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Database: UniProt
Entry: AAP5_ARATH
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Original site: AAP5_ARATH 
ID   AAP5_ARATH              Reviewed;         480 AA.
AC   Q8GUM3; Q39136; Q9C6Y2;
DT   03-NOV-2009, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   24-JAN-2024, entry version 110.
DE   RecName: Full=Amino acid permease 5;
DE   AltName: Full=Amino acid transporter AAP5;
GN   Name=AAP5; OrderedLocusNames=At1g44100; ORFNames=T7O23.19;
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=11130712; DOI=10.1038/35048500;
RA   Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA   Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA   Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA   Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA   Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA   Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA   Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA   Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA   Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA   Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA   Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA   Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA   Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA   Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA   Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT   "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL   Nature 408:816-820(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   CHARACTERIZATION.
RX   PubMed=9148914; DOI=10.1074/jbc.272.20.13040;
RA   Boorer K.J., Fischer W.-N.;
RT   "Specificity and stoichiometry of the Arabidopsis H+/amino acid transporter
RT   AAP5.";
RL   J. Biol. Chem. 272:13040-13046(1997).
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   FUNCTION, AND DISRUPTION PHENOTYPE.
RX   PubMed=18681934; DOI=10.1111/j.1469-8137.2008.02589.x;
RA   Svennerstam H., Ganeteg U., Naesholm T.;
RT   "Root uptake of cationic amino acids by Arabidopsis depends on functional
RT   expression of amino acid permease 5.";
RL   New Phytol. 180:620-630(2008).
CC   -!- FUNCTION: Amino acid-proton symporter. Stereospecific transporter with
CC       a broad specificity for glutamate and both neutral and basic amino
CC       acids. Reduced affinities for asparagine and valine. High affinity
CC       transport of the cationic amino acids arginine and lysine, but not of
CC       histidine. {ECO:0000269|PubMed:18681934, 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, roots, siliques and
CC       flowers. {ECO:0000269|PubMed:7608199}.
CC   -!- DEVELOPMENTAL STAGE: High expression in source leaves, but almost
CC       undetected in sink leaves. {ECO:0000269|PubMed:7608199}.
CC   -!- DISRUPTION PHENOTYPE: No visible phenotype, but decreased uptake of L-
CC       arginine and L-lysine. {ECO:0000269|PubMed:18681934}.
CC   -!- MISCELLANEOUS: Basic amino acids are transported in their fully ionized
CC       form.
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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAG50558.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR   EMBL; X77501; CAA54632.1; -; mRNA.
DR   EMBL; AC074228; AAG50558.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; CP002684; AEE32020.1; -; Genomic_DNA.
DR   EMBL; BT002389; AAO00749.1; -; mRNA.
DR   EMBL; BT009680; AAP81798.1; -; mRNA.
DR   PIR; C57479; C57479.
DR   PIR; C96505; C96505.
DR   RefSeq; NP_175076.2; NM_103536.4.
DR   AlphaFoldDB; Q8GUM3; -.
DR   BioGRID; 26238; 21.
DR   IntAct; Q8GUM3; 14.
DR   STRING; 3702.Q8GUM3; -.
DR   iPTMnet; Q8GUM3; -.
DR   PaxDb; 3702-AT1G44100-1; -.
DR   ProteomicsDB; 244493; -.
DR   EnsemblPlants; AT1G44100.1; AT1G44100.1; AT1G44100.
DR   GeneID; 841013; -.
DR   Gramene; AT1G44100.1; AT1G44100.1; AT1G44100.
DR   KEGG; ath:AT1G44100; -.
DR   Araport; AT1G44100; -.
DR   TAIR; AT1G44100; AAP5.
DR   eggNOG; KOG1303; Eukaryota.
DR   HOGENOM; CLU_031247_4_1_1; -.
DR   InParanoid; Q8GUM3; -.
DR   OMA; KNVPRWG; -.
DR   OrthoDB; 664343at2759; -.
DR   PhylomeDB; Q8GUM3; -.
DR   PRO; PR:Q8GUM3; -.
DR   Proteomes; UP000006548; Chromosome 1.
DR   ExpressionAtlas; Q8GUM3; baseline and differential.
DR   Genevisible; Q8GUM3; AT.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0015171; F:amino acid transmembrane transporter activity; TAS:TAIR.
DR   GO; GO:0015174; F:basic amino acid transmembrane transporter activity; IDA:TAIR.
DR   GO; GO:0015293; F:symporter activity; IEA:UniProtKB-KW.
DR   GO; GO:0015802; P:basic amino acid transport; TAS:TAIR.
DR   InterPro; IPR013057; AA_transpt_TM.
DR   PANTHER; PTHR48017:SF141; AMINO ACID PERMEASE 5; 1.
DR   PANTHER; PTHR48017; OS05G0424000 PROTEIN-RELATED; 1.
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..480
FT                   /note="Amino acid permease 5"
FT                   /id="PRO_0000387503"
FT   TOPO_DOM        1..31
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        32..52
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        53..73
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        74..120
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        121..141
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        142..157
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        158..178
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        179..182
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        183..203
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        204..241
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        242..262
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        263..280
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        281..301
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        302..328
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        329..349
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        350..383
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        384..404
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        405..406
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        407..427
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        428..445
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        446..466
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        467..480
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   REGION          1..25
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CONFLICT        392
FT                   /note="M -> I (in Ref. 1; CAA54632)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   480 AA;  52538 MW;  097CC58E91183E92 CRC64;
     MVVQNVQDLD VLPKHSSDSF DDDGRPKRTG TVWTASAHII TAVIGSGVLS LAWAVAQIGW
     IGGPVAMLLF SFVTFYTSTL LCSCYRSGDS VTGKRNYTYM DAIHSNLGGI KVKVCGVVQY
     VNLFGTAIGY TIASAISLVA IQRTSCQQMN GPNDPCHVNG NVYMIAFGIV QIIFSQIPDF
     DQLWWLSIVA AVMSFAYSAI GLGLGVSKVV ENKEIKGSLT GVTVGTVTLS GTVTSSQKIW
     RTFQSLGNIA FAYSYSMILI EIQDTVKSPP AEVNTMRKAT FVSVAVTTVF YMLCGCVGYA
     AFGDNAPGNL LAHGGFRNPY WLLDIANLAI VIHLVGAYQV YCQPLFAFVE KEASRRFPES
     EFVTKEIKIQ LFPGKPFNLN LFRLVWRTFF VMTTTLISML MPFFNDVVGL LGAIGFWPLT
     VYFPVEMYIA QKNVPRWGTK WVCLQVLSVT CLFVSVAAAA GSVIGIVSDL KVYKPFQSEF
//
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