MCM1_YEAST
ID MCM1_YEAST Reviewed; 286 AA.
AC P11746; D6VZL8;
DT 01-OCT-1989, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1991, sequence version 2.
DT 03-AUG-2022, entry version 198.
DE RecName: Full=Pheromone receptor transcription factor;
DE AltName: Full=GRM/PRTF protein;
GN Name=MCM1; Synonyms=FUN80; OrderedLocusNames=YMR043W; ORFNames=YM9532.08;
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].
RX PubMed=2159934; DOI=10.1101/gad.4.2.299;
RA Ammerer G.;
RT "Identification, purification, and cloning of a polypeptide (PRTF/GRM) that
RT binds to mating-specific promoter elements in yeast.";
RL Genes Dev. 4:299-312(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=3066908; DOI=10.1016/0022-2836(88)90358-0;
RA Passmore S., Maine G.T., Elble R., Christ C., Tye B.K.;
RT "Saccharomyces cerevisiae protein involved in plasmid maintenance is
RT necessary for mating of MAT alpha cells.";
RL J. Mol. Biol. 204:593-606(1988).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=3311883; DOI=10.1016/0378-1119(87)90286-1;
RA Dubois E., Bercy J., Descamps F., Messenguy F.;
RT "Characterization of two new genes essential for vegetative growth in
RT Saccharomyces cerevisiae: nucleotide sequence determination and chromosome
RT mapping.";
RL Gene 55:265-275(1987).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169872;
RA Bowman S., Churcher C.M., Badcock K., Brown D., Chillingworth T.,
RA Connor R., Dedman K., Devlin K., Gentles S., Hamlin N., Hunt S., Jagels K.,
RA Lye G., Moule S., Odell C., Pearson D., Rajandream M.A., Rice P.,
RA Skelton J., Walsh S.V., Whitehead S., Barrell B.G.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XIII.";
RL Nature 387:90-93(1997).
RN [5]
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 [6]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=17322287; DOI=10.1101/gr.6037607;
RA Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F.,
RA Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J.,
RA Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J.,
RA Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D.,
RA LaBaer J.;
RT "Approaching a complete repository of sequence-verified protein-encoding
RT clones for Saccharomyces cerevisiae.";
RL Genome Res. 17:536-543(2007).
RN [7]
RP INTERACTION WITH ALPHA1 AND ALPHA2.
RX PubMed=1756728; DOI=10.1002/j.1460-2075.1991.tb04999.x;
RA Primig M., Winkler H., Ammerer G.;
RT "The DNA binding and oligomerization domain of MCM1 is sufficient for its
RT interaction with other regulatory proteins.";
RL EMBO J. 10:4209-4218(1991).
RN [8]
RP INTERACTION WITH ALPHA2.
RX PubMed=8628280; DOI=10.1128/mcb.16.5.2135;
RA Mead J., Zhong H., Acton T.B., Vershon A.K.;
RT "The yeast alpha2 and Mcm1 proteins interact through a region similar to a
RT motif found in homeodomain proteins of higher eukaryotes.";
RL Mol. Cell. Biol. 16:2135-2143(1996).
RN [9]
RP INTERACTION WITH ARG81 AND ARG82.
RX PubMed=10632874; DOI=10.1046/j.1365-2958.2000.01665.x;
RA El Bakkoury M., Dubois E., Messenguy F.;
RT "Recruitment of the yeast MADS-box proteins, ArgRI and Mcm1 by the
RT pleiotropic factor ArgRIII is required for their stability.";
RL Mol. Microbiol. 35:15-31(2000).
RN [10]
RP INTERACTION WITH YHP1 AND YOX1.
RX PubMed=12464633; DOI=10.1101/gad.1034302;
RA Pramila T., Miles S., GuhaThakurta D., Jemiolo D., Breeden L.L.;
RT "Conserved homeodomain proteins interact with MADS box protein Mcm1 to
RT restrict ECB-dependent transcription to the M/G1 phase of the cell cycle.";
RL Genes Dev. 16:3034-3045(2002).
RN [11]
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 [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2, AND IDENTIFICATION BY MASS
RP 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 [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-144, AND IDENTIFICATION BY
RP 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 [14]
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).
RN [15]
RP X-RAY CRYSTALLOGRAPHY (2.25 ANGSTROMS) OF 1-100 IN COMPLEX WITH ALPHA2.
RX PubMed=9490409; DOI=10.1038/35563;
RA Tan S., Richmond T.J.;
RT "Crystal structure of the yeast MATalpha2/MCM1/DNA ternary complex.";
RL Nature 391:660-666(1998).
CC -!- FUNCTION: Transcription factor required for the efficient replication
CC of minichromosomes and the transcriptional regulation of early cell
CC cycle genes. Activates transcription of ECB-dependent genes during the
CC G1/M phase. Genes that contain a ECB (early cell box) element in their
CC transcription regulatory region are transcribed only during G1/M
CC phases. Interacts with the alpha-2 repressor or with the alpha-1
CC activator thereby regulating the expression of mating-type-specific
CC genes. With ARG80, ARG81 and ARG82, coordinates the expression of
CC arginine anabolic and catabolic genes in response to arginine.
CC -!- SUBUNIT: Homodimer. Binds DNA with a high specificity in complex with
CC mating-type protein ALPHA1. Also binds DNA with a high specificity as a
CC heterotetramer consisting of an ALPHA2 dimer and an MCM1 dimer.
CC Interacts with YHP1 and YOX1, possibly leading to its inactivation.
CC Interacts with ARG80 and ARG82. {ECO:0000269|PubMed:10632874,
CC ECO:0000269|PubMed:12464633, ECO:0000269|PubMed:1756728,
CC ECO:0000269|PubMed:8628280, ECO:0000269|PubMed:9490409}.
CC -!- INTERACTION:
CC P11746; P0CY08: MATALPHA2; NbExp=2; IntAct=EBI-10528, EBI-10443;
CC -!- SUBCELLULAR LOCATION: Nucleus.
CC -!- MISCELLANEOUS: Present with 8970 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
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DR EMBL; X52453; CAA36691.1; -; Genomic_DNA.
DR EMBL; X14187; CAA32389.1; -; Genomic_DNA.
DR EMBL; M17511; AAA34609.1; -; Genomic_DNA.
DR EMBL; Z48502; CAA88409.1; -; Genomic_DNA.
DR EMBL; AY557985; AAS56311.1; -; Genomic_DNA.
DR EMBL; BK006946; DAA09942.1; -; Genomic_DNA.
DR PIR; A34599; A34599.
DR RefSeq; NP_013757.1; NM_001182540.1.
DR PDB; 1MNM; X-ray; 2.25 A; A/B=1-100.
DR PDBsum; 1MNM; -.
DR AlphaFoldDB; P11746; -.
DR SMR; P11746; -.
DR BioGRID; 35216; 407.
DR ComplexPortal; CPX-1152; ARGR-MCM1 transcription regulation complex.
DR ComplexPortal; CPX-692; Mating-type MATalpha2-MCM1 complex.
DR ComplexPortal; CPX-693; Mating-type MATalpha1-MCM1 complex.
DR DIP; DIP-72N; -.
DR IntAct; P11746; 53.
DR MINT; P11746; -.
DR STRING; 4932.YMR043W; -.
DR iPTMnet; P11746; -.
DR PaxDb; P11746; -.
DR PRIDE; P11746; -.
DR EnsemblFungi; YMR043W_mRNA; YMR043W; YMR043W.
DR GeneID; 855060; -.
DR KEGG; sce:YMR043W; -.
DR SGD; S000004646; MCM1.
DR VEuPathDB; FungiDB:YMR043W; -.
DR eggNOG; KOG0015; Eukaryota.
DR GeneTree; ENSGT00400000022158; -.
DR HOGENOM; CLU_063931_2_1_1; -.
DR InParanoid; P11746; -.
DR OMA; HENGNNA; -.
DR BioCyc; YEAST:G3O-32748-MON; -.
DR Reactome; R-SCE-9031628; NGF-stimulated transcription.
DR EvolutionaryTrace; P11746; -.
DR PRO; PR:P11746; -.
DR Proteomes; UP000002311; Chromosome XIII.
DR RNAct; P11746; protein.
DR GO; GO:0000785; C:chromatin; IDA:SGD.
DR GO; GO:0005829; C:cytosol; IDA:SGD.
DR GO; GO:0005634; C:nucleus; IDA:SGD.
DR GO; GO:0090575; C:RNA polymerase II transcription regulator complex; IPI:ComplexPortal.
DR GO; GO:0090571; C:RNA polymerase II transcription repressor complex; IPI:ComplexPortal.
DR GO; GO:0003688; F:DNA replication origin binding; IDA:SGD.
DR GO; GO:0001228; F:DNA-binding transcription activator activity, RNA polymerase II-specific; IDA:SGD.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IDA:SGD.
DR GO; GO:0001227; F:DNA-binding transcription repressor activity, RNA polymerase II-specific; IDA:SGD.
DR GO; GO:0046983; F:protein dimerization activity; IEA:InterPro.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IDA:SGD.
DR GO; GO:0044377; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding, bending; IDA:SGD.
DR GO; GO:0061629; F:RNA polymerase II-specific DNA-binding transcription factor binding; IDA:SGD.
DR GO; GO:0043565; F:sequence-specific DNA binding; HDA:SGD.
DR GO; GO:0006525; P:arginine metabolic process; IEA:UniProtKB-KW.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IDA:SGD.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:SGD.
DR GO; GO:0000821; P:regulation of arginine metabolic process; IC:ComplexPortal.
DR GO; GO:0031494; P:regulation of mating type switching; IMP:SGD.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR CDD; cd00266; MADS_SRF_like; 1.
DR DisProt; DP02397; -.
DR Gene3D; 3.40.1810.10; -; 1.
DR InterPro; IPR033897; MADS_SRF-like.
DR InterPro; IPR002100; TF_MADSbox.
DR InterPro; IPR036879; TF_MADSbox_sf.
DR Pfam; PF00319; SRF-TF; 1.
DR PRINTS; PR00404; MADSDOMAIN.
DR SMART; SM00432; MADS; 1.
DR SUPFAM; SSF55455; SSF55455; 1.
DR PROSITE; PS00350; MADS_BOX_1; 1.
DR PROSITE; PS50066; MADS_BOX_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Activator; Arginine metabolism; Cell cycle;
KW DNA-binding; Nucleus; Phosphoprotein; Reference proteome; Transcription;
KW Transcription regulation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:22814378"
FT CHAIN 2..286
FT /note="Pheromone receptor transcription factor"
FT /id="PRO_0000199439"
FT DOMAIN 18..72
FT /note="MADS-box"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00251"
FT REGION 97..137
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 167..264
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 97..119
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 122..137
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0007744|PubMed:22814378"
FT MOD_RES 2
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956"
FT MOD_RES 144
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT CONFLICT 9
FT /note="P -> S (in Ref. 3; AAA34609)"
FT /evidence="ECO:0000305"
FT CONFLICT 37
FT /note="S -> F (in Ref. 3; AAA34609)"
FT /evidence="ECO:0000305"
FT CONFLICT 156..157
FT /note="GA -> AR (in Ref. 3; AAA34609)"
FT /evidence="ECO:0000305"
FT CONFLICT 158..286
FT /note="Missing (in Ref. 3; AAA34609)"
FT /evidence="ECO:0000305"
FT HELIX 29..54
FT /evidence="ECO:0007829|PDB:1MNM"
FT STRAND 57..63
FT /evidence="ECO:0007829|PDB:1MNM"
FT STRAND 69..73
FT /evidence="ECO:0007829|PDB:1MNM"
FT TURN 75..78
FT /evidence="ECO:0007829|PDB:1MNM"
FT HELIX 79..82
FT /evidence="ECO:0007829|PDB:1MNM"
FT HELIX 84..94
FT /evidence="ECO:0007829|PDB:1MNM"
SQ SEQUENCE 286 AA; 32802 MW; FD75B4BF549E9E3B CRC64;
MSDIEEGTPT NNGQQKERRK IEIKFIENKT RRHVTFSKRK HGIMKKAFEL SVLTGTQVLL
LVVSETGLVY TFSTPKFEPI VTQQEGRNLI QACLNAPDDE EEDEEEDGDD DDDDDDDGND
MQRQQPQQQQ PQQQQQVLNA HANSLGHLNQ DQVPAGALKQ EVKSQLLGGA NPNQNSMIQQ
QQHHTQNSQP QQQQQQQPQQ QMSQQQMSQH PRPQQGIPHP QQSQPQQQQQ QQQQLQQQQQ
QQQQQPLTGI HQPHQQAFAN AASPYLNAEQ NAAYQQYFQE PQQGQY
