ANT1_ARATH
ID ANT1_ARATH Reviewed; 432 AA.
AC Q9SF09; O24406;
DT 27-MAY-2015, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 130.
DE RecName: Full=Amino acid transporter ANT1 {ECO:0000305};
DE AltName: Full=Aromatic and neutral amino acid transporter 1 {ECO:0000303|PubMed:11299361};
GN Name=ANT1 {ECO:0000303|PubMed:11299361, ECO:0000303|PubMed:27925655};
GN OrderedLocusNames=At3g11900 {ECO:0000312|Araport:AT3G11900};
GN ORFNames=F26K24.19 {ECO:0000312|EMBL:AAF23206.1};
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 [MRNA].
RA Chen L., Bush D.R.;
RT "Arabidopsis thaliana amino acid transport protein mRNA.";
RL Submitted (OCT-1995) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130713; DOI=10.1038/35048706;
RA Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., Fartmann B.,
RA Valle G., Bloecker H., Perez-Alonso M., Obermaier B., Delseny M.,
RA Boutry M., Grivell L.A., Mache R., Puigdomenech P., De Simone V.,
RA Choisne N., Artiguenave F., Robert C., Brottier P., Wincker P.,
RA Cattolico L., Weissenbach J., Saurin W., Quetier F., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Benes V., Wurmbach E., Drzonek H.,
RA Erfle H., Jordan N., Bangert S., Wiedelmann R., Kranz H., Voss H.,
RA Holland R., Brandt P., Nyakatura G., Vezzi A., D'Angelo M., Pallavicini A.,
RA Toppo S., Simionati B., Conrad A., Hornischer K., Kauer G., Loehnert T.-H.,
RA Nordsiek G., Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J.,
RA Climent J., Navarro P., Collado C., Perez-Perez A., Ottenwaelder B.,
RA Duchemin D., Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D.,
RA de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E.,
RA Monfort A., Argiriou A., Flores M., Liguori R., Vitale D., Mannhaupt G.,
RA Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., Mayer K.F.X.,
RA Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., Rooney T., Rizzo M.,
RA Walts A., Utterback T., Fujii C.Y., Shea T.P., Creasy T.H., Haas B.,
RA Maiti R., Wu D., Peterson J., Van Aken S., Pai G., Militscher J.,
RA Sellers P., Gill J.E., Feldblyum T.V., Preuss D., Lin X., Nierman W.C.,
RA Salzberg S.L., White O., Venter J.C., Fraser C.M., Kaneko T., Nakamura Y.,
RA Sato S., Kato T., Asamizu E., Sasamoto S., Kimura T., Idesawa K.,
RA Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A.,
RA Muraki A., Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T.,
RA Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT "Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana.";
RL Nature 408:820-822(2000).
RN [3]
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 [4]
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RA Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
RA Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
RA Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
RA Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y.,
RA Shinozaki K.;
RT "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, TOPOLOGY, AND TISSUE SPECIFICITY.
RX PubMed=11299361; DOI=10.1104/pp.125.4.1813;
RA Chen L., Ortiz-Lopez A., Jung A., Bush D.R.;
RT "ANT1, an aromatic and neutral amino acid transporter in Arabidopsis.";
RL Plant Physiol. 125:1813-1820(2001).
RN [7]
RP GENE FAMILY, NOMENCLATURE, SUBCELLULAR LOCATION, AND TISSUE 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 aromatic and neutral amino acids such as
CC tyrosine, tryptophan, phenylalanine, histidine, proline, leucine,
CC valine, glutamine, as well as arginine. Transports the auxins indole-3-
CC acetic acid (IAA) and 2,4-dichlorophenoxyacetic acid (2,4-D).
CC {ECO:0000269|PubMed:11299361}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=163 uM for leucine {ECO:0000269|PubMed:11299361};
CC KM=240 uM for tyrosine {ECO:0000269|PubMed:11299361};
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000269|PubMed:27925655}; Multi-pass membrane protein
CC {ECO:0000255}.
CC -!- TISSUE SPECIFICITY: Ubiquitous (PubMed:27925655). Highly expressed in
CC flowers and cauline leaves and at lower levels in stems, leaves and
CC roots (PubMed:11299361). {ECO:0000269|PubMed:11299361,
CC 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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAB82307.1; Type=Miscellaneous discrepancy; Note=Sequencing errors.; Evidence={ECO:0000305};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; U39783; AAB82307.1; ALT_SEQ; mRNA.
DR EMBL; AC016795; AAF23206.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE75115.1; -; Genomic_DNA.
DR EMBL; CP002686; ANM65575.1; -; Genomic_DNA.
DR EMBL; BT008302; AAP37661.1; -; mRNA.
DR EMBL; AK227614; BAE99605.1; -; mRNA.
DR RefSeq; NP_001327533.1; NM_001337960.1.
DR RefSeq; NP_187796.1; NM_112023.2.
DR AlphaFoldDB; Q9SF09; -.
DR SMR; Q9SF09; -.
DR IntAct; Q9SF09; 1.
DR STRING; 3702.AT3G11900.1; -.
DR iPTMnet; Q9SF09; -.
DR PaxDb; Q9SF09; -.
DR PRIDE; Q9SF09; -.
DR ProteomicsDB; 244481; -.
DR EnsemblPlants; AT3G11900.1; AT3G11900.1; AT3G11900.
DR EnsemblPlants; AT3G11900.2; AT3G11900.2; AT3G11900.
DR GeneID; 820363; -.
DR Gramene; AT3G11900.1; AT3G11900.1; AT3G11900.
DR Gramene; AT3G11900.2; AT3G11900.2; AT3G11900.
DR KEGG; ath:AT3G11900; -.
DR Araport; AT3G11900; -.
DR TAIR; locus:2081471; AT3G11900.
DR eggNOG; KOG1304; Eukaryota.
DR HOGENOM; CLU_009646_6_0_1; -.
DR InParanoid; Q9SF09; -.
DR OMA; ALCYATF; -.
DR OrthoDB; 464614at2759; -.
DR PhylomeDB; Q9SF09; -.
DR SABIO-RK; Q9SF09; -.
DR PRO; PR:Q9SF09; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q9SF09; baseline and differential.
DR Genevisible; Q9SF09; AT.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IDA:UniProtKB.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0016020; C:membrane; ISS:TAIR.
DR GO; GO:0015173; F:aromatic amino acid transmembrane transporter activity; IMP:TAIR.
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; IMP:TAIR.
DR GO; GO:0003333; P:amino acid transmembrane transport; IBA:GO_Central.
DR GO; GO:0009624; P:response to nematode; HEP:TAIR.
DR InterPro; IPR013057; AA_transpt_TM.
DR Pfam; PF01490; Aa_trans; 1.
PE 1: Evidence at protein level;
KW Amino-acid transport; Endoplasmic reticulum; Membrane; Reference proteome;
KW Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..432
FT /note="Amino acid transporter ANT1"
FT /id="PRO_0000433105"
FT TOPO_DOM 1..35
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 36..56
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 57..62
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT TRANSMEM 63..83
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 84..115
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 116..136
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 137..147
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT TRANSMEM 148..168
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 169..172
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 173..193
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 194..219
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT TRANSMEM 220..240
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 241..256
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 257..277
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 278..292
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT TRANSMEM 293..313
FT /note="Helical; Name=8"
FT /evidence="ECO:0000255"
FT TOPO_DOM 314..353
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 354..374
FT /note="Helical; Name=9"
FT /evidence="ECO:0000255"
FT TOPO_DOM 375..379
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT TRANSMEM 380..400
FT /note="Helical; Name=10"
FT /evidence="ECO:0000255"
FT TOPO_DOM 401..410
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 411..431
FT /note="Helical; Name=11"
FT /evidence="ECO:0000255"
FT TOPO_DOM 432
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT REGION 1..30
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 7..30
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 219
FT /note="G -> S (in Ref. 1; AAB82307)"
FT /evidence="ECO:0000305"
FT CONFLICT 244
FT /note="M -> I (in Ref. 1; AAB82307)"
FT /evidence="ECO:0000305"
FT CONFLICT 282
FT /note="D -> N (in Ref. 1; AAB82307)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 432 AA; 46470 MW; 7C2ACD41154B92D3 CRC64;
MAIKDLTATT GDSSLPLIKS PPSETTGGDR TSALQTLGNI IVSIVGTGVL GLPYAFRIAG
WLAGSLGVII VGFATYYCML LLIQCRDKLE SEEGEEESKT YGDLGFKCMG TKGRYLTEFL
IFTAQCGGSV AYLVFIGRNL SSIFSSYGLS MVSFILILVP IEVGLSWITS LSALSPFSIF
ADICNIIAMC FVVKENVEMV IEGDFSFSDR TAISSTIGGL PFAGGVAVFC FEGFAMTLAL
ESSMREREAF PKLLAKVLAG ITFVYVLFGF CGYMAYGDQT KDIITLNLPN NWSAIAVQIG
LCVGLTFTFP IMVHPLNEII EQKLKRIDWL QKHHNGYSNE TGSVSKFAIF TTRTLLVVGL
AAIASLVPGF GTFASLVGST LCALISFVLP ASYHLTLLGP SLNVWNKSID VFIVICGLIF
AVYGTYNTIV GV
