ID   AVT1_YEAST              Reviewed;         602 AA.
AC   P47082; D6VWH5;
DT   01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1996, sequence version 1.
DT   27-MAR-2024, entry version 167.
DE   RecName: Full=Vacuolar amino acid transporter 1;
GN   Name=AVT1; OrderedLocusNames=YJR001W; ORFNames=J1409, YJR83.4;
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=8641269; DOI=10.1002/j.1460-2075.1996.tb00557.x;
RA   Galibert F., Alexandraki D., Baur A., Boles E., Chalwatzis N., Chuat J.-C.,
RA   Coster F., Cziepluch C., de Haan M., Domdey H., Durand P., Entian K.-D.,
RA   Gatius M., Goffeau A., Grivell L.A., Hennemann A., Herbert C.J.,
RA   Heumann K., Hilger F., Hollenberg C.P., Huang M.-E., Jacq C.,
RA   Jauniaux J.-C., Katsoulou C., Kirchrath L., Kleine K., Kordes E.,
RA   Koetter P., Liebl S., Louis E.J., Manus V., Mewes H.-W., Miosga T.,
RA   Obermaier B., Perea J., Pohl T.M., Portetelle D., Pujol A., Purnelle B.,
RA   Ramezani Rad M., Rasmussen S.W., Rose M., Rossau R.,
RA   Schaaff-Gerstenschlaeger I., Smits P.H.M., Scarcez T., Soriano N.,
RA   To Van D., Tzermia M., Van Broekhoven A., Vandenbol M., Wedler H.,
RA   von Wettstein D., Wambutt R., Zagulski M., Zollner A., Karpfinger-Hartl L.;
RT   "Complete nucleotide sequence of Saccharomyces cerevisiae chromosome X.";
RL   EMBO J. 15:2031-2049(1996).
RN   [2]
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   [3]
RP   FUNCTION, AND SUBCELLULAR LOCATION.
RX   PubMed=11274162; DOI=10.1074/jbc.m008028200;
RA   Russnak R., Konczal D., McIntire S.L.;
RT   "A family of yeast proteins mediating bidirectional vacuolar amino acid
RT   transport.";
RL   J. Biol. Chem. 276:23849-23857(2001).
RN   [4]
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   [5]
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   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-181 AND SER-187, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   STRAIN=ADR376;
RX   PubMed=17330950; DOI=10.1021/pr060559j;
RA   Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J.,
RA   Elias J.E., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of alpha-factor-arrested
RT   Saccharomyces cerevisiae.";
RL   J. Proteome Res. 6:1190-1197(2007).
RN   [7]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-8 AND SER-35, AND
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   [8]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-15; THR-181 AND SER-187, AND
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: Required for the vacuolar uptake of large neutral amino acids
CC       including tyrosine, glutamine, asparagine, isoleucine and leucine.
CC       Requires ATP for function. {ECO:0000269|PubMed:11274162}.
CC   -!- SUBCELLULAR LOCATION: Vacuole membrane {ECO:0000269|PubMed:11274162};
CC       Multi-pass membrane protein {ECO:0000269|PubMed:11274162}.
CC   -!- MISCELLANEOUS: Present with 1820 molecules/cell in log phase SD medium.
CC       {ECO:0000269|PubMed:14562106}.
CC   -!- SIMILARITY: Belongs to the amino acid/polyamine transporter 2 family.
CC       {ECO:0000305}.
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DR   EMBL; X87611; CAA60922.1; -; Genomic_DNA.
DR   EMBL; Z49501; CAA89523.1; -; Genomic_DNA.
DR   EMBL; BK006943; DAA08791.1; -; Genomic_DNA.
DR   PIR; S55188; S55188.
DR   RefSeq; NP_012534.1; NM_001181658.1.
DR   AlphaFoldDB; P47082; -.
DR   BioGRID; 33757; 57.
DR   DIP; DIP-5709N; -.
DR   IntAct; P47082; 2.
DR   MINT; P47082; -.
DR   STRING; 4932.YJR001W; -.
DR   TCDB; 2.A.18.5.2; the amino acid/auxin permease (aaap) family.
DR   iPTMnet; P47082; -.
DR   MaxQB; P47082; -.
DR   PaxDb; 4932-YJR001W; -.
DR   PeptideAtlas; P47082; -.
DR   EnsemblFungi; YJR001W_mRNA; YJR001W; YJR001W.
DR   GeneID; 853457; -.
DR   KEGG; sce:YJR001W; -.
DR   AGR; SGD:S000003761; -.
DR   SGD; S000003761; AVT1.
DR   VEuPathDB; FungiDB:YJR001W; -.
DR   eggNOG; KOG1303; Eukaryota.
DR   GeneTree; ENSGT00730000111746; -.
DR   HOGENOM; CLU_009646_8_2_1; -.
DR   InParanoid; P47082; -.
DR   OMA; RSWMMLI; -.
DR   OrthoDB; 54659at2759; -.
DR   BioCyc; YEAST:G3O-31647-MONOMER; -.
DR   Reactome; R-SCE-425393; Transport of inorganic cations/anions and amino acids/oligopeptides.
DR   Reactome; R-SCE-888590; GABA synthesis, release, reuptake and degradation.
DR   BioGRID-ORCS; 853457; 3 hits in 10 CRISPR screens.
DR   PRO; PR:P47082; -.
DR   Proteomes; UP000002311; Chromosome X.
DR   RNAct; P47082; Protein.
DR   GO; GO:0000324; C:fungal-type vacuole; IDA:SGD.
DR   GO; GO:0000329; C:fungal-type vacuole membrane; IMP:SGD.
DR   GO; GO:0015186; F:L-glutamine transmembrane transporter activity; IMP:SGD.
DR   GO; GO:0015188; F:L-isoleucine transmembrane transporter activity; IMP:SGD.
DR   GO; GO:0005302; F:L-tyrosine transmembrane transporter activity; IMP:SGD.
DR   GO; GO:0003333; P:amino acid transmembrane transport; IMP:SGD.
DR   GO; GO:0006865; P:amino acid transport; IMP:SGD.
DR   GO; GO:0015824; P:proline transport; IMP:SGD.
DR   GO; GO:0007034; P:vacuolar transport; IMP:SGD.
DR   InterPro; IPR013057; AA_transpt_TM.
DR   PANTHER; PTHR48017:SF48; MAHOGANY; 1.
DR   PANTHER; PTHR48017; OS05G0424000 PROTEIN-RELATED; 1.
DR   Pfam; PF01490; Aa_trans; 1.
PE   1: Evidence at protein level;
KW   Amino-acid transport; Membrane; Phosphoprotein; Reference proteome;
KW   Transmembrane; Transmembrane helix; Transport; Vacuole.
FT   CHAIN           1..602
FT                   /note="Vacuolar amino acid transporter 1"
FT                   /id="PRO_0000093834"
FT   TOPO_DOM        1..208
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        209..231
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        232..240
FT                   /note="Vacuolar"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        241..261
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        262..286
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        287..307
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        308..321
FT                   /note="Vacuolar"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        322..342
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        343..344
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        345..365
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        366..389
FT                   /note="Vacuolar"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        390..410
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        411..429
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        430..450
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        451..466
FT                   /note="Vacuolar"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        467..487
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        488..517
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        518..538
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        539..543
FT                   /note="Vacuolar"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        544..564
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        565..580
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        581..601
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        602
FT                   /note="Vacuolar"
FT                   /evidence="ECO:0000255"
FT   MOD_RES         8
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:18407956"
FT   MOD_RES         15
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:19779198"
FT   MOD_RES         35
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:18407956"
FT   MOD_RES         181
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0007744|PubMed:17330950,
FT                   ECO:0007744|PubMed:19779198"
FT   MOD_RES         187
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:17330950,
FT                   ECO:0007744|PubMed:19779198"
SQ   SEQUENCE   602 AA;  65346 MW;  C2F321E76C21C2B4 CRC64;
     MPEQEPLSPN GRKRSEVHYI SIPLNRGSAF SPDDSVSQFQ SDGFMTRRQS ILDHPVGSFK
     GVNSLSRFAT SLRRANSFRN IELNADNERS FFKESNDETY DPDTLAPALD GRRLSVTLNN
     AGRPRITNLA NNDRVSTASM AIHDDDYGSI QNSTIGDSGS ILRPTASLTE MMSGGAGRRF
     TNNDMDSIVV KRVEGVDGKV VTLLAGQSTA PQTIFNSINV LIGIGLLALP LGLKYAGWVI
     GLTMLAIFAL ATFCTAELLS RCLDTDPTLI SYADLGYAAF GTKGRALISA LFTLDLLGSG
     VSLVILFGDS LNALFPQYST TFFKIVSFFI VTPPVFIPLS VLSNISLLGI LSTTGTVLVI
     CCCGLYKSSS PGSLVNPMET SMWPIDLKHL CLSIGLLSAC WGGHAVFPNL KTDMRHPDKF
     KDCLKTTYKI TSVTDIGTAV IGFLMFGNLV KDEITKNVLL TEGYPKFVYG LISALMTIIP
     IAKTPLNARP IVSVLDVLMN VQHIDEAASA IKRRAAKGLQ VFNRIFINVV FVLIAINFPE
     FDKIIAFLGA GLCFTICLIL PCWFYLRLCK TTIKPWERVA CHVTICISVV LSTLGVGAAI
     IS
//