ITR2_YEAST
ID ITR2_YEAST Reviewed; 609 AA.
AC P30606; D6W1W5;
DT 01-APR-1993, integrated into UniProtKB/Swiss-Prot.
DT 03-OCT-2006, sequence version 2.
DT 03-AUG-2022, entry version 190.
DE RecName: Full=Myo-inositol transporter 2;
GN Name=ITR2; OrderedLocusNames=YOL103W; ORFNames=HRB612;
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 [GENOMIC DNA].
RX PubMed=7502582; DOI=10.1002/yea.320111108;
RA Vandenbol M., Durand P., Portetelle D., Hilger F.;
RT "Sequence analysis of a 44 kb DNA fragment of yeast chromosome XV including
RT the Ty1-H3 retrotransposon, the suf1(+) frameshift suppressor gene for
RT tRNA-Gly, the yeast transfer RNA-Thr-1a and a delta element.";
RL Yeast 11:1069-1075(1995).
RN [3]
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 [4]
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 [5]
RP SUBCELLULAR LOCATION.
RX PubMed=16233524; DOI=10.1263/jbb.96.291;
RA Miyashita M., Shugyo M., Nikawa J.;
RT "Mutational analysis and localization of the inositol transporters of
RT Saccharomyces cerevisiae.";
RL J. Biosci. Bioeng. 96:291-297(2003).
RN [6]
RP IDENTIFICATION OF PROBABLE INITIATION SITE.
RX PubMed=12748633; DOI=10.1038/nature01644;
RA Kellis M., Patterson N., Endrizzi M., Birren B.W., Lander E.S.;
RT "Sequencing and comparison of yeast species to identify genes and
RT regulatory elements.";
RL Nature 423:241-254(2003).
RN [7]
RP LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX PubMed=14562106; DOI=10.1038/nature02046;
RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA O'Shea E.K., Weissman J.S.;
RT "Global analysis of protein expression in yeast.";
RL Nature 425:737-741(2003).
RN [8]
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 [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE 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 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
CC -!- FUNCTION: Minor 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: Cell membrane {ECO:0000269|PubMed:16233524};
CC Multi-pass membrane protein {ECO:0000269|PubMed:16233524}.
CC -!- MISCELLANEOUS: Present with 468 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the major facilitator superfamily. Sugar
CC transporter (TC 2.A.1.1) family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA14367.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=CAA88159.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=CAA99119.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; D90353; BAA14367.1; ALT_INIT; Genomic_DNA.
DR EMBL; Z48149; CAA88159.1; ALT_INIT; Genomic_DNA.
DR EMBL; Z74845; CAA99119.1; ALT_INIT; Genomic_DNA.
DR EMBL; BK006948; DAA10681.1; -; Genomic_DNA.
DR PIR; B40538; B40538.
DR RefSeq; NP_014538.2; NM_001183357.1.
DR AlphaFoldDB; P30606; -.
DR SMR; P30606; -.
DR BioGRID; 34300; 71.
DR DIP; DIP-6553N; -.
DR IntAct; P30606; 1.
DR STRING; 4932.YOL103W; -.
DR TCDB; 2.A.1.1.104; the major facilitator superfamily (mfs).
DR iPTMnet; P30606; -.
DR MaxQB; P30606; -.
DR PaxDb; P30606; -.
DR PRIDE; P30606; -.
DR EnsemblFungi; YOL103W_mRNA; YOL103W; YOL103W.
DR GeneID; 854050; -.
DR KEGG; sce:YOL103W; -.
DR SGD; S000005463; ITR2.
DR VEuPathDB; FungiDB:YOL103W; -.
DR eggNOG; KOG0254; Eukaryota.
DR GeneTree; ENSGT00940000155870; -.
DR HOGENOM; CLU_001265_30_5_1; -.
DR InParanoid; P30606; -.
DR OMA; VWILYMS; -.
DR BioCyc; YEAST:G3O-33501-MON; -.
DR PRO; PR:P30606; -.
DR Proteomes; UP000002311; Chromosome XV.
DR RNAct; P30606; protein.
DR GO; GO:0071944; C:cell periphery; HDA:SGD.
DR GO; GO:0000324; C:fungal-type vacuole; 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:0055085; P:transmembrane transport; IBA:GO_Central.
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 Cell membrane; Glycoprotein; Membrane; Reference proteome; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..609
FT /note="Myo-inositol transporter 2"
FT /id="PRO_0000050458"
FT TOPO_DOM 1..104
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 105..125
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 126..152
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 153..173
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 174..179
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 180..200
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 201..209
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 210..230
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 231..240
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 241..261
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 262..269
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 270..290
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 291..359
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 360..380
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 381..396
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 397..417
FT /note="Helical; Name=8"
FT /evidence="ECO:0000255"
FT TOPO_DOM 418..423
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 424..444
FT /note="Helical; Name=9"
FT /evidence="ECO:0000255"
FT TOPO_DOM 445..465
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 466..486
FT /note="Helical; Name=10"
FT /evidence="ECO:0000255"
FT TOPO_DOM 487..506
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 507..527
FT /note="Helical; Name=11"
FT /evidence="ECO:0000255"
FT TOPO_DOM 528..533
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 534..554
FT /note="Helical; Name=12"
FT /evidence="ECO:0000255"
FT TOPO_DOM 555..609
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 25..83
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 25..39
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 40..59
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 394
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 609 AA; 66710 MW; 5922363C7DF02EE1 CRC64;
MKNSTAASSR WTKSRLSHFF PSYTNSSGMG AASTDQSSTQ GEELHHRKHC EEDNDGQKPK
KSPVSTSTMQ IKSRQDEDED DGRIVIKPVN DEDDTSVIIT FNQSISPFII TLTFVASISG
FMFGYDTGYI SSALISINRD LDNKVLTYGE KELITAATSL GALITSVGAG TAADVFGRRP
CLMFSNLMFL IGAILQITAH KFWQMAAGRL IMGFGVGIGS LISPLFISEI APKMIRGRLT
VINSLWLTGG QLIAYGCGAG LNHVKNGWRI LVGLSLIPTV LQFSFFCFLP DTPRYYVMKG
DLKRAKMVLK RSYVNTEDEI IDQKVEELSS LNQSIPGKNP ITKFWNMVKE LHTVPSNFRA
LIIGCGLQAI QQFTGWNSLM YFSGTIFETV GFKNSSAVSI IVSGTNFVFT LIAFFCIDKI
GRRYILLIGL PGMTVALVIC AIAFHFLGIK FNGADAVVAS DGFSSWGIVI IVFIIVYAAF
YALGIGTVPW QQSELFPQNV RGVGTSYATA TNWAGSLVIA STFLTMLQNI TPTGTFSFFA
GVACLSTIFC YFCYPELSGL ELEEVQTILK DGFNIKASKA LAKKRKQQVA EGAAHHKLKF
EPTQEIVES
