AGP1_YEAS7
ID AGP1_YEAS7 Reviewed; 633 AA.
AC A6ZTG5;
DT 29-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 11-SEP-2007, sequence version 1.
DT 03-AUG-2022, entry version 60.
DE RecName: Full=General amino acid permease AGP1;
DE AltName: Full=Asparagine/glutamine permease;
GN Name=AGP1; ORFNames=SCY_0558;
OS Saccharomyces cerevisiae (strain YJM789) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=307796;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=YJM789;
RX PubMed=17652520; DOI=10.1073/pnas.0701291104;
RA Wei W., McCusker J.H., Hyman R.W., Jones T., Ning Y., Cao Z., Gu Z.,
RA Bruno D., Miranda M., Nguyen M., Wilhelmy J., Komp C., Tamse R., Wang X.,
RA Jia P., Luedi P., Oefner P.J., David L., Dietrich F.S., Li Y., Davis R.W.,
RA Steinmetz L.M.;
RT "Genome sequencing and comparative analysis of Saccharomyces cerevisiae
RT strain YJM789.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:12825-12830(2007).
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 (By similarity).
CC {ECO:0000250}.
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:0000250}.
CC -!- PTM: Palmitoylated by PFA4. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the amino acid-polyamine-organocation (APC)
CC superfamily. YAT (TC 2.A.3.10) family. {ECO:0000305}.
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DR EMBL; AAFW02000089; EDN62104.1; -; Genomic_DNA.
DR AlphaFoldDB; A6ZTG5; -.
DR SMR; A6ZTG5; -.
DR PRIDE; A6ZTG5; -.
DR EnsemblFungi; EDN62104; EDN62104; SCY_0558.
DR HOGENOM; CLU_007946_12_0_1; -.
DR Proteomes; UP000007060; Unassembled WGS sequence.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0022857; F:transmembrane transporter activity; IEA:UniProt.
DR GO; GO:0006865; P:amino acid transport; IEA:UniProtKB-KW.
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 3: Inferred from homology;
KW Amino-acid transport; Cell membrane; Isopeptide bond; Lipoprotein;
KW Membrane; Palmitate; Phosphoprotein; Transmembrane; Transmembrane helix;
KW Transport; Ubl conjugation.
FT CHAIN 1..633
FT /note="General amino acid permease AGP1"
FT /id="PRO_0000330042"
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..392
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 393..413
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 414..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..557
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 558..578
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 579..633
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 1..54
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 87..116
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 12..28
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 34..50
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 100..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; 69784 MW; EA04F90FD4B75E01 CRC64;
MSSSKSPYEL KDLKNSSTEI HATEQDNEIE YFETGSNDRP SSQPHLGYEQ HNTSAVRRFF
DSFKRADQGP QDEVEATQMN DLTSAISPSS RRAQELEKNE SSDNIGANTG HKSDSLKKTI
QPRHVLMIAL GTGIGTGLLV GNGTALVHAG PAGLLIGYAI MGSILYCIIQ ACGEMALVYS
NLTGGYNAYP SFLVDDGFGF AVAWVYCLQW LCVCPLELVT ASMTIKYWTT SVNPDVFVII
FYVLVITINI FGARGYAEAE FFFNCCKILM MTGFFILGII IDVGGAGNDG FIGGKYWHDP
GAFNGKHAID RFKGVVATLV 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
