ID   AVT3_YEAST              Reviewed;         692 AA.
AC   P36062; D6VX50;
DT   01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-1994, sequence version 1.
DT   27-MAR-2024, entry version 165.
DE   RecName: Full=Vacuolar amino acid transporter 3;
GN   Name=AVT3; OrderedLocusNames=YKL146W; ORFNames=YKL600;
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 204508 / S288c;
RX   PubMed=8091859; DOI=10.1002/yea.320100005;
RA   Vandenbol M., Bolle P.-A., Dion C., Portetelle D., Hilger F.;
RT   "DNA sequencing of a 36.2 kb fragment located between the FAS1 and LAP loci
RT   of chromosome XI of Saccharomyces cerevisiae.";
RL   Yeast 10:S35-S40(1994).
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   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   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-59, AND IDENTIFICATION BY
RP   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   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-121 AND SER-165, 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   [7]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-119 AND SER-121, 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).
RN   [8]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA   Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA   Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA   Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT   "N-terminal acetylome analyses and functional insights of the N-terminal
RT   acetyltransferase NatB.";
RL   Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
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   -!- INTERACTION:
CC       P36062; P32568: SNQ2; NbExp=2; IntAct=EBI-20799445, EBI-17590;
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; Z26877; CAA81508.1; -; Genomic_DNA.
DR   EMBL; Z28146; CAA81988.1; -; Genomic_DNA.
DR   EMBL; BK006944; DAA09016.1; -; Genomic_DNA.
DR   PIR; S37976; S37976.
DR   RefSeq; NP_012776.1; NM_001179712.1.
DR   AlphaFoldDB; P36062; -.
DR   SMR; P36062; -.
DR   BioGRID; 33990; 96.
DR   DIP; DIP-4105N; -.
DR   IntAct; P36062; 1.
DR   MINT; P36062; -.
DR   STRING; 4932.YKL146W; -.
DR   TCDB; 2.A.18.7.1; the amino acid/auxin permease (aaap) family.
DR   iPTMnet; P36062; -.
DR   MaxQB; P36062; -.
DR   PaxDb; 4932-YKL146W; -.
DR   PeptideAtlas; P36062; -.
DR   EnsemblFungi; YKL146W_mRNA; YKL146W; YKL146W.
DR   GeneID; 853710; -.
DR   KEGG; sce:YKL146W; -.
DR   AGR; SGD:S000001629; -.
DR   SGD; S000001629; AVT3.
DR   VEuPathDB; FungiDB:YKL146W; -.
DR   eggNOG; KOG1304; Eukaryota.
DR   HOGENOM; CLU_009646_3_2_1; -.
DR   InParanoid; P36062; -.
DR   OMA; QESMKQP; -.
DR   OrthoDB; 3601817at2759; -.
DR   BioCyc; YEAST:G3O-31921-MONOMER; -.
DR   BioGRID-ORCS; 853710; 1 hit in 10 CRISPR screens.
DR   PRO; PR:P36062; -.
DR   Proteomes; UP000002311; Chromosome XI.
DR   RNAct; P36062; 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:0005774; C:vacuolar membrane; 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   GO; GO:0015824; P:proline transport; IMP:SGD.
DR   InterPro; IPR013057; AA_transpt_TM.
DR   PANTHER; PTHR22950; AMINO ACID TRANSPORTER; 1.
DR   PANTHER; PTHR22950:SF666; VACUOLAR AMINO ACID TRANSPORTER 3; 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..692
FT                   /note="Vacuolar amino acid transporter 3"
FT                   /id="PRO_0000093836"
FT   TRANSMEM        302..322
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        329..349
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        374..394
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        412..432
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        443..463
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        483..503
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        519..539
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        561..581
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        607..627
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        630..650
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        665..685
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   REGION          1..71
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          135..170
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          258..294
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..62
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        136..170
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        258..279
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         59
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:17330950"
FT   MOD_RES         119
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:19779198"
FT   MOD_RES         121
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:18407956,
FT                   ECO:0007744|PubMed:19779198"
FT   MOD_RES         165
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:18407956"
SQ   SEQUENCE   692 AA;  75459 MW;  379054D69094A0F5 CRC64;
     MNGKEVSSGS GRTQSNNNKK NNNGGSTGIS HASGSPLTDG NGGNSNGNSR SRSRSRKSSG
     TTGGLLKKPP LLVNNEAVHA SVPDASHTSC NNGTLEVSIN NPEPHVVDAV ARHLIRNPSN
     SLQLQGGDIT RDLYKWTNDH PSSPSQYQYP SQPALSTSIP SQAPSFSNRK RSMSFSAASI
     ASSSHLNNNS EANGNPLAAI GLAPAPMTHE EIRAPGGFRR SFIIQKRRKH NVDAPIPNFF
     TRNFIEFLTL YGHFAGEDLS EEEEEEEETE EEPEEEALET ESTQLVSREH GRHPHKSSTV
     KAVLLLLKSF VGTGVLFLPK AFHNGGWGFS ALCLLSCALI SYGCFVSLIT TKDKVGVDGY
     GDMGRILYGP KMKFAILSSI ALSQIGFSAA YTVFTATNLQ VFSENFFHLK PGSISLATYI
     FAQVLIFVPL SLTRNIAKLS GTALIADLFI LLGLVYVYVY SIYYIAVNGV ASDTMLMFNK
     ADWSLFIGTA IFTFEGIGLL IPIQESMKHP KHFRPSLSAV MCIVAVIFIS CGLLCYAAFG
     SDVKTVVLLN FPQDTSYTLT VQLLYALAIL LSTPLQLFPA IRILENWTFP SNASGKYNPK
     VKWLKNYFRC AIVVLTSILA WVGANDLDKF VSLVGSFACI PLIYIYPPLL HYKASILSGT
     SRARLLLDLI VIVFGVAVMA YTSWQTIKMW SQ
//