EDMIDQVSKK LSSIEASLKI KNATDLQQAK
310 320 330 340 350
LRESEISQKL TNVNVKIKDV QQQIESNEEQ RNLDSATLKE IKSIIEQRKQ
360 370 380 390 400
KLSKILPRYQ ELTKEEAMYK LQLASLQQKQ RDLILKKGEY ARFKSKDERD
410 420 430 440 450
TWIHSEIEEL KSSIQNLNEL ESQLQMDRTS LRKQYSAIDE EIEELIDSIN
460 470 480 490 500
GPDTKGQLED FDSELIHLKQ KLSESLDTRK ELWRKEQKLQ TVLETLLSDV
510 520 530 540 550
NQNQRNVNET MSRSLANGII NVKEITEKLK ISPESVFGTL GELIKVNDKY
560 570 580 590 600
KTCAEVIGGN SLFHIVVDTE ETATLIMNEL YRMKGGRVTF IPLNRLSLDS
610 620 630 640 650
DVKFPSNTTT QIQFTPLIKK IKYEPRFEKA VKHVFGKTIV VKDLGQGLKL
660 670 680 690 700
AKKHKLNAIT LDGDRADKRG VLTGGYLDQH KRTRLESLKN LNESRSQHKK
710 720 730 740 750
ILEELDFVRN ELNDIDTKID QVNGNIRKVS NDRESVLTNI EVYRTSLNTK
760 770 780 790 800
KNEKLILEES LNAIILKLEK LNTNRTFAQE KLNTFENDLL QEFDSELSKE
810 820 830 840 850
EKERLESLTK EISAAHNKLN ITSDALEGIT TTIDSLNAEL ESKLIPQEND
860 870 880 890 900
LESKMSEVGD AFIFGLQDEL KELQLEKESV EKQHENAVLE LGTVQREIES
910 920 930 940 950
LIAEETNNKK LLEKANNQQR LLLKKLDNFQ KSVEKTMIKK TTLVTRREEL
960 970 980 990 1000
QQRIREIGLL PEDALVNDFS DITSDQLLQR LNDMNTEISG LKNVNKRAFE
1010 1020 1030 1040 1050
NFKKFNERRK DLAERASELD ESKDSIQDLI VKLKQQKVNA VDSTFQKVSE
1060 1070 1080 1090 1100
NFEAVFERLV PRGTAKLIIH RKNDNANDHD ESIDVDMDAE SNESQNGKDS
1110 1120 1130 1140 1150
EIMYTGVSIS VSFNSKQNEQ LHVEQLSGGQ KTVCAIALIL AIQMVDPASF
1160 1170 1180 1190 1200
YLFDEIDAAL DKQYRTAVAT LLKELSKNAQ FICTTFRTDM LQVADKFFRV
1210 1220 1230
KYENKISTVI EVNREEAIGF IRGSNKFAEV
Length:1,230
Mass (Da):141,336
Last modified:February 1, 1996 - v1
Checksum:iB152D88F7780341F
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Y14278 Genomic DNA. Translation: CAA74655.1.
Z49349 Genomic DNA. Translation: CAA89366.1.
X88851 Genomic DNA. Translation: CAA61313.1.
BK006943 Genomic DNA. Translation: DAA08725.1.
PIRiS56850.
RefSeqiNP_012461.1. NM_001181507.1.

Genome annotation databases

EnsemblFungiiYJL074C; YJL074C; YJL074C.
GeneIDi853371.
KEGGisce:YJL074C.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Y14278 Genomic DNA. Translation: CAA74655.1.
Z49349 Genomic DNA. Translation: CAA89366.1.
X88851 Genomic DNA. Translation: CAA61313.1.
BK006943 Genomic DNA. Translation: DAA08725.1.
PIRiS56850.
RefSeqiNP_012461.1. NM_001181507.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4UX3X-ray3.30A2-261[»]
A970-1230[»]
ProteinModelPortaliP47037.
SMRiP47037. Positions 2-250, 458-694, 973-1222.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi33681. 278 interactions.
DIPiDIP-2991N.
IntActiP47037. 55 interactions.
MINTiMINT-435389.
STRINGi4932.YJL074C.

Proteomic databases

MaxQBiP47037.
PaxDbiP47037.
PeptideAtlasiP47037.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYJL074C; YJL074C; YJL074C.
GeneIDi853371.
KEGGisce:YJL074C.

Organism-specific databases

CYGDiYJL074c.
EuPathDBiFungiDB:YJL074C.
SGDiS000003610. SMC3.

Phylogenomic databases

eggNOGiCOG1196.
GeneTreeiENSGT00580000081628.
HOGENOMiHOG000166512.
InParanoidiP47037.
KOiK06669.
OMAiKKERDEW.
OrthoDBiEOG7M0P0T.

Enzyme and pathway databases

BioCyciYEAST:G3O-31532-MONOMER.

Miscellaneous databases

NextBioi973810.
PROiP47037.

Family and domain databases

Gene3Di3.40.50.300. 2 hits.
InterProiIPR027417. P-loop_NTPase.
IPR003395. RecF/RecN/SMC_N.
IPR024704. SMC.
IPR029685. SMC3.
IPR010935. SMC_hinge.
[Graphical view]
PANTHERiPTHR18937:SF8. PTHR18937:SF8. 1 hit.
PfamiPF06470. SMC_hinge. 1 hit.
PF02463. SMC_N. 1 hit.
[Graphical view]
PIRSFiPIRSF005719. SMC. 1 hit.
SMARTiSM00968. SMC_hinge. 1 hit.
[Graphical view]
SUPFAMiSSF52540. SSF52540. 2 hits.
SSF75553. SSF75553. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Cohesins: chromosomal proteins that prevent premature separation of sister chromatids."
    Michaelis C., Ciosk R., Nasmyth K.
    Cell 91:35-45(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: ATCC 200060 / W303.
  2. "Complete nucleotide sequence of Saccharomyces cerevisiae chromosome X."
    Galibert F., Alexandraki D., Baur A., Boles E., Chalwatzis N., Chuat J.-C., Coster F., Cziepluch C., de Haan M., Domdey H., Durand P., Entian K.-D., Gatius M., Goffeau A., Grivell L.A., Hennemann A., Herbert C.J., Heumann K.
    , Hilger F., Hollenberg C.P., Huang M.-E., Jacq C., Jauniaux J.-C., Katsoulou C., Kirchrath L., Kleine K., Kordes E., Koetter P., Liebl S., Louis E.J., Manus V., Mewes H.-W., Miosga T., Obermaier B., Perea J., Pohl T.M., Portetelle D., Pujol A., Purnelle B., Ramezani Rad M., Rasmussen S.W., Rose M., Rossau R., Schaaff-Gerstenschlaeger I., Smits P.H.M., Scarcez T., Soriano N., To Van D., Tzermia M., Van Broekhoven A., Vandenbol M., Wedler H., von Wettstein D., Wambutt R., Zagulski M., Zollner A., Karpfinger-Hartl L.
    EMBO J. 15:2031-2049(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  3. Cited for: GENOME REANNOTATION.
    Strain: ATCC 204508 / S288c.
  4. Sor F.J.
    Submitted (JUN-1995) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: S288c / FY1678.
  5. "Yeast cohesin complex requires a conserved protein, Eco1p(Ctf7), to establish cohesion between sister chromatids during DNA replication."
    Toth A., Ciosk R., Uhlmann F., Galova M., Schleiffer A., Nasmyth K.
    Genes Dev. 13:320-333(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION IN A COHESIN COMPLEX WITH SMC1; IRR1 AND MCD1, INTERACTION OF THE COHESIN COMPLEX WITH SCC2.
  6. "Molecular architecture of SMC proteins and the yeast cohesin complex."
    Haering C.H., Loewe J., Hochwagen A., Nasmyth K.
    Mol. Cell 9:773-788(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION IN A COHESIN COMPLEX WITH SMC3; MCD1 AND IRR1, STRUCTURE.
  7. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
  8. "Acetylation of Smc3 by Eco1 is required for S phase sister chromatid cohesion in both human and yeast."
    Zhang J., Shi X., Li Y., Kim B.J., Jia J., Huang Z., Yang T., Fu X., Jung S.Y., Wang Y., Zhang P., Kim S.T., Pan X., Qin J.
    Mol. Cell 31:143-151(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION AT LYS-112 AND LYS-113.

Entry informationi

Entry nameiSMC3_YEAST
AccessioniPrimary (citable) accession number: P47037
Secondary accession number(s): D6VWA9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1996
Last sequence update: February 1, 1996
Last modified: June 24, 2015
This is version 144 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Miscellaneous

Present with 2660 molecules/cell in log phase SD medium.1 Publication

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families
  3. Yeast
    Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
  4. Yeast chromosome X
    Yeast (Saccharomyces cerevisiae) chromosome X: entries and gene names

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.