AAP2_ARATH
ID AAP2_ARATH Reviewed; 493 AA.
AC Q38967; Q8LFS8;
DT 03-NOV-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 119.
DE RecName: Full=Amino acid permease 2;
DE AltName: Full=Amino acid transporter AAP2;
GN Name=AAP2; OrderedLocusNames=At5g09220; ORFNames=T2K12.6, T5E8.20;
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].
RC STRAIN=cv. Landsberg erecta;
RX PubMed=8618839; DOI=10.1073/pnas.92.26.12036;
RA Frommer W.B., Hummel S., Unseld M., Ninnemann O.;
RT "Seed and vascular expression of a high-affinity transporter for cationic
RT amino acids in Arabidopsis.";
RL Proc. Natl. Acad. Sci. U.S.A. 92:12036-12040(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130714; DOI=10.1038/35048507;
RA Tabata S., Kaneko T., Nakamura Y., Kotani H., Kato T., Asamizu E.,
RA Miyajima N., Sasamoto S., Kimura T., Hosouchi T., Kawashima K., Kohara M.,
RA Matsumoto M., Matsuno A., Muraki A., Nakayama S., Nakazaki N., Naruo K.,
RA Okumura S., Shinpo S., Takeuchi C., Wada T., Watanabe A., Yamada M.,
RA Yasuda M., Sato S., de la Bastide M., Huang E., Spiegel L., Gnoj L.,
RA O'Shaughnessy A., Preston R., Habermann K., Murray J., Johnson D.,
RA Rohlfing T., Nelson J., Stoneking T., Pepin K., Spieth J., Sekhon M.,
RA Armstrong J., Becker M., Belter E., Cordum H., Cordes M., Courtney L.,
RA Courtney W., Dante M., Du H., Edwards J., Fryman J., Haakensen B.,
RA Lamar E., Latreille P., Leonard S., Meyer R., Mulvaney E., Ozersky P.,
RA Riley A., Strowmatt C., Wagner-McPherson C., Wollam A., Yoakum M., Bell M.,
RA Dedhia N., Parnell L., Shah R., Rodriguez M., Hoon See L., Vil D.,
RA Baker J., Kirchoff K., Toth K., King L., Bahret A., Miller B., Marra M.A.,
RA Martienssen R., McCombie W.R., Wilson R.K., Murphy G., Bancroft I.,
RA Volckaert G., Wambutt R., Duesterhoeft A., Stiekema W., Pohl T.,
RA Entian K.-D., Terryn N., Hartley N., Bent E., Johnson S., Langham S.-A.,
RA McCullagh B., Robben J., Grymonprez B., Zimmermann W., Ramsperger U.,
RA Wedler H., Balke K., Wedler E., Peters S., van Staveren M., Dirkse W.,
RA Mooijman P., Klein Lankhorst R., Weitzenegger T., Bothe G., Rose M.,
RA Hauf J., Berneiser S., Hempel S., Feldpausch M., Lamberth S.,
RA Villarroel R., Gielen J., Ardiles W., Bents O., Lemcke K., Kolesov G.,
RA Mayer K.F.X., Rudd S., Schoof H., Schueller C., Zaccaria P., Mewes H.-W.,
RA Bevan M., Fransz P.F.;
RT "Sequence and analysis of chromosome 5 of the plant Arabidopsis thaliana.";
RL Nature 408:823-826(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;
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 FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, AND TISSUE SPECIFICITY.
RX PubMed=8281191; DOI=10.1046/j.1365-313x.1993.04060993.x;
RA Kwart M., Hirner B., Hummel S., Frommer W.B.;
RT "Differential expression of two related amino acid transporters with
RT differing substrate specificity in Arabidopsis thaliana.";
RL Plant J. 4:993-1002(1993).
RN [7]
RP FUNCTION, AND TISSUE SPECIFICITY.
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 [8]
RP DEVELOPMENTAL STAGE, AND TISSUE SPECIFICITY.
RX PubMed=9675899; DOI=10.1046/j.1365-313x.1998.00151.x;
RA Hirner B., Fischer W.-N., Rentsch D., Kwart M., Frommer W.B.;
RT "Developmental control of H+/amino acid permease gene expression during
RT seed development of Arabidopsis.";
RL Plant J. 14:535-544(1998).
RN [9]
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 histidine, arginine, glutamate and neutral
CC amino acids, favoring small amino acids such as alanine, asparagine and
CC glutamine. Accepts also large aromatic residues such as in phenlalanine
CC or tyrosine. Has a much higher affinity for basic amino acids as
CC compared with AAP1. May function in xylem-to-phloem transfer and in
CC uptake of amino acids assimilated in the green silique tissue.
CC {ECO:0000269|PubMed:7608199, ECO:0000269|PubMed:8281191}.
CC -!- ACTIVITY REGULATION: Inhibited by diethylpyrocarbonate (DEPC).
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=140 uM for L-proline {ECO:0000269|PubMed:8281191};
CC pH dependence:
CC Optimum pH is acidic. {ECO:0000269|PubMed:8281191};
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass membrane
CC protein {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Highly expressed in developing pods. Found in the
CC vascular strands of siliques, cotyledons, leaves and roots, in the
CC inner phloem of stems, and in the funiculi. Lower levels of expression
CC in flowers. Not expressed in seeds. {ECO:0000269|PubMed:7608199,
CC ECO:0000269|PubMed:8281191, ECO:0000269|PubMed:9675899}.
CC -!- DEVELOPMENTAL STAGE: Strongly induced at heart stage of embryogenesis.
CC {ECO:0000269|PubMed:9675899}.
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; X71787; CAA50672.1; -; mRNA.
DR EMBL; AL391712; CAC05448.1; -; Genomic_DNA.
DR EMBL; CP002688; AED91352.1; -; Genomic_DNA.
DR EMBL; AY090341; AAL91247.1; -; mRNA.
DR EMBL; AY084665; AAM61227.1; -; mRNA.
DR PIR; S52421; S52421.
DR RefSeq; NP_196484.1; NM_120958.3.
DR AlphaFoldDB; Q38967; -.
DR STRING; 3702.AT5G09220.1; -.
DR TCDB; 2.A.18.2.7; the amino acid/auxin permease (aaap) family.
DR iPTMnet; Q38967; -.
DR PaxDb; Q38967; -.
DR PRIDE; Q38967; -.
DR ProteomicsDB; 244390; -.
DR EnsemblPlants; AT5G09220.1; AT5G09220.1; AT5G09220.
DR GeneID; 830781; -.
DR Gramene; AT5G09220.1; AT5G09220.1; AT5G09220.
DR KEGG; ath:AT5G09220; -.
DR Araport; AT5G09220; -.
DR TAIR; locus:2184707; AT5G09220.
DR eggNOG; KOG1303; Eukaryota.
DR HOGENOM; CLU_031247_4_1_1; -.
DR InParanoid; Q38967; -.
DR OMA; MSENNNQ; -.
DR OrthoDB; 570025at2759; -.
DR PhylomeDB; Q38967; -.
DR SABIO-RK; Q38967; -.
DR PRO; PR:Q38967; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q38967; baseline and differential.
DR Genevisible; Q38967; AT.
DR GO; GO:0005887; C:integral component of plasma membrane; TAS:TAIR.
DR GO; GO:0016020; C:membrane; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; IDA:TAIR.
DR GO; GO:0015171; F:amino acid transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0015293; F:symporter activity; IEA:UniProtKB-KW.
DR GO; GO:0015800; P:acidic amino acid transport; IDA:TAIR.
DR GO; GO:0003333; P:amino acid transmembrane transport; IBA:GO_Central.
DR GO; GO:0006865; P:amino acid transport; IMP:TAIR.
DR GO; GO:0015804; P:neutral amino acid transport; IDA:TAIR.
DR GO; GO:0110126; P:phloem loading; IMP: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..493
FT /note="Amino acid permease 2"
FT /id="PRO_0000387500"
FT TOPO_DOM 1..49
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 50..70
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 71..91
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 92..138
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 139..159
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 160..175
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 176..196
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 197..200
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 201..221
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 222..253
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 254..274
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 275..293
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 294..314
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 315..340
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 341..361
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 362..396
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 397..417
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 418..419
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 420..440
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 441..458
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 459..479
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 480..493
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT CONFLICT 143
FT /note="G -> V (in Ref. 5; AAM61227)"
FT /evidence="ECO:0000305"
FT CONFLICT 461
FT /note="S -> T (in Ref. 5; AAM61227)"
FT /evidence="ECO:0000305"
SQ 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
