AVT4_YEAST
ID AVT4_YEAST Reviewed; 713 AA.
AC P50944; D6W178;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 160.
DE RecName: Full=Vacuolar amino acid transporter 4;
GN Name=AVT4; OrderedLocusNames=YNL101W; ORFNames=N2185;
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].
RC STRAIN=ATCC 96604 / S288c / FY1679;
RX PubMed=8701612;
RX DOI=10.1002/(sici)1097-0061(19960330)12:4<403::aid-yea923>3.0.co;2-h;
RA Saiz J.E., Buitrago M.J., Soler A., del Rey F., Revuelta J.L.;
RT "The sequence of a 21.3 kb DNA fragment from the left arm of yeast
RT chromosome XIV reveals LEU4, MET4, POL1, RAS2, and six new open reading
RT frames.";
RL Yeast 12:403-409(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169873;
RA Philippsen P., Kleine K., Poehlmann R., Duesterhoeft A., Hamberg K.,
RA Hegemann J.H., Obermaier B., Urrestarazu L.A., Aert R., Albermann K.,
RA Altmann R., Andre B., Baladron V., Ballesta J.P.G., Becam A.-M.,
RA Beinhauer J.D., Boskovic J., Buitrago M.J., Bussereau F., Coster F.,
RA Crouzet M., D'Angelo M., Dal Pero F., De Antoni A., del Rey F., Doignon F.,
RA Domdey H., Dubois E., Fiedler T.A., Fleig U., Floeth M., Fritz C.,
RA Gaillardin C., Garcia-Cantalejo J.M., Glansdorff N., Goffeau A.,
RA Gueldener U., Herbert C.J., Heumann K., Heuss-Neitzel D., Hilbert H.,
RA Hinni K., Iraqui Houssaini I., Jacquet M., Jimenez A., Jonniaux J.-L.,
RA Karpfinger-Hartl L., Lanfranchi G., Lepingle A., Levesque H., Lyck R.,
RA Maftahi M., Mallet L., Maurer C.T.C., Messenguy F., Mewes H.-W., Moestl D.,
RA Nasr F., Nicaud J.-M., Niedenthal R.K., Pandolfo D., Pierard A.,
RA Piravandi E., Planta R.J., Pohl T.M., Purnelle B., Rebischung C.,
RA Remacha M.A., Revuelta J.L., Rinke M., Saiz J.E., Sartorello F.,
RA Scherens B., Sen-Gupta M., Soler-Mira A., Urbanus J.H.M., Valle G.,
RA Van Dyck L., Verhasselt P., Vierendeels F., Vissers S., Voet M.,
RA Volckaert G., Wach A., Wambutt R., Wedler H., Zollner A., Hani J.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XIV and its
RT evolutionary implications.";
RL Nature 387:93-98(1997).
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 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].
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-165, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=17287358; DOI=10.1073/pnas.0607084104;
RA Chi A., Huttenhower C., Geer L.Y., Coon J.J., Syka J.E.P., Bai D.L.,
RA Shabanowitz J., Burke D.J., Troyanskaya O.G., Hunt D.F.;
RT "Analysis of phosphorylation sites on proteins from Saccharomyces
RT cerevisiae by electron transfer dissociation (ETD) mass spectrometry.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:2193-2198(2007).
RN [8]
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 [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-88 AND SER-130, 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: Involved in amino acid efflux from the vacuole to the
CC cytoplasm. Capable of transporting large neutral amino acids including
CC tyrosine, glutamine, asparagine, isoleucine and leucine.
CC {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; Z50161; CAA90525.1; -; Genomic_DNA.
DR EMBL; Z71377; CAA95977.1; -; Genomic_DNA.
DR EMBL; BK006947; DAA10444.1; -; Genomic_DNA.
DR PIR; S58251; S58251.
DR RefSeq; NP_014298.1; NM_001182939.1.
DR AlphaFoldDB; P50944; -.
DR BioGRID; 35722; 58.
DR DIP; DIP-6754N; -.
DR IntAct; P50944; 2.
DR MINT; P50944; -.
DR STRING; 4932.YNL101W; -.
DR TCDB; 2.A.18.7.2; the amino acid/auxin permease (aaap) family.
DR iPTMnet; P50944; -.
DR PaxDb; P50944; -.
DR PRIDE; P50944; -.
DR EnsemblFungi; YNL101W_mRNA; YNL101W; YNL101W.
DR GeneID; 855622; -.
DR KEGG; sce:YNL101W; -.
DR SGD; S000005045; AVT4.
DR VEuPathDB; FungiDB:YNL101W; -.
DR eggNOG; KOG1304; Eukaryota.
DR GeneTree; ENSGT00940000169842; -.
DR HOGENOM; CLU_009646_3_2_1; -.
DR InParanoid; P50944; -.
DR OMA; YWCYYIL; -.
DR BioCyc; YEAST:G3O-33129-MON; -.
DR PRO; PR:P50944; -.
DR Proteomes; UP000002311; Chromosome XIV.
DR RNAct; P50944; 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:0005774; C:vacuolar membrane; IBA:GO_Central.
DR GO; GO:1990816; C:vacuole-mitochondrion membrane contact site; IDA:SGD.
DR GO; GO:0015179; F:L-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:0032974; P:amino acid transmembrane export from vacuole; IMP:SGD.
DR GO; GO:0003333; P:amino acid transmembrane transport; IBA:GO_Central.
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..713
FT /note="Vacuolar amino acid transporter 4"
FT /id="PRO_0000093837"
FT TOPO_DOM 1..242
FT /note="Vacuolar"
FT /evidence="ECO:0000255"
FT TRANSMEM 243..263
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 264..301
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 302..322
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 323..326
FT /note="Vacuolar"
FT /evidence="ECO:0000255"
FT TRANSMEM 327..347
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 348..373
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 374..394
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 395..410
FT /note="Vacuolar"
FT /evidence="ECO:0000255"
FT TRANSMEM 411..431
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 432..438
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 439..459
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 460..483
FT /note="Vacuolar"
FT /evidence="ECO:0000255"
FT TRANSMEM 484..504
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 505..515
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 516..536
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 537..561
FT /note="Vacuolar"
FT /evidence="ECO:0000255"
FT TRANSMEM 562..582
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 583..621
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 622..642
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 643..648
FT /note="Vacuolar"
FT /evidence="ECO:0000255"
FT TRANSMEM 649..669
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 670..692
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 693..711
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 712..713
FT /note="Vacuolar"
FT /evidence="ECO:0000255"
FT REGION 1..33
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 99..121
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 200..233
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 18..33
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 208..233
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 88
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 130
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 165
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17287358"
SQ SEQUENCE 713 AA; 80026 MW; EAB458A2FEB660FB CRC64;
MVTNNGDGEH LGIRRNGNLR HPSNNMKIPR RAQSTVLNSN PFYSRKYSMS TLTPRDICRS
VDSRVFVDMS SPNFQTLEDP HRDEIINSVR LNYLNSSKRS SVSHGNEAIP RVNPTKNSSA
STIAAANVDS DDDETNLSSA GGDITHDIYK LVKAEDPKRL RRPRSMENVT PKIEHHTKLS
SASGLNVPGG FRREFIVNKK RQEHQLNDSA SSDFTSHESD SINQSSPSSN QDIDKVPFLT
RNFLEFLYVF GHFAGESFED DFIPDSSNMM IRGEDERSAL LSRPDHMKVL PSAKGTTSTK
KVFLILLKSF IGTGVLFLPN AFHNGGLFFS VSMLAFFGIY SYWCYYILVQ AKSSCGVSSF
GDIGLKLYGP WMRIIILFSL VITQVGFSGA YMIFTAKNLQ AFLDNVFHVG VLPLSYLMVF
QTIIFIPLSF IRNISKLSLP SLLANFFIMA GLVIVIIFTA KRLFFDLMGT PAMGVVYGLN
ADRWTLFIGT AIFAFEGIGL IIPVQDSMRN PEKFPLVLAL VILTATILFI SIATLGYLAY
GSNVQTVILL NLPQSNIFVN LIQLFYSIAI MLSTPLQLFP AIKIIENKFF PKFTKIYVKH
DDLTTRVELR PNSGKLNWKI KWLKNFIRSI IVIIVVSIAY FGSDNLDKFV SVIGSLACIP
LVYIYPSMLH LRGNSLPETK GEFWRFKPML DTILIFFGIA SMLYTSYQSI FGV
