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Protein

Myo-inositol transporter 1

Gene

ITR1

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Major transporter for myo-inositol.

GO - Molecular functioni

  • myo-inositol transmembrane transporter activity Source: SGD

GO - Biological processi

  • myo-inositol transport Source: SGD
  • pseudohyphal growth Source: SGD
  • transmembrane transport Source: SGD
Complete GO annotation...

Keywords - Biological processi

Transport

Enzyme and pathway databases

BioCyciYEAST:G3O-30020-MONOMER.
ReactomeiR-SCE-428790. Facilitative Na+-independent glucose transporters.
R-SCE-429593. Inositol transporters.

Protein family/group databases

TCDBi2.A.1.1.8. the major facilitator superfamily (mfs).

Names & Taxonomyi

Protein namesi
Recommended name:
Myo-inositol transporter 1
Gene namesi
Name:ITR1
Ordered Locus Names:YDR497C
ORF Names:D9719.3
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
Proteomesi
  • UP000002311 Componenti: Chromosome IV

Organism-specific databases

EuPathDBiFungiDB:YDR497C.
SGDiS000002905. ITR1.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 8181CytoplasmicSequence analysisAdd
BLAST
Transmembranei82 – 10221Helical; Name=1Sequence analysisAdd
BLAST
Topological domaini103 – 12927ExtracellularSequence analysisAdd
BLAST
Transmembranei130 – 15021Helical; Name=2Sequence analysisAdd
BLAST
Topological domaini151 – 16313CytoplasmicSequence analysisAdd
BLAST
Transmembranei164 – 18421Helical; Name=3Sequence analysisAdd
BLAST
Topological domaini185 – 1862ExtracellularSequence analysis
Transmembranei187 – 20721Helical; Name=4Sequence analysisAdd
BLAST
Topological domaini208 – 2158CytoplasmicSequence analysis
Transmembranei216 – 23621Helical; Name=5Sequence analysisAdd
BLAST
Topological domaini237 – 24610ExtracellularSequence analysis
Transmembranei247 – 26721Helical; Name=6Sequence analysisAdd
BLAST
Topological domaini268 – 34982CytoplasmicSequence analysisAdd
BLAST
Transmembranei350 – 37021Helical; Name=7Sequence analysisAdd
BLAST
Topological domaini371 – 3766ExtracellularSequence analysis
Transmembranei377 – 39721Helical; Name=8Sequence analysisAdd
BLAST
Topological domaini398 – 4003CytoplasmicSequence analysis
Transmembranei401 – 42121Helical; Name=9Sequence analysisAdd
BLAST
Topological domaini422 – 44120ExtracellularSequence analysisAdd
BLAST
Transmembranei442 – 46221Helical; Name=10Sequence analysisAdd
BLAST
Topological domaini463 – 48624CytoplasmicSequence analysisAdd
BLAST
Transmembranei487 – 50721Helical; Name=11Sequence analysisAdd
BLAST
Topological domaini508 – 5103ExtracellularSequence analysis
Transmembranei511 – 53121Helical; Name=12Sequence analysisAdd
BLAST
Topological domaini532 – 58453CytoplasmicSequence analysisAdd
BLAST

GO - Cellular componenti

  • integral component of membrane Source: UniProtKB-KW
  • membrane Source: SGD
  • plasma membrane Source: SGD
Complete GO annotation...

Keywords - Cellular componenti

Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 584584Myo-inositol transporter 1PRO_0000050455Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei12 – 121PhosphothreonineCombined sources
Modified residuei26 – 261PhosphoserineCombined sources
Modified residuei31 – 311PhosphoserineCombined sources
Modified residuei35 – 351PhosphoserineCombined sources
Modified residuei37 – 371PhosphoserineCombined sources
Modified residuei46 – 461PhosphoserineCombined sources
Glycosylationi371 – 3711N-linked (GlcNAc...)Sequence analysis
Cross-linki573 – 573Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)2 Publications

Keywords - PTMi

Glycoprotein, Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

MaxQBiP30605.
TopDownProteomicsiP30605.

PTM databases

iPTMnetiP30605.

Interactioni

Protein-protein interaction databases

BioGridi32548. 82 interactions.
DIPiDIP-7406N.
IntActiP30605. 23 interactions.
MINTiMINT-1356907.

Structurei

3D structure databases

ProteinModelPortaliP30605.
SMRiP30605. Positions 103-536.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

GeneTreeiENSGT00590000083062.
HOGENOMiHOG000202868.
InParanoidiP30605.
KOiK08150.
OMAiQNITPAG.
OrthoDBiEOG7QG4D1.

Family and domain databases

InterProiIPR020846. MFS_dom.
IPR005828. MFS_sugar_transport_like.
IPR003663. Sugar/inositol_transpt.
IPR005829. Sugar_transporter_CS.
[Graphical view]
PfamiPF00083. Sugar_tr. 1 hit.
[Graphical view]
PRINTSiPR00171. SUGRTRNSPORT.
SUPFAMiSSF103473. SSF103473. 1 hit.
TIGRFAMsiTIGR00879. SP. 1 hit.
PROSITEiPS50850. MFS. 1 hit.
PS00216. SUGAR_TRANSPORT_1. 2 hits.
PS00217. SUGAR_TRANSPORT_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P30605-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MGIHIPYLTS KTSQSNVGDA VGNADSVEFN SEHDSPSKRG KITLESHEIQ
60 70 80 90 100
RAPASDDEDR IQIKPVNDED DTSVMITFNQ SLSPFIITLT FVASISGFMF
110 120 130 140 150
GYDTGYISSA LISIGTDLDH KVLTYGEKEI VTAATSLGAL ITSIFAGTAA
160 170 180 190 200
DIFGRKRCLM GSNLMFVIGA ILQVSAHTFW QMAVGRLIMG FGVGIGSLIA
210 220 230 240 250
PLFISEIAPK MIRGRLTVIN SLWLTGGQLV AYGCGAGLNY VNNGWRILVG
260 270 280 290 300
LSLIPTAVQF TCLCFLPDTP RYYVMKGDLA RATEVLKRSY TDTSEEIIER
310 320 330 340 350
KVEELVTLNQ SIPGKNVPEK VWNTIKELHT VPSNLRALII GCGLQAIQQF
360 370 380 390 400
TGWNSLMYFS GTIFETVGFK NSSAVSIIVS GTNFIFTLVA FFSIDKIGRR
410 420 430 440 450
TILLIGLPGM TMALVVCSIA FHFLGIKFDG AVAVVVSSGF SSWGIVIIVF
460 470 480 490 500
IIVFAAFYAL GIGTVPWQQS ELFPQNVRGI GTSYATATNW AGSLVIASTF
510 520 530 540 550
LTMLQNITPA GTFAFFAGLS CLSTIFCYFC YPELSGLELE EVQTILKDGF
560 570 580
NIKASKALAK KRKQQVARVH ELKYEPTQEI IEDI
Length:584
Mass (Da):63,570
Last modified:October 1, 1996 - v2
Checksum:i42543E30A102DC65
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti43 – 442TL → HI in BAA14366 (PubMed:2040626).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D90352 Genomic DNA. Translation: BAA14366.1.
U33057 Genomic DNA. Translation: AAB64939.1.
BK006938 Genomic DNA. Translation: DAA12329.1.
PIRiS69555.
RefSeqiNP_010785.1. NM_001180805.1.

Genome annotation databases

EnsemblFungiiYDR497C; YDR497C; YDR497C.
GeneIDi852108.
KEGGisce:YDR497C.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D90352 Genomic DNA. Translation: BAA14366.1.
U33057 Genomic DNA. Translation: AAB64939.1.
BK006938 Genomic DNA. Translation: DAA12329.1.
PIRiS69555.
RefSeqiNP_010785.1. NM_001180805.1.

3D structure databases

ProteinModelPortaliP30605.
SMRiP30605. Positions 103-536.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi32548. 82 interactions.
DIPiDIP-7406N.
IntActiP30605. 23 interactions.
MINTiMINT-1356907.

Protein family/group databases

TCDBi2.A.1.1.8. the major facilitator superfamily (mfs).

PTM databases

iPTMnetiP30605.

Proteomic databases

MaxQBiP30605.
TopDownProteomicsiP30605.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYDR497C; YDR497C; YDR497C.
GeneIDi852108.
KEGGisce:YDR497C.

Organism-specific databases

EuPathDBiFungiDB:YDR497C.
SGDiS000002905. ITR1.

Phylogenomic databases

GeneTreeiENSGT00590000083062.
HOGENOMiHOG000202868.
InParanoidiP30605.
KOiK08150.
OMAiQNITPAG.
OrthoDBiEOG7QG4D1.

Enzyme and pathway databases

BioCyciYEAST:G3O-30020-MONOMER.
ReactomeiR-SCE-428790. Facilitative Na+-independent glucose transporters.
R-SCE-429593. Inositol transporters.

Miscellaneous databases

PROiP30605.

Family and domain databases

InterProiIPR020846. MFS_dom.
IPR005828. MFS_sugar_transport_like.
IPR003663. Sugar/inositol_transpt.
IPR005829. Sugar_transporter_CS.
[Graphical view]
PfamiPF00083. Sugar_tr. 1 hit.
[Graphical view]
PRINTSiPR00171. SUGRTRNSPORT.
SUPFAMiSSF103473. SSF103473. 1 hit.
TIGRFAMsiTIGR00879. SP. 1 hit.
PROSITEiPS50850. MFS. 1 hit.
PS00216. SUGAR_TRANSPORT_1. 2 hits.
PS00217. SUGAR_TRANSPORT_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Isolation and characterization of two distinct myo-inositol transporter genes of Saccharomyces cerevisiae."
    Nikawa J., Tsukagoshi Y., Yamashita S.
    J. Biol. Chem. 266:11184-11191(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  2. "The nucleotide sequence of Saccharomyces cerevisiae chromosome IV."
    Jacq C., Alt-Moerbe J., Andre B., Arnold W., Bahr A., Ballesta J.P.G., Bargues M., Baron L., Becker A., Biteau N., Bloecker H., Blugeon C., Boskovic J., Brandt P., Brueckner M., Buitrago M.J., Coster F., Delaveau T.
    , del Rey F., Dujon B., Eide L.G., Garcia-Cantalejo J.M., Goffeau A., Gomez-Peris A., Granotier C., Hanemann V., Hankeln T., Hoheisel J.D., Jaeger W., Jimenez A., Jonniaux J.-L., Kraemer C., Kuester H., Laamanen P., Legros Y., Louis E.J., Moeller-Rieker S., Monnet A., Moro M., Mueller-Auer S., Nussbaumer B., Paricio N., Paulin L., Perea J., Perez-Alonso M., Perez-Ortin J.E., Pohl T.M., Prydz H., Purnelle B., Rasmussen S.W., Remacha M.A., Revuelta J.L., Rieger M., Salom D., Saluz H.P., Saiz J.E., Saren A.-M., Schaefer M., Scharfe M., Schmidt E.R., Schneider C., Scholler P., Schwarz S., Soler-Mira A., Urrestarazu L.A., Verhasselt P., Vissers S., Voet M., Volckaert G., Wagner G., Wambutt R., Wedler E., Wedler H., Woelfl S., Harris D.E., Bowman S., Brown D., Churcher C.M., Connor R., Dedman K., Gentles S., Hamlin N., Hunt S., Jones L., McDonald S., Murphy L.D., Niblett D., Odell C., Oliver K., Rajandream M.A., Richards C., Shore L., Walsh S.V., Barrell B.G., Dietrich F.S., Mulligan J.T., Allen E., Araujo R., Aviles E., Berno A., Carpenter J., Chen E., Cherry J.M., Chung E., Duncan M., Hunicke-Smith S., Hyman R.W., Komp C., Lashkari D., Lew H., Lin D., Mosedale D., Nakahara K., Namath A., Oefner P., Oh C., Petel F.X., Roberts D., Schramm S., Schroeder M., Shogren T., Shroff N., Winant A., Yelton M.A., Botstein D., Davis R.W., Johnston M., Andrews S., Brinkman R., Cooper J., Ding H., Du Z., Favello A., Fulton L., Gattung S., Greco T., Hallsworth K., Hawkins J., Hillier L.W., Jier M., Johnson D., Johnston L., Kirsten J., Kucaba T., Langston Y., Latreille P., Le T., Mardis E., Menezes S., Miller N., Nhan M., Pauley A., Peluso D., Rifkin L., Riles L., Taich A., Trevaskis E., Vignati D., Wilcox L., Wohldman P., Vaudin M., Wilson R., Waterston R., Albermann K., Hani J., Heumann K., Kleine K., Mewes H.-W., Zollner A., Zaccaria P.
    Nature 387:75-78(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  3. Cited for: GENOME REANNOTATION.
    Strain: ATCC 204508 / S288c.
  4. Cited for: UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-573.
    Strain: SUB592.
  5. "A subset of membrane-associated proteins is ubiquitinated in response to mutations in the endoplasmic reticulum degradation machinery."
    Hitchcock A.L., Auld K., Gygi S.P., Silver P.A.
    Proc. Natl. Acad. Sci. U.S.A. 100:12735-12740(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-573.
  6. "Quantitative phosphoproteomics applied to the yeast pheromone signaling pathway."
    Gruhler A., Olsen J.V., Mohammed S., Mortensen P., Faergeman N.J., Mann M., Jensen O.N.
    Mol. Cell. Proteomics 4:310-327(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-46, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Strain: YAL6B.
  7. "A global topology map of the Saccharomyces cerevisiae membrane proteome."
    Kim H., Melen K., Oesterberg M., von Heijne G.
    Proc. Natl. Acad. Sci. U.S.A. 103:11142-11147(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: TOPOLOGY [LARGE SCALE ANALYSIS].
    Strain: ATCC 208353 / W303-1A.
  8. "Large-scale phosphorylation analysis of alpha-factor-arrested Saccharomyces cerevisiae."
    Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J., Elias J.E., Gygi S.P.
    J. Proteome Res. 6:1190-1197(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Strain: ADR376.
  9. "Global analysis of Cdk1 substrate phosphorylation sites provides insights into evolution."
    Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.
    Science 325:1682-1686(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-12; SER-26; SER-31; SER-35; SER-37 AND SER-46, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  10. "Sites of ubiquitin attachment in Saccharomyces cerevisiae."
    Starita L.M., Lo R.S., Eng J.K., von Haller P.D., Fields S.
    Proteomics 12:236-240(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiITR1_YEAST
AccessioniPrimary (citable) accession number: P30605
Secondary accession number(s): D6VTB9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 1, 1993
Last sequence update: October 1, 1996
Last modified: June 8, 2016
This is version 147 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families
  2. Yeast
    Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
  3. Yeast chromosome IV
    Yeast (Saccharomyces cerevisiae) chromosome IV: entries and gene names

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.