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MCH2_YEAST
ID   MCH2_YEAST              Reviewed;         473 AA.
AC   P36032; D6VWY2;
DT   01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT   21-SEP-2011, sequence version 2.
DT   03-AUG-2022, entry version 152.
DE   RecName: Full=Probable transporter MCH2;
GN   Name=MCH2; OrderedLocusNames=YKL221W;
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].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=8091865; DOI=10.1002/yea.320100011;
RA   Alexandraki D., Tzermia M.;
RT   "Sequencing of a 13.2 kb segment next to the left telomere of yeast
RT   chromosome XI revealed five open reading frames and recent recombination
RT   events with the right arms of chromosomes III and V.";
RL   Yeast 10:S81-S91(1994).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=8196765; DOI=10.1038/369371a0;
RA   Dujon B., Alexandraki D., Andre B., Ansorge W., Baladron V.,
RA   Ballesta J.P.G., Banrevi A., Bolle P.-A., Bolotin-Fukuhara M., Bossier P.,
RA   Bou G., Boyer J., Buitrago M.J., Cheret G., Colleaux L.,
RA   Daignan-Fornier B., del Rey F., Dion C., Domdey H., Duesterhoeft A.,
RA   Duesterhus S., Entian K.-D., Erfle H., Esteban P.F., Feldmann H.,
RA   Fernandes L., Fobo G.M., Fritz C., Fukuhara H., Gabel C., Gaillon L.,
RA   Garcia-Cantalejo J.M., Garcia-Ramirez J.J., Gent M.E., Ghazvini M.,
RA   Goffeau A., Gonzalez A., Grothues D., Guerreiro P., Hegemann J.H.,
RA   Hewitt N., Hilger F., Hollenberg C.P., Horaitis O., Indge K.J.,
RA   Jacquier A., James C.M., Jauniaux J.-C., Jimenez A., Keuchel H.,
RA   Kirchrath L., Kleine K., Koetter P., Legrain P., Liebl S., Louis E.J.,
RA   Maia e Silva A., Marck C., Monnier A.-L., Moestl D., Mueller S.,
RA   Obermaier B., Oliver S.G., Pallier C., Pascolo S., Pfeiffer F.,
RA   Philippsen P., Planta R.J., Pohl F.M., Pohl T.M., Poehlmann R.,
RA   Portetelle D., Purnelle B., Puzos V., Ramezani Rad M., Rasmussen S.W.,
RA   Remacha M.A., Revuelta J.L., Richard G.-F., Rieger M.,
RA   Rodrigues-Pousada C., Rose M., Rupp T., Santos M.A., Schwager C.,
RA   Sensen C., Skala J., Soares H., Sor F., Stegemann J., Tettelin H.,
RA   Thierry A., Tzermia M., Urrestarazu L.A., van Dyck L.,
RA   van Vliet-Reedijk J.C., Valens M., Vandenbol M., Vilela C., Vissers S.,
RA   von Wettstein D., Voss H., Wiemann S., Xu G., Zimmermann J., Haasemann M.,
RA   Becker I., Mewes H.-W.;
RT   "Complete DNA sequence of yeast chromosome XI.";
RL   Nature 369:371-378(1994).
RN   [3]
RP   GENOME REANNOTATION, AND SEQUENCE REVISION TO 342.
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   [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).
CC   -!- FUNCTION: Probable transporter. Does not act in the transport of
CC       monocarboxylic acids across the plasma membrane.
CC   -!- SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein.
CC   -!- SIMILARITY: Belongs to the major facilitator superfamily.
CC       Monocarboxylate porter (TC 2.A.1.13) family. {ECO:0000305}.
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DR   EMBL; X75950; CAA53552.1; -; Genomic_DNA.
DR   EMBL; Z28221; CAA82066.1; -; Genomic_DNA.
DR   EMBL; BK006944; DAA08948.2; -; Genomic_DNA.
DR   PIR; S38065; S38065.
DR   RefSeq; NP_012701.2; NM_001179786.2.
DR   AlphaFoldDB; P36032; -.
DR   SMR; P36032; -.
DR   BioGRID; 33944; 42.
DR   DIP; DIP-4126N; -.
DR   IntAct; P36032; 1.
DR   MINT; P36032; -.
DR   STRING; 4932.YKL221W; -.
DR   TCDB; 2.A.1.13.18; the major facilitator superfamily (mfs).
DR   PaxDb; P36032; -.
DR   PRIDE; P36032; -.
DR   EnsemblFungi; YKL221W_mRNA; YKL221W; YKL221W.
DR   GeneID; 853659; -.
DR   KEGG; sce:YKL221W; -.
DR   SGD; S000001704; MCH2.
DR   VEuPathDB; FungiDB:YKL221W; -.
DR   eggNOG; KOG2504; Eukaryota.
DR   HOGENOM; CLU_001265_1_2_1; -.
DR   InParanoid; P36032; -.
DR   OMA; LSYRIWA; -.
DR   BioCyc; YEAST:G3O-31976-MON; -.
DR   Reactome; R-SCE-352230; Amino acid transport across the plasma membrane.
DR   Reactome; R-SCE-879518; Transport of organic anions.
DR   PRO; PR:P36032; -.
DR   Proteomes; UP000002311; Chromosome XI.
DR   RNAct; P36032; protein.
DR   GO; GO:0071627; C:integral component of fungal-type vacuolar membrane; IBA:GO_Central.
DR   GO; GO:0016021; C:integral component of membrane; IBA:GO_Central.
DR   GO; GO:0016020; C:membrane; ISM:SGD.
DR   GO; GO:0015293; F:symporter activity; IEA:UniProtKB-KW.
DR   Gene3D; 1.20.1250.20; -; 2.
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; Reference proteome; Symport; Transmembrane;
KW   Transmembrane helix; Transport.
FT   CHAIN           1..473
FT                   /note="Probable transporter MCH2"
FT                   /id="PRO_0000211403"
FT   TOPO_DOM        1..37
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        38..58
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        59..83
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        84..105
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        106..111
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        112..135
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        136..141
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        142..163
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        164..169
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        170..186
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        187..200
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        201..220
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        221..243
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        244..268
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        269..286
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        287..304
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        305..312
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        313..332
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        333..342
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        343..362
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        363..370
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        371..394
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        395..408
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        409..433
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        434..473
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        72
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CONFLICT        342
FT                   /note="A -> R (in Ref. 1; CAA53552 and 2; CAA82066)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   473 AA;  52257 MW;  6C58D5DB3BAB5510 CRC64;
     MSEERHEDHH RDVENKLNLN GKDDINGNTS ISIEVPDGGY GWFILLAFIL YNFSTWGANS
     GYAIYLAHYL ENNTFAGGSK LDYASIGGLA FSCGLFFAPV ITWLYHIFSI QFIIGLGILF
     QGAALLLAAF SVTLWEIYLT QGVLIGFGLA FIFIPSVTLI PLWFRNKRSL ASGIGTAGSG
     LGGIVFNLGM QSILQKRGVK WALIAQCIIC TSLSTIALML TRTTHQGLRQ HKRSYKFELL
     DYDVLSNFAV WLLFGFVSFA MLGYVVLLYS LSDFTVSLGY TSKQGSYVSC MVSVGSLLGR
     PIVGHIADKY GSLTVGMILH LVMAILCWAM WIPCKNLATA IAFGLLVGSI MGTIWPTIAS
     IVTRIVGLQK LPGTFGSTWI FMAAFALVAP IIGLELRSTD TNGNDYYRTA IFVGFAYFGV
     SLCQWLLRGF IIARDEIAVR EAYSADQNEL HLNVKLSHMS KCLFRYKQLP RRV
 
 
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