Q12158 (SCC1_YEAST) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Sister chromatid cohesion protein 1

Gene names

Name:	MCD1
Synonyms:	PDS3, RHC21, SCC1
Ordered Locus Names:	YDL003W
ORF Names:	YD8119.04

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	566 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Cleavable component of the cohesin complex involved in chromosome cohesion during cell cycle. 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 metaphase-anaphase transition, this protein is cleaved by ESP1 and dissociates from chromatin, allowing sister chromatids to segregate. Ref.1 Ref.2 Ref.5 Ref.7
Subunit structure	Interacts directly with IRR1/SCC3 in cohesin complex. Cohesin complexes are composed of the SMC1 and SMC3 heterodimer attached via their hinge domain, MCD1/SCC1 which link them, and IRR1, which interacts with MCD1. The cohesin complex also interacts with SCC2, which is required for its association with chromosomes. Ref.6 Ref.9
Subcellular location	Nucleus. Chromosome. Chromosome › centromere. Note: Associates with chromatin. Before prophase it is scattered along chromosome arms. During prophase, most of cohesin complexes dissociate from chromatin except at centromeres, where cohesin complexes remain. At anaphase, it is cleaved by ESP1, leading to the dissociation of the complex from chromosomes, allowing chromosome separation. Ref.1 Ref.2 Ref.6
Domain	The C-terminal part associates with the head of SMC1, while the N-terminal part binds to the head of SMC3.
Post-translational modification	Cleaved by ESP1 at the onset of anaphase. Phosphorylated by CDC5/Polo-like kinase at the onset of anaphase. Phosphorylation takes places at proximity to cleavage sites and is required for an efficient cleavage by ESP1. Ref.8 Acetylated by ECO1.
Miscellaneous	Present with 1040 molecules/cell in log phase SD medium.
Sequence similarities	Belongs to the rad21 family.

Ontologies

Keywords
Biological process	Cell cycle Cell division Chromosome partition Mitosis
Cellular component	Centromere Chromosome Nucleus
PTM	Acetylation Phosphoprotein
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	apoptotic process Inferred from mutant phenotype PubMed 18321989. Source: SGD cell division Inferred from electronic annotation. Source: UniProtKB-KW double-strand break repair Inferred from mutant phenotype PubMed 11448778. Source: SGD establishment of mitotic sister chromatid cohesion Inferred from mutant phenotype PubMed 16962805. Source: SGD mitotic chromosome condensation Inferred from mutant phenotype Ref.2. Source: SGD protein acetylation Inferred from direct assay Ref.10. Source: UniProtKB
Cellular_component	chromosome, centromeric region Inferred from electronic annotation. Source: UniProtKB-SubCell mitochondrion Inferred from direct assay PubMed 18321989. Source: SGD nuclear mitotic cohesin complex Inferred from direct assay Ref.6. Source: SGD
Molecular_function	chromatin binding Inferred from direct assay PubMed 18614046Ref.6. Source: SGD
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
IRR1	P40541	5	EBI-16655,EBI-16667
SMC1	P32908	7	EBI-16655,EBI-17402
SMC3	P47037	11	EBI-16655,EBI-17423

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 566

566

Sister chromatid cohesion protein 1

PRO_0000097881

Regions

Compositional bias

258 – 261

4

Poly-Asp

Sites

Site

180 – 181

2

Cleavage; by ESP1

Site

268 – 269

2

Cleavage; by ESP1

Amino acid modifications

Modified residue

161

1

Phosphoserine Ref.13

Modified residue

174

1

Phosphothreonine Ref.13

Modified residue

175

1

Phosphoserine; by CDC5 Ref.13

Modified residue

210

1

N6-acetyllysine; by ECO1 Ref.10

Modified residue

263

1

Phosphoserine; by CDC5 Ref.12

Modified residue

307

1

Phosphoserine Ref.13

Modified residue

354

1

Phosphothreonine Ref.13

Experimental info

Mutagenesis

175

1

S → A: Reduces phosphorylation. Abolishes phosphorylation; when associated with A-263. Ref.8

Mutagenesis

180

1

R → D: Abolishes cleavage by ESP1; when associated with D-268. Ref.7

Mutagenesis

210

1

K → R: Loss of acetylation by ECO1. Ref.10

Mutagenesis

252

1

K → R: No effect on acetylation by ECO1. Ref.10

Mutagenesis

263

1

S → A: Reduces phosphorylation. Abolishes phosphorylation; when associated with A-175. Ref.8

Mutagenesis

268

1

R → D: Abolishes first cleavage by ESP1. Abolishes all cleavage by ESP1; when associated with D-180. Ref.7

Mutagenesis

290

1

K → R: No effect on acetylation by ECO1. Ref.10

Mutagenesis

310

1

K → R: No effect on acetylation by ECO1. Ref.10

Mutagenesis

319

1

K → R: No effect on acetylation by ECO1. Ref.10

Mutagenesis

324

1

K → R: No effect on acetylation by ECO1. Ref.10

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

566

Helix Strand Turn

Details...

Helix

484 – 495

12

Helix

504 – 509

6

Helix

522 – 537

16

Beta strand

539 – 544

6

Beta strand

551 – 555

5

Helix

557 – 559

3

Sequences

	Sequence		Length	Mass (Da)
	Q12158 [UniParc]. Last modified November 1, 1996. Version 1. Checksum: EB6C7CA33BAC208F	FASTA	566	63,290
	10 20 30 40 50 60 MVTENPQRLT VLRLATNKGP LAQIWLASNM SNIPRGSVIQ THIAESAKEI AKASGCDDES 70 80 90 100 110 120 GDNEYITLRT SGELLQGIVR VYSKQATFLL TDIKDTLTKI SMLFKTSQKM TSTVNRLNTV 130 140 150 160 170 180 TRVHQLMLED AVTEREVLVT PGLEFLDDTT IPVGLMAQEN SMERKVQGAA PWDTSLEVGR 190 200 210 220 230 240 RFSPDEDFEH NNLSSMNLDF DIEEGPITSK SWEEGTRQSS RNFDTHENYI QDDDFPLDDA 250 260 270 280 290 300 GTIGWDLGIT EKNDQNNDDD DNSVEQGRRL GESIMSEEPT DFGFDLDIEK EAPAGNIDTI 310 320 330 340 350 360 TDAMTESQPK QTGTRRNSKL LNTKSIQIDE ETENSESIAS SNTYKEERSN NLLTPQPTNF 370 380 390 400 410 420 TTKRLWSEIT ESMSYLPDPI LKNFLSYESL KKRKIHNGRE GSIEEPELNV SLNLTDDVIS 430 440 450 460 470 480 NAGTNDNSFN ELTDNMSDFV PIDAGLNEAP FPEENIIDAK TRNEQTTIQT EKVRPTPGEV 490 500 510 520 530 540 ASKAIVQMAK ILRKELSEEK EVIFTDVLKS QANTEPENIT KREASRGFFD ILSLATEGCI 550 560 GLSQTEAFGN IKIDAKPALF ERFINA

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], FUNCTION, SUBCELLULAR LOCATION. Strain: ATCC 200060 / W303.
[2]	"A direct link between sister chromatid cohesion and chromosome condensation revealed through the analysis of MCD1 in S. cerevisiae." Guacci V., Koshland D., Strunnikov A.V. Cell 91:47-57(1997) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, SUBCELLULAR LOCATION. Strain: S288c / FY1678.
[3]	"The nucleotide sequence of Saccharomyces cerevisiae chromosome IV." Jacq C., Alt-Moerbe J., Andre B., Arnold W., Bahr A., Ballesta J.P.G., Bargues M., Baron L., Becker A., Biteau N., Bloecker H., Blugeon C., Boskovic J., Brandt P., Brueckner M., Buitrago M.J., Coster F., Delaveau T. , del Rey F., Dujon B., Eide L.G., Garcia-Cantalejo J.M., Goffeau A., Gomez-Peris A., Granotier C., Hanemann V., Hankeln T., Hoheisel J.D., Jaeger W., Jimenez A., Jonniaux J.-L., Kraemer C., Kuester H., Laamanen P., Legros Y., Louis E.J., Moeller-Rieker S., Monnet A., Moro M., Mueller-Auer S., Nussbaumer B., Paricio N., Paulin L., Perea J., Perez-Alonso M., Perez-Ortin J.E., Pohl T.M., Prydz H., Purnelle B., Rasmussen S.W., Remacha M.A., Revuelta J.L., Rieger M., Salom D., Saluz H.P., Saiz J.E., Saren A.-M., Schaefer M., Scharfe M., Schmidt E.R., Schneider C., Scholler P., Schwarz S., Soler-Mira A., Urrestarazu L.A., Verhasselt P., Vissers S., Voet M., Volckaert G., Wagner G., Wambutt R., Wedler E., Wedler H., Woelfl S., Harris D.E., Bowman S., Brown D., Churcher C.M., Connor R., Dedman K., Gentles S., Hamlin N., Hunt S., Jones L., McDonald S., Murphy L.D., Niblett D., Odell C., Oliver K., Rajandream M.A., Richards C., Shore L., Walsh S.V., Barrell B.G., Dietrich F.S., Mulligan J.T., Allen E., Araujo R., Aviles E., Berno A., Carpenter J., Chen E., Cherry J.M., Chung E., Duncan M., Hunicke-Smith S., Hyman R.W., Komp C., Lashkari D., Lew H., Lin D., Mosedale D., Nakahara K., Namath A., Oefner P., Oh C., Petel F.X., Roberts D., Schramm S., Schroeder M., Shogren T., Shroff N., Winant A., Yelton M.A., Botstein D., Davis R.W., Johnston M., Andrews S., Brinkman R., Cooper J., Ding H., Du Z., Favello A., Fulton L., Gattung S., Greco T., Hallsworth K., Hawkins J., Hillier L.W., Jier M., Johnson D., Johnston L., Kirsten J., Kucaba T., Langston Y., Latreille P., Le T., Mardis E., Menezes S., Miller N., Nhan M., Pauley A., Peluso D., Rifkin L., Riles L., Taich A., Trevaskis E., Vignati D., Wilcox L., Wohldman P., Vaudin M., Wilson R., Waterston R., Albermann K., Hani J., Heumann K., Kleine K., Mewes H.-W., Zollner A., Zaccaria P. Nature 387:75-78(1997) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: S288c / FY1678.
[4]	Saccharomyces Genome Database Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases Cited for: GENOME REANNOTATION. Strain: ATCC 204508 / S288c.
[5]	"The RHC21 gene of budding yeast, a homologue of the fission yeast rad21+ gene, is essential for chromosome segregation." Heo S.-J., Tatebayashi K., Kato J., Ikeda H. Mol. Gen. Genet. 257:149-156(1998) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION.
[6]	"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: SUBCELLULAR LOCATION, INTERACTION WITH IRR1, IDENTIFICATION IN A COHESIN COMPLEX WITH SMC1; SMC3 AND IRR1, INTERACTION OF THE COHESIN COMPLEX WITH SCC2.
[7]	"Sister-chromatid separation at anaphase onset is promoted by cleavage of the cohesin subunit Scc1." Uhlmann F., Lottspeich F., Nasmyth K. Nature 400:37-42(1999) [PubMed] [Europe PMC] [Abstract] Cited for: CLEAVAGE BY ESP1, FUNCTION, MUTAGENESIS OF ARG-180 AND ARG-268.
[8]	"Phosphorylation of the cohesin subunit Scc1 by Polo/Cdc5 kinase regulates sister chromatid separation in yeast." Alexandru G., Uhlmann F., Mechtler K., Poupart M.-A., Nasmyth K. Cell 105:459-472(2001) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION BY CDC5, MUTAGENESIS OF SER-175 AND SER-263.
[9]	"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 SMC1; SMC3 AND IRR1, STRUCTURE.
[10]	"Eco1 is a novel acetyltransferase that can acetylate proteins involved in cohesion." Ivanov D., Schleiffer A., Eisenhaber F., Mechtler K., Haering C.H., Nasmyth K. Curr. Biol. 12:323-328(2002) [PubMed] [Europe PMC] [Abstract] Cited for: ACETYLATION AT LYS-210, MUTAGENESIS OF LYS-210; LYS-252; LYS-290; LYS-310; LYS-319 AND LYS-324.
[11]	"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].
[12]	"Proteome-wide identification of in vivo targets of DNA damage checkpoint kinases." Smolka M.B., Albuquerque C.P., Chen S.H., Zhou H. Proc. Natl. Acad. Sci. U.S.A. 104:10364-10369(2007) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-263, MASS SPECTROMETRY.
[13]	"A multidimensional chromatography technology for in-depth phosphoproteome analysis." Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H. Mol. Cell. Proteomics 7:1389-1396(2008) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-161; THR-174; SER-175; SER-307 AND THR-354, MASS SPECTROMETRY.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

Y14280 Genomic DNA. Translation: CAA74657.1.
U23759 Genomic DNA. Translation: AAB38803.1.
Z48008 Genomic DNA. Translation: CAA88058.1.
Z48432 Genomic DNA. Translation: CAA88356.1.
Z74051 Genomic DNA. Translation: CAA98559.1.
BK006938 Genomic DNA. Translation: DAA11845.1.

PIR

S50979.

RefSeq

NP_010281.1. NM_001180062.1.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1W1W	X-ray	2.90	E/F/G/H	451-564	[»]

ProteinModelPortal

Q12158.

SMR

Q12158. Positions 483-560.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-5812N.

IntAct

Q12158. 35 interactions.

MINT

MINT-627334.

Proteomic databases

PaxDb

Q12158.

PeptideAtlas

Q12158.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblFungi

YDL003W; YDL003W; YDL003W.

GeneID

851561.

KEGG

sce:YDL003W.

Organism-specific databases

CYGD

YDL003w.

SGD

S000002161. MCD1.

Phylogenomic databases

eggNOG

NOG249424.

HOGENOM

HOG000141751.

KO

K06670.

OrthoDB

EOG4C2MKJ.

Gene expression databases

Genevestigator

Q12158.

GermOnline

YDL003W. Saccharomyces cerevisiae.

Family and domain databases

Gene3D

1.10.10.580. 1 hit.

InterPro

IPR023093. Rad21/Rec8_C.
IPR006909. Rad21/Rec8_C_eu.
IPR006910. Rad21_Rec8_N.
[Graphical view]

Pfam

PF04824. Rad21_Rec8. 1 hit.
PF04825. Rad21_Rec8_N. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

EvolutionaryTrace

Q12158.

NextBio

968995.

PMAP-CutDB

Q12158.

Entry information

Entry name

SCC1_YEAST

Accession

Primary (citable) accession number: Q12158
Secondary accession number(s): D6VRY5, Q05325

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 9, 2003
Last sequence update:	November 1, 1996
Last modified:	April 3, 2013
This is version 112 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program