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P47037 (SMC3_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 135. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Structural maintenance of chromosomes protein 3
Alternative name(s):
DA-box protein SMC3
Gene names
Name:SMC3
Ordered Locus Names:YJL074C
ORF Names:J1049
OrganismSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]
Taxonomic identifier559292 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces

Protein attributes

Sequence length1230 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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.

Subunit structure

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. Ref.5 Ref.6

Subcellular location

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.

Domain

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.

Post-translational modification

Acetylation at Lys-112 and Lys-113 by ECO1 is important for genome stability and S phase sister chromatid cohesion. Ref.8

Miscellaneous

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

Sequence similarities

Belongs to the SMC family. SMC3 subfamily.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 12301230Structural maintenance of chromosomes protein 3
PRO_0000119015

Regions

Nucleotide binding32 – 398ATP Potential
Region483 – 684202Flexible hinge
Coiled coil172 – 482311 Potential
Coiled coil685 – 1041357 Potential
Compositional bias1126 – 116136Ala/Asp-rich (DA-box)

Amino acid modifications

Modified residue1121N6-acetyllysine Ref.8
Modified residue1131N6-acetyllysine Ref.8

Sequences

Sequence LengthMass (Da)Tools
P47037 [UniParc].

Last modified February 1, 1996. Version 1.
Checksum: B152D88F7780341F

FASTA1,230141,336
        10         20         30         40         50         60 
MYIKRVIIKG FKTYRNETII DNFSPHQNVI IGSNGSGKSN FFAAIRFVLS DDYSNLKREE 

        70         80         90        100        110        120 
RQGLIHQGSG GSVMSASVEI VFHDPDHSMI LPSGVLSRGD DEVTIRRTVG LKKDDYQLND 

       130        140        150        160        170        180 
RNVTKGDIVR MLETAGFSMN NPYNIVPQGK IVALTNAKDK ERLQLLEDVV GAKSFEVKLK 

       190        200        210        220        230        240 
ASLKKMEETE QKKIQINKEM GELNSKLSEM EQERKELEKY NELERNRKIY QFTLYDRELN 

       250        260        270        280        290        300 
EVINQMERLD GDYNNTVYSS EQYIQELDKR EDMIDQVSKK LSSIEASLKI KNATDLQQAK 

       310        320        330        340        350        360 
LRESEISQKL TNVNVKIKDV QQQIESNEEQ RNLDSATLKE IKSIIEQRKQ KLSKILPRYQ 

       370        380        390        400        410        420 
ELTKEEAMYK LQLASLQQKQ RDLILKKGEY ARFKSKDERD TWIHSEIEEL KSSIQNLNEL 

       430        440        450        460        470        480 
ESQLQMDRTS LRKQYSAIDE EIEELIDSIN GPDTKGQLED FDSELIHLKQ KLSESLDTRK 

       490        500        510        520        530        540 
ELWRKEQKLQ TVLETLLSDV NQNQRNVNET MSRSLANGII NVKEITEKLK ISPESVFGTL 

       550        560        570        580        590        600 
GELIKVNDKY KTCAEVIGGN SLFHIVVDTE ETATLIMNEL YRMKGGRVTF IPLNRLSLDS 

       610        620        630        640        650        660 
DVKFPSNTTT QIQFTPLIKK IKYEPRFEKA VKHVFGKTIV VKDLGQGLKL AKKHKLNAIT 

       670        680        690        700        710        720 
LDGDRADKRG VLTGGYLDQH KRTRLESLKN LNESRSQHKK ILEELDFVRN ELNDIDTKID 

       730        740        750        760        770        780 
QVNGNIRKVS NDRESVLTNI EVYRTSLNTK KNEKLILEES LNAIILKLEK LNTNRTFAQE 

       790        800        810        820        830        840 
KLNTFENDLL QEFDSELSKE EKERLESLTK EISAAHNKLN ITSDALEGIT TTIDSLNAEL 

       850        860        870        880        890        900 
ESKLIPQEND LESKMSEVGD AFIFGLQDEL KELQLEKESV EKQHENAVLE LGTVQREIES 

       910        920        930        940        950        960 
LIAEETNNKK LLEKANNQQR LLLKKLDNFQ KSVEKTMIKK TTLVTRREEL QQRIREIGLL 

       970        980        990       1000       1010       1020 
PEDALVNDFS DITSDQLLQR LNDMNTEISG LKNVNKRAFE NFKKFNERRK DLAERASELD 

      1030       1040       1050       1060       1070       1080 
ESKDSIQDLI VKLKQQKVNA VDSTFQKVSE NFEAVFERLV PRGTAKLIIH RKNDNANDHD 

      1090       1100       1110       1120       1130       1140 
ESIDVDMDAE SNESQNGKDS EIMYTGVSIS VSFNSKQNEQ LHVEQLSGGQ KTVCAIALIL 

      1150       1160       1170       1180       1190       1200 
AIQMVDPASF YLFDEIDAAL DKQYRTAVAT LLKELSKNAQ FICTTFRTDM LQVADKFFRV 

      1210       1220       1230 
KYENKISTVI EVNREEAIGF IRGSNKFAEV 

« Hide

References

« Hide 'large scale' references
[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. expand/collapse author list , 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]"The reference genome sequence of Saccharomyces cerevisiae: Then and now."
Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R., Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S., Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.
G3 (Bethesda) 4:389-398(2014) [PubMed] [Europe PMC] [Abstract]
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]"Global analysis of protein expression in yeast."
Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N., O'Shea E.K., Weissman J.S.
Nature 425:737-741(2003) [PubMed] [Europe PMC] [Abstract]
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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
Y14278 Genomic DNA. Translation: CAA74655.1.
Z49349 Genomic DNA. Translation: CAA89366.1.
X88851 Genomic DNA. Translation: CAA61313.1.
BK006943 Genomic DNA. Translation: DAA08725.1.
PIRS56850.
RefSeqNP_012461.1. NM_001181507.1.

3D structure databases

ProteinModelPortalP47037.
SMRP47037. Positions 1-256, 504-694, 999-1218.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid33681. 275 interactions.
DIPDIP-2991N.
IntActP47037. 55 interactions.
MINTMINT-435389.
STRING4932.YJL074C.

Proteomic databases

MaxQBP47037.
PaxDbP47037.
PeptideAtlasP47037.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiYJL074C; YJL074C; YJL074C.
GeneID853371.
KEGGsce:YJL074C.

Organism-specific databases

CYGDYJL074c.
SGDS000003610. SMC3.

Phylogenomic databases

eggNOGCOG1196.
GeneTreeENSGT00580000081628.
HOGENOMHOG000166512.
KOK06669.
OMAKKERDEW.
OrthoDBEOG7M0P0T.

Enzyme and pathway databases

BioCycYEAST:G3O-31532-MONOMER.

Gene expression databases

GenevestigatorP47037.

Family and domain databases

Gene3D3.40.50.300. 2 hits.
InterProIPR027417. P-loop_NTPase.
IPR003395. RecF/RecN/SMC_N.
IPR010935. SMC_hinge.
[Graphical view]
PfamPF06470. SMC_hinge. 1 hit.
PF02463. SMC_N. 1 hit.
[Graphical view]
SMARTSM00968. SMC_hinge. 1 hit.
[Graphical view]
SUPFAMSSF52540. SSF52540. 2 hits.
SSF75553. SSF75553. 1 hit.
ProtoNetSearch...

Other

NextBio973810.
PROP47037.

Entry information

Entry nameSMC3_YEAST
AccessionPrimary (citable) accession number: P47037
Secondary accession number(s): D6VWA9
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1996
Last sequence update: February 1, 1996
Last modified: July 9, 2014
This is version 135 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

Yeast chromosome X

Yeast (Saccharomyces cerevisiae) chromosome X: entries and gene names

Yeast

Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD

SIMILARITY comments

Index of protein domains and families