MCH1_YEAST
ID MCH1_YEAST Reviewed; 486 AA.
AC Q07376; D6VRU2;
DT 25-OCT-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 137.
DE RecName: Full=Probable transporter MCH1;
DE AltName: Full=Monocarboxylate transporter homolog 1;
GN Name=MCH1; OrderedLocusNames=YDL054C;
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=9169867;
RA Jacq C., Alt-Moerbe J., Andre B., Arnold W., Bahr A., Ballesta J.P.G.,
RA Bargues M., Baron L., Becker A., Biteau N., Bloecker H., Blugeon C.,
RA Boskovic J., Brandt P., Brueckner M., Buitrago M.J., Coster F.,
RA Delaveau T., del Rey F., Dujon B., Eide L.G., Garcia-Cantalejo J.M.,
RA Goffeau A., Gomez-Peris A., Granotier C., Hanemann V., Hankeln T.,
RA Hoheisel J.D., Jaeger W., Jimenez A., Jonniaux J.-L., Kraemer C.,
RA Kuester H., Laamanen P., Legros Y., Louis E.J., Moeller-Rieker S.,
RA Monnet A., Moro M., Mueller-Auer S., Nussbaumer B., Paricio N., Paulin L.,
RA Perea J., Perez-Alonso M., Perez-Ortin J.E., Pohl T.M., Prydz H.,
RA Purnelle B., Rasmussen S.W., Remacha M.A., Revuelta J.L., Rieger M.,
RA Salom D., Saluz H.P., Saiz J.E., Saren A.-M., Schaefer M., Scharfe M.,
RA Schmidt E.R., Schneider C., Scholler P., Schwarz S., Soler-Mira A.,
RA Urrestarazu L.A., Verhasselt P., Vissers S., Voet M., Volckaert G.,
RA Wagner G., Wambutt R., Wedler E., Wedler H., Woelfl S., Harris D.E.,
RA Bowman S., Brown D., Churcher C.M., Connor R., Dedman K., Gentles S.,
RA Hamlin N., Hunt S., Jones L., McDonald S., Murphy L.D., Niblett D.,
RA Odell C., Oliver K., Rajandream M.A., Richards C., Shore L., Walsh S.V.,
RA Barrell B.G., Dietrich F.S., Mulligan J.T., Allen E., Araujo R., Aviles E.,
RA Berno A., Carpenter J., Chen E., Cherry J.M., Chung E., Duncan M.,
RA Hunicke-Smith S., Hyman R.W., Komp C., Lashkari D., Lew H., Lin D.,
RA Mosedale D., Nakahara K., Namath A., Oefner P., Oh C., Petel F.X.,
RA Roberts D., Schramm S., Schroeder M., Shogren T., Shroff N., Winant A.,
RA Yelton M.A., Botstein D., Davis R.W., Johnston M., Andrews S., Brinkman R.,
RA Cooper J., Ding H., Du Z., Favello A., Fulton L., Gattung S., Greco T.,
RA Hallsworth K., Hawkins J., Hillier L.W., Jier M., Johnson D., Johnston L.,
RA Kirsten J., Kucaba T., Langston Y., Latreille P., Le T., Mardis E.,
RA Menezes S., Miller N., Nhan M., Pauley A., Peluso D., Rifkin L., Riles L.,
RA Taich A., Trevaskis E., Vignati D., Wilcox L., Wohldman P., Vaudin M.,
RA Wilson R., Waterston R., Albermann K., Hani J., Heumann K., Kleine K.,
RA Mewes H.-W., Zollner A., Zaccaria P.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome IV.";
RL Nature 387:75-78(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 SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=14562095; DOI=10.1038/nature02026;
RA Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W.,
RA Weissman J.S., O'Shea E.K.;
RT "Global analysis of protein localization in budding yeast.";
RL Nature 425:686-691(2003).
RN [4]
RP LACK OF FUNCTION AS A MONOCARBOXYLATE TRANSPORTER.
RX PubMed=11536335; DOI=10.1002/yea.763;
RA Makuc J., Paiva S., Schauen M., Kramer R., Andre B., Casal M., Leao C.,
RA Boles E.;
RT "The putative monocarboxylate permeases of the yeast Saccharomyces
RT cerevisiae do not transport monocarboxylic acids across the plasma
RT membrane.";
RL Yeast 18:1131-1143(2001).
RN [5]
RP TOPOLOGY [LARGE SCALE ANALYSIS].
RC STRAIN=ATCC 208353 / W303-1A;
RX PubMed=16847258; DOI=10.1073/pnas.0604075103;
RA Kim H., Melen K., Oesterberg M., von Heijne G.;
RT "A global topology map of the Saccharomyces cerevisiae membrane proteome.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:11142-11147(2006).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-255, AND IDENTIFICATION BY
RP 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).
CC -!- FUNCTION: Probable transporter. Does not act in the transport of
CC monocarboxylic acids across the plasma membrane.
CC -!- SUBCELLULAR LOCATION: Vacuole membrane {ECO:0000269|PubMed:14562095};
CC Multi-pass membrane protein {ECO:0000269|PubMed:14562095}.
CC -!- SIMILARITY: Belongs to the major facilitator superfamily.
CC {ECO:0000305}.
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DR EMBL; Z74102; CAA98616.1; -; Genomic_DNA.
DR EMBL; BK006938; DAA11802.1; -; Genomic_DNA.
DR PIR; S67589; S67589.
DR RefSeq; NP_010229.1; NM_001180113.1.
DR AlphaFoldDB; Q07376; -.
DR SMR; Q07376; -.
DR BioGRID; 32005; 86.
DR DIP; DIP-5410N; -.
DR MINT; Q07376; -.
DR STRING; 4932.YDL054C; -.
DR TCDB; 2.A.1.75.1; the major facilitator superfamily (mfs).
DR iPTMnet; Q07376; -.
DR MaxQB; Q07376; -.
DR PaxDb; Q07376; -.
DR PRIDE; Q07376; -.
DR EnsemblFungi; YDL054C_mRNA; YDL054C; YDL054C.
DR GeneID; 851506; -.
DR KEGG; sce:YDL054C; -.
DR SGD; S000002212; MCH1.
DR VEuPathDB; FungiDB:YDL054C; -.
DR eggNOG; ENOG502QTNE; Eukaryota.
DR HOGENOM; CLU_012596_3_0_1; -.
DR InParanoid; Q07376; -.
DR OMA; WRGPGGW; -.
DR BioCyc; YEAST:G3O-29471-MON; -.
DR PRO; PR:Q07376; -.
DR Proteomes; UP000002311; Chromosome IV.
DR RNAct; Q07376; protein.
DR GO; GO:0000329; C:fungal-type vacuole membrane; IDA:SGD.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0016020; C:membrane; IBA:GO_Central.
DR GO; GO:0022857; F:transmembrane transporter activity; IEA:InterPro.
DR Gene3D; 1.20.1250.20; -; 1.
DR InterPro; IPR011701; MFS.
DR InterPro; IPR036259; MFS_trans_sf.
DR Pfam; PF07690; MFS_1; 1.
DR SUPFAM; SSF103473; SSF103473; 1.
PE 1: Evidence at protein level;
KW Glycoprotein; Membrane; Phosphoprotein; Reference proteome; Transmembrane;
KW Transmembrane helix; Transport; Vacuole.
FT CHAIN 1..486
FT /note="Probable transporter MCH1"
FT /id="PRO_0000084877"
FT TOPO_DOM 1..29
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 30..50
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 51..67
FT /note="Vacuolar"
FT /evidence="ECO:0000255"
FT TRANSMEM 68..88
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 89..93
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 94..114
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 115..133
FT /note="Vacuolar"
FT /evidence="ECO:0000255"
FT TRANSMEM 134..154
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 155..163
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 164..184
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 185..212
FT /note="Vacuolar"
FT /evidence="ECO:0000255"
FT TRANSMEM 213..233
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 234..279
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 280..300
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 301..320
FT /note="Vacuolar"
FT /evidence="ECO:0000255"
FT TRANSMEM 321..343
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 344..347
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 348..368
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 369..385
FT /note="Vacuolar"
FT /evidence="ECO:0000255"
FT TRANSMEM 386..406
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 407..413
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 414..434
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 435..456
FT /note="Vacuolar"
FT /evidence="ECO:0000255"
FT TRANSMEM 457..477
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 478..486
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT MOD_RES 255
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956"
FT CARBOHYD 60
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 131
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 194
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 486 AA; 53566 MW; F233A3FE854C53DB CRC64;
MPLSKVEHYL SYHTRLLLPH VLSLQSSHRV AYIFSLLSAV STGFITLISL YSQPWQKHLN
YSSWQINTIA SMTNLGMYLT PPILGMIADS HGPITLSLLA IIGFIPSYSY LAYVFNHPEL
SLGGNGDSSF NLSIICFVFI GISTSALYFS ALLTCTKLYP HTKLLSISLP TTCYGISSVV
GSQLLRIKWF WSSNASSSSS NSDLNLGRVF QTFALVYVVI GLLAWIATSV VSLLHFNEEQ
DNQKRLDDQT DVEQSPLLER SNHVQEKFTQ TMLRIFSDPV TYILAVSILL SLGPLEMFIA
NMGSLTNLLV QLDAPTLSTK LLSTYALSST FTRLLTGIVA DFFAKKKISI KWILLTFLSL
GVCAQLFLLK MTSSASPWGL VPTGSLVGIV YGGLFTVYPT LVLLVWGERS FGTVYGSLLI
APAIGSMIFC MLYAKFYDSR CMSGGGDLRN PSCISAVYKY SSIAFVVSAV LSAVVFWKLK
SRKLRI
