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P25376 (AGP1_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified December 14, 2011. Version 109. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
General amino acid permease AGP1
Alternative name(s):
Asparagine/glutamine permease
Gene names
Name:AGP1
Ordered Locus Names:YCL025C
ORF Names:YCL25C
OrganismSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifier559292 [NCBI]
Taxonomic lineageEukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces

Protein attributes

Sequence length633 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.5 Ref.6

Subcellular location

Cell membrane; Multi-pass membrane protein By similarity.

Induction

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. Ref.7 Ref.8 Ref.12

Post-translational modification

Palmitoylated by PFA4. Ref.13

Miscellaneous

Present with 21100 molecules/cell in log phase SD medium. Ref.10

Sequence similarities

Belongs to the amino acid-polyamine-organocation (APC) superfamily. YAT (TC 2.A.3.10) family. [View classification]

Biophysicochemical properties

Kinetic parameters:

KM=0.23 mM for leucine Ref.11

Vmax=2.6 nmol/min/mg enzyme for leucine transport

Sequence caution

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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 633633General amino acid permease AGP1
PRO_0000054142

Regions

Topological domain1 – 124124Cytoplasmic Potential
Transmembrane125 – 14521Helical; Potential
Topological domain146 – 1483Extracellular Potential
Transmembrane149 – 16921Helical; Potential
Topological domain170 – 19728Cytoplasmic Potential
Transmembrane198 – 21821Helical; Potential
Topological domain219 – 23113Extracellular Potential
Transmembrane232 – 25221Helical; Potential
Topological domain253 – 2608Cytoplasmic Potential
Transmembrane261 – 28121Helical; Potential
Topological domain282 – 31332Extracellular Potential
Transmembrane314 – 33421Helical; Potential
Topological domain335 – 35218Cytoplasmic Potential
Transmembrane353 – 37321Helical; Potential
Topological domain374 – 40229Extracellular Potential
Transmembrane403 – 42523Helical; Potential
Topological domain426 – 45227Cytoplasmic Potential
Transmembrane453 – 47321Helical; Potential
Topological domain474 – 4774Extracellular Potential
Transmembrane478 – 49821Helical; Potential
Topological domain499 – 53133Cytoplasmic Potential
Transmembrane532 – 55221Helical; Potential
Topological domain553 – 5608Extracellular Potential
Transmembrane561 – 58121Helical; Potential
Topological domain582 – 63352Cytoplasmic Potential

Amino acid modifications

Modified residue871Phosphoserine Ref.15
Lipidation6331S-palmitoyl cysteine By similarity

Sequences

Sequence LengthMass (Da)Tools
P25376 [UniParc].

Last modified April 29, 2008. Version 3.
Checksum: 8E19A836C2F6C50F

FASTA63369,671
        10         20         30         40         50         60 
MSSSKSLYEL KDLKNSSTEI HATGQDNEIE YFETGSNDRP SSQPHLGYEQ HNTSAVRRFF 

        70         80         90        100        110        120 
DSFKRADQGP QDEVEATQMN DLTSAISPSS RQAQELEKNE SSDNIGANTG HKSDSLKKTI 

       130        140        150        160        170        180 
QPRHVLMIAL GTGIGTGLLV GNGTALVHAG PAGLLIGYAI MGSILYCIIQ ACGEMALVYS 

       190        200        210        220        230        240 
NLTGGYNAYP SFLVDDGFGF AVAWVYCLQW LCVCPLELVT ASMTIKYWTT SVNPDVFVII 

       250        260        270        280        290        300 
FYVLVITINI FGARGYAEAE FFFNCCKILM MTGFFILGII IDVGGAGNDG FIGGKYWHDP 

       310        320        330        340        350        360 
GAFNGKHAID RFKGVAATLV TAAFAFGGSE FIAITTAEQS NPRKAIPGAA KQMIYRILFL 

       370        380        390        400        410        420 
FLATIILLGF LVPYNSDQLL GSTGGGTKAS PYVIAVASHG VRVVPHFINA VILLSVLSMA 

       430        440        450        460        470        480 
NSSFYSSARL FLTLSEQGYA PKVFSYIDRA GRPLIAMGVS ALFAVIAFCA ASPKEEQVFT 

       490        500        510        520        530        540 
WLLAISGLSQ LFTWTAICLS HLRFRRAMKV QGRSLGELGF KSQTGVWGSA YACIMMILIL 

       550        560        570        580        590        600 
IAQFWVAIAP IGEGKLDAQA FFENYLAMPI LIALYVGYKV WHKDWKLFIR ADKIDLDSHR 

       610        620        630 
QIFDEELIKQ EDEEYRERLR NGPYWKRVVA FWC

« Hide

References

« Hide 'large scale' references
[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. expand/collapse author list , 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: 1574125] [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]Saccharomyces Genome Database
Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases
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: 9573211] [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: 10467005] [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: 10654085] [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: 9891035] [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: 11154269] [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: 12844361] [Abstract]
Cited for: IDENTIFICATION OF FRAMESHIFT.
[10]"Global analysis of protein expression in yeast."
Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N., O'Shea E.K., Weissman J.S.
Nature 425:737-741(2003) [PubMed: 14562106] [Abstract]
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: 14697254] [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: 15126393] [Abstract]
Cited for: INDUCTION BY DAL81 AND STP1.
[13]"Global analysis of protein palmitoylation in yeast."
Roth A.F., Wan J., Bailey A.O., Sun B., Kuchar J.A., Green W.N., Phinney B.S., Yates J.R. III, Davis N.G.
Cell 125:1003-1013(2006) [PubMed: 16751107] [Abstract]
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: 16847258] [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: 18407956] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-87, MASS SPECTROMETRY.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		X59720 Genomic DNA. Translation: CAA42360.2. Frameshift.
BK006937 Genomic DNA. Translation: DAA07460.1.
PIRS19352.
RefSeqNP_009905.3. NM_001178671.1.

3D structure databases

ProteinModelPortalP25376.
ModBaseSearch...

Protein-protein interaction databases

DIPDIP-4973N.
IntActP25376. 173 interactions.
MINTMINT-566554.
STRINGP25376.

Protein family/group databases

TCDB2.A.3.10.7. amino acid-polyamine-organocation (APC) family.

Proteomic databases

PeptideAtlasP25376.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiYCL025C; YCL025C; YCL025C.
GeneID850333.
KEGGsce:YCL025C.
NMPDRfig|4932.3.peg.626.

Organism-specific databases

SGDS000000530. AGP1.

Phylogenomic databases

eggNOGfuNOG07978.
GeneTreeEFGT00050000001131.
HOGENOMHBG492579.
OMAICISHVR.
OrthoDBEOG47Q1FD.

Gene expression databases

ArrayExpressP25376.
GenevestigatorP25376.
GermOnlineYCL025C. Saccharomyces cerevisiae.

Family and domain databases

InterProIPR004841. AA-permease_dom.
IPR002293. AA/rel_permease1.
IPR004762. Amino_acid_permease_fungi.
IPR004840. Amoino_acid_permease_CS.
[Graphical view]
PANTHERPTHR11785. AA/rel_permease1. 1 hit.
PfamPF00324. AA_permease. 1 hit.
[Graphical view]
PIRSFPIRSF006060. AA_transporter. 1 hit.
TIGRFAMsTIGR00913. 2A0310. 1 hit.
PROSITEPS00218. AMINO_ACID_PERMEASE_1. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio965769.

Entry information

Entry nameAGP1_YEAST
AccessionPrimary (citable) accession number: P25376
Secondary accession number(s): D6VQZ1
Entry history
Integrated into UniProtKB/Swiss-Prot: May 1, 1992
Last sequence update: April 29, 2008
Last modified: December 14, 2011
This is version 109 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

Yeast

Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD

Yeast chromosome III

Yeast (Saccharomyces cerevisiae) chromosome III: entries and gene names

SIMILARITY comments

Index of protein domains and families

to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents