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Protein

General amino acid permease AGP1

Gene

AGP1

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

Broad substrate range permease which transports asparagine and glutamine with intermediate specificity. Also transports Ala, Cys, Gly, Ile, Leu, Met, Phe, Ser, Thr, Tyr and Val. Important for the utilization of amino acids as a nitrogen source.2 Publications

Kineticsi

  1. KM=0.23 mM for leucine1 Publication
  1. Vmax=2.6 nmol/min/mg enzyme for leucine transport1 Publication

GO - Molecular functioni

  • amino acid transmembrane transporter activity Source: SGD
  • L-phenylalanine transmembrane transporter activity Source: CACAO
  • L-proline transmembrane transporter activity Source: SGD

GO - Biological processi

  • amino acid transport Source: SGD
  • phenylalanine transport Source: GOC
  • proline transmembrane transport Source: GOC
  • transmembrane transport Source: SGD
Complete GO annotation...

Keywords - Biological processi

Amino-acid transport, Transport

Enzyme and pathway databases

BioCyciYEAST:G3O-29287-MONOMER.
SABIO-RKP25376.

Protein family/group databases

TCDBi2.A.3.10.7. the amino acid-polyamine-organocation (apc) family.

Names & Taxonomyi

Protein namesi
Recommended name:
General amino acid permease AGP1
Alternative name(s):
Asparagine/glutamine permease
Gene namesi
Name:AGP1
Ordered Locus Names:YCL025C
ORF Names:YCL25C
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
Proteomesi
  • UP000002311 Componenti: Chromosome III

Organism-specific databases

EuPathDBiFungiDB:YCL025C.
SGDiS000000530. AGP1.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 124124CytoplasmicSequence analysisAdd
BLAST
Transmembranei125 – 14521HelicalSequence analysisAdd
BLAST
Topological domaini146 – 1483ExtracellularSequence analysis
Transmembranei149 – 16921HelicalSequence analysisAdd
BLAST
Topological domaini170 – 19728CytoplasmicSequence analysisAdd
BLAST
Transmembranei198 – 21821HelicalSequence analysisAdd
BLAST
Topological domaini219 – 23113ExtracellularSequence analysisAdd
BLAST
Transmembranei232 – 25221HelicalSequence analysisAdd
BLAST
Topological domaini253 – 2608CytoplasmicSequence analysis
Transmembranei261 – 28121HelicalSequence analysisAdd
BLAST
Topological domaini282 – 31332ExtracellularSequence analysisAdd
BLAST
Transmembranei314 – 33421HelicalSequence analysisAdd
BLAST
Topological domaini335 – 35218CytoplasmicSequence analysisAdd
BLAST
Transmembranei353 – 37321HelicalSequence analysisAdd
BLAST
Topological domaini374 – 40229ExtracellularSequence analysisAdd
BLAST
Transmembranei403 – 42523HelicalSequence analysisAdd
BLAST
Topological domaini426 – 45227CytoplasmicSequence analysisAdd
BLAST
Transmembranei453 – 47321HelicalSequence analysisAdd
BLAST
Topological domaini474 – 4774ExtracellularSequence analysis
Transmembranei478 – 49821HelicalSequence analysisAdd
BLAST
Topological domaini499 – 53133CytoplasmicSequence analysisAdd
BLAST
Transmembranei532 – 55221HelicalSequence analysisAdd
BLAST
Topological domaini553 – 5608ExtracellularSequence analysis
Transmembranei561 – 58121HelicalSequence analysisAdd
BLAST
Topological domaini582 – 63352CytoplasmicSequence analysisAdd
BLAST

GO - Cellular componenti

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

Keywords - Cellular componenti

Cell membrane, Membrane

Pathology & Biotechi

Chemistry

ChEMBLiCHEMBL1741178.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 633633General amino acid permease AGP1PRO_0000054142Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei6 – 61PhosphoserineBy similarity
Lipidationi633 – 6331S-palmitoyl cysteineBy similarity

Post-translational modificationi

Palmitoylated by PFA4.1 Publication

Keywords - PTMi

Lipoprotein, Palmitate, Phosphoprotein

Proteomic databases

MaxQBiP25376.
PeptideAtlasiP25376.

PTM databases

iPTMnetiP25376.
SwissPalmiP25376.

Expressioni

Inductioni

Induced by transcription factors DAL81 and STP1, which are activated by a signal initiated by the plasma membrane SPS (SSY1-PTR3-SSY5) amino acid sensor system in response to external amino acid levels.3 Publications

Interactioni

Protein-protein interaction databases

BioGridi30959. 117 interactions.
DIPiDIP-4973N.
IntActiP25376. 36 interactions.
MINTiMINT-566554.

Chemistry

BindingDBiP25376.

Structurei

3D structure databases

ProteinModelPortaliP25376.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

GeneTreeiENSGT00510000049744.
HOGENOMiHOG000261848.
InParanoidiP25376.
KOiK16261.
OMAiLSQIFTW.
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]
TIGRFAMsiTIGR00913. 2A0310. 1 hit.
PROSITEiPS00218. AMINO_ACID_PERMEASE_1. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P25376-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSSSKSLYEL KDLKNSSTEI HATGQDNEIE YFETGSNDRP SSQPHLGYEQ
60 70 80 90 100
HNTSAVRRFF DSFKRADQGP QDEVEATQMN DLTSAISPSS RQAQELEKNE
110 120 130 140 150
SSDNIGANTG HKSDSLKKTI QPRHVLMIAL GTGIGTGLLV GNGTALVHAG
160 170 180 190 200
PAGLLIGYAI MGSILYCIIQ ACGEMALVYS NLTGGYNAYP SFLVDDGFGF
210 220 230 240 250
AVAWVYCLQW LCVCPLELVT ASMTIKYWTT SVNPDVFVII FYVLVITINI
260 270 280 290 300
FGARGYAEAE FFFNCCKILM MTGFFILGII IDVGGAGNDG FIGGKYWHDP
310 320 330 340 350
GAFNGKHAID RFKGVAATLV TAAFAFGGSE FIAITTAEQS NPRKAIPGAA
360 370 380 390 400
KQMIYRILFL FLATIILLGF LVPYNSDQLL GSTGGGTKAS PYVIAVASHG
410 420 430 440 450
VRVVPHFINA VILLSVLSMA NSSFYSSARL FLTLSEQGYA PKVFSYIDRA
460 470 480 490 500
GRPLIAMGVS ALFAVIAFCA ASPKEEQVFT WLLAISGLSQ LFTWTAICLS
510 520 530 540 550
HLRFRRAMKV QGRSLGELGF KSQTGVWGSA YACIMMILIL IAQFWVAIAP
560 570 580 590 600
IGEGKLDAQA FFENYLAMPI LIALYVGYKV WHKDWKLFIR ADKIDLDSHR
610 620 630
QIFDEELIKQ EDEEYRERLR NGPYWKRVVA FWC
Length:633
Mass (Da):69,671
Last modified:April 29, 2008 - v3
Checksum:i8E19A836C2F6C50F
GO

Sequence cautioni

The sequence CAA42360.2 differs from that shown. Reason: Frameshift at position 591. Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X59720 Genomic DNA. Translation: CAA42360.2. Frameshift.
BK006937 Genomic DNA. Translation: DAA07460.1.
PIRiS19352.
RefSeqiNP_009905.3. NM_001178671.1.

Genome annotation databases

EnsemblFungiiCAA42360; CAA42360; CAA42360.
YCL025C; YCL025C; YCL025C.
GeneIDi850333.
KEGGisce:YCL025C.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X59720 Genomic DNA. Translation: CAA42360.2. Frameshift.
BK006937 Genomic DNA. Translation: DAA07460.1.
PIRiS19352.
RefSeqiNP_009905.3. NM_001178671.1.

3D structure databases

ProteinModelPortaliP25376.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi30959. 117 interactions.
DIPiDIP-4973N.
IntActiP25376. 36 interactions.
MINTiMINT-566554.

Chemistry

BindingDBiP25376.
ChEMBLiCHEMBL1741178.

Protein family/group databases

TCDBi2.A.3.10.7. the amino acid-polyamine-organocation (apc) family.

PTM databases

iPTMnetiP25376.
SwissPalmiP25376.

Proteomic databases

MaxQBiP25376.
PeptideAtlasiP25376.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiCAA42360; CAA42360; CAA42360.
YCL025C; YCL025C; YCL025C.
GeneIDi850333.
KEGGisce:YCL025C.

Organism-specific databases

EuPathDBiFungiDB:YCL025C.
SGDiS000000530. AGP1.

Phylogenomic databases

GeneTreeiENSGT00510000049744.
HOGENOMiHOG000261848.
InParanoidiP25376.
KOiK16261.
OMAiLSQIFTW.
OrthoDBiEOG74J9HZ.

Enzyme and pathway databases

BioCyciYEAST:G3O-29287-MONOMER.
SABIO-RKP25376.

Miscellaneous databases

PROiP25376.

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]
TIGRFAMsiTIGR00913. 2A0310. 1 hit.
PROSITEiPS00218. AMINO_ACID_PERMEASE_1. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "The complete DNA sequence of yeast chromosome III."
    Oliver S.G., van der Aart Q.J.M., Agostoni-Carbone M.L., Aigle M., Alberghina L., Alexandraki D., Antoine G., Anwar R., Ballesta J.P.G., Benit P., Berben G., Bergantino E., Biteau N., Bolle P.-A., Bolotin-Fukuhara M., Brown A., Brown A.J.P., Buhler J.-M.
    , Carcano C., Carignani G., Cederberg H., Chanet R., Contreras R., Crouzet M., Daignan-Fornier B., Defoor E., Delgado M.D., Demolder J., Doira C., Dubois E., Dujon B., Duesterhoeft A., Erdmann D., Esteban M., Fabre F., Fairhead C., Faye G., Feldmann H., Fiers W., Francingues-Gaillard M.-C., Franco L., Frontali L., Fukuhara H., Fuller L.J., Galland P., Gent M.E., Gigot D., Gilliquet V., Glansdorff N., Goffeau A., Grenson M., Grisanti P., Grivell L.A., de Haan M., Haasemann M., Hatat D., Hoenicka J., Hegemann J.H., Herbert C.J., Hilger F., Hohmann S., Hollenberg C.P., Huse K., Iborra F., Indge K.J., Isono K., Jacq C., Jacquet M., James C.M., Jauniaux J.-C., Jia Y., Jimenez A., Kelly A., Kleinhans U., Kreisl P., Lanfranchi G., Lewis C., van der Linden C.G., Lucchini G., Lutzenkirchen K., Maat M.J., Mallet L., Mannhaupt G., Martegani E., Mathieu A., Maurer C.T.C., McConnell D., McKee R.A., Messenguy F., Mewes H.-W., Molemans F., Montague M.A., Muzi Falconi M., Navas L., Newlon C.S., Noone D., Pallier C., Panzeri L., Pearson B.M., Perea J., Philippsen P., Pierard A., Planta R.J., Plevani P., Poetsch B., Pohl F.M., Purnelle B., Ramezani Rad M., Rasmussen S.W., Raynal A., Remacha M.A., Richterich P., Roberts A.B., Rodriguez F., Sanz E., Schaaff-Gerstenschlaeger I., Scherens B., Schweitzer B., Shu Y., Skala J., Slonimski P.P., Sor F., Soustelle C., Spiegelberg R., Stateva L.I., Steensma H.Y., Steiner S., Thierry A., Thireos G., Tzermia M., Urrestarazu L.A., Valle G., Vetter I., van Vliet-Reedijk J.C., Voet M., Volckaert G., Vreken P., Wang H., Warmington J.R., von Wettstein D., Wicksteed B.L., Wilson C., Wurst H., Xu G., Yoshikawa A., Zimmermann F.K., Sgouros J.G.
    Nature 357:38-46(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  2. Valles G., Volckaerts G.
    Submitted (JUN-2001) to the EMBL/GenBank/DDBJ databases
    Cited for: SEQUENCE REVISION TO 191-192; 194-197; 316 AND C-TERMINUS.
  3. Cited for: GENOME REANNOTATION.
    Strain: ATCC 204508 / S288c.
  4. "The Saccharomyces cerevisiae YCC5 (YCL025c) gene encodes an amino acid permease, Agp1, which transports asparagine and glutamine."
    Schreve J.L., Sin J.K., Garrett J.M.
    J. Bacteriol. 180:2556-2559(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: CHARACTERIZATION, IDENTIFICATION OF FRAMESHIFT.
  5. "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.
  6. "Substrate specificity and gene expression of the amino-acid permeases in Saccharomyces cerevisiae."
    Regenberg B., During-Olsen L., Kielland-Brandt M.C., Holmberg S.
    Curr. Genet. 36:317-328(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  7. "Amino acid signaling in Saccharomyces cerevisiae: a permease-like sensor of external amino acids and F-Box protein Grr1p are required for transcriptional induction of the AGP1 gene, which encodes a broad-specificity amino acid permease."
    Iraqui I., Vissers S., Bernard F., de Craene J.-O., Boles E., Urrestarazu A., Andre B.
    Mol. Cell. Biol. 19:989-1001(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: INDUCTION.
  8. "Genetic and biochemical analysis of the yeast plasma membrane Ssy1p-Ptr3p-Ssy5p sensor of extracellular amino acids."
    Forsberg H., Ljungdahl P.O.
    Mol. Cell. Biol. 21:814-826(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: INDUCTION BY SPS.
  9. "Reinvestigation of the Saccharomyces cerevisiae genome annotation by comparison to the genome of a related fungus: Ashbya gossypii."
    Brachat S., Dietrich F.S., Voegeli S., Zhang Z., Stuart L., Lerch A., Gates K., Gaffney T.D., Philippsen P.
    Genome Biol. 4:R45.1-R45.13(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION OF FRAMESHIFT.
  10. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
  11. "Yeast Agp2p and Agp3p function as amino acid permeases in poor nutrient conditions."
    Schreve J.L., Garrett J.M.
    Biochem. Biophys. Res. Commun. 313:745-751(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: BIOPHYSICOCHEMICAL PROPERTIES.
  12. "The external amino acid signaling pathway promotes activation of Stp1 and Uga35/Dal81 transcription factors for induction of the AGP1 gene in Saccharomyces cerevisiae."
    Abdel-Sater F., Iraqui I., Urrestarazu A., Andre B.
    Genetics 166:1727-1739(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: INDUCTION BY DAL81 AND STP1.
  13. Cited for: PALMITOYLATION.
  14. "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.
  15. "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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  16. "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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiAGP1_YEAST
AccessioniPrimary (citable) accession number: P25376
Secondary accession number(s): D6VQZ1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 1, 1992
Last sequence update: April 29, 2008
Last modified: June 8, 2016
This is version 145 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Miscellaneous

Present with 21100 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 III
    Yeast (Saccharomyces cerevisiae) chromosome III: 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.