MCH4_YEAST
ID MCH4_YEAST Reviewed; 501 AA.
AC Q08268; D6W1U9;
DT 03-JUL-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 157.
DE RecName: Full=Probable transporter MCH4;
GN Name=MCH4; OrderedLocusNames=YOL119C;
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 96604 / S288c / FY1679;
RX PubMed=8896268;
RX DOI=10.1002/(sici)1097-0061(199609)12:10b<1041::aid-yea989>3.0.co;2-i;
RA Lafuente M.J., Gamo F.-J., Gancedo C.;
RT "DNA sequence analysis of a 10 624 bp fragment of the left arm of
RT chromosome XV from Saccharomyces cerevisiae reveals a RNA binding protein,
RT a mitochondrial protein, two ribosomal proteins and two new open reading
RT frames.";
RL Yeast 12:1041-1045(1996).
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.
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).
RN [6]
RP UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-54, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22106047; DOI=10.1002/pmic.201100166;
RA Starita L.M., Lo R.S., Eng J.K., von Haller P.D., Fields S.;
RT "Sites of ubiquitin attachment in Saccharomyces cerevisiae.";
RL Proteomics 12:236-240(2012).
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; X95258; CAA64551.1; -; Genomic_DNA.
DR EMBL; Z74861; CAA99138.1; -; Genomic_DNA.
DR EMBL; BK006948; DAA10665.1; -; Genomic_DNA.
DR PIR; S66816; S66816.
DR RefSeq; NP_014522.1; NM_001183373.1.
DR AlphaFoldDB; Q08268; -.
DR SMR; Q08268; -.
DR BioGRID; 34282; 138.
DR STRING; 4932.YOL119C; -.
DR TCDB; 2.A.1.13.19; the major facilitator superfamily (mfs).
DR iPTMnet; Q08268; -.
DR MaxQB; Q08268; -.
DR PaxDb; Q08268; -.
DR PRIDE; Q08268; -.
DR EnsemblFungi; YOL119C_mRNA; YOL119C; YOL119C.
DR GeneID; 854030; -.
DR KEGG; sce:YOL119C; -.
DR SGD; S000005479; MCH4.
DR VEuPathDB; FungiDB:YOL119C; -.
DR eggNOG; KOG2504; Eukaryota.
DR GeneTree; ENSGT00940000176470; -.
DR HOGENOM; CLU_001265_1_0_1; -.
DR InParanoid; Q08268; -.
DR OMA; ALNWPVR; -.
DR BioCyc; YEAST:G3O-33515-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:Q08268; -.
DR Proteomes; UP000002311; Chromosome XV.
DR RNAct; Q08268; protein.
DR GO; GO:0071944; C:cell periphery; HDA:SGD.
DR GO; GO:0000329; C:fungal-type vacuole membrane; IDA:SGD.
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:0015293; F:symporter activity; IEA:UniProtKB-KW.
DR Gene3D; 1.20.1250.20; -; 2.
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 Glycoprotein; Isopeptide bond; Membrane; Reference proteome; Symport;
KW Transmembrane; Transmembrane helix; Transport; Ubl conjugation.
FT CHAIN 1..501
FT /note="Probable transporter MCH4"
FT /id="PRO_0000211404"
FT TOPO_DOM 1..97
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 98..120
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 121..134
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 135..157
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 158..163
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 164..183
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 184..187
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 188..210
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 211..222
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 223..245
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 246..254
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 255..274
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 275..310
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 311..333
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 334..342
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 343..365
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 366..371
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 372..394
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 395..403
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 404..426
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 427..438
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 439..461
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 462..470
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 471..493
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 494..501
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT CARBOHYD 131
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CROSSLNK 54
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0007744|PubMed:22106047"
SQ SEQUENCE 501 AA; 54707 MW; 45149348C4724275 CRC64;
MLNIPIIANS KRFLFSKDHE AQSTRDHDVE LETREGPSSG YNPNFNAADA ILKKNSDQVD
LDVNKLTNVT SRVLNTPEAS LIYDDDREFP DGGLKAWLVV FGAFMGLVPV FGLINSLGAI
ESYISKHQLA NISSSTISWI FSLYLAISFL SCILSGGYFD RNGSIGLMCT GTVIYAGGLF
ALANCKSVWQ FILAFSVCSG LGTGILMTPL IGTVATWFLK RRGIATSIST MGGSIGGIVF
PIMLRKLYKE VGFQWAIRIL SFICLTCLIC ASVLARERTK PVVQPFKSKA EVAKWYISSV
FNWRYFLEGK FLFVAIGASF AESSLTSCAT YLASYSMTRG NTENVAYTMI TASNAVGILG
RYIPGYFADK FIGRFNVEII TISMAALFNF VMWLPFGGNT KVLWAYVCLW GFSTGSILSL
TPVCIGQISK TTDFGKRYAT VYLLQALVTI PVLPIGGTLI GKGTVANYNH FIIFNSALMA
AGAACYIISR HICVGAKLCK F
