AVT1_YEAST
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 03-AUG-2022, entry version 161.
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; P47082; -.
DR PRIDE; P47082; -.
DR EnsemblFungi; YJR001W_mRNA; YJR001W; YJR001W.
DR GeneID; 853457; -.
DR KEGG; sce:YJR001W; -.
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; KTFFQDG; -.
DR BioCyc; YEAST:G3O-31647-MON; -.
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 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:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0016020; C:membrane; IBA:GO_Central.
DR GO; GO:0015171; F:amino acid transmembrane transporter activity; IBA:GO_Central.
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 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
