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MTAL1_YEAST
ID   MTAL1_YEAST             Reviewed;         175 AA.
AC   P0CY06; D6VQV3; P01365;
DT   28-JUN-2011, integrated into UniProtKB/Swiss-Prot.
DT   28-JUN-2011, sequence version 1.
DT   03-AUG-2022, entry version 61.
DE   RecName: Full=Mating-type protein ALPHA1;
DE            Short=MATalpha1 protein;
DE   AltName: Full=Alpha-1 activator;
GN   Name=MATALPHA1; Synonyms=ALPHA-1, MAT1A, MATAL1; OrderedLocusNames=YCR040W;
GN   ORFNames=YCR40W;
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=7021055; DOI=10.1101/sqb.1981.045.01.113;
RA   Nasmyth K.A., Tatchell K., Hall B.D., Astell C., Smith M.;
RT   "Physical analysis of mating-type loci in Saccharomyces cerevisiae.";
RL   Cold Spring Harb. Symp. Quant. Biol. 45:961-981(1981).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=1789011; DOI=10.1002/yea.320070815;
RA   Jacquet M., Buhler J.-M., Iborra F., Francingues-Gaillard M.-C.,
RA   Soustelle C.;
RT   "The MAT locus revisited within a 9.8 kb fragment of chromosome III
RT   containing BUD5 and two new open reading frames.";
RL   Yeast 7:881-888(1991).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=1574125; DOI=10.1038/357038a0;
RA   Oliver S.G., van der Aart Q.J.M., Agostoni-Carbone M.L., Aigle M.,
RA   Alberghina L., Alexandraki D., Antoine G., Anwar R., Ballesta J.P.G.,
RA   Benit P., Berben G., Bergantino E., Biteau N., Bolle P.-A.,
RA   Bolotin-Fukuhara M., Brown A., Brown A.J.P., Buhler J.-M., Carcano C.,
RA   Carignani G., Cederberg H., Chanet R., Contreras R., Crouzet M.,
RA   Daignan-Fornier B., Defoor E., Delgado M.D., Demolder J., Doira C.,
RA   Dubois E., Dujon B., Duesterhoeft A., Erdmann D., Esteban M., Fabre F.,
RA   Fairhead C., Faye G., Feldmann H., Fiers W., Francingues-Gaillard M.-C.,
RA   Franco L., Frontali L., Fukuhara H., Fuller L.J., Galland P., Gent M.E.,
RA   Gigot D., Gilliquet V., Glansdorff N., Goffeau A., Grenson M., Grisanti P.,
RA   Grivell L.A., de Haan M., Haasemann M., Hatat D., Hoenicka J.,
RA   Hegemann J.H., Herbert C.J., Hilger F., Hohmann S., Hollenberg C.P.,
RA   Huse K., Iborra F., Indge K.J., Isono K., Jacq C., Jacquet M., James C.M.,
RA   Jauniaux J.-C., Jia Y., Jimenez A., Kelly A., Kleinhans U., Kreisl P.,
RA   Lanfranchi G., Lewis C., van der Linden C.G., Lucchini G.,
RA   Lutzenkirchen K., Maat M.J., Mallet L., Mannhaupt G., Martegani E.,
RA   Mathieu A., Maurer C.T.C., McConnell D., McKee R.A., Messenguy F.,
RA   Mewes H.-W., Molemans F., Montague M.A., Muzi Falconi M., Navas L.,
RA   Newlon C.S., Noone D., Pallier C., Panzeri L., Pearson B.M., Perea J.,
RA   Philippsen P., Pierard A., Planta R.J., Plevani P., Poetsch B., Pohl F.M.,
RA   Purnelle B., Ramezani Rad M., Rasmussen S.W., Raynal A., Remacha M.A.,
RA   Richterich P., Roberts A.B., Rodriguez F., Sanz E.,
RA   Schaaff-Gerstenschlaeger I., Scherens B., Schweitzer B., Shu Y., Skala J.,
RA   Slonimski P.P., Sor F., Soustelle C., Spiegelberg R., Stateva L.I.,
RA   Steensma H.Y., Steiner S., Thierry A., Thireos G., Tzermia M.,
RA   Urrestarazu L.A., Valle G., Vetter I., van Vliet-Reedijk J.C., Voet M.,
RA   Volckaert G., Vreken P., Wang H., Warmington J.R., von Wettstein D.,
RA   Wicksteed B.L., Wilson C., Wurst H., Xu G., Yoshikawa A., Zimmermann F.K.,
RA   Sgouros J.G.;
RT   "The complete DNA sequence of yeast chromosome III.";
RL   Nature 357:38-46(1992).
RN   [4]
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   [5]
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   [6]
RP   DNA-BINDING SPECIFICITY.
RX   PubMed=8413280; DOI=10.1128/mcb.13.11.6866-6875.1993;
RA   Hagen D.C., Bruhn L., Westby C.A., Sprague G.F. Jr.;
RT   "Transcription of alpha-specific genes in Saccharomyces cerevisiae: DNA
RT   sequence requirements for activity of the coregulator alpha 1.";
RL   Mol. Cell. Biol. 13:6866-6875(1993).
RN   [7]
RP   INTERACTION WITH MCM1.
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 STE12.
RX   PubMed=8339934; DOI=10.1101/gad.7.8.1584;
RA   Yuan Y.-L.O., Stroke I., Fields S.;
RT   "Coupling of cell identity to signal response in yeast: interaction between
RT   the alpha-1 and STE12 proteins.";
RL   Genes Dev. 7:1584-1597(1993).
RN   [9]
RP   FUNCTION IN MATING-TYPE REGULATION.
RX   PubMed=8664541; DOI=10.1016/0959-437x(95)80022-0;
RA   Johnson A.D.;
RT   "Molecular mechanisms of cell-type determination in budding yeast.";
RL   Curr. Opin. Genet. Dev. 5:552-558(1995).
CC   -!- FUNCTION: Mating type proteins are sequence specific DNA-binding
CC       proteins that act as master switches in yeast differentiation by
CC       controlling gene expression in a cell type-specific fashion.
CC       Transcriptional coactivator that, in alpha-cells, binds cooperatively
CC       with MCM1 and STE12 to a DNA sequence termed the QP' element, to
CC       activate the transcription of alpha-specific genes.
CC       {ECO:0000269|PubMed:8664541}.
CC   -!- SUBUNIT: Binds DNA with a high specificity in complex with an MCM1
CC       dimer. Interacts with STE12. {ECO:0000269|PubMed:1756728,
CC       ECO:0000269|PubMed:8339934}.
CC   -!- INTERACTION:
CC       P0CY06; P13574: STE12; NbExp=2; IntAct=EBI-10438, EBI-18264;
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00655}.
CC   -!- DEVELOPMENTAL STAGE: Only present in alpha-cells.
CC   -!- INDUCTION: Repressed in a/alpha diploid cells by A1/ALPHA2.
CC   -!- MISCELLANEOUS: There are three genetic loci for mating type genes in
CC       S.cerevisiae. MAT is the expression locus that determines the mating
CC       type of the cell, whereas HML (containing HMLALPHA1 and HMLALPHA2) and
CC       HMR (containing HMRA1 and HMRA2) represent silenced repositories of
CC       mating type information. The mating type is determined by the MAT
CC       locus, which contains either a copy of HML or of HMR. Diploid cells are
CC       usually heterozygous for the MAT locus.
CC   -!- SIMILARITY: Belongs to the MATALPHA1 family. {ECO:0000255|PROSITE-
CC       ProRule:PRU00655}.
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DR   EMBL; L00060; AAA34763.1; -; Genomic_DNA.
DR   EMBL; X63853; CAA45336.1; -; Genomic_DNA.
DR   EMBL; X59720; CAA42401.1; -; Genomic_DNA.
DR   EMBL; AY692791; AAT92810.1; -; Genomic_DNA.
DR   EMBL; BK006937; DAA07422.1; -; Genomic_DNA.
DR   PIR; S19397; JFBYA1.
DR   RefSeq; NP_009867.1; NM_001178707.1.
DR   RefSeq; NP_009869.3; NM_001178754.1.
DR   AlphaFoldDB; P0CY06; -.
DR   BioGRID; 30923; 6.
DR   BioGRID; 31023; 4.
DR   ComplexPortal; CPX-693; Mating-type MATalpha1-MCM1 complex.
DR   IntAct; P0CY06; 5.
DR   MINT; P0CY06; -.
DR   EnsemblFungi; YCL066W_mRNA; YCL066W; YCL066W.
DR   EnsemblFungi; YCR040W_mRNA; YCR040W; YCR040W.
DR   GeneID; 850293; -.
DR   GeneID; 850407; -.
DR   KEGG; sce:YCL066W; -.
DR   KEGG; sce:YCR040W; -.
DR   SGD; S000000636; MATALPHA1.
DR   VEuPathDB; FungiDB:YCL066W; -.
DR   VEuPathDB; FungiDB:YCR040W; -.
DR   HOGENOM; CLU_118234_0_0_1; -.
DR   InParanoid; P0CY06; -.
DR   BioCyc; YEAST:G3O-29352-MON; -.
DR   PRO; PR:P0CY06; -.
DR   Proteomes; UP000002311; Chromosome III.
DR   RNAct; P0CY06; protein.
DR   GO; GO:0005634; C:nucleus; IC:SGD.
DR   GO; GO:0090575; C:RNA polymerase II transcription regulator complex; IPI:ComplexPortal.
DR   GO; GO:0008301; F:DNA binding, bending; IDA:SGD.
DR   GO; GO:0003713; F:transcription coactivator activity; IMP:SGD.
DR   GO; GO:0045895; P:positive regulation of mating-type specific transcription, DNA-templated; IEA:InterPro.
DR   GO; GO:0007532; P:regulation of mating-type specific transcription, DNA-templated; IMP:SGD.
DR   GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IMP:SGD.
DR   InterPro; IPR006856; MATalpha_HMGbox.
DR   Pfam; PF04769; MATalpha_HMGbox; 1.
DR   PROSITE; PS51325; ALPHA_BOX; 1.
PE   1: Evidence at protein level;
KW   Activator; DNA-binding; Nucleus; Reference proteome; Transcription;
KW   Transcription regulation.
FT   CHAIN           1..175
FT                   /note="Mating-type protein ALPHA1"
FT                   /id="PRO_0000096610"
FT   DNA_BIND        88..144
FT                   /note="Alpha box"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00655"
SQ   SEQUENCE   175 AA;  20413 MW;  697199A7686D19C0 CRC64;
     MFTSKPAFKI KNKASKSYRN TAVSKKLKEK RLAEHVRPSC FNIIRPLKKD IQIPVPSSRF
     LNKIQIHRIA SGSQNTQFRQ FNKTSIKSSK KYLNSFMAFR AYYSQFGSGV KQNVLSSLLA
     EEWHADKMQH GIWDYFAQQY NFINPGFGFV EWLTNNYAEV RGDGYWEDVF VHLAL
 
 
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