GAP1_YEAST
ID GAP1_YEAST Reviewed; 602 AA.
AC P19145; D6VXA2;
DT 01-NOV-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1994, sequence version 2.
DT 03-AUG-2022, entry version 192.
DE RecName: Full=General amino-acid permease GAP1 {ECO:0000303|PubMed:5474888};
GN Name=GAP1 {ECO:0000303|PubMed:5474888}; OrderedLocusNames=YKR039W;
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 [GENOMIC DNA], AND INDUCTION.
RX PubMed=2194797; DOI=10.1111/j.1432-1033.1990.tb15542.x;
RA Jauniaux J.-C., Grenson M.;
RT "GAP1, the general amino acid permease gene of Saccharomyces cerevisiae.
RT Nucleotide sequence, protein similarity with the other bakers yeast amino
RT acid permeases, and nitrogen catabolite repression.";
RL Eur. J. Biochem. 190:39-44(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=8196765; DOI=10.1038/369371a0;
RA Dujon B., Alexandraki D., Andre B., Ansorge W., Baladron V.,
RA Ballesta J.P.G., Banrevi A., Bolle P.-A., Bolotin-Fukuhara M., Bossier P.,
RA Bou G., Boyer J., Buitrago M.J., Cheret G., Colleaux L.,
RA Daignan-Fornier B., del Rey F., Dion C., Domdey H., Duesterhoeft A.,
RA Duesterhus S., Entian K.-D., Erfle H., Esteban P.F., Feldmann H.,
RA Fernandes L., Fobo G.M., Fritz C., Fukuhara H., Gabel C., Gaillon L.,
RA Garcia-Cantalejo J.M., Garcia-Ramirez J.J., Gent M.E., Ghazvini M.,
RA Goffeau A., Gonzalez A., Grothues D., Guerreiro P., Hegemann J.H.,
RA Hewitt N., Hilger F., Hollenberg C.P., Horaitis O., Indge K.J.,
RA Jacquier A., James C.M., Jauniaux J.-C., Jimenez A., Keuchel H.,
RA Kirchrath L., Kleine K., Koetter P., Legrain P., Liebl S., Louis E.J.,
RA Maia e Silva A., Marck C., Monnier A.-L., Moestl D., Mueller S.,
RA Obermaier B., Oliver S.G., Pallier C., Pascolo S., Pfeiffer F.,
RA Philippsen P., Planta R.J., Pohl F.M., Pohl T.M., Poehlmann R.,
RA Portetelle D., Purnelle B., Puzos V., Ramezani Rad M., Rasmussen S.W.,
RA Remacha M.A., Revuelta J.L., Richard G.-F., Rieger M.,
RA Rodrigues-Pousada C., Rose M., Rupp T., Santos M.A., Schwager C.,
RA Sensen C., Skala J., Soares H., Sor F., Stegemann J., Tettelin H.,
RA Thierry A., Tzermia M., Urrestarazu L.A., van Dyck L.,
RA van Vliet-Reedijk J.C., Valens M., Vandenbol M., Vilela C., Vissers S.,
RA von Wettstein D., Voss H., Wiemann S., Xu G., Zimmermann J., Haasemann M.,
RA Becker I., Mewes H.-W.;
RT "Complete DNA sequence of yeast chromosome XI.";
RL Nature 369:371-378(1994).
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 NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=17322287; DOI=10.1101/gr.6037607;
RA Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F.,
RA Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J.,
RA Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J.,
RA Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D.,
RA LaBaer J.;
RT "Approaching a complete repository of sequence-verified protein-encoding
RT clones for Saccharomyces cerevisiae.";
RL Genome Res. 17:536-543(2007).
RN [5]
RP FUNCTION.
RX PubMed=5474888; DOI=10.1128/jb.103.3.770-777.1970;
RA Grenson M., Hou C., Crabeel M.;
RT "Multiplicity of the amino acid permeases in Saccharomyces cerevisiae. IV.
RT Evidence for a general amino acid permease.";
RL J. Bacteriol. 103:770-777(1970).
RN [6]
RP FUNCTION, AND PHOSPHORYLATION.
RX PubMed=7798155; DOI=10.1128/jb.177.1.94-102.1995;
RA Stanbrough M., Magasanik B.;
RT "Transcriptional and posttranslational regulation of the general amino acid
RT permease of Saccharomyces cerevisiae.";
RL J. Bacteriol. 177:94-102(1995).
RN [7]
RP INDUCTION.
RX PubMed=8636059; DOI=10.1128/jb.178.8.2465-2468.1996;
RA Stanbrough M., Magasanik B.;
RT "Two transcription factors, Gln3p and Nil1p, use the same GATAAG sites to
RT activate the expression of GAP1 of Saccharomyces cerevisiae.";
RL J. Bacteriol. 178:2465-2468(1996).
RN [8]
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 [9]
RP FUNCTION IN BETA-ALANINE UPTAKE.
RX PubMed=10373490; DOI=10.1074/jbc.274.26.18747;
RA Stolz J., Sauer N.;
RT "The fenpropimorph resistance gene FEN2 from Saccharomyces cerevisiae
RT encodes a plasma membrane H+-pantothenate symporter.";
RL J. Biol. Chem. 274:18747-18752(1999).
RN [10]
RP UBIQUITINATION BY RSP5.
RX PubMed=9614172; DOI=10.1091/mbc.9.6.1253;
RA Springael J.Y., Andre B.;
RT "Nitrogen-regulated ubiquitination of the Gap1 permease of Saccharomyces
RT cerevisiae.";
RL Mol. Biol. Cell 9:1253-1263(1998).
RN [11]
RP UBIQUITINATION BY RSP5.
RX PubMed=10194416; DOI=10.1242/jcs.112.9.1375;
RA Springael J.-Y., Galan J.-M., Haguenauer-Tsapis R., Andre B.;
RT "NH4+-induced down-regulation of the Saccharomyces cerevisiae Gap1p
RT permease involves its ubiquitination with lysine-63-linked chains.";
RL J. Cell Sci. 112:1375-1383(1999).
RN [12]
RP FUNCTION.
RX PubMed=10953083;
RX DOI=10.1002/1097-0061(20000915)16:12<1111::aid-yea611>3.0.co;2-3;
RA Regenberg B., Hansen J.;
RT "GAP1, a novel selection and counter-selection marker for multiple gene
RT disruptions in Saccharomyces cerevisiae.";
RL Yeast 16:1111-1119(2000).
RN [13]
RP SUBCELLULAR LOCATION, AND UBIQUITINATION BY RSP5.
RX PubMed=11500494; DOI=10.1074/jbc.m102945200;
RA Soetens O., De Craene J.-O., Andre B.;
RT "Ubiquitin is required for sorting to the vacuole of the yeast general
RT amino acid permease, Gap1.";
RL J. Biol. Chem. 276:43949-43957(2001).
RN [14]
RP UBIQUITINATION BY RSP5, AND SUBCELLULAR LOCATION.
RX PubMed=11352928; DOI=10.1083/jcb.153.4.649;
RA Helliwell S.B., Losko S., Kaiser C.A.;
RT "Components of a ubiquitin ligase complex specify polyubiquitination and
RT intracellular trafficking of the general amino acid permease.";
RL J. Cell Biol. 153:649-662(2001).
RN [15]
RP SUBCELLULAR LOCATION.
RX PubMed=12499351; DOI=10.1083/jcb.200208074;
RA Malkus P., Jiang F., Schekman R.;
RT "Concentrative sorting of secretory cargo proteins into COPII-coated
RT vesicles.";
RL J. Cell Biol. 159:915-921(2002).
RN [16]
RP SUBCELLULAR LOCATION.
RX PubMed=12417748; DOI=10.1073/pnas.232591899;
RA Chen E.J., Kaiser C.A.;
RT "Amino acids regulate the intracellular trafficking of the general amino
RT acid permease of Saccharomycescerevisiae.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:14837-14842(2002).
RN [17]
RP UBIQUITINATION, AND SUBCELLULAR LOCATION.
RX PubMed=14523026; DOI=10.1074/jbc.m306953200;
RA Nikko E., Marini A.-M., Andre B.;
RT "Permease recycling and ubiquitination status reveal a particular role for
RT Bro1 in the multivesicular body pathway.";
RL J. Biol. Chem. 278:50732-50743(2003).
RN [18]
RP UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-76, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RC STRAIN=SUB592;
RX PubMed=12872131; DOI=10.1038/nbt849;
RA Peng J., Schwartz D., Elias J.E., Thoreen C.C., Cheng D., Marsischky G.,
RA Roelofs J., Finley D., Gygi S.P.;
RT "A proteomics approach to understanding protein ubiquitination.";
RL Nat. Biotechnol. 21:921-926(2003).
RN [19]
RP UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-76, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RX PubMed=14557538; DOI=10.1073/pnas.2135500100;
RA Hitchcock A.L., Auld K., Gygi S.P., Silver P.A.;
RT "A subset of membrane-associated proteins is ubiquitinated in response to
RT mutations in the endoplasmic reticulum degradation machinery.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:12735-12740(2003).
RN [20]
RP UBIQUITINATION, AND SUBCELLULAR LOCATION.
RX PubMed=15039776; DOI=10.1038/ncb1107;
RA Scott P.M., Bilodeau P.S., Zhdankina O., Winistorfer S.C., Hauglund M.J.,
RA Allaman M.M., Kearney W.R., Robertson A.D., Boman A.L., Piper R.C.;
RT "GGA proteins bind ubiquitin to facilitate sorting at the trans-Golgi
RT network.";
RL Nat. Cell Biol. 6:252-259(2004).
RN [21]
RP FUNCTION.
RX PubMed=14968425; DOI=10.1002/yea.1052;
RA Andreasson C., Neve E.P., Ljungdahl P.O.;
RT "Four permeases import proline and the toxic proline analogue azetidine-2-
RT carboxylate into yeast.";
RL Yeast 21:193-199(2004).
RN [22]
RP FUNCTION, SUBCELLULAR LOCATION, AND INDUCTION.
RX PubMed=15707981; DOI=10.1016/j.bbrc.2005.01.064;
RA Uemura T., Kashiwagi K., Igarashi K.;
RT "Uptake of putrescine and spermidine by Gap1p on the plasma membrane in
RT Saccharomyces cerevisiae.";
RL Biochem. Biophys. Res. Commun. 328:1028-1033(2005).
RN [23]
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 [24]
RP FUNCTION, SUBCELLULAR LOCATION, AND MUTAGENESIS OF ALA-297.
RX PubMed=21471002; DOI=10.1091/mbc.e10-10-0800;
RA Cain N.E., Kaiser C.A.;
RT "Transport activity-dependent intracellular sorting of the yeast general
RT amino acid permease.";
RL Mol. Biol. Cell 22:1919-1929(2011).
RN [25]
RP FUNCTION.
RX PubMed=22844449; DOI=10.1371/journal.pone.0041272;
RA Torbensen R., Moeller H.D., Gresham D., Alizadeh S., Ochmann D., Boles E.,
RA Regenberg B.;
RT "Amino acid transporter genes are essential for FLO11-dependent and FLO11-
RT independent biofilm formation and invasive growth in Saccharomyces
RT cerevisiae.";
RL PLoS ONE 7:E41272-E41272(2012).
CC -!- FUNCTION: General amino-acid permease involved in the uptake of all the
CC naturally occurring L-amino-acids, related compounds such as ornithine
CC and citrulline, some D-amino acids, toxic amino acid analogs such as
CC azetidine-2-carboxylate, and the polyamines putrescine and spermidine
CC (PubMed:5474888, PubMed:10467005, PubMed:10373490, PubMed:10953083,
CC PubMed:14968425, PubMed:15707981). Senses its transport substrates to
CC set an appropriate level of transporter activity at the cell surface
CC (PubMed:21471002). Required for FLO11 expression and invasive growth
CC (PubMed:22844449). {ECO:0000269|PubMed:10373490,
CC ECO:0000269|PubMed:10467005, ECO:0000269|PubMed:10953083,
CC ECO:0000269|PubMed:14968425, ECO:0000269|PubMed:15707981,
CC ECO:0000269|PubMed:21471002, ECO:0000269|PubMed:22844449,
CC ECO:0000269|PubMed:5474888}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:11352928,
CC ECO:0000269|PubMed:11500494, ECO:0000269|PubMed:12417748,
CC ECO:0000269|PubMed:12499351, ECO:0000269|PubMed:14523026,
CC ECO:0000269|PubMed:15039776, ECO:0000269|PubMed:15707981,
CC ECO:0000269|PubMed:21471002}; Multi-pass membrane protein
CC {ECO:0000255}. Endoplasmic reticulum membrane
CC {ECO:0000269|PubMed:15707981}; Multi-pass membrane protein
CC {ECO:0000255}. Note=Depending on nitrogen source, GAP1 is transported
CC to the plasma membrane, where it functions for amino acid uptake, or to
CC the vacuole, where it is degraded (PubMed:11500494, PubMed:11352928,
CC PubMed:12499351, PubMed:12417748, PubMed:14523026, PubMed:15039776,
CC PubMed:21471002). {ECO:0000269|PubMed:11352928,
CC ECO:0000269|PubMed:11500494, ECO:0000269|PubMed:12417748,
CC ECO:0000269|PubMed:12499351, ECO:0000269|PubMed:14523026,
CC ECO:0000269|PubMed:15039776, ECO:0000269|PubMed:21471002}.
CC -!- INDUCTION: Expression is repressed by ammonia (PubMed:2194797).
CC Expression is induced by polyamines (PubMed:15707981). Both GLN3 and
CC NIL1 bind the 5'-GATAAG-3' motif within the GAP1 promoter to activate
CC transcription (PubMed:8636059). {ECO:0000269|PubMed:15707981,
CC ECO:0000269|PubMed:2194797, ECO:0000269|PubMed:8636059}.
CC -!- PTM: Active permease is phosphorylated (PubMed:7798155). The addition
CC of glutamine causes rapid dephosphorylation and inactivation of the
CC permease (PubMed:7798155). {ECO:0000269|PubMed:7798155}.
CC -!- PTM: Ubiquitination by RSP5 and the RSP5-associated proteins BUL1 and
CC BUL2, leads the addition of poly-ubiquitin chains being specifically
CC formed by linkage through the lysine 63 residue of ubiquitin and
CC mediates ammonium-induced endocytosis and degradation in the vacuole
CC (PubMed:9614172, PubMed:10194416, PubMed:11500494, PubMed:11352928,
CC PubMed:14523026, PubMed:15039776). {ECO:0000269|PubMed:10194416,
CC ECO:0000269|PubMed:11352928, ECO:0000269|PubMed:11500494,
CC ECO:0000269|PubMed:14523026, ECO:0000269|PubMed:15039776,
CC ECO:0000269|PubMed:9614172}.
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; X52633; CAA36858.1; -; Genomic_DNA.
DR EMBL; Z28264; CAA82113.1; -; Genomic_DNA.
DR EMBL; AY723840; AAU09757.1; -; Genomic_DNA.
DR EMBL; BK006944; DAA09192.1; -; Genomic_DNA.
DR PIR; S38111; S38111.
DR RefSeq; NP_012965.3; NM_001179829.3.
DR AlphaFoldDB; P19145; -.
DR SMR; P19145; -.
DR BioGRID; 34171; 176.
DR DIP; DIP-8010N; -.
DR IntAct; P19145; 4.
DR MINT; P19145; -.
DR STRING; 4932.YKR039W; -.
DR BindingDB; P19145; -.
DR ChEMBL; CHEMBL3308953; -.
DR TCDB; 2.A.3.10.2; the amino acid-polyamine-organocation (apc) family.
DR iPTMnet; P19145; -.
DR SwissPalm; P19145; -.
DR MaxQB; P19145; -.
DR PaxDb; P19145; -.
DR PRIDE; P19145; -.
DR EnsemblFungi; YKR039W_mRNA; YKR039W; YKR039W.
DR GeneID; 853912; -.
DR KEGG; sce:YKR039W; -.
DR SGD; S000001747; GAP1.
DR VEuPathDB; FungiDB:YKR039W; -.
DR eggNOG; KOG1286; Eukaryota.
DR HOGENOM; CLU_007946_12_0_1; -.
DR InParanoid; P19145; -.
DR OMA; VIMYLTP; -.
DR BioCyc; YEAST:G3O-32011-MON; -.
DR SABIO-RK; P19145; -.
DR PRO; PR:P19145; -.
DR Proteomes; UP000002311; Chromosome XI.
DR RNAct; P19145; protein.
DR GO; GO:0030134; C:COPII-coated ER to Golgi transport vesicle; IDA:SGD.
DR GO; GO:0005783; C:endoplasmic reticulum; HDA:SGD.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005768; C:endosome; IDA:SGD.
DR GO; GO:0000328; C:fungal-type vacuole lumen; IDA:SGD.
DR GO; GO:0016021; C:integral component of membrane; IBA:GO_Central.
DR GO; GO:0005887; C:integral component of plasma membrane; IDA:SGD.
DR GO; GO:0005771; C:multivesicular body; IMP:SGD.
DR GO; GO:0005886; C:plasma membrane; IDA:SGD.
DR GO; GO:0015171; F:amino acid transmembrane transporter activity; IMP:SGD.
DR GO; GO:0001761; F:beta-alanine transmembrane transporter activity; IMP: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:0015203; F:polyamine transmembrane transporter activity; IMP:SGD.
DR GO; GO:0003333; P:amino acid transmembrane transport; IBA:GO_Central.
DR GO; GO:0006865; P:amino acid transport; IMP:SGD.
DR GO; GO:0015846; P:polyamine transport; IMP: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; Endoplasmic reticulum;
KW Isopeptide bond; Membrane; Reference proteome; Transmembrane;
KW Transmembrane helix; Transport; Ubl conjugation.
FT CHAIN 1..602
FT /note="General amino-acid permease GAP1"
FT /id="PRO_0000054151"
FT TOPO_DOM 1..95
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 96..116
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 117..121
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 122..142
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 143..165
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 166..185
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 186..204
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 205..224
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 225..237
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 238..256
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 257..280
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 281..298
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 299..321
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 322..342
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 343..376
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 377..396
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 397..421
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 422..442
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 443..451
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 452..472
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 473..491
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 492..510
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 511..529
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 530..548
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 549..602
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT CROSSLNK 76
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000269|PubMed:12872131,
FT ECO:0000269|PubMed:14557538"
FT MUTAGEN 297
FT /note="A->V: Impairs basic amino-acids transport and
FT regulation by these amino-acids."
FT /evidence="ECO:0000269|PubMed:21471002"
FT CONFLICT 122
FT /note="Missing (in Ref. 1; CAA36858)"
FT /evidence="ECO:0000305"
FT CONFLICT 189
FT /note="S -> A (in Ref. 1; CAA36858)"
FT /evidence="ECO:0000305"
FT CONFLICT 338
FT /note="I -> V (in Ref. 1; CAA36858)"
FT /evidence="ECO:0000305"
FT CONFLICT 518
FT /note="V -> L (in Ref. 1; CAA36858)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 602 AA; 65656 MW; 5363616447907458 CRC64;
MSNTSSYEKN NPDNLKHNGI TIDSEFLTQE PITIPSNGSA VSIDETGSGS KWQDFKDSFK
RVKPIEVDPN LSEAEKVAII TAQTPLKHHL KNRHLQMIAI GGAIGTGLLV GSGTALRTGG
PASLLIGWGS TGTMIYAMVM ALGELAVIFP ISGGFTTYAT RFIDESFGYA NNFNYMLQWL
VVLPLEIVSA SITVNFWGTD PKYRDGFVAL FWLAIVIINM FGVKGYGEAE FVFSFIKVIT
VVGFIILGII LNCGGGPTGG YIGGKYWHDP GAFAGDTPGA KFKGVCSVFV TAAFSFAGSE
LVGLAASESV EPRKSVPKAA KQVFWRITLF YILSLLMIGL LVPYNDKSLI GASSVDAAAS
PFVIAIKTHG IKGLPSVVNV VILIAVLSVG NSAIYACSRT MVALAEQRFL PEIFSYVDRK
GRPLVGIAVT SAFGLIAFVA ASKKEGEVFN WLLALSGLSS LFTWGGICIC HIRFRKALAA
QGRGLDELSF KSPTGVWGSY WGLFMVIIMF IAQFYVAVFP VGDSPSAEGF FEAYLSFPLV
MVMYIGHKIY KRNWKLFIPA EKMDIDTGRR EVDLDLLKQE IAEEKAIMAT KPRWYRIWNF
WC
