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 04-NOV-2026, entry version 200. 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}; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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; 287. DR DIP; DIP-4973N; -. DR FunCoup; P25376; 309. DR IntAct; P25376; 42. 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 PaxDb; 4932-YCL025C; -. DR PeptideAtlas; P25376; -. DR EnsemblFungi; YCL025C_mRNA; YCL025C; YCL025C. DR GeneID; 850333; -. DR KEGG; sce:YCL025C; -. DR AGR; SGD:S000000530; -. DR SGD; S000000530; AGP1. DR VEuPathDB; FungiDB:YCL025C; -. DR eggNOG; KOG1286; Eukaryota. DR HOGENOM; CLU_007946_12_0_1; -. DR InParanoid; P25376; -. DR OMA; AAIMMFM; -. DR OrthoDB; 3900342at2759; -. DR BioCyc; YEAST:G3O-29287-MONOMER; -. DR SABIO-RK; P25376; -. DR BioGRID-ORCS; 850333; 5 hits in 10 CRISPR screens. 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:0016020; C: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 FunFam; 1.20.1740.10:FF:000017; Amino acid permease; 1. DR Gene3D; 1.20.1740.10; Amino acid/polyamine transporter I; 1. DR InterPro; IPR004841; AA-permease/SLC12A_dom. DR InterPro; IPR004840; Amino_acid_permease_CS. DR InterPro; IPR004762; Amino_acid_permease_fungi. DR InterPro; IPR050524; APC_YAT. DR NCBIfam; TIGR00913; 2A0310; 1. DR PANTHER; PTHR43341; AMINO ACID PERMEASE; 1. DR PANTHER; PTHR43341:SF17; GENERAL AMINO ACID PERMEASE AGP1-RELATED; 1. DR Pfam; PF00324; AA_permease; 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 34..52 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 //