P40541 (SCC3_YEAST) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Cohesin subunit SCC3

Alternative name(s):
Irregular cell behavior protein 1

Gene names

Name:	IRR1
Synonyms:	SCC3
Ordered Locus Names:	YIL026C

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	1150 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Component of cohesin complex, a complex 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 MCD1/SCC1 subunit of the complex is cleaved and dissociates from chromatin, allowing sister chromatids to segregate. The cohesin complex may also play a role in spindle pole assembly during mitosis.
Subunit structure	Interacts directly with MCD1 in cohesin complex. Cohesin complexes are composed of the SMC1 and SMC3 heterodimer attached via their hinge domain, MCD1 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. Interacts with LIN1. Ref.4 Ref.5 Ref.6
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, the MCD1 subunit of the cohesin complex is cleaved, leading to the dissociation of the complex from chromosomes, allowing chromosome separation. Ref.4
Post-translational modification	Acetylated by ECO1.
Miscellaneous	Present with 4090 molecules/cell in log phase SD medium.
Sequence similarities	Belongs to the SCC3 family. Contains 1 SCD (stromalin conservative) domain.

Ontologies

Keywords
Biological process	Cell cycle Cell division Chromosome partition Mitosis
Cellular component	Centromere Chromosome Nucleus
Domain	Coiled coil
PTM	Acetylation Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	cell division Inferred from electronic annotation. Source: UniProtKB-KW cytogamy Inferred from mutant phenotype PubMed 10028182. Source: SGD fungal-type cell wall organization Inferred from mutant phenotype PubMed 17229992. Source: SGD mitotic sister chromatid cohesion Inferred from mutant phenotype Ref.4. Source: SGD protein acetylation Inferred from direct assay Ref.7. Source: UniProtKB spore germination Inferred from mutant phenotype PubMed 10028182. Source: SGD
Cellular_component	chromosome, centromeric region Inferred from electronic annotation. Source: UniProtKB-SubCell nuclear mitotic cohesin complex Inferred from direct assay Ref.4. Source: SGD
Molecular_function	chromatin binding Inferred from direct assay Ref.4. Source: SGD
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
MCD1	Q12158	5	EBI-16667,EBI-16655

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 1150	1150	Cohesin subunit SCC3		PRO_0000120191
Regions
	Domain	367 – 457	91	SCD
	Coiled coil	305 – 349	45	Potential
	Compositional bias	44 – 48	5	Poly-Glu
	Compositional bias	65 – 70	6	Poly-Asp
Amino acid modifications
	Modified residue	27	1	Phosphothreonine Ref.10
	Modified residue	28	1	Phosphoserine Ref.9 Ref.10
	Modified residue	343	1	Phosphoserine Ref.10
Experimental info
	Sequence conflict	939	1	V → G in AAC49039. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	P40541 [UniParc]. Last modified February 1, 1995. Version 1. Checksum: 89688EA09485AC28	FASTA	1,150	133,009
	10 20 30 40 50 60 MTAVRRSTRI RTKSQVIEED YDDEQNTSAQ HVESDKITAK TQHEEEEEQD TGESEESSSE 70 80 90 100 110 120 DDYEDQDDDD YVDTATAKRK SRKRKPKSAS NTSSKRQKKK PTSAQKSAVS HAPAYHRSKK 130 140 150 160 170 180 DQDQYLEIAK DFQPTELFDI LSTSEDVSIE ELLREWLETY SENRDKFLQE FINLLLNCCG 190 200 210 220 230 240 SVARVEDHDV HSNESSNETI GEIQLLFQRQ KLHEFYLLIS KENKKRKNFK MGPLYQNFAE 250 260 270 280 290 300 FMTKLLEVAN DLQLLYVESD EDDTQIVTGN LVLDLLTWLS SFSVCKIRCF RYISTLTLYL 310 320 330 340 350 360 FQDYLTQQAV NLEKNYLAKL SKQLSLEEKK KRPNNKTLEK LESTIAETQG SKVVIDSIID 370 380 390 400 410 420 NIVKLCFVHR YKDVSDLIRS ESMLHLSIWI KNYPEYFLKV TFLKYFGWLL SDNSVSVRLQ 430 440 450 460 470 480 VTKILPHLII QNHNSKSTDN SAIRQVFERF KTKILEVAIR DVNLDVRIHS IQVLTEASSL 490 500 510 520 530 540 GYLDDSEILI ISSLMFDEEF DPFKTSSFNK RSKFLSTVAK FLARVIKEKF DEFIKTHEDL 550 560 570 580 590 600 PKEVDGLEVG PVVQVGIFIK ILNDSLIYHL KDCAEVDSRT KIRMLTQAAE FLSPYISTHL 610 620 630 640 650 660 KTICNLLISD TESNELIQKL QNSANNNSDD EDVDDEELDI TPLFPIDRNS TILYLNVFHG 670 680 690 700 710 720 LCAGANNPKI QTKDSVKEIV LPLFYDLLNA ASIESADILC PLLESFITFS LDDWISIGYE 730 740 750 760 770 780 TELKKITDKT IKAFMDSTIG NSKVDMKYDI FAKFIHHIHH FEKKELQEKF LNQIATLKIH 790 800 810 820 830 840 LKKFLQEKMD PNNSRDDYKD LTCSLYELYI NKLTILGRDY PIEVDEELLQ LFLNNFVSRI 850 860 870 880 890 900 PIMFQDFDDS TAQEINFKML VLLATWNLEK WREIIEKVRD YENSISKDLR SVWKPIAAII 910 920 930 940 950 960 GRLNTLVISL AATNETFENI NSLFYLKWSA CTSLMDIIVA IKIFELKLPA DATTWRYSMS 970 980 990 1000 1010 1020 EQFPFYLHDN ASKVLLKIFL YLESLFAKQV DVQLERVADE DANLNDLPET GFFENIETEF 1030 1040 1050 1060 1070 1080 LLFTVKLKGL MKLNILDERF ASRVALNKEK LGPLFKKIVD DTIMENPEPN KKNIQKAKSN 1090 1100 1110 1120 1130 1140 QTQREKAPLQ PNSERETDHA NTENNDPDIP MTIDLEPIEE SSQNNSELAP IEEHPTVVDA 1150 IDNSDEITQD

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"A new essential gene located on Saccharomyces cerevisiae chromosome IX." Kurlandzka A., Rytka J., Gromadka R., Murawski M. Yeast 11:885-890(1995) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], CHARACTERIZATION.
[2]	"The nucleotide sequence of Saccharomyces cerevisiae chromosome IX." Churcher C.M., Bowman S., Badcock K., Bankier A.T., Brown D., Chillingworth T., Connor R., Devlin K., Gentles S., Hamlin N., Harris D.E., Horsnell T., Hunt S., Jagels K., Jones M., Lye G., Moule S., Odell C. , Pearson D., Rajandream M.A., Rice P., Rowley N., Skelton J., Smith V., Walsh S.V., Whitehead S., Barrell B.G. Nature 387:84-87(1997) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 204511 / S288c / AB972.
[3]	Saccharomyces Genome Database Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases Cited for: GENOME REANNOTATION. Strain: ATCC 204508 / S288c.
[4]	"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 MCD1, IDENTIFICATION IN A COHESIN COMPLEX WITH SMC1; SMC3 AND MCD1, INTERACTION OF THE COHESIN COMPLEX WITH SCC2.
[5]	"Proteins interacting with Lin 1p, a putative link between chromosome segregation, mRNA splicing and DNA replication in Saccharomyces cerevisiae." Bialkowska A., Kurlandzka A. Yeast 19:1323-1333(2002) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH LIN1.
[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 SMC1; SMC3 AND MCD1, STRUCTURE.
[7]	"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.
[8]	"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].
[9]	"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-28, MASS SPECTROMETRY.
[10]	"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 THR-27; SER-28 AND SER-343, MASS SPECTROMETRY.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	U17918 Genomic DNA. Translation: AAC49039.1. Z46881 Genomic DNA. Translation: CAA86966.1. BK006942 Genomic DNA. Translation: DAA08520.1.
PIR	S49956.
RefSeq	NP_012238.1. NM_001179376.1.
3D structure databases
ProteinModelPortal	P40541.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-5640N.
IntAct	P40541. 20 interactions.
MINT	MINT-567741.
STRING	4932.YIL026C.
Proteomic databases
PaxDb	P40541.
PeptideAtlas	P40541.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblFungi	YIL026C; YIL026C; YIL026C.
GeneID	854786.
KEGG	sce:YIL026C.
Organism-specific databases
CYGD	YIL026c.
SGD	S000001288. IRR1.
Phylogenomic databases
eggNOG	COG5537.
GeneTree	ENSGT00390000014094.
HOGENOM	HOG000141696.
KO	K06671.
OMA	KLCFVHR.
OrthoDB	EOG4SXRMN.
Gene expression databases
Genevestigator	P40541.
GermOnline	YIL026C. Saccharomyces cerevisiae.
Family and domain databases
InterPro	IPR016024. ARM-type_fold. IPR020839. SCD. IPR013721. STAG. [Graphical view]
Pfam	PF08514. STAG. 1 hit. [Graphical view]
SUPFAM	SSF48371. ARM-type_fold. 1 hit.
PROSITE	PS51425. SCD. 1 hit. [Graphical view]
ProtoNet	Search...
Other
NextBio	977573.

Entry information

Entry name

SCC3_YEAST

Accession

Primary (citable) accession number: P40541
Secondary accession number(s): D6VVQ4, Q02511

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 1, 1995
Last sequence update:	February 1, 1995
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