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Amino acid permease 2 (Amino acid transporter AAP2)

 AAP2_ARATH              Reviewed;         493 AA.
Q38967; Q8LFS8;
03-NOV-2009, integrated into UniProtKB/Swiss-Prot.
01-NOV-1996, sequence version 1.
07-JUN-2017, entry version 100.
RecName: Full=Amino acid permease 2;
AltName: Full=Amino acid transporter AAP2;
Name=AAP2; OrderedLocusNames=At5g09220; ORFNames=T2K12.6, T5E8.20;
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].
STRAIN=cv. Landsberg erecta;
PubMed=8618839; DOI=10.1073/pnas.92.26.12036;
Frommer W.B., Hummel S., Unseld M., Ninnemann O.;
"Seed and vascular expression of a high-affinity transporter for
cationic amino acids in Arabidopsis.";
Proc. Natl. Acad. Sci. U.S.A. 92:12036-12040(1995).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=cv. Columbia;
PubMed=11130714; DOI=10.1038/35048507;
Tabata S., Kaneko T., Nakamura Y., Kotani H., Kato T., Asamizu E.,
Miyajima N., Sasamoto S., Kimura T., Hosouchi T., Kawashima K.,
Kohara M., Matsumoto M., Matsuno A., Muraki A., Nakayama S.,
Nakazaki N., Naruo K., Okumura S., Shinpo S., Takeuchi C., Wada T.,
Watanabe A., Yamada M., Yasuda M., Sato S., de la Bastide M.,
Huang E., Spiegel L., Gnoj L., O'Shaughnessy A., Preston R.,
Habermann K., Murray J., Johnson D., Rohlfing T., Nelson J.,
Stoneking T., Pepin K., Spieth J., Sekhon M., Armstrong J., Becker M.,
Belter E., Cordum H., Cordes M., Courtney L., Courtney W., Dante M.,
Du H., Edwards J., Fryman J., Haakensen B., Lamar E., Latreille P.,
Leonard S., Meyer R., Mulvaney E., Ozersky P., Riley A., Strowmatt C.,
Wagner-McPherson C., Wollam A., Yoakum M., Bell M., Dedhia N.,
Parnell L., Shah R., Rodriguez M., Hoon See L., Vil D., Baker J.,
Kirchoff K., Toth K., King L., Bahret A., Miller B., Marra M.A.,
Martienssen R., McCombie W.R., Wilson R.K., Murphy G., Bancroft I.,
Volckaert G., Wambutt R., Duesterhoeft A., Stiekema W., Pohl T.,
Entian K.-D., Terryn N., Hartley N., Bent E., Johnson S.,
Langham S.-A., McCullagh B., Robben J., Grymonprez B., Zimmermann W.,
Ramsperger U., Wedler H., Balke K., Wedler E., Peters S.,
van Staveren M., Dirkse W., Mooijman P., Klein Lankhorst R.,
Weitzenegger T., Bothe G., Rose M., Hauf J., Berneiser S., Hempel S.,
Feldpausch M., Lamberth S., Villarroel R., Gielen J., Ardiles W.,
Bents O., Lemcke K., Kolesov G., Mayer K.F.X., Rudd S., Schoof H.,
Schueller C., Zaccaria P., Mewes H.-W., Bevan M., Fransz P.F.;
"Sequence and analysis of chromosome 5 of the plant Arabidopsis
thaliana.";
Nature 408:823-826(2000).
[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]
FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, AND TISSUE SPECIFICITY.
PubMed=8281191; DOI=10.1046/j.1365-313X.1993.04060993.x;
Kwart M., Hirner B., Hummel S., Frommer W.B.;
"Differential expression of two related amino acid transporters with
differing substrate specificity in Arabidopsis thaliana.";
Plant J. 4:993-1002(1993).
[7]
FUNCTION, AND TISSUE SPECIFICITY.
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).
[8]
DEVELOPMENTAL STAGE, AND TISSUE SPECIFICITY.
PubMed=9675899; DOI=10.1046/j.1365-313X.1998.00151.x;
Hirner B., Fischer W.-N., Rentsch D., Kwart M., Frommer W.B.;
"Developmental control of H+/amino acid permease gene expression
during seed development of Arabidopsis.";
Plant J. 14:535-544(1998).
[9]
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 histidine, arginine, glutamate and
neutral amino acids, favoring small amino acids such as alanine,
asparagine and glutamine. Accepts also large aromatic residues
such as in phenlalanine or tyrosine. Has a much higher affinity
for basic amino acids as compared with AAP1. May function in
xylem-to-phloem transfer and in uptake of amino acids assimilated
in the green silique tissue. {ECO:0000269|PubMed:7608199,
ECO:0000269|PubMed:8281191}.
-!- ENZYME REGULATION: Inhibited by diethylpyrocarbonate (DEPC).
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Kinetic parameters:
KM=140 uM for L-proline {ECO:0000269|PubMed:8281191};
pH dependence:
Optimum pH is acidic. {ECO:0000269|PubMed:8281191};
-!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass
membrane protein {ECO:0000305}.
-!- TISSUE SPECIFICITY: Highly expressed in developing pods. Found in
the vascular strands of siliques, cotyledons, leaves and roots, in
the inner phloem of stems, and in the funiculi. Lower levels of
expression in flowers. Not expressed in seeds.
{ECO:0000269|PubMed:7608199, ECO:0000269|PubMed:8281191,
ECO:0000269|PubMed:9675899}.
-!- DEVELOPMENTAL STAGE: Strongly induced at heart stage of
embryogenesis. {ECO:0000269|PubMed:9675899}.
-!- 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; X71787; CAA50672.1; -; mRNA.
EMBL; AL391712; CAC05448.1; -; Genomic_DNA.
EMBL; CP002688; AED91352.1; -; Genomic_DNA.
EMBL; AY090341; AAL91247.1; -; mRNA.
EMBL; AY084665; AAM61227.1; -; mRNA.
PIR; S52421; S52421.
RefSeq; NP_196484.1; NM_120958.3.
UniGene; At.23992; -.
UniGene; At.72977; -.
ProteinModelPortal; Q38967; -.
STRING; 3702.AT5G09220.1; -.
TCDB; 2.A.18.2.7; the amino acid/auxin permease (aaap) family.
iPTMnet; Q38967; -.
PaxDb; Q38967; -.
EnsemblPlants; AT5G09220.1; AT5G09220.1; AT5G09220.
GeneID; 830781; -.
Gramene; AT5G09220.1; AT5G09220.1; AT5G09220.
KEGG; ath:AT5G09220; -.
Araport; AT5G09220; -.
TAIR; locus:2184707; AT5G09220.
eggNOG; KOG1303; Eukaryota.
eggNOG; COG0814; LUCA.
HOGENOM; HOG000238530; -.
InParanoid; Q38967; -.
OMA; ERYPDND; -.
OrthoDB; EOG09360984; -.
PhylomeDB; Q38967; -.
SABIO-RK; Q38967; -.
PRO; PR:Q38967; -.
Proteomes; UP000006548; Chromosome 5.
ExpressionAtlas; Q38967; baseline and differential.
Genevisible; Q38967; AT.
GO; GO:0005887; C:integral component of plasma membrane; TAS:TAIR.
GO; GO:0015293; F:symporter activity; IEA:UniProtKB-KW.
GO; GO:0015800; P:acidic amino acid transport; IDA:TAIR.
GO; GO:0015804; P:neutral amino acid transport; IDA: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 1 493 Amino acid permease 2.
/FTId=PRO_0000387500.
TOPO_DOM 1 49 Cytoplasmic. {ECO:0000305}.
TRANSMEM 50 70 Helical. {ECO:0000255}.
TRANSMEM 71 91 Helical. {ECO:0000255}.
TOPO_DOM 92 138 Cytoplasmic. {ECO:0000305}.
TRANSMEM 139 159 Helical. {ECO:0000255}.
TOPO_DOM 160 175 Extracellular. {ECO:0000305}.
TRANSMEM 176 196 Helical. {ECO:0000255}.
TOPO_DOM 197 200 Cytoplasmic. {ECO:0000305}.
TRANSMEM 201 221 Helical. {ECO:0000255}.
TOPO_DOM 222 253 Extracellular. {ECO:0000305}.
TRANSMEM 254 274 Helical. {ECO:0000255}.
TOPO_DOM 275 293 Cytoplasmic. {ECO:0000305}.
TRANSMEM 294 314 Helical. {ECO:0000255}.
TOPO_DOM 315 340 Extracellular. {ECO:0000305}.
TRANSMEM 341 361 Helical. {ECO:0000255}.
TOPO_DOM 362 396 Cytoplasmic. {ECO:0000305}.
TRANSMEM 397 417 Helical. {ECO:0000255}.
TOPO_DOM 418 419 Extracellular. {ECO:0000305}.
TRANSMEM 420 440 Helical. {ECO:0000255}.
TOPO_DOM 441 458 Cytoplasmic. {ECO:0000305}.
TRANSMEM 459 479 Helical. {ECO:0000255}.
TOPO_DOM 480 493 Extracellular. {ECO:0000305}.
COMPBIAS 10 18 His-rich.
CONFLICT 143 143 G -> V (in Ref. 5; AAM61227).
{ECO:0000305}.
CONFLICT 461 461 S -> T (in Ref. 5; AAM61227).
{ECO:0000305}.
SEQUENCE 493 AA; 54147 MW; 7CA882E3E011C5C3 CRC64;
MGETAAANNH RHHHHHGHQV FDVASHDFVP PQPAFKCFDD DGRLKRTGTV WTASAHIITA
VIGSGVLSLA WAIAQLGWIA GPAVMLLFSL VTLYSSTLLS DCYRTGDAVS GKRNYTYMDA
VRSILGGFKF KICGLIQYLN LFGIAIGYTI AASISMMAIK RSNCFHKSGG KDPCHMSSNP
YMIVFGVAEI LLSQVPDFDQ IWWISIVAAV MSFTYSAIGL ALGIVQVAAN GVFKGSLTGI
SIGTVTQTQK IWRTFQALGD IAFAYSYSVV LIEIQDTVRS PPAESKTMKK ATKISIAVTT
IFYMLCGSMG YAAFGDAAPG NLLTGFGFYN PFWLLDIANA AIVVHLVGAY QVFAQPIFAF
IEKSVAERYP DNDFLSKEFE IRIPGFKSPY KVNVFRMVYR SGFVVTTTVI SMLMPFFNDV
VGILGALGFW PLTVYFPVEM YIKQRKVEKW STRWVCLQML SVACLVISVV AGVGSIAGVM
LDLKVYKPFK STY


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