AAP4_ARATH
ID AAP4_ARATH Reviewed; 466 AA.
AC Q9FN04; Q39135; Q8LFM7; Q8RWA8;
DT 03-NOV-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 104.
DE RecName: Full=Amino acid permease 4;
DE AltName: Full=Amino acid transporter AAP4;
GN Name=AAP4; OrderedLocusNames=At5g63850; ORFNames=MGI19.5;
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, ACTIVITY REGULATION, DEVELOPMENTAL
RP STAGE, AND TISSUE SPECIFICITY.
RC STRAIN=cv. Landsberg erecta;
RX PubMed=7608199; DOI=10.1074/jbc.270.27.16315;
RA Fischer W.-N., Kwart M., Hummel S., Frommer W.B.;
RT "Substrate specificity and expression profile of amino acid transporters
RT (AAPs) in Arabidopsis.";
RL J. Biol. Chem. 270:16315-16320(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=9501997; DOI=10.1093/dnares/4.6.401;
RA Nakamura Y., Sato S., Kaneko T., Kotani H., Asamizu E., Miyajima N.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. III. Sequence
RT features of the regions of 1,191,918 bp covered by seventeen physically
RT assigned P1 clones.";
RL DNA Res. 4:401-414(1997).
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].
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 [6]
RP INDUCTION.
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 [7]
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).
CC -!- FUNCTION: Amino acid-proton symporter. Stereospecific transporter with
CC a broad specificity for neutral amino acids, favoring small amino acids
CC such as alanine, asparagine and glutamine. Accepts also large aromatic
CC residues such as in phenlalanine or tyrosine.
CC {ECO:0000269|PubMed:7608199}.
CC -!- ACTIVITY REGULATION: Inhibited by 2,4-dinitrophenol.
CC {ECO:0000269|PubMed:7608199}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass membrane
CC protein {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Expressed in leaves, stems and flowers.
CC {ECO:0000269|PubMed:7608199}.
CC -!- DEVELOPMENTAL STAGE: High expression in source leaves, but almost
CC undetected in sink leaves. {ECO:0000269|PubMed:7608199}.
CC -!- INDUCTION: Down-regulated by drought. {ECO:0000269|PubMed:8776904}.
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; X77500; CAA54631.1; -; mRNA.
DR EMBL; AB007646; BAB11033.1; -; Genomic_DNA.
DR EMBL; CP002688; AED97804.1; -; Genomic_DNA.
DR EMBL; AY093224; AAM13223.1; -; mRNA.
DR EMBL; BT003395; AAO30058.1; -; mRNA.
DR EMBL; AY084749; AAM61320.1; -; mRNA.
DR PIR; B57479; B57479.
DR RefSeq; NP_201190.1; NM_125780.3.
DR AlphaFoldDB; Q9FN04; -.
DR BioGRID; 21747; 6.
DR IntAct; Q9FN04; 4.
DR STRING; 3702.AT5G63850.1; -.
DR PaxDb; Q9FN04; -.
DR PRIDE; Q9FN04; -.
DR ProteomicsDB; 244561; -.
DR EnsemblPlants; AT5G63850.1; AT5G63850.1; AT5G63850.
DR GeneID; 836505; -.
DR Gramene; AT5G63850.1; AT5G63850.1; AT5G63850.
DR KEGG; ath:AT5G63850; -.
DR Araport; AT5G63850; -.
DR TAIR; locus:2163981; AT5G63850.
DR eggNOG; KOG1303; Eukaryota.
DR HOGENOM; CLU_031247_4_1_1; -.
DR InParanoid; Q9FN04; -.
DR OMA; TMKIATR; -.
DR OrthoDB; 570025at2759; -.
DR PhylomeDB; Q9FN04; -.
DR PRO; PR:Q9FN04; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q9FN04; baseline and differential.
DR Genevisible; Q9FN04; 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:0015399; F:primary active transmembrane transporter activity; IDA:TAIR.
DR GO; GO:0015293; F:symporter activity; IEA:UniProtKB-KW.
DR GO; GO:0003333; P:amino acid transmembrane transport; IBA:GO_Central.
DR GO; GO:0006865; P:amino acid transport; TAS: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..466
FT /note="Amino acid permease 4"
FT /id="PRO_0000387502"
FT TOPO_DOM 1..22
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 23..43
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 44..64
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 65..111
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 112..132
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 133..177
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 178..198
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 199..226
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 227..247
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 248..266
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 267..287
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 288..290
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 291..311
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 312..313
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 314..334
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 335..369
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 370..390
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 391..392
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 393..413
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 414..435
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 436..456
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 457..466
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT CONFLICT 338
FT /note="A -> L (in Ref. 1; CAA54631)"
FT /evidence="ECO:0000305"
FT CONFLICT 341
FT /note="R -> S (in Ref. 4; AAO30058/AAM13223)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 466 AA; 51429 MW; 11B1D5332C63BD88 CRC64;
MDVPRPAFKC FDDDGRLKRS GTVWTASAHI ITAVIGSGVL SLAWAIGQLG WIAGPTVMLL
FSFVTYYSST LLSDCYRTGD PVSGKRNYTY MDAVRSILGG FRFKICGLIQ YLNLFGITVG
YTIAASISMM AIKRSNCFHE SGGKNPCHMS SNPYMIMFGV TEILLSQIKD FDQIWWLSIV
AAIMSFTYSA IGLALGIIQV AANGVVKGSL TGISIGAVTQ TQKIWRTFQA LGDIAFAYSY
SVVLIEIQDT VRSPPAESKT MKIATRISIA VTTTFYMLCG CMGYAAFGDK APGNLLTGFG
FYNPFWLLDV ANAAIVIHLV GAYQVFAQPI FAFIEKQAAA RFPDSDLVTK EYEIRIPGFR
SPYKVNVFRA VYRSGFVVLT TVISMLMPFF NDVVGILGAL GFWPLTVYFP VEMYIRQRKV
ERWSMKWVCL QMLSCGCLMI TLVAGVGSIA GVMLDLKVYK PFKTTY
