MCH5_YEAST
ID MCH5_YEAST Reviewed; 521 AA.
AC Q08777; D6W306;
DT 31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 21-SEP-2011, sequence version 2.
DT 03-AUG-2022, entry version 154.
DE RecName: Full=Riboflavin transporter MCH5;
GN Name=MCH5; OrderedLocusNames=YOR306C;
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=9153758;
RX DOI=10.1002/(sici)1097-0061(199704)13:5<479::aid-yea104>3.0.co;2-g;
RA Poirey R., Cziepluch C., Tobiasch E., Pujol A., Kordes E., Jauniaux J.-C.;
RT "Sequence and analysis of a 36.2 kb fragment from the right arm of yeast
RT chromosome XV reveals 19 open reading frames including SNF2 (5' end), CPA1,
RT SLY41, a putative transport ATPase, a putative ribosomal protein and an
RT SNF2 homologue.";
RL Yeast 13:479-482(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169874;
RA Dujon B., Albermann K., Aldea M., Alexandraki D., Ansorge W., Arino J.,
RA Benes V., Bohn C., Bolotin-Fukuhara M., Bordonne R., Boyer J., Camasses A.,
RA Casamayor A., Casas C., Cheret G., Cziepluch C., Daignan-Fornier B.,
RA Dang V.-D., de Haan M., Delius H., Durand P., Fairhead C., Feldmann H.,
RA Gaillon L., Galisson F., Gamo F.-J., Gancedo C., Goffeau A., Goulding S.E.,
RA Grivell L.A., Habbig B., Hand N.J., Hani J., Hattenhorst U., Hebling U.,
RA Hernando Y., Herrero E., Heumann K., Hiesel R., Hilger F., Hofmann B.,
RA Hollenberg C.P., Hughes B., Jauniaux J.-C., Kalogeropoulos A.,
RA Katsoulou C., Kordes E., Lafuente M.J., Landt O., Louis E.J., Maarse A.C.,
RA Madania A., Mannhaupt G., Marck C., Martin R.P., Mewes H.-W., Michaux G.,
RA Paces V., Parle-McDermott A.G., Pearson B.M., Perrin A., Pettersson B.,
RA Poch O., Pohl T.M., Poirey R., Portetelle D., Pujol A., Purnelle B.,
RA Ramezani Rad M., Rechmann S., Schwager C., Schweizer M., Sor F., Sterky F.,
RA Tarassov I.A., Teodoru C., Tettelin H., Thierry A., Tobiasch E.,
RA Tzermia M., Uhlen M., Unseld M., Valens M., Vandenbol M., Vetter I.,
RA Vlcek C., Voet M., Volckaert G., Voss H., Wambutt R., Wedler H.,
RA Wiemann S., Winsor B., Wolfe K.H., Zollner A., Zumstein E., Kleine K.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XV.";
RL Nature 387:98-102(1997).
RN [3]
RP GENOME REANNOTATION, AND SEQUENCE REVISION TO 495.
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 FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, AND INDUCTION.
RX PubMed=16204239; DOI=10.1074/jbc.m505002200;
RA Reihl P., Stolz J.;
RT "The monocarboxylate transporter homolog Mch5p catalyzes riboflavin
RT (vitamin B2) uptake in Saccharomyces cerevisiae.";
RL J. Biol. Chem. 280:39809-39817(2005).
RN [6]
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: Riboflavin transporter involved in riboflavin (vitamin B2)
CC uptake. Does not act in the transport of monocarboxylic acids across
CC the plasma membrane. {ECO:0000269|PubMed:16204239}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=17 uM for riboflavin {ECO:0000269|PubMed:16204239};
CC pH dependence:
CC Optimum pH is 7.5. {ECO:0000269|PubMed:16204239};
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass membrane
CC protein {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the major facilitator superfamily.
CC Monocarboxylate porter (TC 2.A.1.13) family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; Z75214; CAA99626.1; -; Genomic_DNA.
DR EMBL; BK006948; DAA11072.2; -; Genomic_DNA.
DR PIR; S67210; S67210.
DR RefSeq; NP_014951.4; NM_001183726.4.
DR AlphaFoldDB; Q08777; -.
DR SMR; Q08777; -.
DR BioGRID; 34695; 29.
DR IntAct; Q08777; 2.
DR MINT; Q08777; -.
DR STRING; 4932.YOR306C; -.
DR TCDB; 2.A.1.13.4; the major facilitator superfamily (mfs).
DR PaxDb; Q08777; -.
DR PRIDE; Q08777; -.
DR EnsemblFungi; YOR306C_mRNA; YOR306C; YOR306C.
DR GeneID; 854483; -.
DR KEGG; sce:YOR306C; -.
DR SGD; S000005833; MCH5.
DR VEuPathDB; FungiDB:YOR306C; -.
DR eggNOG; KOG2504; Eukaryota.
DR GeneTree; ENSGT00940000176470; -.
DR HOGENOM; CLU_001265_1_0_1; -.
DR InParanoid; Q08777; -.
DR OMA; IGIFFME; -.
DR BioCyc; YEAST:G3O-33790-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:Q08777; -.
DR Proteomes; UP000002311; Chromosome XV.
DR RNAct; Q08777; 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:0005886; C:plasma membrane; IDA:SGD.
DR GO; GO:0032217; F:riboflavin transmembrane transporter activity; IGI:SGD.
DR GO; GO:0032218; P:riboflavin transport; IGI:SGD.
DR Gene3D; 1.20.1250.20; -; 1.
DR InterPro; IPR011701; MFS.
DR InterPro; IPR020846; MFS_dom.
DR InterPro; IPR036259; MFS_trans_sf.
DR Pfam; PF07690; MFS_1; 1.
DR SUPFAM; SSF103473; SSF103473; 1.
DR PROSITE; PS50850; MFS; 1.
PE 1: Evidence at protein level;
KW Cell membrane; Glycoprotein; Membrane; Reference proteome; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..521
FT /note="Riboflavin transporter MCH5"
FT /id="PRO_0000257810"
FT TOPO_DOM 1..103
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 104..124
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 125..143
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 144..164
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 165..172
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 173..193
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 194..200
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 201..221
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 222..233
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 234..254
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 255..269
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 270..290
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 291..325
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 326..346
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 347..367
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 368..388
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 389..396
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 397..417
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 418..422
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 423..443
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 444..461
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 462..482
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 483..487
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 488..508
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 509..521
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 1..33
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 65..96
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..20
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 125
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 194
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 419
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CONFLICT 495
FT /note="C -> S (in Ref. 1 and 2; CAA99626)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 521 AA; 57582 MW; E80E29340A7D5B9C CRC64;
MSSDSLTPKD TIVPEEQTNQ LRQPDLDEDS IHYDPEADDL ESLETTASYA STSVSAKVYT
KKEVNKGTDI ESQPHWGENT SSTHDSDKEE DSNEEIESFP EGGFKAWVVT FGCFLGLIAC
FGLLNSTGVI ESHLQDNQLS SESVSTIGWL FSLFLFVCSA SCIISGTYFD RNGFRTIMIV
GTVFHVAGLF ATANSTKYWH FILSFAIVCG FGNGIVLSPL VSVPAHYFFK RRGTALAMAT
IGGSVGGVVF PIMLRSFFSM KSDTDPTYGF VWGIRTLGFL DLALLTLSII LVKERLPHVI
ENSKDGESRW RYILRVYILQ CFDAKAFLDM KYLFCVLGTV FSELSINSAL TYYGSYATSH
GISANDAYTL IMIINVCGIP GRWVPGYLSD KFGRFNVAIA TLLTLFIVMF VGWLPFGTNL
TNMYVISALY GFCSGSVFSL LPVCCGQISK TEEFGKRYST MYFVVGFGTL VGIPITGAII
SIKTTADYQH YIIFCGLATF VSAVCYIISR AYCVGFKWVR F
