P11746 (MCM1_YEAST) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Pheromone receptor transcription factor

Alternative name(s):
GRM/PRTF protein

Gene names

Name:	MCM1
Synonyms:	FUN80
Ordered Locus Names:	YMR043W
ORF Names:	YM9532.08

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

General annotation (Comments)

Function	Transcription factor required for the efficient replication of minichromosomes and the transcriptional regulation of early cell cycle genes. Activates transcription of ECB-dependent genes during the G1/M phase. Genes that contain a ECB (early cell box) element in their transcription regulatory region are transcribed only during G1/M phases. Interacts with the alpha-2 repressor or with the alpha-1 activator thereby regulating the expression of mating-type-specific genes. With ARG80, ARG81 and ARG82, coordinates the expression of arginine anabolic and catabolic genes in response to arginine.
Subunit structure	Homodimer. Binds DNA with a high specificity in complex with mating-type protein ALPHA1. Also binds DNA with a high specificity as a heterotetramer consisting of an ALPHA2 dimer and an MCM1 dimer. Interacts with YHP1 and YOX1, possibly leading to its inactivation. Interacts with ARG80 and ARG82. Ref.7 Ref.8 Ref.9 Ref.10
Subcellular location	Nucleus.
Miscellaneous	Present with 8970 molecules/cell in log phase SD medium.
Sequence similarities	Contains 1 MADS-box domain.

Ontologies

Keywords
Biological process	Arginine metabolism Cell cycle Transcription Transcription regulation
Cellular component	Nucleus
Ligand	DNA-binding
Molecular function	Activator
PTM	Phosphoprotein
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	DNA replication initiation Inferred from mutant phenotype PubMed 12473677. Source: SGD arginine metabolic process Inferred from electronic annotation. Source: UniProtKB-KW negative regulation of arginine catabolic process by negative regulation of transcription from RNA polymerase II promoter Inferred from mutant phenotype PubMed 8455631. Source: SGD negative regulation of mating-type specific transcription from RNA polymerase II promoter Inferred from mutant phenotype PubMed 1961765. Source: SGD positive regulation of arginine biosynthetic process by positive regulation of transcription from RNA polymerase II promoter Inferred from mutant phenotype PubMed 19233144PubMed 8455631. Source: SGD positive regulation of mating-type specific transcription from RNA polymerase II promoter Inferred from direct assay PubMed 11060038. Source: SGD positive regulation of transcription involved in G2/M-phase of mitotic cell cycle Inferred from mutant phenotype PubMed 7565744PubMed 9171372. Source: SGD regulation of mating type switching Inferred from mutant phenotype PubMed 9620858. Source: SGD
Cellular_component	nuclear chromatin Inferred from direct assay PubMed 12473677. Source: SGD
Molecular_function	DNA replication origin binding Inferred from direct assay PubMed 12473677. Source: SGD RNA polymerase II activating transcription factor binding Inferred from mutant phenotype PubMed 12052870PubMed 12711672. Source: SGD RNA polymerase II core promoter proximal region sequence-specific DNA binding transcription factor activity involved in negative regulation of transcription Inferred from direct assay PubMed 9121436. Source: SGD RNA polymerase II core promoter proximal region sequence-specific DNA binding transcription factor activity involved in positive regulation of transcription Inferred from direct assay PubMed 12052870PubMed 9121436. Source: SGD RNA polymerase II core promoter proximal region sequence-specific DNA binding, bending Inferred from direct assay PubMed 7739902PubMed 9121436Ref.13. Source: SGD sequence-specific transcription regulatory region DNA binding RNA polymerase II transcription factor recruiting transcription factor activity Inferred from direct assay PubMed 11562353. Source: SGD
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 286

286

Pheromone receptor transcription factor

PRO_0000199439

Regions

Domain

18 – 72

55

MADS-box

Compositional bias

98 – 120

23

Asp/Glu-rich (acidic)

Amino acid modifications

Modified residue

2

1

Phosphoserine Ref.12

Modified residue

8

1

Phosphothreonine Ref.12

Modified residue

144

1

Phosphoserine Ref.12

Experimental info

Sequence conflict

9

1

P → S in AAA34609. Ref.3

Sequence conflict

37

1

S → F in AAA34609. Ref.3

Sequence conflict

156 – 157

2

GA → AR in AAA34609. Ref.3

Sequence conflict

158 – 286

129

Missing in AAA34609. Ref.3

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

286

Helix Strand Turn

Details...

Helix

29 – 54

26

Beta strand

57 – 63

7

Beta strand

69 – 73

5

Turn

75 – 78

4

Helix

79 – 82

4

Helix

84 – 94

11

Sequences

	Sequence		Length	Mass (Da)
	P11746 [UniParc]. Last modified February 1, 1991. Version 2. Checksum: FD75B4BF549E9E3B	FASTA	286	32,802
	10 20 30 40 50 60 MSDIEEGTPT NNGQQKERRK IEIKFIENKT RRHVTFSKRK HGIMKKAFEL SVLTGTQVLL 70 80 90 100 110 120 LVVSETGLVY TFSTPKFEPI VTQQEGRNLI QACLNAPDDE EEDEEEDGDD DDDDDDDGND 130 140 150 160 170 180 MQRQQPQQQQ PQQQQQVLNA HANSLGHLNQ DQVPAGALKQ EVKSQLLGGA NPNQNSMIQQ 190 200 210 220 230 240 QQHHTQNSQP QQQQQQQPQQ QMSQQQMSQH PRPQQGIPHP QQSQPQQQQQ QQQQLQQQQQ 250 260 270 280 QQQQQPLTGI HQPHQQAFAN AASPYLNAEQ NAAYQQYFQE PQQGQY

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Identification, purification, and cloning of a polypeptide (PRTF/GRM) that binds to mating-specific promoter elements in yeast." Ammerer G. Genes Dev. 4:299-312(1990) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]	"Saccharomyces cerevisiae protein involved in plasmid maintenance is necessary for mating of MAT alpha cells." Passmore S., Maine G.T., Elble R., Christ C., Tye B.K. J. Mol. Biol. 204:593-606(1988) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[3]	"Characterization of two new genes essential for vegetative growth in Saccharomyces cerevisiae: nucleotide sequence determination and chromosome mapping." Dubois E., Bercy J., Descamps F., Messenguy F. Gene 55:265-275(1987) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[4]	"The nucleotide sequence of Saccharomyces cerevisiae chromosome XIII." Bowman S., Churcher C.M., Badcock K., Brown D., Chillingworth T., Connor R., Dedman K., Devlin K., Gentles S., Hamlin N., Hunt S., Jagels K., Lye G., Moule S., Odell C., Pearson D., Rajandream M.A., Rice P. , Skelton J., Walsh S.V., Whitehead S., Barrell B.G. Nature 387:90-93(1997) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 204511 / S288c / AB972.
[5]	Saccharomyces Genome Database Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases Cited for: GENOME REANNOTATION. Strain: ATCC 204508 / S288c.
[6]	"Approaching a complete repository of sequence-verified protein-encoding clones for Saccharomyces cerevisiae." Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F., Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J., Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J. , Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D., LaBaer J. Genome Res. 17:536-543(2007) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: ATCC 204508 / S288c.
[7]	"The DNA binding and oligomerization domain of MCM1 is sufficient for its interaction with other regulatory proteins." Primig M., Winkler H., Ammerer G. EMBO J. 10:4209-4218(1991) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH ALPHA1 AND ALPHA2.
[8]	"The yeast alpha2 and Mcm1 proteins interact through a region similar to a motif found in homeodomain proteins of higher eukaryotes." Mead J., Zhong H., Acton T.B., Vershon A.K. Mol. Cell. Biol. 16:2135-2143(1996) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH ALPHA2.
[9]	"Recruitment of the yeast MADS-box proteins, ArgRI and Mcm1 by the pleiotropic factor ArgRIII is required for their stability." El Bakkoury M., Dubois E., Messenguy F. Mol. Microbiol. 35:15-31(2000) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH ARG81 AND ARG82.
[10]	"Conserved homeodomain proteins interact with MADS box protein Mcm1 to restrict ECB-dependent transcription to the M/G1 phase of the cell cycle." Pramila T., Miles S., GuhaThakurta D., Jemiolo D., Breeden L.L. Genes Dev. 16:3034-3045(2002) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH YHP1 AND YOX1.
[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]	"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-2; THR-8 AND SER-144, MASS SPECTROMETRY.
[13]	"Crystal structure of the yeast MATalpha2/MCM1/DNA ternary complex." Tan S., Richmond T.J. Nature 391:660-666(1998) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.25 ANGSTROMS) OF 1-100 IN COMPLEX WITH ALPHA2.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

X52453 Genomic DNA. Translation: CAA36691.1.
X14187 Genomic DNA. Translation: CAA32389.1.
M17511 Genomic DNA. Translation: AAA34609.1.
Z48502 Genomic DNA. Translation: CAA88409.1.
AY557985 Genomic DNA. Translation: AAS56311.1.
BK006946 Genomic DNA. Translation: DAA09942.1.

PIR

A34599.

RefSeq

NP_013757.1. NM_001182540.1.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1MNM	X-ray	2.25	A/B	1-100	[»]

ProteinModelPortal

P11746.

SMR

P11746. Positions 18-98.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-72N.

IntAct

P11746. 51 interactions.

MINT

MINT-478633.

STRING

4932.YMR043W.

Proteomic databases

PaxDb

P11746.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblFungi

YMR043W; YMR043W; YMR043W.

GeneID

855060.

KEGG

sce:YMR043W.

Organism-specific databases

CYGD

YMR043w.

SGD

S000004646. MCM1.

Phylogenomic databases

eggNOG

COG5068.

GeneTree

ENSGT00400000022158.

KO

K12412.

OMA

CLNAPDD.

OrthoDB

EOG4P2TC4.

Gene expression databases

Genevestigator

P11746.

GermOnline

YMR043W. Saccharomyces cerevisiae.

Family and domain databases

InterPro

IPR002100. TF_MADSbox.
[Graphical view]

Pfam

PF00319. SRF-TF. 1 hit.
[Graphical view]

PRINTS

PR00404. MADSDOMAIN.

SMART

SM00432. MADS. 1 hit.
[Graphical view]

SUPFAM

SSF55455. TF_MADSbox. 1 hit.

PROSITE

PS00350. MADS_BOX_1. 1 hit.
PS50066. MADS_BOX_2. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

EvolutionaryTrace

P11746.

NextBio

978315.

Entry information

Entry name

MCM1_YEAST

Accession

Primary (citable) accession number: P11746
Secondary accession number(s): D6VZL8

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1989
Last sequence update:	February 1, 1991
Last modified:	April 3, 2013
This is version 134 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program