AAP6_ARATH
ID AAP6_ARATH Reviewed; 481 AA.
AC P92934;
DT 03-NOV-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1997, sequence version 1.
DT 03-AUG-2022, entry version 120.
DE RecName: Full=Amino acid permease 6;
DE AltName: Full=Amino acid transporter AAP6;
GN Name=AAP6; OrderedLocusNames=At5g49630; ORFNames=MNI5.1;
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], FUNCTION, INDUCTION, AND TISSUE SPECIFICITY.
RC STRAIN=cv. Landsberg erecta;
RX PubMed=8776904; DOI=10.2307/3870312;
RA Rentsch D., Hirner B., Schmelzer E., Frommer W.B.;
RT "Salt stress-induced proline transporters and salt stress-repressed broad
RT specificity amino acid permeases identified by suppression of a yeast amino
RT acid permease-targeting mutant.";
RL Plant Cell 8:1437-1446(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10718197; DOI=10.1093/dnares/7.1.31;
RA Sato S., Nakamura Y., Kaneko T., Katoh T., Asamizu E., Kotani H.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. X. Sequence
RT features of the regions of 3,076,755 bp covered by sixty P1 and TAC
RT clones.";
RL DNA Res. 7:31-63(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;
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 [5]
RP TISSUE SPECIFICITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=12244056; DOI=10.1074/jbc.m207730200;
RA Okumoto S., Schmidt R., Tegeder M., Fischer W.-N., Rentsch D.,
RA Frommer W.B., Koch W.;
RT "High affinity amino acid transporters specifically expressed in xylem
RT parenchyma and developing seeds of Arabidopsis.";
RL J. Biol. Chem. 277:45338-45346(2002).
RN [6]
RP CHARACTERIZATION.
RX PubMed=12148530; DOI=10.1046/j.1365-313x.2002.01248.x;
RA Fischer W.-N., Loo D.D.F., Koch W., Ludewig U., Boorer K.J., Tegeder M.,
RA Rentsch D., Wright E.M., Frommer W.B.;
RT "Low and high affinity amino acid H+-cotransporters for cellular import of
RT neutral and charged amino acids.";
RL Plant J. 29:717-731(2002).
RN [7]
RP DISRUPTION PHENOTYPE.
RX PubMed=19755569; DOI=10.1093/jxb/erp274;
RA Hunt E., Gattolin S., Newbury H.J., Bale J.S., Tseng H.-M., Barrett D.A.,
RA Pritchard J.;
RT "A mutation in amino acid permease AAP6 reduces the amino acid content of
RT the Arabidopsis sieve elements but leaves aphid herbivores unaffected.";
RL J. Exp. Bot. 61:55-64(2010).
CC -!- FUNCTION: Amino acid-proton symporter. Stereospecific transporter with
CC a broad specificity for tryptophan, proline, and neutral and acidic
CC amino acids. Has an affinity for aspartate in a physiological range.
CC Involved in the uptake of amino acids diffusing out of the xylem
CC tracheids into the xylem parenchyma. {ECO:0000269|PubMed:8776904}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=248 uM for aspartate {ECO:0000269|PubMed:12244056};
CC Vmax=0.342 nmol/min/mg enzyme toward aspartate
CC {ECO:0000269|PubMed:12244056};
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass membrane
CC protein {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Expressed in roots and leaves, and at lower levels
CC in stems and flowers. Found in the xylem parenchyma.
CC {ECO:0000269|PubMed:12244056, ECO:0000269|PubMed:8776904}.
CC -!- DEVELOPMENTAL STAGE: Expressed at higher levels in sink as compared
CC with source leaves.
CC -!- INDUCTION: Down-regulated by drought and salt stress.
CC {ECO:0000269|PubMed:8776904}.
CC -!- DISRUPTION PHENOTYPE: Larger seeds and rosette leaves and increased
CC number of cauline leaves at flowering. Decreased concentration of
CC lysine, phenylalanine, leucine and aspartic acid in the sieve element
CC sap, but no significant effect on aphid feeding behavior or
CC reproduction. {ECO:0000269|PubMed:19755569}.
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}.
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DR EMBL; X95736; CAA65051.1; -; mRNA.
DR EMBL; AB025627; BAA97227.1; -; Genomic_DNA.
DR EMBL; CP002688; AED95838.1; -; Genomic_DNA.
DR EMBL; AK229102; BAF00980.1; -; mRNA.
DR PIR; T50691; T50691.
DR RefSeq; NP_199774.1; NM_124341.4.
DR AlphaFoldDB; P92934; -.
DR BioGRID; 20271; 3.
DR IntAct; P92934; 2.
DR STRING; 3702.AT5G49630.1; -.
DR TCDB; 2.A.18.2.4; the amino acid/auxin permease (aaap) family.
DR SwissPalm; P92934; -.
DR PaxDb; P92934; -.
DR PRIDE; P92934; -.
DR ProteomicsDB; 244602; -.
DR EnsemblPlants; AT5G49630.1; AT5G49630.1; AT5G49630.
DR GeneID; 835025; -.
DR Gramene; AT5G49630.1; AT5G49630.1; AT5G49630.
DR KEGG; ath:AT5G49630; -.
DR Araport; AT5G49630; -.
DR TAIR; locus:2168912; AT5G49630.
DR eggNOG; KOG1303; Eukaryota.
DR HOGENOM; CLU_031247_4_1_1; -.
DR InParanoid; P92934; -.
DR OMA; MGMERQE; -.
DR OrthoDB; 570025at2759; -.
DR PhylomeDB; P92934; -.
DR SABIO-RK; P92934; -.
DR PRO; PR:P92934; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; P92934; baseline and differential.
DR Genevisible; P92934; 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:0015172; F:acidic amino acid transmembrane transporter activity; IDA:TAIR.
DR GO; GO:0015171; F:amino acid transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0015175; F:neutral amino acid transmembrane transporter activity; IDA:TAIR.
DR GO; GO:0015293; F:symporter activity; IEA:UniProtKB-KW.
DR GO; GO:0015800; P:acidic amino acid transport; IBA:GO_Central.
DR GO; GO:0003333; P:amino acid transmembrane transport; IBA:GO_Central.
DR GO; GO:0015810; P:aspartate transmembrane transport; IDA:TAIR.
DR GO; GO:0015804; P:neutral amino acid transport; IBA:GO_Central.
DR GO; GO:0015827; P:tryptophan transport; IDA:TAIR.
DR InterPro; IPR013057; AA_transpt_TM.
DR Pfam; PF01490; Aa_trans; 1.
PE 1: Evidence at protein level;
KW Amino-acid transport; Cell membrane; Membrane; Reference proteome; Symport;
KW Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..481
FT /note="Amino acid permease 6"
FT /id="PRO_0000387504"
FT TOPO_DOM 1..36
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 37..57
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 58..78
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 79..125
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 126..146
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 147..167
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 168..188
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 189..190
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 191..211
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 212..242
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 243..263
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 264..283
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 284..304
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 305..321
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 322..342
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 343..385
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 386..405
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 406..408
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 409..427
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 428..447
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 448..468
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 469..481
FT /note="Extracellular"
FT /evidence="ECO:0000255"
SQ SEQUENCE 481 AA; 53021 MW; DEB1CA7348760AD1 CRC64;
MEKKKSMFVE QSFPEHEIGD TNKNFDEDGR DKRTGTWMTG SAHIITAVIG SGVLSLAWAI
AQLGWVAGPA VLMAFSFITY FTSTMLADCY RSPDPVTGKR NYTYMEVVRS YLGGRKVQLC
GLAQYGNLIG ITIGYTITAS ISMVAVKRSN CFHKNGHNVK CATSNTPFMI IFAIIQIILS
QIPNFHNLSW LSILAAVMSF CYASIGVGLS IAKAAGGGEH VRTTLTGVTV GIDVSGAEKI
WRTFQAIGDI AFAYAYSTVL IEIQDTLKAG PPSENKAMKR ASLVGVSTTT FFYMLCGCVG
YAAFGNDAPG NFLTGFGFYE PFWLIDFANV CIAVHLIGAY QVFCQPIFQF VESQSAKRWP
DNKFITGEYK IHVPCCGDFS INFLRLVWRT SYVVVTAVVA MIFPFFNDFL GLIGAASFWP
LTVYFPIEMH IAQKKIPKFS FTWTWLKILS WTCFIVSLVA AAGSVQGLIQ SLKDFKPFQA
P
