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Amino acid permease 4 (Amino acid transporter AAP4)

 AAP4_ARATH              Reviewed;         466 AA.
Q9FN04; Q39135; Q8LFM7; Q8RWA8;
03-NOV-2009, integrated into UniProtKB/Swiss-Prot.
01-MAR-2001, sequence version 1.
12-APR-2017, entry version 85.
RecName: Full=Amino acid permease 4;
AltName: Full=Amino acid transporter AAP4;
Name=AAP4; OrderedLocusNames=At5g63850; ORFNames=MGI19.5;
Arabidopsis thaliana (Mouse-ear cress).
Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
Spermatophyta; Magnoliophyta; eudicotyledons; Gunneridae;
Pentapetalae; rosids; malvids; Brassicales; Brassicaceae; Camelineae;
Arabidopsis.
NCBI_TaxID=3702;
[1]
NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, ENZYME REGULATION, DEVELOPMENTAL
STAGE, AND TISSUE SPECIFICITY.
STRAIN=cv. Landsberg erecta;
PubMed=7608199; DOI=10.1074/jbc.270.27.16315;
Fischer W.-N., Kwart M., Hummel S., Frommer W.B.;
"Substrate specificity and expression profile of amino acid
transporters (AAPs) in Arabidopsis.";
J. Biol. Chem. 270:16315-16320(1995).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=cv. Columbia;
PubMed=9501997; DOI=10.1093/dnares/4.6.401;
Nakamura Y., Sato S., Kaneko T., Kotani H., Asamizu E., Miyajima N.,
Tabata S.;
"Structural analysis of Arabidopsis thaliana chromosome 5. III.
Sequence features of the regions of 1,191,918 bp covered by seventeen
physically assigned P1 clones.";
DNA Res. 4:401-414(1997).
[3]
GENOME REANNOTATION.
STRAIN=cv. Columbia;
The Arabidopsis Information Portal (Araport);
Submitted (MAY-2016) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=cv. Columbia;
PubMed=14593172; DOI=10.1126/science.1088305;
Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J.,
Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F.,
Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G.,
Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J.,
Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y.,
Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P.,
Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F.,
Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M.,
Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J.,
Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T.,
Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y.,
Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R.;
"Empirical analysis of transcriptional activity in the Arabidopsis
genome.";
Science 302:842-846(2003).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
Feldmann K.A.;
"Full-length cDNA from Arabidopsis thaliana.";
Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
[6]
INDUCTION.
STRAIN=cv. Landsberg erecta;
PubMed=8776904; DOI=10.1105/tpc.8.8.1437;
Rentsch D., Hirner B., Schmelzer E., Frommer W.B.;
"Salt stress-induced proline transporters and salt stress-repressed
broad specificity amino acid permeases identified by suppression of a
yeast amino acid permease-targeting mutant.";
Plant Cell 8:1437-1446(1996).
[7]
CHARACTERIZATION.
PubMed=12148530; DOI=10.1046/j.1365-313X.2002.01248.x;
Fischer W.-N., Loo D.D.F., Koch W., Ludewig U., Boorer K.J.,
Tegeder M., Rentsch D., Wright E.M., Frommer W.B.;
"Low and high affinity amino acid H+-cotransporters for cellular
import of neutral and charged amino acids.";
Plant J. 29:717-731(2002).
-!- FUNCTION: Amino acid-proton symporter. Stereospecific transporter
with a broad specificity for neutral amino acids, favoring small
amino acids such as alanine, asparagine and glutamine. Accepts
also large aromatic residues such as in phenlalanine or tyrosine.
{ECO:0000269|PubMed:7608199}.
-!- ENZYME REGULATION: Inhibited by 2,4-dinitrophenol.
{ECO:0000269|PubMed:7608199}.
-!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass
membrane protein {ECO:0000305}.
-!- TISSUE SPECIFICITY: Expressed in leaves, stems and flowers.
{ECO:0000269|PubMed:7608199}.
-!- DEVELOPMENTAL STAGE: High expression in source leaves, but almost
undetected in sink leaves. {ECO:0000269|PubMed:7608199}.
-!- INDUCTION: Down-regulated by drought.
{ECO:0000269|PubMed:8776904}.
-!- SIMILARITY: Belongs to the amino acid/polyamine transporter 2
family. Amino acid/auxin permease (AAAP) (TC 2.A.18.2) subfamily.
{ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; X77500; CAA54631.1; -; mRNA.
EMBL; AB007646; BAB11033.1; -; Genomic_DNA.
EMBL; CP002688; AED97804.1; -; Genomic_DNA.
EMBL; AY093224; AAM13223.1; -; mRNA.
EMBL; BT003395; AAO30058.1; -; mRNA.
EMBL; AY084749; AAM61320.1; -; mRNA.
PIR; B57479; B57479.
RefSeq; NP_201190.1; NM_125780.3.
UniGene; At.24102; -.
ProteinModelPortal; Q9FN04; -.
BioGrid; 21747; 6.
IntAct; Q9FN04; 4.
STRING; 3702.AT5G63850.1; -.
PaxDb; Q9FN04; -.
EnsemblPlants; AT5G63850.1; AT5G63850.1; AT5G63850.
GeneID; 836505; -.
Gramene; AT5G63850.1; AT5G63850.1; AT5G63850.
KEGG; ath:AT5G63850; -.
Araport; AT5G63850; -.
TAIR; locus:2163981; AT5G63850.
eggNOG; KOG1303; Eukaryota.
eggNOG; COG0814; LUCA.
HOGENOM; HOG000238530; -.
InParanoid; Q9FN04; -.
OMA; TKEYEIR; -.
OrthoDB; EOG09360984; -.
PhylomeDB; Q9FN04; -.
PRO; PR:Q9FN04; -.
Proteomes; UP000006548; Chromosome 5.
ExpressionAtlas; Q9FN04; baseline and differential.
Genevisible; Q9FN04; AT.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
GO; GO:0015172; F:acidic amino acid transmembrane transporter activity; IDA:TAIR.
GO; GO:0015175; F:neutral amino acid transmembrane transporter activity; IDA:TAIR.
GO; GO:0015399; F:primary active transmembrane transporter activity; IDA:TAIR.
GO; GO:0015293; F:symporter activity; IEA:UniProtKB-KW.
GO; GO:0006865; P:amino acid transport; TAS:TAIR.
InterPro; IPR013057; AA_transpt_TM.
Pfam; PF01490; Aa_trans; 1.
1: Evidence at protein level;
Amino-acid transport; Cell membrane; Complete proteome; Membrane;
Reference proteome; Symport; Transmembrane; Transmembrane helix;
Transport.
CHAIN 1 466 Amino acid permease 4.
/FTId=PRO_0000387502.
TOPO_DOM 1 22 Cytoplasmic. {ECO:0000255}.
TRANSMEM 23 43 Helical. {ECO:0000255}.
TRANSMEM 44 64 Helical. {ECO:0000255}.
TOPO_DOM 65 111 Cytoplasmic. {ECO:0000255}.
TRANSMEM 112 132 Helical. {ECO:0000255}.
TOPO_DOM 133 177 Extracellular. {ECO:0000255}.
TRANSMEM 178 198 Helical. {ECO:0000255}.
TOPO_DOM 199 226 Cytoplasmic. {ECO:0000255}.
TRANSMEM 227 247 Helical. {ECO:0000255}.
TOPO_DOM 248 266 Extracellular. {ECO:0000255}.
TRANSMEM 267 287 Helical. {ECO:0000255}.
TOPO_DOM 288 290 Cytoplasmic. {ECO:0000255}.
TRANSMEM 291 311 Helical. {ECO:0000255}.
TOPO_DOM 312 313 Extracellular. {ECO:0000255}.
TRANSMEM 314 334 Helical. {ECO:0000255}.
TOPO_DOM 335 369 Cytoplasmic. {ECO:0000255}.
TRANSMEM 370 390 Helical. {ECO:0000255}.
TOPO_DOM 391 392 Extracellular. {ECO:0000255}.
TRANSMEM 393 413 Helical. {ECO:0000255}.
TOPO_DOM 414 435 Cytoplasmic. {ECO:0000255}.
TRANSMEM 436 456 Helical. {ECO:0000255}.
TOPO_DOM 457 466 Extracellular. {ECO:0000255}.
CONFLICT 338 338 A -> L (in Ref. 1; CAA54631).
{ECO:0000305}.
CONFLICT 341 341 R -> S (in Ref. 4; AAO30058/AAM13223).
{ECO:0000305}.
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


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