AVT3_YEAST
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 03-AUG-2022, entry version 159.
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; 89.
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; P36062; -.
DR PRIDE; P36062; -.
DR EnsemblFungi; YKL146W_mRNA; YKL146W; YKL146W.
DR GeneID; 853710; -.
DR KEGG; sce:YKL146W; -.
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 BioCyc; YEAST:G3O-31921-MON; -.
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:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005774; C:vacuolar membrane; IBA:GO_Central.
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 GO; GO:0015824; P:proline 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..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
