SCC3_YEAST
ID SCC3_YEAST Reviewed; 1150 AA.
AC P40541; D6VVQ4; Q02511;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1995, sequence version 1.
DT 03-AUG-2022, entry version 179.
DE RecName: Full=Cohesin subunit SCC3;
DE AltName: Full=Irregular cell behavior protein 1;
GN Name=IRR1; Synonyms=SCC3; OrderedLocusNames=YIL026C;
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND CHARACTERIZATION.
RX PubMed=7483852; DOI=10.1002/yea.320110910;
RA Kurlandzka A., Rytka J., Gromadka R., Murawski M.;
RT "A new essential gene located on Saccharomyces cerevisiae chromosome IX.";
RL Yeast 11:885-890(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169870;
RA Churcher C.M., Bowman S., Badcock K., Bankier A.T., Brown D.,
RA Chillingworth T., Connor R., Devlin K., Gentles S., Hamlin N., Harris D.E.,
RA Horsnell T., Hunt S., Jagels K., Jones M., Lye G., Moule S., Odell C.,
RA Pearson D., Rajandream M.A., Rice P., Rowley N., Skelton J., Smith V.,
RA Walsh S.V., Whitehead S., Barrell B.G.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome IX.";
RL Nature 387:84-87(1997).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=24374639; DOI=10.1534/g3.113.008995;
RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [4]
RP SUBCELLULAR LOCATION, INTERACTION WITH MCD1, IDENTIFICATION IN A COHESIN
RP COMPLEX WITH SMC1; SMC3 AND MCD1, AND INTERACTION OF THE COHESIN COMPLEX
RP WITH SCC2.
RX PubMed=9990856; DOI=10.1101/gad.13.3.320;
RA Toth A., Ciosk R., Uhlmann F., Galova M., Schleiffer A., Nasmyth K.;
RT "Yeast cohesin complex requires a conserved protein, Eco1p(Ctf7), to
RT establish cohesion between sister chromatids during DNA replication.";
RL Genes Dev. 13:320-333(1999).
RN [5]
RP INTERACTION WITH LIN1.
RX PubMed=12402242; DOI=10.1002/yea.919;
RA Bialkowska A., Kurlandzka A.;
RT "Proteins interacting with Lin 1p, a putative link between chromosome
RT segregation, mRNA splicing and DNA replication in Saccharomyces
RT cerevisiae.";
RL Yeast 19:1323-1333(2002).
RN [6]
RP IDENTIFICATION IN A COHESIN COMPLEX WITH SMC1; SMC3 AND MCD1, AND
RP STRUCTURE.
RX PubMed=11983169; DOI=10.1016/s1097-2765(02)00515-4;
RA Haering C.H., Loewe J., Hochwagen A., Nasmyth K.;
RT "Molecular architecture of SMC proteins and the yeast cohesin complex.";
RL Mol. Cell 9:773-788(2002).
RN [7]
RP ACETYLATION.
RX PubMed=11864574; DOI=10.1016/s0960-9822(02)00681-4;
RA Ivanov D., Schleiffer A., Eisenhaber F., Mechtler K., Haering C.H.,
RA Nasmyth K.;
RT "Eco1 is a novel acetyltransferase that can acetylate proteins involved in
RT cohesion.";
RL Curr. Biol. 12:323-328(2002).
RN [8]
RP LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX PubMed=14562106; DOI=10.1038/nature02046;
RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA O'Shea E.K., Weissman J.S.;
RT "Global analysis of protein expression in yeast.";
RL Nature 425:737-741(2003).
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=18407956; DOI=10.1074/mcp.m700468-mcp200;
RA Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
RT "A multidimensional chromatography technology for in-depth phosphoproteome
RT analysis.";
RL Mol. Cell. Proteomics 7:1389-1396(2008).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-28 AND SER-628, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19779198; DOI=10.1126/science.1172867;
RA Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.;
RT "Global analysis of Cdk1 substrate phosphorylation sites provides insights
RT into evolution.";
RL Science 325:1682-1686(2009).
CC -!- FUNCTION: Component of cohesin complex, a complex required for the
CC cohesion of sister chromatids after DNA replication. The cohesin
CC complex apparently forms a large proteinaceous ring within which sister
CC chromatids can be trapped. At anaphase, the MCD1/SCC1 subunit of the
CC complex is cleaved and dissociates from chromatin, allowing sister
CC chromatids to segregate. The cohesin complex may also play a role in
CC spindle pole assembly during mitosis.
CC -!- SUBUNIT: Interacts directly with MCD1 in cohesin complex. Cohesin
CC complexes are composed of the SMC1 and SMC3 heterodimer attached via
CC their hinge domain, MCD1 which link them, and IRR1/SCC3, which
CC interacts with MCD1. The cohesin complex also interacts with SCC2,
CC which is required for its association with chromosomes. Interacts with
CC LIN1. {ECO:0000269|PubMed:11983169, ECO:0000269|PubMed:12402242,
CC ECO:0000269|PubMed:9990856}.
CC -!- INTERACTION:
CC P40541; Q12158: MCD1; NbExp=7; IntAct=EBI-16667, EBI-16655;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00750,
CC ECO:0000269|PubMed:9990856}. Chromosome {ECO:0000269|PubMed:9990856}.
CC Chromosome, centromere {ECO:0000269|PubMed:9990856}. Note=Associates
CC with chromatin. Before prophase it is scattered along chromosome arms.
CC During prophase, most of cohesin complexes dissociate from chromatin
CC except at centromeres, where cohesin complexes remain. At anaphase, the
CC MCD1 subunit of the cohesin complex is cleaved, leading to the
CC dissociation of the complex from chromosomes, allowing chromosome
CC separation.
CC -!- PTM: Acetylated by ECO1. {ECO:0000269|PubMed:11864574}.
CC -!- MISCELLANEOUS: Present with 4090 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the SCC3 family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; U17918; AAC49039.1; -; Genomic_DNA.
DR EMBL; Z46881; CAA86966.1; -; Genomic_DNA.
DR EMBL; BK006942; DAA08520.1; -; Genomic_DNA.
DR PIR; S49956; S49956.
DR RefSeq; NP_012238.1; NM_001179376.1.
DR PDB; 4UVJ; X-ray; 2.10 A; A/B=674-1072.
DR PDB; 6H8Q; X-ray; 3.63 A; A/B=1-1150.
DR PDBsum; 4UVJ; -.
DR PDBsum; 6H8Q; -.
DR AlphaFoldDB; P40541; -.
DR SMR; P40541; -.
DR BioGRID; 34963; 99.
DR ComplexPortal; CPX-1408; Nuclear meiotic cohesin complex.
DR ComplexPortal; CPX-1867; Nuclear mitotic cohesin complex.
DR DIP; DIP-5640N; -.
DR IntAct; P40541; 20.
DR MINT; P40541; -.
DR STRING; 4932.YIL026C; -.
DR iPTMnet; P40541; -.
DR MaxQB; P40541; -.
DR PaxDb; P40541; -.
DR PRIDE; P40541; -.
DR EnsemblFungi; YIL026C_mRNA; YIL026C; YIL026C.
DR GeneID; 854786; -.
DR KEGG; sce:YIL026C; -.
DR SGD; S000001288; IRR1.
DR VEuPathDB; FungiDB:YIL026C; -.
DR eggNOG; KOG2011; Eukaryota.
DR GeneTree; ENSGT00950000182972; -.
DR HOGENOM; CLU_008263_0_0_1; -.
DR InParanoid; P40541; -.
DR OMA; FVHRFKD; -.
DR BioCyc; YEAST:G3O-31300-MON; -.
DR Reactome; R-SCE-2468052; Establishment of Sister Chromatid Cohesion.
DR Reactome; R-SCE-2500257; Resolution of Sister Chromatid Cohesion.
DR Reactome; R-SCE-3108214; SUMOylation of DNA damage response and repair proteins.
DR PRO; PR:P40541; -.
DR Proteomes; UP000002311; Chromosome IX.
DR RNAct; P40541; protein.
DR GO; GO:0000785; C:chromatin; IBA:GO_Central.
DR GO; GO:0000775; C:chromosome, centromeric region; IEA:UniProtKB-SubCell.
DR GO; GO:0008278; C:cohesin complex; IBA:GO_Central.
DR GO; GO:0005737; C:cytoplasm; IDA:SGD.
DR GO; GO:0005829; C:cytosol; IDA:SGD.
DR GO; GO:0034991; C:nuclear meiotic cohesin complex; IC:ComplexPortal.
DR GO; GO:0034990; C:nuclear mitotic cohesin complex; IDA:SGD.
DR GO; GO:0005634; C:nucleus; IDA:SGD.
DR GO; GO:0003682; F:chromatin binding; IDA:SGD.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0034089; P:establishment of meiotic sister chromatid cohesion; IC:ComplexPortal.
DR GO; GO:0034087; P:establishment of mitotic sister chromatid cohesion; IC:ComplexPortal.
DR GO; GO:0007064; P:mitotic sister chromatid cohesion; IMP:SGD.
DR GO; GO:0006473; P:protein acetylation; IDA:UniProtKB.
DR GO; GO:0007062; P:sister chromatid cohesion; IBA:GO_Central.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR039662; Cohesin_Scc3/SA.
DR InterPro; IPR020839; SCD.
DR InterPro; IPR013721; STAG.
DR PANTHER; PTHR11199; PTHR11199; 1.
DR Pfam; PF08514; STAG; 1.
DR SUPFAM; SSF48371; SSF48371; 1.
DR PROSITE; PS51425; SCD; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Cell cycle; Cell division; Centromere;
KW Chromosome; Chromosome partition; Coiled coil; Mitosis; Nucleus;
KW Phosphoprotein; Reference proteome.
FT CHAIN 1..1150
FT /note="Cohesin subunit SCC3"
FT /id="PRO_0000120191"
FT DOMAIN 367..457
FT /note="SCD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00750"
FT REGION 1..122
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1065..1150
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 305..349
FT /evidence="ECO:0000255"
FT COMPBIAS 11..47
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 48..71
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 78..102
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1073..1088
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1089..1103
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 28
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 628
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT CONFLICT 939
FT /note="V -> G (in Ref. 1; AAC49039)"
FT /evidence="ECO:0000305"
FT HELIX 675..678
FT /evidence="ECO:0007829|PDB:4UVJ"
FT HELIX 680..691
FT /evidence="ECO:0007829|PDB:4UVJ"
FT HELIX 700..707
FT /evidence="ECO:0007829|PDB:4UVJ"
FT HELIX 721..736
FT /evidence="ECO:0007829|PDB:4UVJ"
FT TURN 742..744
FT /evidence="ECO:0007829|PDB:4UVJ"
FT HELIX 747..761
FT /evidence="ECO:0007829|PDB:4UVJ"
FT HELIX 764..788
FT /evidence="ECO:0007829|PDB:4UVJ"
FT HELIX 798..808
FT /evidence="ECO:0007829|PDB:4UVJ"
FT HELIX 810..819
FT /evidence="ECO:0007829|PDB:4UVJ"
FT HELIX 826..835
FT /evidence="ECO:0007829|PDB:4UVJ"
FT HELIX 837..839
FT /evidence="ECO:0007829|PDB:4UVJ"
FT HELIX 840..843
FT /evidence="ECO:0007829|PDB:4UVJ"
FT HELIX 844..846
FT /evidence="ECO:0007829|PDB:4UVJ"
FT HELIX 849..854
FT /evidence="ECO:0007829|PDB:4UVJ"
FT HELIX 858..876
FT /evidence="ECO:0007829|PDB:4UVJ"
FT TURN 890..893
FT /evidence="ECO:0007829|PDB:4UVJ"
FT HELIX 894..911
FT /evidence="ECO:0007829|PDB:4UVJ"
FT TURN 917..919
FT /evidence="ECO:0007829|PDB:4UVJ"
FT HELIX 920..946
FT /evidence="ECO:0007829|PDB:4UVJ"
FT HELIX 953..962
FT /evidence="ECO:0007829|PDB:4UVJ"
FT HELIX 969..989
FT /evidence="ECO:0007829|PDB:4UVJ"
FT HELIX 1002..1005
FT /evidence="ECO:0007829|PDB:4UVJ"
FT HELIX 1016..1032
FT /evidence="ECO:0007829|PDB:4UVJ"
FT HELIX 1038..1045
FT /evidence="ECO:0007829|PDB:4UVJ"
FT TURN 1046..1050
FT /evidence="ECO:0007829|PDB:4UVJ"
FT HELIX 1053..1058
FT /evidence="ECO:0007829|PDB:4UVJ"
SQ SEQUENCE 1150 AA; 133009 MW; 89688EA09485AC28 CRC64;
MTAVRRSTRI RTKSQVIEED YDDEQNTSAQ HVESDKITAK TQHEEEEEQD TGESEESSSE
DDYEDQDDDD YVDTATAKRK SRKRKPKSAS NTSSKRQKKK PTSAQKSAVS HAPAYHRSKK
DQDQYLEIAK DFQPTELFDI LSTSEDVSIE ELLREWLETY SENRDKFLQE FINLLLNCCG
SVARVEDHDV HSNESSNETI GEIQLLFQRQ KLHEFYLLIS KENKKRKNFK MGPLYQNFAE
FMTKLLEVAN DLQLLYVESD EDDTQIVTGN LVLDLLTWLS SFSVCKIRCF RYISTLTLYL
FQDYLTQQAV NLEKNYLAKL SKQLSLEEKK KRPNNKTLEK LESTIAETQG SKVVIDSIID
NIVKLCFVHR YKDVSDLIRS ESMLHLSIWI KNYPEYFLKV TFLKYFGWLL SDNSVSVRLQ
VTKILPHLII QNHNSKSTDN SAIRQVFERF KTKILEVAIR DVNLDVRIHS IQVLTEASSL
GYLDDSEILI ISSLMFDEEF DPFKTSSFNK RSKFLSTVAK FLARVIKEKF DEFIKTHEDL
PKEVDGLEVG PVVQVGIFIK ILNDSLIYHL KDCAEVDSRT KIRMLTQAAE FLSPYISTHL
KTICNLLISD TESNELIQKL QNSANNNSDD EDVDDEELDI TPLFPIDRNS TILYLNVFHG
LCAGANNPKI QTKDSVKEIV LPLFYDLLNA ASIESADILC PLLESFITFS LDDWISIGYE
TELKKITDKT IKAFMDSTIG NSKVDMKYDI FAKFIHHIHH FEKKELQEKF LNQIATLKIH
LKKFLQEKMD PNNSRDDYKD LTCSLYELYI NKLTILGRDY PIEVDEELLQ LFLNNFVSRI
PIMFQDFDDS TAQEINFKML VLLATWNLEK WREIIEKVRD YENSISKDLR SVWKPIAAII
GRLNTLVISL AATNETFENI NSLFYLKWSA CTSLMDIIVA IKIFELKLPA DATTWRYSMS
EQFPFYLHDN ASKVLLKIFL YLESLFAKQV DVQLERVADE DANLNDLPET GFFENIETEF
LLFTVKLKGL MKLNILDERF ASRVALNKEK LGPLFKKIVD DTIMENPEPN KKNIQKAKSN
QTQREKAPLQ PNSERETDHA NTENNDPDIP MTIDLEPIEE SSQNNSELAP IEEHPTVVDA
IDNSDEITQD
