Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Valine/tyrosine/tryptophan amino-acid permease 1

Gene

TAT1

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

Functioni

High-affinity transport of valine and tyrosine. Low-affinity transport of tryptophan. Can also transport L-cysteine.1 Publication

GO - Molecular functioni

  • amino acid transmembrane transporter activity Source: SGD
  • antiporter activity Source: GO_Central
  • low-affinity tryptophan transmembrane transporter activity Source: SGD

GO - Biological processi

  • amino acid transport Source: SGD
  • transmembrane transport Source: SGD
  • tryptophan transport Source: SGD
  • tyrosine transport Source: SGD
Complete GO annotation...

Keywords - Biological processi

Amino-acid transport, Transport

Enzyme and pathway databases

BioCyciYEAST:G3O-29038-MONOMER.

Protein family/group databases

TCDBi2.A.3.10.9. the amino acid-polyamine-organocation (apc) family.

Names & Taxonomyi

Protein namesi
Recommended name:
Valine/tyrosine/tryptophan amino-acid permease 1
Alternative name(s):
Tyrosine and tryptophan amino acid transporter 1
Gene namesi
Name:TAT1
Synonyms:TAP1, VAP1
Ordered Locus Names:YBR069C
ORF Names:YBR0710
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
Proteomesi
  • UP000002311 Componenti: Chromosome II

Organism-specific databases

EuPathDBiFungiDB:YBR069C.
SGDiS000000273. TAT1.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 9999CytoplasmicSequence analysisAdd
BLAST
Transmembranei100 – 12021HelicalSequence analysisAdd
BLAST
Topological domaini121 – 1222ExtracellularSequence analysis
Transmembranei123 – 14321HelicalSequence analysisAdd
BLAST
Topological domaini144 – 17229CytoplasmicSequence analysisAdd
BLAST
Transmembranei173 – 19321HelicalSequence analysisAdd
BLAST
Topological domaini194 – 20411ExtracellularSequence analysisAdd
BLAST
Transmembranei205 – 22521HelicalSequence analysisAdd
BLAST
Topological domaini226 – 2338CytoplasmicSequence analysis
Transmembranei234 – 25421HelicalSequence analysisAdd
BLAST
Topological domaini255 – 28127ExtracellularSequence analysisAdd
BLAST
Transmembranei282 – 30221HelicalSequence analysisAdd
BLAST
Topological domaini303 – 32018CytoplasmicSequence analysisAdd
BLAST
Transmembranei321 – 34121HelicalSequence analysisAdd
BLAST
Topological domaini342 – 36827ExtracellularSequence analysisAdd
BLAST
Transmembranei369 – 38921HelicalSequence analysisAdd
BLAST
Topological domaini390 – 42233CytoplasmicSequence analysisAdd
BLAST
Transmembranei423 – 44321HelicalSequence analysisAdd
BLAST
Topological domaini444 – 4463ExtracellularSequence analysis
Transmembranei447 – 46721HelicalSequence analysisAdd
BLAST
Topological domaini468 – 49932CytoplasmicSequence analysisAdd
BLAST
Transmembranei500 – 52021HelicalSequence analysisAdd
BLAST
Topological domaini521 – 5299ExtracellularSequence analysis
Transmembranei530 – 55021HelicalSequence analysisAdd
BLAST
Topological domaini551 – 61969CytoplasmicSequence analysisAdd
BLAST

GO - Cellular componenti

  • integral component of plasma membrane Source: GO_Central
  • plasma membrane Source: SGD
  • vacuole Source: GO_Central
Complete GO annotation...

Keywords - Cellular componenti

Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 619619Valine/tyrosine/tryptophan amino-acid permease 1PRO_0000054162Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei13 – 131PhosphoserineCombined sources
Cross-linki39 – 39Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)Combined sources1 Publication
Modified residuei80 – 801PhosphoserineCombined sources
Modified residuei84 – 841PhosphoserineCombined sources

Keywords - PTMi

Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

MaxQBiP38085.

PTM databases

iPTMnetiP38085.
SwissPalmiP38085.

Interactioni

Binary interactionsi

WithEntry#Exp.IntActNotes
MIR1P236413EBI-20222,EBI-11178

Protein-protein interaction databases

BioGridi32772. 67 interactions.
DIPiDIP-4912N.
IntActiP38085. 32 interactions.
MINTiMINT-574517.

Structurei

3D structure databases

ProteinModelPortaliP38085.
SMRiP38085. Positions 214-411.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

GeneTreeiENSGT00510000049744.
InParanoidiP38085.
KOiK16261.
OMAiVFCYAAF.
OrthoDBiEOG74J9HZ.

Family and domain databases

InterProiIPR004841. AA-permease/SLC12A_dom.
IPR002293. AA/rel_permease1.
IPR004762. Amino_acid_permease_fungi.
IPR004840. Amoino_acid_permease_CS.
[Graphical view]
PANTHERiPTHR11785. PTHR11785. 1 hit.
PfamiPF00324. AA_permease. 1 hit.
[Graphical view]
PIRSFiPIRSF006060. AA_transporter. 1 hit.
TIGRFAMsiTIGR00913. 2A0310. 1 hit.
PROSITEiPS00218. AMINO_ACID_PERMEASE_1. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P38085-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MDDSVSFIAK EASPAQYSHS LHERTHSEKQ KRDFTITEKQ DEVSGQTAEP
60 70 80 90 100
RRTDSKSILQ RKCKEFFDSF KRQLPPDRNS ELESQEKNNL TKSIKSRHLV
110 120 130 140 150
MISLGTGIGT GLLVGNGQVL GTAGPAGLVL GYGIASIMLY CIIQAAGELG
160 170 180 190 200
LCYAGLTGNY TRYPSILVDP SLGFAVSVVY TIQWLTVLPL QLVTAAMTVK
210 220 230 240 250
YWTSVNADIF VAVVFVFVII INLFGSRGYA EAEFIFNSCK ILMVIGFVIL
260 270 280 290 300
AIIINCGGAG DRRYIGAEYW HNPGPFAHGF KGVCTVFCYA AFSYGGIEVL
310 320 330 340 350
LLSAAEQENP TKSIPNACKK VVYRILLIYM LTTILVCFLV PYNSDELLGS
360 370 380 390 400
SDSSGSHASP FVIAVASHGV KVVPHFINAV ILISVISVAN SSLYSGPRLL
410 420 430 440 450
LSLAEQGVLP KCLAYVDRNG RPLLCFFVSL VFGCIGFVAT SDAEEQVFTW
460 470 480 490 500
LLAISSLSQL FIWMSMSLSH IRFRDAMAKQ GRSMNEVGYK AQTGYWGSWL
510 520 530 540 550
AVLIAIFFLV CQFWVAIAPV NEHGKLNVKV FFQNYLAMPI VLFAYFGHKI
560 570 580 590 600
YFKSWSFWIP AEKIDLDSHR NIFVSPSLTE IDKVDDNDDL KEYENSESSE
610
NPNSSRSRKF FKRMTNFWC
Length:619
Mass (Da):68,758
Last modified:October 1, 1994 - v1
Checksum:i7A575A9BF2A084F8
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U10503 Genomic DNA. Translation: AAA50552.1.
X79151 Genomic DNA. Translation: CAA55778.1.
X76294 Genomic DNA. Translation: CAA53926.1.
Z35938 Genomic DNA. Translation: CAA85013.1.
BK006936 Genomic DNA. Translation: DAA07188.1.
PIRiS45932.
RefSeqiNP_009625.1. NM_001178417.1.

Genome annotation databases

EnsemblFungiiYBR069C; YBR069C; YBR069C.
GeneIDi852361.
KEGGisce:YBR069C.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U10503 Genomic DNA. Translation: AAA50552.1.
X79151 Genomic DNA. Translation: CAA55778.1.
X76294 Genomic DNA. Translation: CAA53926.1.
Z35938 Genomic DNA. Translation: CAA85013.1.
BK006936 Genomic DNA. Translation: DAA07188.1.
PIRiS45932.
RefSeqiNP_009625.1. NM_001178417.1.

3D structure databases

ProteinModelPortaliP38085.
SMRiP38085. Positions 214-411.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi32772. 67 interactions.
DIPiDIP-4912N.
IntActiP38085. 32 interactions.
MINTiMINT-574517.

Protein family/group databases

TCDBi2.A.3.10.9. the amino acid-polyamine-organocation (apc) family.

PTM databases

iPTMnetiP38085.
SwissPalmiP38085.

Proteomic databases

MaxQBiP38085.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYBR069C; YBR069C; YBR069C.
GeneIDi852361.
KEGGisce:YBR069C.

Organism-specific databases

EuPathDBiFungiDB:YBR069C.
SGDiS000000273. TAT1.

Phylogenomic databases

GeneTreeiENSGT00510000049744.
InParanoidiP38085.
KOiK16261.
OMAiVFCYAAF.
OrthoDBiEOG74J9HZ.

Enzyme and pathway databases

BioCyciYEAST:G3O-29038-MONOMER.

Miscellaneous databases

PROiP38085.

Family and domain databases

InterProiIPR004841. AA-permease/SLC12A_dom.
IPR002293. AA/rel_permease1.
IPR004762. Amino_acid_permease_fungi.
IPR004840. Amoino_acid_permease_CS.
[Graphical view]
PANTHERiPTHR11785. PTHR11785. 1 hit.
PfamiPF00324. AA_permease. 1 hit.
[Graphical view]
PIRSFiPIRSF006060. AA_transporter. 1 hit.
TIGRFAMsiTIGR00913. 2A0310. 1 hit.
PROSITEiPS00218. AMINO_ACID_PERMEASE_1. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. Andersen H.A., Kielland-Brandt M.C.
    Submitted (JUN-1994) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: JH 13-5C.
  2. "Two FK506 resistance-conferring genes in Saccharomyces cerevisiae, TAT1 and TAT2, encode amino acid permeases mediating tyrosine and tryptophan uptake."
    Schmidt A., Hall M.N., Koller A.
    Mol. Cell. Biol. 14:6597-6606(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: JK9-3D.
  3. "Complete DNA sequence of yeast chromosome II."
    Feldmann H., Aigle M., Aljinovic G., Andre B., Baclet M.C., Barthe C., Baur A., Becam A.-M., Biteau N., Boles E., Brandt T., Brendel M., Brueckner M., Bussereau F., Christiansen C., Contreras R., Crouzet M., Cziepluch C.
    , Demolis N., Delaveau T., Doignon F., Domdey H., Duesterhus S., Dubois E., Dujon B., El Bakkoury M., Entian K.-D., Feuermann M., Fiers W., Fobo G.M., Fritz C., Gassenhuber J., Glansdorff N., Goffeau A., Grivell L.A., de Haan M., Hein C., Herbert C.J., Hollenberg C.P., Holmstroem K., Jacq C., Jacquet M., Jauniaux J.-C., Jonniaux J.-L., Kallesoee T., Kiesau P., Kirchrath L., Koetter P., Korol S., Liebl S., Logghe M., Lohan A.J.E., Louis E.J., Li Z.Y., Maat M.J., Mallet L., Mannhaupt G., Messenguy F., Miosga T., Molemans F., Mueller S., Nasr F., Obermaier B., Perea J., Pierard A., Piravandi E., Pohl F.M., Pohl T.M., Potier S., Proft M., Purnelle B., Ramezani Rad M., Rieger M., Rose M., Schaaff-Gerstenschlaeger I., Scherens B., Schwarzlose C., Skala J., Slonimski P.P., Smits P.H.M., Souciet J.-L., Steensma H.Y., Stucka R., Urrestarazu L.A., van der Aart Q.J.M., Van Dyck L., Vassarotti A., Vetter I., Vierendeels F., Vissers S., Wagner G., de Wergifosse P., Wolfe K.H., Zagulski M., Zimmermann F.K., Mewes H.-W., Kleine K.
    EMBO J. 13:5795-5809(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  4. Cited for: GENOME REANNOTATION.
    Strain: ATCC 204508 / S288c.
  5. "Sequence analysis of a 31 kb DNA fragment from the right arm of Saccharomyces cerevisiae chromosome II."
    van der Aart Q.J.M., Barthe C., Doignon F., Aigle M., Crouzet M., Steensma H.Y.
    Yeast 10:959-964(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-356.
    Strain: ATCC 204508 / S288c.
  6. "Cysteine uptake by Saccharomyces cerevisiae is accomplished by multiple permeases."
    During-Olsen L., Regenberg B., Gjermansen C., Kielland-Brandt M.C., Hansen J.
    Curr. Genet. 35:609-617(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN L-CYSTEINE UPTAKE.
  7. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
  8. "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-39.
  9. "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.
  10. "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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-84, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Strain: ADR376.
  11. "Analysis of phosphorylation sites on proteins from Saccharomyces cerevisiae by electron transfer dissociation (ETD) mass spectrometry."
    Chi A., Huttenhower C., Geer L.Y., Coon J.J., Syka J.E.P., Bai D.L., Shabanowitz J., Burke D.J., Troyanskaya O.G., Hunt D.F.
    Proc. Natl. Acad. Sci. U.S.A. 104:2193-2198(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-13; SER-80 AND SER-84, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  12. "A multidimensional chromatography technology for in-depth phosphoproteome analysis."
    Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.
    Mol. Cell. Proteomics 7:1389-1396(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-84, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  13. "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 SER-84, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  14. "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: UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-39, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiTAT1_YEAST
AccessioniPrimary (citable) accession number: P38085
Secondary accession number(s): D6VQ68
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1994
Last sequence update: October 1, 1994
Last modified: July 6, 2016
This is version 155 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Miscellaneous

Present with 504 molecules/cell in log phase SD medium.1 Publication

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 II
    Yeast (Saccharomyces cerevisiae) chromosome II: 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.