AGP1_SACU7
ID AGP1_SACU7 Reviewed; 633 AA.
AC Q876K6;
DT 29-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 65.
DE RecName: Full=General amino acid permease AGP1;
DE AltName: Full=Asparagine/glutamine permease;
GN Name=AGP1;
OS Saccharomyces uvarum (strain ATCC 76518 / CBS 7001 / CLIB 283 / NBRC 10550
OS / MCYC 623 / NCYC 2669 / NRRL Y-11845) (Yeast) (Saccharomyces bayanus var.
OS uvarum).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=659244;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=623-6C / CBS 9787 / CLIB 533;
RX PubMed=12594514; DOI=10.1038/nature01419;
RA Langkjaer R.B., Cliften P.F., Johnston M., Piskur J.;
RT "Yeast genome duplication was followed by asynchronous differentiation of
RT duplicated genes.";
RL Nature 421:848-852(2003).
CC -!- FUNCTION: Broad substrate range permease which transports asparagine
CC and glutamine with intermediate specificity. Also transports Ala, Cys,
CC Gly, Ser, Thr, Cys, Met, Phe, Tyr, Ile, Leu 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 -!- 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; AY144805; AAO32369.1; -; Genomic_DNA.
DR AlphaFoldDB; Q876K6; -.
DR SMR; Q876K6; -.
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; Lipoprotein; Membrane; Palmitate;
KW Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..633
FT /note="General amino acid permease AGP1"
FT /id="PRO_0000330041"
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..52
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 81..116
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 14..52
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 92..116
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT LIPID 633
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000250"
SQ SEQUENCE 633 AA; 70083 MW; 7B40E6095951AAB0 CRC64;
MSSSTSPYEL KDLKNSSTEV HAAEQENEIE YFETDSNDRP SQQPHLDYEQ HNTSAVRRFL
DSFKRADQDQ EQEAEVAQMN DLTSAISPSS RQAHELEKDE TTDKIAPHTG HKSDSLKKTI
QPRHVLMIAL GTGIGTGLLV GNGTALVHAG PAGLLIGYAI MGSILYCIIQ ACGEMALVYS
NLTGGYNAYP SFLVDDGFGF AVAWVYCLQW LCVCPLELVT ASMTIKYWTT SVNPDVFVII
FYVLVITINI FGARGYAEAE FFFNCCKILM MTGFFILGII IDVGGAGNDG YIGGKYWHEP
GAFNGVHAID RFKGVVATLV TAAFAFGGSE FIAITTAEQS NPRKAIPGAA KQMIYRILFL
FLATIIIVGF LVPYNSDQLL GSSGGGTKAS PYVIAIASHG VRVAPHFVNA VILLSVLSMA
NSSFYSSARL FLTLSEQGYA PKIFSYIDRA GRPLIAMCVS ALFAVIAFCA ASPKEDQVFT
WLLAISGLSQ LFTWTAICLS HIRFRRAMKV QGRSLGELGF KSQTGVWGSI YSCIMMILIL
IGQFWVAIAP IGEGKLDAQA FFENYLAMPI LIVLYVGYKM WNKDWKLFIR ADKIDLTSHR
QIFDEELIKQ EDDEYRERLR TGPYWRRVLA FWC
