LHT1_ARATH
ID LHT1_ARATH Reviewed; 446 AA.
AC Q9FKS8; O24405; Q3E8J8;
DT 03-NOV-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 106.
DE RecName: Full=Lysine histidine transporter 1;
GN Name=LHT1; OrderedLocusNames=At5g40780; ORFNames=K1B16.3;
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] (ISOFORM 1), FUNCTION, TISSUE SPECIFICITY,
RP ACTIVITY REGULATION, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=9390441; DOI=10.1104/pp.115.3.1127;
RA Chen L., Bush D.R.;
RT "LHT1, a lysine- and histidine-specific amino acid transporter in
RT arabidopsis.";
RL Plant Physiol. 115:1127-1134(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=9679202; DOI=10.1093/dnares/5.2.131;
RA Kaneko T., Kotani H., Nakamura Y., Sato S., Asamizu E., Miyajima N.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. V. Sequence
RT features of the regions of 1,381,565 bp covered by twenty one physically
RT assigned P1 and TAC clones.";
RL DNA Res. 5:131-145(1998).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=9872454; DOI=10.1093/dnares/5.5.297;
RA Nakamura Y., Sato S., Asamizu E., Kaneko T., Kotani H., Miyajima N.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. VII. Sequence
RT features of the regions of 1,013,767 bp covered by sixteen physically
RT assigned P1 and TAC clones.";
RL DNA Res. 5:297-308(1998).
RN [4]
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
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 [6]
RP GENE FAMILY.
RC STRAIN=cv. C24;
RX PubMed=15361141; DOI=10.1111/j.1365-313x.2004.02186.x;
RA Lee Y.-H., Tegeder M.;
RT "Selective expression of a novel high-affinity transport system for acidic
RT and neutral amino acids in the tapetum cells of Arabidopsis flowers.";
RL Plant J. 40:60-74(2004).
RN [7]
RP FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, INDUCTION, ACTIVITY REGULATION,
RP TISSUE SPECIFICITY, SUBCELLULAR LOCATION, AND DISRUPTION PHENOTYPE.
RX PubMed=16816136; DOI=10.1105/tpc.106.041012;
RA Hirner A., Ladwig F., Stransky H., Okumoto S., Keinath M., Harms A.,
RA Frommer W.B., Koch W.;
RT "Arabidopsis LHT1 is a high-affinity transporter for cellular amino acid
RT uptake in both root epidermis and leaf mesophyll.";
RL Plant Cell 18:1931-1946(2006).
RN [8]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=17293438; DOI=10.1104/pp.106.092205;
RA Svennerstam H., Ganeteg U., Bellini C., Naesholm T.;
RT "Comprehensive screening of Arabidopsis mutants suggests the lysine
RT histidine transporter 1 to be involved in plant uptake of amino acids.";
RL Plant Physiol. 143:1853-1860(2007).
RN [9]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=18681934; DOI=10.1111/j.1469-8137.2008.02589.x;
RA Svennerstam H., Ganeteg U., Naesholm T.;
RT "Root uptake of cationic amino acids by Arabidopsis depends on functional
RT expression of amino acid permease 5.";
RL New Phytol. 180:620-630(2008).
CC -!- FUNCTION: Amino acid-proton symporter. Transporter with a broad
CC specificity for histidine, lysine, glutamic acid, alanine, serine,
CC proline and glycine. Involved in both apoplastic transport of amino
CC acids in leaves and their uptake by roots.
CC {ECO:0000269|PubMed:16816136, ECO:0000269|PubMed:17293438,
CC ECO:0000269|PubMed:18681934, ECO:0000269|PubMed:9390441}.
CC -!- ACTIVITY REGULATION: Inhibited by carbonlycyanide m-
CC chlorophenylhydrazone (CCCP) and DEPC. {ECO:0000269|PubMed:16816136,
CC ECO:0000269|PubMed:9390441}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=175 uM for lysine {ECO:0000269|PubMed:16816136,
CC ECO:0000269|PubMed:9390441};
CC KM=11 mM for leucine {ECO:0000269|PubMed:16816136,
CC ECO:0000269|PubMed:9390441};
CC KM=10 uM for proline {ECO:0000269|PubMed:16816136,
CC ECO:0000269|PubMed:9390441};
CC KM=14 uM for glutamic acid {ECO:0000269|PubMed:16816136,
CC ECO:0000269|PubMed:9390441};
CC KM=360 uM for histidine {ECO:0000269|PubMed:16816136,
CC ECO:0000269|PubMed:9390441};
CC Vmax=80 nmol/min/g enzyme toward proline
CC {ECO:0000269|PubMed:16816136, ECO:0000269|PubMed:9390441};
CC Vmax=100 nmol/min/g enzyme toward glutamic acid
CC {ECO:0000269|PubMed:16816136, ECO:0000269|PubMed:9390441};
CC Vmax=105 nmol/min/g enzyme toward histidine
CC {ECO:0000269|PubMed:16816136, ECO:0000269|PubMed:9390441};
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:16816136};
CC Multi-pass membrane protein {ECO:0000269|PubMed:16816136}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9FKS8-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9FKS8-2; Sequence=VSP_038321;
CC -!- TISSUE SPECIFICITY: Expressed in roots, stems, flowers, leaves,
CC siliques and pollen. Found in the tips of roots and in the rhizodermis
CC of emerging roots and in lateral roots. Higher expression in older
CC leaves as compared to joung leaves. Detected first at the hydathodes,
CC then in the epidermis and finally in matures leaves in all mesophyll
CC cells. Not detected in vascular bundles or in seeds.
CC {ECO:0000269|PubMed:16816136, ECO:0000269|PubMed:9390441}.
CC -!- INDUCTION: By amino acids. {ECO:0000269|PubMed:16816136}.
CC -!- DISRUPTION PHENOTYPE: Lower biomass at the time of harvest, but no
CC visible phenotype until bolting. Decreased uptake of L-histidine, L-
CC glutamine, glutamic acid, L-serine, glycine, L-asparagine, aspartic
CC acid, L-proline and L- or D-alanine. {ECO:0000269|PubMed:16816136,
CC ECO:0000269|PubMed:17293438, ECO:0000269|PubMed:18681934}.
CC -!- SIMILARITY: Belongs to the amino acid/polyamine transporter 2 family.
CC Amino acid/auxin permease (AAAP) (TC 2.A.18.2) subfamily.
CC {ECO:0000305}.
CC -!- CAUTION: PubMed:9390441 shows a high affinity for lysine while
CC PubMed:16816136 and PubMed:17293438 found no significant transport of
CC this amino acid. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAC49885.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; U39782; AAC49885.1; ALT_FRAME; mRNA.
DR EMBL; AB011477; BAB11340.1; -; Genomic_DNA.
DR EMBL; AB015470; BAB11340.1; JOINED; Genomic_DNA.
DR EMBL; CP002688; AED94593.1; -; Genomic_DNA.
DR EMBL; AF367281; AAK56270.1; -; mRNA.
DR EMBL; AY133550; AAM91380.1; -; mRNA.
DR RefSeq; NP_851109.1; NM_180778.4. [Q9FKS8-1]
DR AlphaFoldDB; Q9FKS8; -.
DR SMR; Q9FKS8; -.
DR BioGRID; 19329; 4.
DR IntAct; Q9FKS8; 2.
DR STRING; 3702.AT5G40780.1; -.
DR TCDB; 2.A.18.2.2; the amino acid/auxin permease (aaap) family.
DR PaxDb; Q9FKS8; -.
DR PRIDE; Q9FKS8; -.
DR ProteomicsDB; 238467; -. [Q9FKS8-1]
DR EnsemblPlants; AT5G40780.1; AT5G40780.1; AT5G40780. [Q9FKS8-1]
DR GeneID; 834078; -.
DR Gramene; AT5G40780.1; AT5G40780.1; AT5G40780. [Q9FKS8-1]
DR KEGG; ath:AT5G40780; -.
DR Araport; AT5G40780; -.
DR TAIR; locus:2154815; AT5G40780.
DR eggNOG; KOG1303; Eukaryota.
DR InParanoid; Q9FKS8; -.
DR OMA; NDITQFG; -.
DR PhylomeDB; Q9FKS8; -.
DR PRO; PR:Q9FKS8; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q9FKS8; baseline and differential.
DR Genevisible; Q9FKS8; AT.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0016020; C:membrane; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0009536; C:plastid; HDA:TAIR.
DR GO; GO:0015172; F:acidic amino acid transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0015171; F:amino acid transmembrane transporter activity; IMP:TAIR.
DR GO; GO:0015293; F:symporter activity; IEA:UniProtKB-KW.
DR GO; GO:0043090; P:amino acid import; IMP:TAIR.
DR GO; GO:0003333; P:amino acid transmembrane transport; IBA:GO_Central.
DR GO; GO:0006952; P:defense response; IEP:TAIR.
DR InterPro; IPR013057; AA_transpt_TM.
DR Pfam; PF01490; Aa_trans; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Amino-acid transport; Cell membrane; Membrane;
KW Reference proteome; Symport; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..446
FT /note="Lysine histidine transporter 1"
FT /id="PRO_0000387969"
FT TOPO_DOM 1..37
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 38..58
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 59..63
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 64..84
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 85..115
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 116..136
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 137..157
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 158..178
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 179..180
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 181..201
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 202..227
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 228..248
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 249..268
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 269..289
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 290..305
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 306..326
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 327..352
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 353..375
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 376..378
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 379..401
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 402..409
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 410..430
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 431..446
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT VAR_SEQ 11
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_038321"
SQ SEQUENCE 446 AA; 49814 MW; 0F26B5A6542D8B77 CRC64;
MVAQAPHDDH QDDEKLAAAR QKEIEDWLPI TSSRNAKWWY SAFHNVTAMV GAGVLGLPYA
MSQLGWGPGI AVLVLSWVIT LYTLWQMVEM HEMVPGKRFD RYHELGQHAF GEKLGLYIVV
PQQLIVEIGV CIVYMVTGGK SLKKFHELVC DDCKPIKLTY FIMIFASVHF VLSHLPNFNS
ISGVSLAAAV MSLSYSTIAW ASSASKGVQE DVQYGYKAKT TAGTVFNFFS GLGDVAFAYA
GHNVVLEIQA TIPSTPEKPS KGPMWRGVIV AYIVVALCYF PVALVGYYIF GNGVEDNILM
SLKKPAWLIA TANIFVVIHV IGSYQIYAMP VFDMMETLLV KKLNFRPTTT LRFFVRNFYV
AATMFVGMTF PFFGGLLAFF GGFAFAPTTY FLPCVIWLAI YKPKKYSLSW WANWVCIVFG
LFLMVLSPIG GLRTIVIQAK GYKFYS
