AVT6_YEAST
ID AVT6_YEAST Reviewed; 448 AA.
AC P40074; D3DM25;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1995, sequence version 1.
DT 03-AUG-2022, entry version 159.
DE RecName: Full=Vacuolar amino acid transporter 6;
GN Name=AVT6; OrderedLocusNames=YER119C;
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=9169868;
RA Dietrich F.S., Mulligan J.T., Hennessy K.M., Yelton M.A., Allen E.,
RA Araujo R., Aviles E., Berno A., Brennan T., Carpenter J., Chen E.,
RA Cherry J.M., Chung E., Duncan M., Guzman E., Hartzell G., Hunicke-Smith S.,
RA Hyman R.W., Kayser A., Komp C., Lashkari D., Lew H., Lin D., Mosedale D.,
RA Nakahara K., Namath A., Norgren R., Oefner P., Oh C., Petel F.X.,
RA Roberts D., Sehl P., Schramm S., Shogren T., Smith V., Taylor P., Wei Y.,
RA Botstein D., Davis R.W.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome V.";
RL Nature 387:78-81(1997).
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 NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 270-448.
RX PubMed=7668045; DOI=10.1002/yea.320110807;
RA Berroteran R.W., Hampsey M.;
RT "Sequence, map position and genome organization of the RPL17B gene,
RT encoding ribosomal protein L17b in Saccharomyces cerevisiae.";
RL Yeast 11:761-766(1995).
RN [4]
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 [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 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 [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-344, AND IDENTIFICATION BY
RP 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: Involved in amino acid efflux from the vacuole to the
CC cytoplasm. Capable of transporting aspartate and glutamate. Requires
CC 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 -!- SIMILARITY: Belongs to the amino acid/polyamine transporter 2 family.
CC {ECO:0000305}.
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DR EMBL; U18916; AAC03217.1; -; Genomic_DNA.
DR EMBL; U15653; AAA61905.1; -; Genomic_DNA.
DR EMBL; BK006939; DAA07779.1; -; Genomic_DNA.
DR PIR; S50622; S50622.
DR RefSeq; NP_011044.1; NM_001179009.1.
DR AlphaFoldDB; P40074; -.
DR BioGRID; 36864; 57.
DR DIP; DIP-4489N; -.
DR IntAct; P40074; 1.
DR STRING; 4932.YER119C; -.
DR TCDB; 2.A.18.6.6; the amino acid/auxin permease (aaap) family.
DR iPTMnet; P40074; -.
DR PaxDb; P40074; -.
DR PRIDE; P40074; -.
DR EnsemblFungi; YER119C_mRNA; YER119C; YER119C.
DR GeneID; 856855; -.
DR KEGG; sce:YER119C; -.
DR SGD; S000000921; AVT6.
DR VEuPathDB; FungiDB:YER119C; -.
DR eggNOG; KOG1305; Eukaryota.
DR GeneTree; ENSGT00940000170090; -.
DR HOGENOM; CLU_009020_1_1_1; -.
DR InParanoid; P40074; -.
DR OMA; QFWITAF; -.
DR BioCyc; YEAST:G3O-30283-MON; -.
DR PRO; PR:P40074; -.
DR Proteomes; UP000002311; Chromosome V.
DR RNAct; P40074; protein.
DR GO; GO:0000324; C:fungal-type vacuole; IDA:SGD.
DR GO; GO:0000329; C:fungal-type vacuole membrane; IDA:SGD.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0015179; F:L-amino acid transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0061459; F:L-arginine transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0015183; F:L-aspartate transmembrane transporter activity; IMP:SGD.
DR GO; GO:0005313; F:L-glutamate transmembrane transporter activity; IMP:SGD.
DR GO; GO:0005290; F:L-histidine transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0015189; F:L-lysine transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0015194; F:L-serine transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0005302; F:L-tyrosine transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0032974; P:amino acid transmembrane export from vacuole; IMP:SGD.
DR GO; GO:0003333; P:amino acid transmembrane transport; IBA:GO_Central.
DR GO; GO:0055085; P:transmembrane 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..448
FT /note="Vacuolar amino acid transporter 6"
FT /id="PRO_0000093839"
FT TOPO_DOM 1..7
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 8..28
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 29..32
FT /note="Vacuolar"
FT /evidence="ECO:0000255"
FT TRANSMEM 33..53
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 54..80
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 81..101
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 102..125
FT /note="Vacuolar"
FT /evidence="ECO:0000255"
FT TRANSMEM 126..146
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 147..150
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 151..171
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 172..195
FT /note="Vacuolar"
FT /evidence="ECO:0000255"
FT TRANSMEM 196..216
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 217..229
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 230..250
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 251..267
FT /note="Vacuolar"
FT /evidence="ECO:0000255"
FT TRANSMEM 268..288
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 289..357
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 358..378
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 379..381
FT /note="Vacuolar"
FT /evidence="ECO:0000255"
FT TRANSMEM 382..402
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 403..424
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 425..445
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 446..448
FT /note="Vacuolar"
FT /evidence="ECO:0000255"
FT MOD_RES 344
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
SQ SEQUENCE 448 AA; 48840 MW; 77F4642429E7D1CF CRC64;
MVASIRSGVL TLLHTACGAG ILAMPYAFKP FGLIPGVIMI VLCGACAMQS LFIQARVAKY
VPQGRASFSA LTRLINPNLG IVFDLAIAIK CFGVGVSYMI VVGDLMPQIM SVWTRNAWLL
NRNVQISLIM LFFVAPLSFL KKLNSLRYAS MVAISSVAYL CVLVLLHYVA PSDEILRLKG
RISYLLPPQS HDLNVLNTLP IFVFAYTCHH NMFSIINEQR SSRFEHVMKI PLIAISLALI
LYIAIGCAGY LTFGDNIIGN IIMLYPQAVS STIGRIAIVL LVMLAFPLQC HPARASIHQI
LQHFAEENVS ISATSADEPT VATESSPLIR DSSLDLNEVI EEESIYQPKE TPLRGKSFIV
ITCSILVASY LVAISVSSLA RVLAIVGATG STSISFILPG LFGYKLIGTE HKTAVPLTTK
IFKYTGLLLF IWGLIIMITC LTAALKLN
