AGP1_YEAST
ID AGP1_YEAST Reviewed; 633 AA.
AC P25376; D6VQZ1;
DT 01-MAY-1992, integrated into UniProtKB/Swiss-Prot.
DT 29-APR-2008, sequence version 3.
DT 03-AUG-2022, entry version 184.
DE RecName: Full=General amino acid permease AGP1;
DE AltName: Full=Asparagine/glutamine permease;
GN Name=AGP1; OrderedLocusNames=YCL025C; ORFNames=YCL25C;
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 [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=1574125; DOI=10.1038/357038a0;
RA Oliver S.G., van der Aart Q.J.M., Agostoni-Carbone M.L., Aigle M.,
RA Alberghina L., Alexandraki D., Antoine G., Anwar R., Ballesta J.P.G.,
RA Benit P., Berben G., Bergantino E., Biteau N., Bolle P.-A.,
RA Bolotin-Fukuhara M., Brown A., Brown A.J.P., Buhler J.-M., Carcano C.,
RA Carignani G., Cederberg H., Chanet R., Contreras R., Crouzet M.,
RA Daignan-Fornier B., Defoor E., Delgado M.D., Demolder J., Doira C.,
RA Dubois E., Dujon B., Duesterhoeft A., Erdmann D., Esteban M., Fabre F.,
RA Fairhead C., Faye G., Feldmann H., Fiers W., Francingues-Gaillard M.-C.,
RA Franco L., Frontali L., Fukuhara H., Fuller L.J., Galland P., Gent M.E.,
RA Gigot D., Gilliquet V., Glansdorff N., Goffeau A., Grenson M., Grisanti P.,
RA Grivell L.A., de Haan M., Haasemann M., Hatat D., Hoenicka J.,
RA Hegemann J.H., Herbert C.J., Hilger F., Hohmann S., Hollenberg C.P.,
RA Huse K., Iborra F., Indge K.J., Isono K., Jacq C., Jacquet M., James C.M.,
RA Jauniaux J.-C., Jia Y., Jimenez A., Kelly A., Kleinhans U., Kreisl P.,
RA Lanfranchi G., Lewis C., van der Linden C.G., Lucchini G.,
RA Lutzenkirchen K., Maat M.J., Mallet L., Mannhaupt G., Martegani E.,
RA Mathieu A., Maurer C.T.C., McConnell D., McKee R.A., Messenguy F.,
RA Mewes H.-W., Molemans F., Montague M.A., Muzi Falconi M., Navas L.,
RA Newlon C.S., Noone D., Pallier C., Panzeri L., Pearson B.M., Perea J.,
RA Philippsen P., Pierard A., Planta R.J., Plevani P., Poetsch B., Pohl F.M.,
RA Purnelle B., Ramezani Rad M., Rasmussen S.W., Raynal A., Remacha M.A.,
RA Richterich P., Roberts A.B., Rodriguez F., Sanz E.,
RA Schaaff-Gerstenschlaeger I., Scherens B., Schweitzer B., Shu Y., Skala J.,
RA Slonimski P.P., Sor F., Soustelle C., Spiegelberg R., Stateva L.I.,
RA Steensma H.Y., Steiner S., Thierry A., Thireos G., Tzermia M.,
RA Urrestarazu L.A., Valle G., Vetter I., van Vliet-Reedijk J.C., Voet M.,
RA Volckaert G., Vreken P., Wang H., Warmington J.R., von Wettstein D.,
RA Wicksteed B.L., Wilson C., Wurst H., Xu G., Yoshikawa A., Zimmermann F.K.,
RA Sgouros J.G.;
RT "The complete DNA sequence of yeast chromosome III.";
RL Nature 357:38-46(1992).
RN [2]
RP SEQUENCE REVISION TO 191-192; 194-197; 316 AND C-TERMINUS.
RA Valles G., Volckaerts G.;
RL Submitted (JUN-2001) to the EMBL/GenBank/DDBJ databases.
RN [3]
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 [4]
RP CHARACTERIZATION, AND IDENTIFICATION OF FRAMESHIFT.
RX PubMed=9573211; DOI=10.1128/jb.180.9.2556-2559.1998;
RA Schreve J.L., Sin J.K., Garrett J.M.;
RT "The Saccharomyces cerevisiae YCC5 (YCL025c) gene encodes an amino acid
RT permease, Agp1, which transports asparagine and glutamine.";
RL J. Bacteriol. 180:2556-2559(1998).
RN [5]
RP FUNCTION IN L-CYSTEINE UPTAKE.
RX PubMed=10467005; DOI=10.1007/s002940050459;
RA During-Olsen L., Regenberg B., Gjermansen C., Kielland-Brandt M.C.,
RA Hansen J.;
RT "Cysteine uptake by Saccharomyces cerevisiae is accomplished by multiple
RT permeases.";
RL Curr. Genet. 35:609-617(1999).
RN [6]
RP FUNCTION.
RX PubMed=10654085; DOI=10.1007/s002940050506;
RA Regenberg B., During-Olsen L., Kielland-Brandt M.C., Holmberg S.;
RT "Substrate specificity and gene expression of the amino-acid permeases in
RT Saccharomyces cerevisiae.";
RL Curr. Genet. 36:317-328(1999).
RN [7]
RP INDUCTION.
RX PubMed=9891035; DOI=10.1128/mcb.19.2.989;
RA Iraqui I., Vissers S., Bernard F., de Craene J.-O., Boles E.,
RA Urrestarazu A., Andre B.;
RT "Amino acid signaling in Saccharomyces cerevisiae: a permease-like sensor
RT of external amino acids and F-Box protein Grr1p are required for
RT transcriptional induction of the AGP1 gene, which encodes a broad-
RT specificity amino acid permease.";
RL Mol. Cell. Biol. 19:989-1001(1999).
RN [8]
RP INDUCTION BY SPS.
RX PubMed=11154269; DOI=10.1128/mcb.21.3.814-826.2001;
RA Forsberg H., Ljungdahl P.O.;
RT "Genetic and biochemical analysis of the yeast plasma membrane Ssy1p-Ptr3p-
RT Ssy5p sensor of extracellular amino acids.";
RL Mol. Cell. Biol. 21:814-826(2001).
RN [9]
RP IDENTIFICATION OF FRAMESHIFT.
RX PubMed=12844361; DOI=10.1186/gb-2003-4-7-r45;
RA Brachat S., Dietrich F.S., Voegeli S., Zhang Z., Stuart L., Lerch A.,
RA Gates K., Gaffney T.D., Philippsen P.;
RT "Reinvestigation of the Saccharomyces cerevisiae genome annotation by
RT comparison to the genome of a related fungus: Ashbya gossypii.";
RL Genome Biol. 4:R45.1-R45.13(2003).
RN [10]
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 [11]
RP BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=14697254; DOI=10.1016/j.bbrc.2003.11.172;
RA Schreve J.L., Garrett J.M.;
RT "Yeast Agp2p and Agp3p function as amino acid permeases in poor nutrient
RT conditions.";
RL Biochem. Biophys. Res. Commun. 313:745-751(2004).
RN [12]
RP INDUCTION BY DAL81 AND STP1.
RX PubMed=15126393; DOI=10.1534/genetics.166.4.1727;
RA Abdel-Sater F., Iraqui I., Urrestarazu A., Andre B.;
RT "The external amino acid signaling pathway promotes activation of Stp1 and
RT Uga35/Dal81 transcription factors for induction of the AGP1 gene in
RT Saccharomyces cerevisiae.";
RL Genetics 166:1727-1739(2004).
RN [13]
RP PALMITOYLATION.
RX PubMed=16751107; DOI=10.1016/j.cell.2006.03.042;
RA Roth A.F., Wan J., Bailey A.O., Sun B., Kuchar J.A., Green W.N.,
RA Phinney B.S., Yates J.R. III, Davis N.G.;
RT "Global analysis of protein palmitoylation in yeast.";
RL Cell 125:1003-1013(2006).
RN [14]
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 [15]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=18407956; DOI=10.1074/mcp.m700468-mcp200;
RA Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
RT "A multidimensional chromatography technology for in-depth phosphoproteome
RT analysis.";
RL Mol. Cell. Proteomics 7:1389-1396(2008).
RN [16]
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).
CC -!- FUNCTION: Broad substrate range permease which transports asparagine
CC and glutamine with intermediate specificity. Also transports Ala, Cys,
CC Gly, Ile, Leu, Met, Phe, Ser, Thr, Tyr and Val. Important for the
CC utilization of amino acids as a nitrogen source.
CC {ECO:0000269|PubMed:10467005, ECO:0000269|PubMed:10654085}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.23 mM for leucine {ECO:0000269|PubMed:14697254};
CC Vmax=2.6 nmol/min/mg enzyme for leucine transport
CC {ECO:0000269|PubMed:14697254};
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Multi-pass membrane
CC protein {ECO:0000250}.
CC -!- INDUCTION: Induced by transcription factors DAL81 and STP1, which are
CC activated by a signal initiated by the plasma membrane SPS (SSY1-PTR3-
CC SSY5) amino acid sensor system in response to external amino acid
CC levels. {ECO:0000269|PubMed:11154269, ECO:0000269|PubMed:15126393,
CC ECO:0000269|PubMed:9891035}.
CC -!- PTM: Palmitoylated by PFA4. {ECO:0000269|PubMed:16751107}.
CC -!- MISCELLANEOUS: Present with 21100 molecules/cell in log phase SD
CC medium. {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the amino acid-polyamine-organocation (APC)
CC superfamily. YAT (TC 2.A.3.10) family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAA42360.2; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; X59720; CAA42360.2; ALT_FRAME; Genomic_DNA.
DR EMBL; BK006937; DAA07460.1; -; Genomic_DNA.
DR PIR; S19352; S19352.
DR RefSeq; NP_009905.3; NM_001178671.1.
DR AlphaFoldDB; P25376; -.
DR SMR; P25376; -.
DR BioGRID; 30959; 279.
DR DIP; DIP-4973N; -.
DR IntAct; P25376; 40.
DR MINT; P25376; -.
DR STRING; 4932.YCL025C; -.
DR BindingDB; P25376; -.
DR ChEMBL; CHEMBL1741178; -.
DR TCDB; 2.A.3.10.7; the amino acid-polyamine-organocation (apc) family.
DR iPTMnet; P25376; -.
DR SwissPalm; P25376; -.
DR MaxQB; P25376; -.
DR PaxDb; P25376; -.
DR PRIDE; P25376; -.
DR EnsemblFungi; YCL025C_mRNA; YCL025C; YCL025C.
DR GeneID; 850333; -.
DR KEGG; sce:YCL025C; -.
DR SGD; S000000530; AGP1.
DR VEuPathDB; FungiDB:YCL025C; -.
DR eggNOG; KOG1286; Eukaryota.
DR GeneTree; ENSGT00940000176482; -.
DR HOGENOM; CLU_007946_12_0_1; -.
DR InParanoid; P25376; -.
DR OMA; VITINIF; -.
DR BioCyc; YEAST:G3O-29287-MON; -.
DR SABIO-RK; P25376; -.
DR PRO; PR:P25376; -.
DR Proteomes; UP000002311; Chromosome III.
DR RNAct; P25376; protein.
DR GO; GO:0005783; C:endoplasmic reticulum; HDA:SGD.
DR GO; GO:0016021; C:integral component of membrane; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; IDA:SGD.
DR GO; GO:0015171; F:amino acid transmembrane transporter activity; IDA:SGD.
DR GO; GO:0015192; F:L-phenylalanine transmembrane transporter activity; IMP:CACAO.
DR GO; GO:0015193; F:L-proline transmembrane transporter activity; IGI:SGD.
DR GO; GO:0003333; P:amino acid transmembrane transport; IBA:GO_Central.
DR GO; GO:0006865; P:amino acid transport; IDA:SGD.
DR GO; GO:0098718; P:serine import across plasma membrane; IMP:SGD.
DR GO; GO:0055085; P:transmembrane transport; IDA:SGD.
DR InterPro; IPR004841; AA-permease/SLC12A_dom.
DR InterPro; IPR004762; Amino_acid_permease_fungi.
DR InterPro; IPR004840; Amoino_acid_permease_CS.
DR Pfam; PF00324; AA_permease; 1.
DR TIGRFAMs; TIGR00913; 2A0310; 1.
DR PROSITE; PS00218; AMINO_ACID_PERMEASE_1; 1.
PE 1: Evidence at protein level;
KW Amino-acid transport; Cell membrane; Isopeptide bond; Lipoprotein;
KW Membrane; Palmitate; Phosphoprotein; Reference proteome; Transmembrane;
KW Transmembrane helix; Transport; Ubl conjugation.
FT CHAIN 1..633
FT /note="General amino acid permease AGP1"
FT /id="PRO_0000054142"
FT TOPO_DOM 1..124
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 125..145
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 146..148
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 149..169
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 170..197
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 198..218
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 219..231
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 232..252
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 253..260
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 261..281
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 282..313
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 314..334
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 335..352
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 353..373
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 374..402
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 403..425
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 426..452
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 453..473
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 474..477
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 478..498
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 499..531
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 532..552
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 553..560
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 561..581
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 582..633
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 32..52
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 86..116
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 32..50
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 86..115
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 6
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P48813"
FT LIPID 633
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000250"
FT CROSSLNK 11
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000250|UniProtKB:P48813"
SQ SEQUENCE 633 AA; 69671 MW; 8E19A836C2F6C50F CRC64;
MSSSKSLYEL KDLKNSSTEI HATGQDNEIE YFETGSNDRP SSQPHLGYEQ HNTSAVRRFF
DSFKRADQGP QDEVEATQMN DLTSAISPSS RQAQELEKNE SSDNIGANTG HKSDSLKKTI
QPRHVLMIAL GTGIGTGLLV GNGTALVHAG PAGLLIGYAI MGSILYCIIQ ACGEMALVYS
NLTGGYNAYP SFLVDDGFGF AVAWVYCLQW LCVCPLELVT ASMTIKYWTT SVNPDVFVII
FYVLVITINI FGARGYAEAE FFFNCCKILM MTGFFILGII IDVGGAGNDG FIGGKYWHDP
GAFNGKHAID RFKGVAATLV TAAFAFGGSE FIAITTAEQS NPRKAIPGAA KQMIYRILFL
FLATIILLGF LVPYNSDQLL GSTGGGTKAS PYVIAVASHG VRVVPHFINA VILLSVLSMA
NSSFYSSARL FLTLSEQGYA PKVFSYIDRA GRPLIAMGVS ALFAVIAFCA ASPKEEQVFT
WLLAISGLSQ LFTWTAICLS HLRFRRAMKV QGRSLGELGF KSQTGVWGSA YACIMMILIL
IAQFWVAIAP IGEGKLDAQA FFENYLAMPI LIALYVGYKV WHKDWKLFIR ADKIDLDSHR
QIFDEELIKQ EDEEYRERLR NGPYWKRVVA FWC
