SMC4_YEAST
ID SMC4_YEAST Reviewed; 1418 AA.
AC Q12267; D6VY86;
DT 28-MAR-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 179.
DE RecName: Full=Structural maintenance of chromosomes protein 4;
GN Name=SMC4; OrderedLocusNames=YLR086W; ORFNames=L9449.5;
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 [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169871;
RA Johnston M., Hillier L.W., Riles L., Albermann K., Andre B., Ansorge W.,
RA Benes V., Brueckner M., Delius H., Dubois E., Duesterhoeft A.,
RA Entian K.-D., Floeth M., Goffeau A., Hebling U., Heumann K.,
RA Heuss-Neitzel D., Hilbert H., Hilger F., Kleine K., Koetter P., Louis E.J.,
RA Messenguy F., Mewes H.-W., Miosga T., Moestl D., Mueller-Auer S.,
RA Nentwich U., Obermaier B., Piravandi E., Pohl T.M., Portetelle D.,
RA Purnelle B., Rechmann S., Rieger M., Rinke M., Rose M., Scharfe M.,
RA Scherens B., Scholler P., Schwager C., Schwarz S., Underwood A.P.,
RA Urrestarazu L.A., Vandenbol M., Verhasselt P., Vierendeels F., Voet M.,
RA Volckaert G., Voss H., Wambutt R., Wedler E., Wedler H., Zimmermann F.K.,
RA Zollner A., Hani J., Hoheisel J.D.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XII.";
RL Nature 387:87-90(1997).
RN [2]
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 [3]
RP IDENTIFICATION IN A CONDENSIN COMPLEX WITH SMC2; BRN1; YCS4 AND YCG1.
RX PubMed=10811823; DOI=10.1083/jcb.149.4.811;
RA Freeman L., Aragon-Alcaide L., Strunnikov A.V.;
RT "The condensin complex governs chromosome condensation and mitotic
RT transmission of rDNA.";
RL J. Cell Biol. 149:811-824(2000).
RN [4]
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 [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-43 AND SER-113, AND
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 [6]
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).
RN [7]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
CC -!- FUNCTION: Central component of the condensin complex, a complex
CC required for conversion of interphase chromatin into mitotic-like
CC condense chromosomes. The condensin complex probably introduces
CC positive supercoils into relaxed DNA in the presence of type I
CC topoisomerases and converts nicked DNA into positive knotted forms in
CC the presence of type II topoisomerases.
CC -!- SUBUNIT: Forms a heterodimer with SMC2. Component of the condensin
CC complex, which contains the SMC2 and SMC4 heterodimer, and three non
CC SMC subunits that probably regulate the complex: BRN1, YCS4 and
CC YCG1/YCS5. {ECO:0000269|PubMed:10811823}.
CC -!- INTERACTION:
CC Q12267; Q06680: YCG1; NbExp=2; IntAct=EBI-17430, EBI-4799;
CC -!- SUBCELLULAR LOCATION: Nucleus. Cytoplasm. Chromosome. Note=In
CC interphase cells, the majority of the condensin complex is found in the
CC cytoplasm, while a minority of the complex is associated with
CC chromatin. A subpopulation of the complex however remains associated
CC with chromosome foci in interphase cells. During mitosis, most of the
CC condensin complex is associated with the chromatin. At the onset of
CC prophase, condensin associates with chromosome arms and to chromosome
CC condensation. Dissociation from chromosomes is observed in late
CC telophase.
CC -!- DOMAIN: The flexible SMC hinge domain, which separates the large
CC intramolecular coiled coil regions, allows the heterodimerization with
CC SMC2, forming a V-shaped heterodimer. {ECO:0000250}.
CC -!- MISCELLANEOUS: Present with 573 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the SMC family. SMC4 subfamily. {ECO:0000305}.
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DR EMBL; Z73258; CAA97646.1; -; Genomic_DNA.
DR EMBL; Z73259; CAA97648.1; -; Genomic_DNA.
DR EMBL; U53880; AAB67590.1; -; Genomic_DNA.
DR EMBL; BK006945; DAA09402.1; -; Genomic_DNA.
DR PIR; S64918; S64918.
DR RefSeq; NP_013187.1; NM_001181973.1.
DR PDB; 4RSI; X-ray; 2.90 A; B=555-951.
DR PDB; 6YVD; EM; 7.60 A; D=1-1418.
DR PDB; 6YVU; EM; 7.50 A; B=1-1418.
DR PDB; 6YVV; EM; 7.50 A; B=1-1418.
DR PDB; 7Q2X; EM; 3.00 A; B=1-1418.
DR PDB; 7Q2Y; EM; -; B=1-1418.
DR PDBsum; 4RSI; -.
DR PDBsum; 6YVD; -.
DR PDBsum; 6YVU; -.
DR PDBsum; 6YVV; -.
DR PDBsum; 7Q2X; -.
DR PDBsum; 7Q2Y; -.
DR AlphaFoldDB; Q12267; -.
DR SMR; Q12267; -.
DR BioGRID; 31359; 337.
DR ComplexPortal; CPX-1869; Nuclear condensin complex.
DR DIP; DIP-3007N; -.
DR IntAct; Q12267; 14.
DR MINT; Q12267; -.
DR STRING; 4932.YLR086W; -.
DR iPTMnet; Q12267; -.
DR MaxQB; Q12267; -.
DR PaxDb; Q12267; -.
DR PRIDE; Q12267; -.
DR EnsemblFungi; YLR086W_mRNA; YLR086W; YLR086W.
DR GeneID; 850775; -.
DR KEGG; sce:YLR086W; -.
DR SGD; S000004076; SMC4.
DR VEuPathDB; FungiDB:YLR086W; -.
DR eggNOG; KOG0996; Eukaryota.
DR GeneTree; ENSGT00900000141094; -.
DR HOGENOM; CLU_001042_4_1_1; -.
DR InParanoid; Q12267; -.
DR OMA; QIYIDEC; -.
DR BioCyc; YEAST:G3O-32237-MON; -.
DR Reactome; R-SCE-2514853; Condensation of Prometaphase Chromosomes.
DR PRO; PR:Q12267; -.
DR Proteomes; UP000002311; Chromosome XII.
DR RNAct; Q12267; protein.
DR GO; GO:0000796; C:condensin complex; IDA:SGD.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; HDA:SGD.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0003682; F:chromatin binding; IDA:SGD.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0030261; P:chromosome condensation; IC:ComplexPortal.
DR GO; GO:0010032; P:meiotic chromosome condensation; IC:SGD.
DR GO; GO:0051307; P:meiotic chromosome separation; IC:SGD.
DR GO; GO:0007076; P:mitotic chromosome condensation; IMP:SGD.
DR GO; GO:0000070; P:mitotic sister chromatid segregation; IMP:SGD.
DR GO; GO:0070550; P:rDNA chromatin condensation; IMP:SGD.
DR GO; GO:0007130; P:synaptonemal complex assembly; IC:SGD.
DR GO; GO:0070058; P:tRNA gene clustering; IMP:SGD.
DR CDD; cd03274; ABC_SMC4_euk; 2.
DR Gene3D; 3.40.50.300; -; 2.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR003395; RecF/RecN/SMC_N.
DR InterPro; IPR024704; SMC.
DR InterPro; IPR041738; SMC4_ABC_euk.
DR InterPro; IPR010935; SMC_hinge.
DR InterPro; IPR036277; SMC_hinge_sf.
DR Pfam; PF06470; SMC_hinge; 1.
DR Pfam; PF02463; SMC_N; 1.
DR PIRSF; PIRSF005719; SMC; 1.
DR SMART; SM00968; SMC_hinge; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR SUPFAM; SSF75553; SSF75553; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; ATP-binding; Cell cycle; Cell division;
KW Chromosome; Coiled coil; Cytoplasm; DNA condensation; Mitosis;
KW Nucleotide-binding; Nucleus; Phosphoprotein; Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:22814378"
FT CHAIN 2..1418
FT /note="Structural maintenance of chromosomes protein 4"
FT /id="PRO_0000119018"
FT DOMAIN 686..799
FT /note="SMC hinge"
FT REGION 1..122
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 345..673
FT /evidence="ECO:0000255"
FT COILED 849..1172
FT /evidence="ECO:0000255"
FT COILED 1224..1263
FT /evidence="ECO:0000255"
FT COMPBIAS 1..19
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 60..96
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 185..192
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0007744|PubMed:22814378"
FT MOD_RES 43
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18407956"
FT MOD_RES 113
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956"
FT HELIX 562..681
FT /evidence="ECO:0007829|PDB:4RSI"
FT STRAND 688..691
FT /evidence="ECO:0007829|PDB:4RSI"
FT HELIX 692..694
FT /evidence="ECO:0007829|PDB:4RSI"
FT STRAND 695..698
FT /evidence="ECO:0007829|PDB:4RSI"
FT HELIX 700..702
FT /evidence="ECO:0007829|PDB:4RSI"
FT HELIX 703..709
FT /evidence="ECO:0007829|PDB:4RSI"
FT HELIX 711..714
FT /evidence="ECO:0007829|PDB:4RSI"
FT STRAND 715..719
FT /evidence="ECO:0007829|PDB:4RSI"
FT HELIX 721..734
FT /evidence="ECO:0007829|PDB:4RSI"
FT STRAND 738..744
FT /evidence="ECO:0007829|PDB:4RSI"
FT HELIX 758..760
FT /evidence="ECO:0007829|PDB:4RSI"
FT TURN 764..767
FT /evidence="ECO:0007829|PDB:4RSI"
FT STRAND 768..772
FT /evidence="ECO:0007829|PDB:4RSI"
FT HELIX 773..775
FT /evidence="ECO:0007829|PDB:4RSI"
FT HELIX 778..782
FT /evidence="ECO:0007829|PDB:4RSI"
FT STRAND 784..787
FT /evidence="ECO:0007829|PDB:4RSI"
FT HELIX 794..797
FT /evidence="ECO:0007829|PDB:4RSI"
FT STRAND 800..803
FT /evidence="ECO:0007829|PDB:4RSI"
FT STRAND 806..808
FT /evidence="ECO:0007829|PDB:4RSI"
FT STRAND 821..823
FT /evidence="ECO:0007829|PDB:4RSI"
FT STRAND 832..834
FT /evidence="ECO:0007829|PDB:4RSI"
FT HELIX 850..883
FT /evidence="ECO:0007829|PDB:4RSI"
FT HELIX 886..910
FT /evidence="ECO:0007829|PDB:4RSI"
FT TURN 911..913
FT /evidence="ECO:0007829|PDB:4RSI"
FT HELIX 914..925
FT /evidence="ECO:0007829|PDB:4RSI"
FT HELIX 929..947
FT /evidence="ECO:0007829|PDB:4RSI"
SQ SEQUENCE 1418 AA; 162189 MW; F0E6B72FE8BFD374 CRC64;
MSDSPLSKRQ KRKSAQEPEL SLDQGDAEED SQVENRVNLS ENTPEPDLPA LEASYSKSYT
PRKLVLSSGE NRYAFSQPTN STTTSLHVPN LQPPKTSSRG RDHKSYSQSP PRSPGRSPTR
RLELLQLSPV KNSRVELQKI YDRHQSSSKQ QSRLFINELV LENFKSYAGK QVVGPFHTSF
SAVVGPNGSG KSNVIDSMLF VFGFRANKMR QDRLSDLIHK SEAFPSLQSC SVAVHFQYVI
DESSGTSRID EEKPGLIITR KAFKNNSSKY YINEKESSYT EVTKLLKNEG IDLDHKRFLI
LQGEVENIAQ MKPKAEKESD DGLLEYLEDI IGTANYKPLI EERMGQIENL NEVCLEKENR
FEIVDREKNS LESGKETALE FLEKEKQLTL LRSKLFQFKL LQSNSKLAST LEKISSSNKD
LEDEKMKFQE SLKKVDEIKA QRKEIKDRIS SCSSKEKTLV LERRELEGTR VSLEERTKNL
VSKMEKAEKT LKSTKHSISE AENMLEELRG QQTEHETEIK DLTQLLEKER SILDDIKLSL
KDKTKNISAE IIRHEKELEP WDLQLQEKES QIQLAESELS LLEETQAKLK KNVETLEEKI
LAKKTHKQEL QDLILDLKKK LNSLKDERSQ GEKNFTSAHL KLKEMQKVLN AHRQRAMEAR
SSLSKAQNKS KVLTALSRLQ KSGRINGFHG RLGDLGVIDD SFDVAISTAC PRLDDVVVDT
VECAQHCIDY LRKNKLGYAR FILLDRLRQF NLQPISTPEN VPRLFDLVKP KNPKFSNAFY
SVLRDTLVAQ NLKQANNVAY GKKRFRVVTV DGKLIDISGT MSGGGNHVAK GLMKLGTNQS
DKVDDYTPEE VDKIERELSE RENNFRVASD TVHEMEEELK KLRDHEPDLE SQISKAEMEA
DSLASELTLA EQQVKEAEMA YVKAVSDKAQ LNVVMKNLER LRGEYNDLQS ETKTKKEKIK
GLQDEIMKIG GIKLQMQNSK VESVCQKLDI LVAKLKKVKS ASKKSGGDVV KFQKLLQNSE
RDVELSSDEL KVIEEQLKHT KLALAENDTN MNETLNLKVE LKEQSEQLKE QMEDMEESIN
EFKSIEIEMK NKLEKLNSLL TYIKSEITQQ EKGLNELSIR DVTHTLGMLD DNKMDSVKED
VKNNQELDQE YRSCETQDES EIKDAETSCD NYHPMNIDET SDEVSRGIPR LSEDELRELD
VELIESKINE LSYYVEETNV DIGVLEEYAR RLAEFKRRKL DLNNAVQKRD EVKEQLGILK
KKRFDEFMAG FNIISMTLKE MYQMITMGGN AELELVDSLD PFSEGVTFSV MPPKKSWRNI
TNLSGGEKTL SSLALVFALH KYKPTPLYVM DEIDAALDFR NVSIVANYIK ERTKNAQFIV
ISLRNNMFEL AQQLVGVYKR DNRTKSTTIK NIDILNRT
