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General amino acid permease AGP1 (Asparagine/glutamine permease)

 AGP1_YEAST              Reviewed;         633 AA.
P25376; D6VQZ1;
01-MAY-1992, integrated into UniProtKB/Swiss-Prot.
29-APR-2008, sequence version 3.
18-SEP-2019, entry version 171.
RecName: Full=General amino acid permease AGP1;
AltName: Full=Asparagine/glutamine permease;
Name=AGP1; OrderedLocusNames=YCL025C; ORFNames=YCL25C;
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina;
Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Saccharomyces.
NCBI_TaxID=559292;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 204508 / S288c;
PubMed=1574125; DOI=10.1038/357038a0;
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.;
"The complete DNA sequence of yeast chromosome III.";
Nature 357:38-46(1992).
[2]
SEQUENCE REVISION TO 191-192; 194-197; 316 AND C-TERMINUS.
Valles G., Volckaerts G.;
Submitted (JUN-2001) to the EMBL/GenBank/DDBJ databases.
[3]
GENOME REANNOTATION.
STRAIN=ATCC 204508 / S288c;
PubMed=24374639; DOI=10.1534/g3.113.008995;
Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M.,
Cherry J.M.;
"The reference genome sequence of Saccharomyces cerevisiae: Then and
now.";
G3 (Bethesda) 4:389-398(2014).
[4]
CHARACTERIZATION, AND IDENTIFICATION OF FRAMESHIFT.
PubMed=9573211;
Schreve J.L., Sin J.K., Garrett J.M.;
"The Saccharomyces cerevisiae YCC5 (YCL025c) gene encodes an amino
acid permease, Agp1, which transports asparagine and glutamine.";
J. Bacteriol. 180:2556-2559(1998).
[5]
FUNCTION IN L-CYSTEINE UPTAKE.
PubMed=10467005; DOI=10.1007/s002940050459;
During-Olsen L., Regenberg B., Gjermansen C., Kielland-Brandt M.C.,
Hansen J.;
"Cysteine uptake by Saccharomyces cerevisiae is accomplished by
multiple permeases.";
Curr. Genet. 35:609-617(1999).
[6]
FUNCTION.
PubMed=10654085; DOI=10.1007/s002940050506;
Regenberg B., During-Olsen L., Kielland-Brandt M.C., Holmberg S.;
"Substrate specificity and gene expression of the amino-acid permeases
in Saccharomyces cerevisiae.";
Curr. Genet. 36:317-328(1999).
[7]
INDUCTION.
PubMed=9891035; DOI=10.1128/mcb.19.2.989;
Iraqui I., Vissers S., Bernard F., de Craene J.-O., Boles E.,
Urrestarazu A., Andre B.;
"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.";
Mol. Cell. Biol. 19:989-1001(1999).
[8]
INDUCTION BY SPS.
PubMed=11154269; DOI=10.1128/mcb.21.3.814-826.2001;
Forsberg H., Ljungdahl P.O.;
"Genetic and biochemical analysis of the yeast plasma membrane Ssy1p-
Ptr3p-Ssy5p sensor of extracellular amino acids.";
Mol. Cell. Biol. 21:814-826(2001).
[9]
IDENTIFICATION OF FRAMESHIFT.
PubMed=12844361; DOI=10.1186/gb-2003-4-7-r45;
Brachat S., Dietrich F.S., Voegeli S., Zhang Z., Stuart L., Lerch A.,
Gates K., Gaffney T.D., Philippsen P.;
"Reinvestigation of the Saccharomyces cerevisiae genome annotation by
comparison to the genome of a related fungus: Ashbya gossypii.";
Genome Biol. 4:R45.1-R45.13(2003).
[10]
LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
PubMed=14562106; DOI=10.1038/nature02046;
Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A.,
Dephoure N., O'Shea E.K., Weissman J.S.;
"Global analysis of protein expression in yeast.";
Nature 425:737-741(2003).
[11]
BIOPHYSICOCHEMICAL PROPERTIES.
PubMed=14697254; DOI=10.1016/j.bbrc.2003.11.172;
Schreve J.L., Garrett J.M.;
"Yeast Agp2p and Agp3p function as amino acid permeases in poor
nutrient conditions.";
Biochem. Biophys. Res. Commun. 313:745-751(2004).
[12]
INDUCTION BY DAL81 AND STP1.
PubMed=15126393; DOI=10.1534/genetics.166.4.1727;
Abdel-Sater F., Iraqui I., Urrestarazu A., Andre B.;
"The external amino acid signaling pathway promotes activation of Stp1
and Uga35/Dal81 transcription factors for induction of the AGP1 gene
in Saccharomyces cerevisiae.";
Genetics 166:1727-1739(2004).
[13]
PALMITOYLATION.
PubMed=16751107; DOI=10.1016/j.cell.2006.03.042;
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.;
"Global analysis of protein palmitoylation in yeast.";
Cell 125:1003-1013(2006).
[14]
TOPOLOGY [LARGE SCALE ANALYSIS].
STRAIN=ATCC 208353 / W303-1A;
PubMed=16847258; DOI=10.1073/pnas.0604075103;
Kim H., Melen K., Oesterberg M., von Heijne G.;
"A global topology map of the Saccharomyces cerevisiae membrane
proteome.";
Proc. Natl. Acad. Sci. U.S.A. 103:11142-11147(2006).
[15]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=18407956; DOI=10.1074/mcp.m700468-mcp200;
Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
"A multidimensional chromatography technology for in-depth
phosphoproteome analysis.";
Mol. Cell. Proteomics 7:1389-1396(2008).
[16]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19779198; DOI=10.1126/science.1172867;
Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.;
"Global analysis of Cdk1 substrate phosphorylation sites provides
insights into evolution.";
Science 325:1682-1686(2009).
-!- 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. {ECO:0000269|PubMed:10467005,
ECO:0000269|PubMed:10654085}.
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Kinetic parameters:
KM=0.23 mM for leucine {ECO:0000269|PubMed:14697254};
Vmax=2.6 nmol/min/mg enzyme for leucine transport
{ECO:0000269|PubMed:14697254};
-!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Multi-pass
membrane protein {ECO:0000250}.
-!- 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. {ECO:0000269|PubMed:11154269,
ECO:0000269|PubMed:15126393, ECO:0000269|PubMed:9891035}.
-!- PTM: Palmitoylated by PFA4. {ECO:0000269|PubMed:16751107}.
-!- MISCELLANEOUS: Present with 21100 molecules/cell in log phase SD
medium. {ECO:0000269|PubMed:14562106}.
-!- SIMILARITY: Belongs to the amino acid-polyamine-organocation (APC)
superfamily. YAT (TC 2.A.3.10) family. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=CAA42360.2; Type=Frameshift; Positions=591; Evidence={ECO:0000305};
-----------------------------------------------------------------------
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EMBL; X59720; CAA42360.2; ALT_FRAME; Genomic_DNA.
EMBL; BK006937; DAA07460.1; -; Genomic_DNA.
PIR; S19352; S19352.
RefSeq; NP_009905.3; NM_001178671.1.
BioGrid; 30959; 275.
DIP; DIP-4973N; -.
IntAct; P25376; 38.
MINT; P25376; -.
STRING; 4932.YCL025C; -.
BindingDB; P25376; -.
ChEMBL; CHEMBL1741178; -.
TCDB; 2.A.3.10.7; the amino acid-polyamine-organocation (apc) family.
iPTMnet; P25376; -.
SwissPalm; P25376; -.
MaxQB; P25376; -.
PaxDb; P25376; -.
PRIDE; P25376; -.
EnsemblFungi; YCL025C_mRNA; YCL025C; YCL025C.
GeneID; 850333; -.
KEGG; sce:YCL025C; -.
EuPathDB; FungiDB:YCL025C; -.
SGD; S000000530; AGP1.
HOGENOM; HOG000261848; -.
InParanoid; P25376; -.
KO; K16261; -.
OMA; QACGEMA; -.
BioCyc; YEAST:G3O-29287-MONOMER; -.
SABIO-RK; P25376; -.
PRO; PR:P25376; -.
Proteomes; UP000002311; Chromosome III.
GO; GO:0005783; C:endoplasmic reticulum; HDA:SGD.
GO; GO:0016021; C:integral component of membrane; IBA:GO_Central.
GO; GO:0005886; C:plasma membrane; IDA:SGD.
GO; GO:0015171; F:amino acid transmembrane transporter activity; IDA:SGD.
GO; GO:0015192; F:L-phenylalanine transmembrane transporter activity; IMP:CACAO.
GO; GO:0015193; F:L-proline transmembrane transporter activity; IGI:SGD.
GO; GO:0003333; P:amino acid transmembrane transport; IBA:GO_Central.
GO; GO:0006865; P:amino acid transport; IDA:SGD.
GO; GO:0055085; P:transmembrane transport; IDA:SGD.
InterPro; IPR004841; AA-permease/SLC12A_dom.
InterPro; IPR002293; AA/rel_permease1.
InterPro; IPR004762; Amino_acid_permease_fungi.
InterPro; IPR004840; Amoino_acid_permease_CS.
Pfam; PF00324; AA_permease; 1.
PIRSF; PIRSF006060; AA_transporter; 1.
TIGRFAMs; TIGR00913; 2A0310; 1.
PROSITE; PS00218; AMINO_ACID_PERMEASE_1; 1.
1: Evidence at protein level;
Amino-acid transport; Cell membrane; Complete proteome;
Isopeptide bond; Lipoprotein; Membrane; Palmitate; Phosphoprotein;
Reference proteome; Transmembrane; Transmembrane helix; Transport;
Ubl conjugation.
CHAIN 1 633 General amino acid permease AGP1.
/FTId=PRO_0000054142.
TOPO_DOM 1 124 Cytoplasmic. {ECO:0000255}.
TRANSMEM 125 145 Helical. {ECO:0000255}.
TOPO_DOM 146 148 Extracellular. {ECO:0000255}.
TRANSMEM 149 169 Helical. {ECO:0000255}.
TOPO_DOM 170 197 Cytoplasmic. {ECO:0000255}.
TRANSMEM 198 218 Helical. {ECO:0000255}.
TOPO_DOM 219 231 Extracellular. {ECO:0000255}.
TRANSMEM 232 252 Helical. {ECO:0000255}.
TOPO_DOM 253 260 Cytoplasmic. {ECO:0000255}.
TRANSMEM 261 281 Helical. {ECO:0000255}.
TOPO_DOM 282 313 Extracellular. {ECO:0000255}.
TRANSMEM 314 334 Helical. {ECO:0000255}.
TOPO_DOM 335 352 Cytoplasmic. {ECO:0000255}.
TRANSMEM 353 373 Helical. {ECO:0000255}.
TOPO_DOM 374 402 Extracellular. {ECO:0000255}.
TRANSMEM 403 425 Helical. {ECO:0000255}.
TOPO_DOM 426 452 Cytoplasmic. {ECO:0000255}.
TRANSMEM 453 473 Helical. {ECO:0000255}.
TOPO_DOM 474 477 Extracellular. {ECO:0000255}.
TRANSMEM 478 498 Helical. {ECO:0000255}.
TOPO_DOM 499 531 Cytoplasmic. {ECO:0000255}.
TRANSMEM 532 552 Helical. {ECO:0000255}.
TOPO_DOM 553 560 Extracellular. {ECO:0000255}.
TRANSMEM 561 581 Helical. {ECO:0000255}.
TOPO_DOM 582 633 Cytoplasmic. {ECO:0000255}.
MOD_RES 6 6 Phosphoserine.
{ECO:0000250|UniProtKB:P48813}.
LIPID 633 633 S-palmitoyl cysteine. {ECO:0000250}.
CROSSLNK 11 11 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in ubiquitin).
{ECO:0000250|UniProtKB:P48813}.
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


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WP1252: amino acid conjugation of benzoic acid
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WP891: amino acid conjugation of benzoic acid
WP1287: amino acid conjugation of benzoic acid
WP521: amino acid conjugation of benzoic acid
WP1621: Arginine and proline metabolism
WP1127: amino acid conjugation of benzoic acid
WP7: Sulfur Amino Acid biosynthesis
WP16: Fatty Acid Elongation, Unsaturated
WP25: Fatty Acid Beta Oxidation 3
WP789: Fatty Acid Biosynthesis
WP1718: Vitamin B6 metabolism
WP498: Mitochondrial LC-Fatty Acid Beta-Oxidation
WP1273: Folic Acid Network
WP1817: Fatty acid, triacylglycerol, and ketone body metabolism
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Bibliography :