P47037 (SMC3_YEAST) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended 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

Organism

Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]

Taxonomic identifier

559292 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Fungi › Dikarya › Ascomycota › saccharomyceta › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces › Saccharomyces cerevisiae

Protein attributes

Sequence length	1230 AA.
Sequence status	Complete.
Protein existence	Evidence 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.
Miscellaneous	Present with 2660 molecules/cell in log phase SD medium.
Sequence similarities	Belongs to the SMC family. SMC3 subfamily.

Ontologies

Keywords
Biological process	Cell cycle Cell division Mitosis
Cellular component	Chromosome Nucleus
Domain	Coiled coil
Ligand	ATP-binding Nucleotide-binding
PTM	Acetylation
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	ascospore formation Inferred from mutant phenotype PubMed 10412984. Source: SGD cell division Inferred from electronic annotation. Source: UniProtKB-KW meiotic sister chromatid cohesion Inferred from mutant phenotype PubMed 10412984. Source: SGD mitotic sister chromatid cohesion Inferred from genetic interaction Ref.1. Source: SGD reciprocal meiotic recombination Inferred from mutant phenotype PubMed 10412984. Source: SGD synaptonemal complex assembly Inferred from mutant phenotype PubMed 10412984. Source: SGD
Cellular_component	nuclear mitotic cohesin complex Inferred from direct assay Ref.5. Source: SGD
Molecular_function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW ATPase activity Inferred from sequence or structural similarity PubMed 9887095. Source: SGD
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
itself		5	EBI-17423,EBI-17423
MCD1	Q12158	11	EBI-17423,EBI-16655
SMC1	P32908	13	EBI-17423,EBI-17402

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 1230	1230	Structural maintenance of chromosomes protein 3		PRO_0000119015
Regions
	Nucleotide binding	32 – 39	8	ATP Potential
	Region	483 – 684	202	Flexible hinge
	Coiled coil	172 – 482	311	Potential
	Coiled coil	685 – 1041	357	Potential
	Compositional bias	1126 – 1161	36	Ala/Asp-rich (DA-box)
Amino acid modifications
	Modified residue	112	1	N6-acetyllysine Ref.8
	Modified residue	113	1	N6-acetyllysine Ref.8

Sequences

	Sequence		Length	Mass (Da)
	P47037 [UniParc]. Last modified February 1, 1996. Version 1. Checksum: B152D88F7780341F	FASTA	1,230	141,336
	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

References

	« Hide 'large scale' referencesShow '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. , 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 96604 / S288c / FY1679.
[3]	Saccharomyces Genome Database Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases 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.
PIR	S56850.
RefSeq	NP_012461.1. NM_001181507.1.
3D structure databases
ProteinModelPortal	P47037.
SMR	P47037. Positions 2-171, 504-694, 1044-1218.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-2991N.
IntAct	P47037. 55 interactions.
MINT	MINT-435389.
STRING	4932.YJL074C.
Proteomic databases
PaxDb	P47037.
PeptideAtlas	P47037.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblFungi	YJL074C; YJL074C; YJL074C.
GeneID	853371.
KEGG	sce:YJL074C.
Organism-specific databases
CYGD	YJL074c.
SGD	S000003610. SMC3.
Phylogenomic databases
eggNOG	COG1196.
GeneTree	ENSGT00580000081628.
HOGENOM	HOG000166512.
KO	K06669.
OMA	NIRMENI.
OrthoDB	EOG4TB7KF.
Gene expression databases
Genevestigator	P47037.
GermOnline	YJL074C. Saccharomyces cerevisiae.
Family and domain databases
InterPro	IPR003395. RecF/RecN/SMC. IPR010935. SMC_hinge. [Graphical view]
Pfam	PF06470. SMC_hinge. 1 hit. PF02463. SMC_N. 1 hit. [Graphical view]
SMART	SM00968. SMC_hinge. 1 hit. [Graphical view]
SUPFAM	SSF75553. SMC_hinge. 1 hit.
ProtoNet	Search...
Other
NextBio	973810.

Entry information

Entry name

SMC3_YEAST

Accession

Primary (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:	May 1, 2013
This is version 122 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program