ITR1_YEAST
ID ITR1_YEAST Reviewed; 584 AA.
AC P30605; D6VTB9;
DT 01-APR-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 2.
DT 03-AUG-2022, entry version 193.
DE RecName: Full=Myo-inositol transporter 1;
GN Name=ITR1; OrderedLocusNames=YDR497C; ORFNames=D9719.3;
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], AND FUNCTION.
RX PubMed=2040626; DOI=10.1016/s0021-9258(18)99146-5;
RA Nikawa J., Tsukagoshi Y., Yamashita S.;
RT "Isolation and characterization of two distinct myo-inositol transporter
RT genes of Saccharomyces cerevisiae.";
RL J. Biol. Chem. 266:11184-11191(1991).
RN [2]
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 [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 UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-573, AND IDENTIFICATION BY
RP MASS SPECTROMETRY.
RC STRAIN=SUB592;
RX PubMed=12872131; DOI=10.1038/nbt849;
RA Peng J., Schwartz D., Elias J.E., Thoreen C.C., Cheng D., Marsischky G.,
RA Roelofs J., Finley D., Gygi S.P.;
RT "A proteomics approach to understanding protein ubiquitination.";
RL Nat. Biotechnol. 21:921-926(2003).
RN [5]
RP UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-573, AND IDENTIFICATION BY
RP MASS SPECTROMETRY.
RX PubMed=14557538; DOI=10.1073/pnas.2135500100;
RA Hitchcock A.L., Auld K., Gygi S.P., Silver P.A.;
RT "A subset of membrane-associated proteins is ubiquitinated in response to
RT mutations in the endoplasmic reticulum degradation machinery.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:12735-12740(2003).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-46, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=YAL6B;
RX PubMed=15665377; DOI=10.1074/mcp.m400219-mcp200;
RA Gruhler A., Olsen J.V., Mohammed S., Mortensen P., Faergeman N.J., Mann M.,
RA Jensen O.N.;
RT "Quantitative phosphoproteomics applied to the yeast pheromone signaling
RT pathway.";
RL Mol. Cell. Proteomics 4:310-327(2005).
RN [7]
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 [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=ADR376;
RX PubMed=17330950; DOI=10.1021/pr060559j;
RA Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J.,
RA Elias J.E., Gygi S.P.;
RT "Large-scale phosphorylation analysis of alpha-factor-arrested
RT Saccharomyces cerevisiae.";
RL J. Proteome Res. 6:1190-1197(2007).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-12; SER-26; SER-31; SER-35;
RP SER-37 AND SER-46, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP ANALYSIS].
RX PubMed=19779198; DOI=10.1126/science.1172867;
RA Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.;
RT "Global analysis of Cdk1 substrate phosphorylation sites provides insights
RT into evolution.";
RL Science 325:1682-1686(2009).
RN [10]
RP UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-573, AND IDENTIFICATION BY
RP MASS 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: Major transporter for myo-inositol.
CC {ECO:0000269|PubMed:2040626}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H(+)(out) + myo-inositol(out) = H(+)(in) + myo-inositol(in);
CC Xref=Rhea:RHEA:60364, ChEBI:CHEBI:15378, ChEBI:CHEBI:17268;
CC Evidence={ECO:0000305|PubMed:2040626};
CC -!- SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein.
CC -!- SIMILARITY: Belongs to the major facilitator superfamily. Sugar
CC transporter (TC 2.A.1.1) family. {ECO:0000305}.
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DR EMBL; D90352; BAA14366.1; -; Genomic_DNA.
DR EMBL; U33057; AAB64939.1; -; Genomic_DNA.
DR EMBL; BK006938; DAA12329.1; -; Genomic_DNA.
DR PIR; S69555; S69555.
DR RefSeq; NP_010785.1; NM_001180805.1.
DR AlphaFoldDB; P30605; -.
DR SMR; P30605; -.
DR BioGRID; 32548; 124.
DR DIP; DIP-7406N; -.
DR IntAct; P30605; 25.
DR MINT; P30605; -.
DR STRING; 4932.YDR497C; -.
DR TCDB; 2.A.1.1.8; the major facilitator superfamily (mfs).
DR iPTMnet; P30605; -.
DR MaxQB; P30605; -.
DR PaxDb; P30605; -.
DR PRIDE; P30605; -.
DR TopDownProteomics; P30605; -.
DR EnsemblFungi; YDR497C_mRNA; YDR497C; YDR497C.
DR GeneID; 852108; -.
DR KEGG; sce:YDR497C; -.
DR SGD; S000002905; ITR1.
DR VEuPathDB; FungiDB:YDR497C; -.
DR eggNOG; KOG0254; Eukaryota.
DR GeneTree; ENSGT00940000155870; -.
DR HOGENOM; CLU_001265_30_5_1; -.
DR InParanoid; P30605; -.
DR OMA; GRKMAIY; -.
DR BioCyc; YEAST:G3O-30020-MON; -.
DR Reactome; R-SCE-429593; Inositol transporters.
DR PRO; PR:P30605; -.
DR Proteomes; UP000002311; Chromosome IV.
DR RNAct; P30605; protein.
DR GO; GO:0071944; C:cell periphery; HDA:SGD.
DR GO; GO:0000324; C:fungal-type vacuole; HDA:SGD.
DR GO; GO:0000329; C:fungal-type vacuole membrane; HDA: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:0005886; C:plasma membrane; IDA:SGD.
DR GO; GO:0005365; F:myo-inositol transmembrane transporter activity; IMP:SGD.
DR GO; GO:0005366; F:myo-inositol:proton symporter activity; IBA:GO_Central.
DR GO; GO:0022857; F:transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:1904679; P:myo-inositol import across plasma membrane; IBA:GO_Central.
DR GO; GO:0015798; P:myo-inositol transport; IMP:SGD.
DR GO; GO:0007124; P:pseudohyphal growth; IMP:SGD.
DR GO; GO:0055085; P:transmembrane transport; IMP:SGD.
DR Gene3D; 1.20.1250.20; -; 1.
DR InterPro; IPR020846; MFS_dom.
DR InterPro; IPR005828; MFS_sugar_transport-like.
DR InterPro; IPR036259; MFS_trans_sf.
DR InterPro; IPR003663; Sugar/inositol_transpt.
DR InterPro; IPR005829; Sugar_transporter_CS.
DR Pfam; PF00083; Sugar_tr; 1.
DR PRINTS; PR00171; SUGRTRNSPORT.
DR SUPFAM; SSF103473; SSF103473; 1.
DR TIGRFAMs; TIGR00879; SP; 1.
DR PROSITE; PS50850; MFS; 1.
DR PROSITE; PS00216; SUGAR_TRANSPORT_1; 2.
DR PROSITE; PS00217; SUGAR_TRANSPORT_2; 1.
PE 1: Evidence at protein level;
KW Glycoprotein; Isopeptide bond; Membrane; Phosphoprotein;
KW Reference proteome; Transmembrane; Transmembrane helix; Transport;
KW Ubl conjugation.
FT CHAIN 1..584
FT /note="Myo-inositol transporter 1"
FT /id="PRO_0000050455"
FT TOPO_DOM 1..81
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 82..102
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 103..129
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 130..150
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 151..163
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 164..184
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 185..186
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 187..207
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 208..215
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 216..236
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 237..246
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 247..267
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 268..349
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 350..370
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 371..376
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 377..397
FT /note="Helical; Name=8"
FT /evidence="ECO:0000255"
FT TOPO_DOM 398..400
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 401..421
FT /note="Helical; Name=9"
FT /evidence="ECO:0000255"
FT TOPO_DOM 422..441
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 442..462
FT /note="Helical; Name=10"
FT /evidence="ECO:0000255"
FT TOPO_DOM 463..486
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 487..507
FT /note="Helical; Name=11"
FT /evidence="ECO:0000255"
FT TOPO_DOM 508..510
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 511..531
FT /note="Helical; Name=12"
FT /evidence="ECO:0000255"
FT TOPO_DOM 532..584
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 13..42
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 12
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 26
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 31
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 35
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 37
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 46
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:15665377,
FT ECO:0007744|PubMed:19779198"
FT CARBOHYD 371
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CROSSLNK 573
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0007744|PubMed:22106047"
FT CONFLICT 43..44
FT /note="TL -> HI (in Ref. 1; BAA14366)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 584 AA; 63570 MW; 42543E30A102DC65 CRC64;
MGIHIPYLTS KTSQSNVGDA VGNADSVEFN SEHDSPSKRG KITLESHEIQ RAPASDDEDR
IQIKPVNDED DTSVMITFNQ SLSPFIITLT FVASISGFMF GYDTGYISSA LISIGTDLDH
KVLTYGEKEI VTAATSLGAL ITSIFAGTAA DIFGRKRCLM GSNLMFVIGA ILQVSAHTFW
QMAVGRLIMG FGVGIGSLIA PLFISEIAPK MIRGRLTVIN SLWLTGGQLV AYGCGAGLNY
VNNGWRILVG LSLIPTAVQF TCLCFLPDTP RYYVMKGDLA RATEVLKRSY TDTSEEIIER
KVEELVTLNQ SIPGKNVPEK VWNTIKELHT VPSNLRALII GCGLQAIQQF TGWNSLMYFS
GTIFETVGFK NSSAVSIIVS GTNFIFTLVA FFSIDKIGRR TILLIGLPGM TMALVVCSIA
FHFLGIKFDG AVAVVVSSGF SSWGIVIIVF IIVFAAFYAL GIGTVPWQQS ELFPQNVRGI
GTSYATATNW AGSLVIASTF LTMLQNITPA GTFAFFAGLS CLSTIFCYFC YPELSGLELE
EVQTILKDGF NIKASKALAK KRKQQVARVH ELKYEPTQEI IEDI
