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 03-AUG-2022, entry version 103.
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};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
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.AT1G44100.1; -.
DR iPTMnet; Q8GUM3; -.
DR PaxDb; Q8GUM3; -.
DR PRIDE; Q8GUM3; -.
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; locus:2205876; AT1G44100.
DR eggNOG; KOG1303; Eukaryota.
DR HOGENOM; CLU_031247_4_1_1; -.
DR InParanoid; Q8GUM3; -.
DR OMA; NVYMIAF; -.
DR OrthoDB; 570025at2759; -.
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: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:0015171; F:amino acid transmembrane transporter activity; IBA:GO_Central.
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:0003333; P:amino acid transmembrane transport; IBA:GO_Central.
DR GO; GO:0015802; P:basic amino acid transport; IBA:GO_Central.
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..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
