AVT3C_ARATH
ID AVT3C_ARATH Reviewed; 436 AA.
AC Q9SVG0; Q8LAI4;
DT 27-MAY-2015, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 136.
DE RecName: Full=Amino acid transporter AVT3C {ECO:0000305};
DE Short=AtAvt3C {ECO:0000303|PubMed:27925655};
DE AltName: Full=Aromatic and neutral amino acid transporter-like protein 2 {ECO:0000305};
GN Name=AVT3C {ECO:0000303|PubMed:27925655};
GN OrderedLocusNames=At4g38250 {ECO:0000312|Araport:AT4G38250};
GN ORFNames=F22I13.20 {ECO:0000312|EMBL:CAB37481.1};
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10617198; DOI=10.1038/47134;
RA Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T.,
RA Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B.,
RA Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M.,
RA de Simone V., Obermaier B., Mache R., Mueller M., Kreis M., Delseny M.,
RA Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D.,
RA Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J.,
RA Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B.,
RA Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J.,
RA Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R.,
RA Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M.,
RA Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P.,
RA Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S.,
RA Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C.,
RA Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J.,
RA Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S.,
RA Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A.,
RA Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M.,
RA Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D.,
RA Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E.,
RA Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S.,
RA Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R.,
RA Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M.,
RA Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E.,
RA Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P.,
RA Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K.,
RA Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K.,
RA de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K.,
RA Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M.,
RA Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G.,
RA Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K.,
RA Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K.,
RA Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W.,
RA Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H.,
RA Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B.,
RA Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J.,
RA Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K.,
RA O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N.,
RA Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A.,
RA Martienssen R., McCombie W.R.;
RT "Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana.";
RL Nature 402:769-777(1999).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
RA Feldmann K.A.;
RT "Full-length cDNA from Arabidopsis thaliana.";
RL Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19376835; DOI=10.1104/pp.109.138677;
RA Reiland S., Messerli G., Baerenfaller K., Gerrits B., Endler A.,
RA Grossmann J., Gruissem W., Baginsky S.;
RT "Large-scale Arabidopsis phosphoproteome profiling reveals novel
RT chloroplast kinase substrates and phosphorylation networks.";
RL Plant Physiol. 150:889-903(2009).
RN [6]
RP GENE FAMILY, NOMENCLATURE, SUBCELLULAR LOCATION, FUNCTION, AND TISSUE
RP SPECIFICITY.
RX PubMed=27925655; DOI=10.1002/1873-3468.12507;
RA Fujiki Y., Teshima H., Kashiwao S., Kawano-Kawada M., Ohsumi Y.,
RA Kakinuma Y., Sekito T.;
RT "Functional identification of AtAVT3, a family of vacuolar amino acid
RT transporters, in Arabidopsis.";
RL FEBS Lett. 591:5-15(2017).
CC -!- FUNCTION: Translocates preferentially neutral amino acids from the
CC vacuole to the cytoplasm. {ECO:0000269|PubMed:27925655}.
CC -!- SUBCELLULAR LOCATION: Vacuole membrane {ECO:0000269|PubMed:27925655};
CC Multi-pass membrane protein {ECO:0000255}.
CC -!- TISSUE SPECIFICITY: Ubiquitous. {ECO:0000269|PubMed:27925655}.
CC -!- SIMILARITY: Belongs to the amino acid/polyamine transporter 2 family.
CC Amino acid/auxin permease (AAAP) (TC 2.A.18.8) subfamily.
CC {ECO:0000305}.
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DR EMBL; AL035539; CAB37481.1; -; Genomic_DNA.
DR EMBL; AL161593; CAB80490.1; -; Genomic_DNA.
DR EMBL; CP002687; AEE86905.1; -; Genomic_DNA.
DR EMBL; AY050451; AAK91466.1; -; mRNA.
DR EMBL; AY133541; AAM91371.1; -; mRNA.
DR EMBL; AY087791; AAM65327.1; -; mRNA.
DR PIR; T05653; T05653.
DR RefSeq; NP_195538.1; NM_119987.3.
DR AlphaFoldDB; Q9SVG0; -.
DR SMR; Q9SVG0; -.
DR IntAct; Q9SVG0; 4.
DR STRING; 3702.AT4G38250.1; -.
DR iPTMnet; Q9SVG0; -.
DR PaxDb; Q9SVG0; -.
DR PRIDE; Q9SVG0; -.
DR ProteomicsDB; 241019; -.
DR EnsemblPlants; AT4G38250.1; AT4G38250.1; AT4G38250.
DR GeneID; 829982; -.
DR Gramene; AT4G38250.1; AT4G38250.1; AT4G38250.
DR KEGG; ath:AT4G38250; -.
DR Araport; AT4G38250; -.
DR TAIR; locus:2121733; AT4G38250.
DR eggNOG; KOG1304; Eukaryota.
DR HOGENOM; CLU_009646_6_0_1; -.
DR InParanoid; Q9SVG0; -.
DR OMA; HELCRRY; -.
DR OrthoDB; 464614at2759; -.
DR PhylomeDB; Q9SVG0; -.
DR PRO; PR:Q9SVG0; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; Q9SVG0; differential.
DR Genevisible; Q9SVG0; AT.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005774; C:vacuolar membrane; IDA:UniProtKB.
DR GO; GO:0015179; F:L-amino acid transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0015175; F:neutral amino acid transmembrane transporter activity; IDA:UniProtKB.
DR GO; GO:0003333; P:amino acid transmembrane transport; IBA:GO_Central.
DR GO; GO:0015804; P:neutral amino acid transport; IDA:UniProtKB.
DR InterPro; IPR013057; AA_transpt_TM.
DR Pfam; PF01490; Aa_trans; 1.
PE 1: Evidence at protein level;
KW Amino-acid transport; Membrane; Reference proteome; Transmembrane;
KW Transmembrane helix; Transport; Vacuole.
FT CHAIN 1..436
FT /note="Amino acid transporter AVT3C"
FT /id="PRO_0000433107"
FT TOPO_DOM 1..38
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 39..59
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 60..65
FT /note="Vacuolar"
FT /evidence="ECO:0000305"
FT TRANSMEM 66..86
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 87..118
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 119..139
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 140..166
FT /note="Vacuolar"
FT /evidence="ECO:0000305"
FT TRANSMEM 167..187
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 188..195
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 196..216
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 217..228
FT /note="Vacuolar"
FT /evidence="ECO:0000305"
FT TRANSMEM 229..249
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 250..273
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 274..294
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 295..309
FT /note="Vacuolar"
FT /evidence="ECO:0000305"
FT TRANSMEM 310..330
FT /note="Helical; Name=8"
FT /evidence="ECO:0000255"
FT TOPO_DOM 331..352
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 353..373
FT /note="Helical; Name=9"
FT /evidence="ECO:0000255"
FT TOPO_DOM 374..376
FT /note="Vacuolar"
FT /evidence="ECO:0000305"
FT TRANSMEM 377..397
FT /note="Helical; Name=10"
FT /evidence="ECO:0000255"
FT TOPO_DOM 398..411
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 412..432
FT /note="Helical; Name=11"
FT /evidence="ECO:0000255"
FT TOPO_DOM 433..436
FT /note="Vacuolar"
FT /evidence="ECO:0000305"
FT REGION 1..21
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..15
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 24
FT /note="S -> T (in Ref. 4; AAM65327)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 436 AA; 47211 MW; B7DD03C23F1F3033 CRC64;
MGFQNEASSS SYTLKIPPPA REDSPLLGKG PPLSSQFKTF ANVFIAVVGA GVLGLPYAFK
RTGWLMGVLL LVSVSVLTHH CMMLLVYTRR KLDSFNAGIS KIGSFGDLGF AVCGSLGRIV
VDLFIILSQA GFCVGYLIFI GTTLANLSDP ESPTSLRHQF TRLGSEFLGV SSKSLYIWGC
FPFQLGLNSI KTLTHLAPLS IFADIVDLGA MAVVIVEDSM IILKQRPDVV AFGGMSLFLY
GMGVAVYSFE GVGMVLPLES EMKDKDKFGK VLALGMGFIS LIYIAFGILG YLAFGEDTMD
IITANLGAGL VSTVVQLGLC INLFFTFPLM MNPVFEIVER RFSRGMYSAW LRWVLVLAVT
LVALFVPNFA DFLSLVGSST CCVLGFVLPA LFHLLVFKEE MGWLQWSSDT AIVVLGVVLA
VSGTWSSLSE IFSVKV
