AAP3_ARATH
ID AAP3_ARATH Reviewed; 476 AA.
AC Q39134; Q8LE75;
DT 03-NOV-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1999, sequence version 2.
DT 03-AUG-2022, entry version 120.
DE RecName: Full=Amino acid permease 3;
DE AltName: Full=Amino acid transporter AAP3;
GN Name=AAP3; OrderedLocusNames=At1g77380; ORFNames=F2P24.9;
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, AND TISSUE
RP 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 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 BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=10359089; DOI=10.1016/s0014-5793(99)00516-5;
RA Breitkreuz K.E., Shelp B.J., Fischer W.-N., Schwacke R., Rentsch D.;
RT "Identification and characterization of GABA, proline and quaternary
RT ammonium compound transporters from Arabidopsis thaliana.";
RL FEBS Lett. 450:280-284(1999).
RN [7]
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 [8]
RP TISSUE SPECIFICITY, SUBCELLULAR LOCATION, REGULATION, AND DISRUPTION
RP PHENOTYPE.
RX PubMed=15361541; DOI=10.1093/jxb/erh233;
RA Okumoto S., Koch W., Tegeder M., Fischer W.-N., Biehl A., Leister D.,
RA Stierhof Y.D., Frommer W.B.;
RT "Root phloem-specific expression of the plasma membrane amino acid proton
RT co-transporter AAP3.";
RL J. Exp. Bot. 55:2155-2168(2004).
RN [9]
RP 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 GABA, tryptophan and both neutral and basic
CC amino acids. High affinity transport of cationic amino acids.
CC {ECO:0000269|PubMed:7608199}.
CC -!- ACTIVITY REGULATION: Inhibited by carbonylcyanide m-
CC chlorophenylhydrazone and 2,4-dinitrophenol.
CC {ECO:0000269|PubMed:7608199}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=12.9 mM for GABA {ECO:0000269|PubMed:10359089};
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:15361541}.
CC Nucleus membrane {ECO:0000269|PubMed:15361541}. Endomembrane system
CC {ECO:0000269|PubMed:15361541}. Note=Not found in vacuole membrane.
CC -!- TISSUE SPECIFICITY: Expressed in the root phloem. Detected in stamens,
CC in cotyledons, and in major veins of mature leaves.
CC {ECO:0000269|PubMed:15361541, ECO:0000269|PubMed:7608199}.
CC -!- DEVELOPMENTAL STAGE: Induced in the connective tissue of stamens
CC shortly before dehiscence.
CC -!- DISRUPTION PHENOTYPE: No visible phenotype.
CC {ECO:0000269|PubMed:15361541, ECO:0000269|PubMed:18681934}.
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; X77499; CAA54630.1; -; mRNA.
DR EMBL; AC078898; AAG29203.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE35971.1; -; Genomic_DNA.
DR EMBL; AY099788; AAM20639.1; -; mRNA.
DR EMBL; AY128905; AAM91305.1; -; mRNA.
DR EMBL; AY085581; AAM62803.1; -; mRNA.
DR PIR; H96802; H96802.
DR RefSeq; NP_177862.1; NM_106387.3.
DR AlphaFoldDB; Q39134; -.
DR BioGRID; 29293; 32.
DR IntAct; Q39134; 32.
DR STRING; 3702.AT1G77380.1; -.
DR TCDB; 2.A.18.2.3; the amino acid/auxin permease (aaap) family.
DR PaxDb; Q39134; -.
DR PRIDE; Q39134; -.
DR ProteomicsDB; 244544; -.
DR EnsemblPlants; AT1G77380.1; AT1G77380.1; AT1G77380.
DR GeneID; 844074; -.
DR Gramene; AT1G77380.1; AT1G77380.1; AT1G77380.
DR KEGG; ath:AT1G77380; -.
DR Araport; AT1G77380; -.
DR TAIR; locus:2031402; AT1G77380.
DR eggNOG; KOG1303; Eukaryota.
DR HOGENOM; CLU_031247_4_1_1; -.
DR InParanoid; Q39134; -.
DR OMA; DAGRLMF; -.
DR OrthoDB; 570025at2759; -.
DR PhylomeDB; Q39134; -.
DR PRO; PR:Q39134; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q39134; baseline and differential.
DR Genevisible; Q39134; 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:0031965; C:nuclear membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0015171; F:amino acid transmembrane transporter activity; ISS:TAIR.
DR GO; GO:0015174; F:basic amino acid transmembrane transporter activity; IBA:GO_Central.
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; IDA:TAIR.
DR GO; GO:0006952; P:defense response; IEP: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; Nucleus; Reference proteome;
KW Symport; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..476
FT /note="Amino acid permease 3"
FT /id="PRO_0000387501"
FT TOPO_DOM 1..33
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 34..54
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 55..57
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 58..78
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 79..122
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 123..143
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 144..166
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 167..187
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 188..208
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 209..277
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 278..298
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 299..300
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 301..321
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 322..324
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 325..345
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 346..384
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 385..405
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 406..426
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 427..441
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 442..462
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 463..476
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT CONFLICT 74
FT /note="A -> V (in Ref. 5; AAM62803)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 476 AA; 52037 MW; FEC8C42037804F67 CRC64;
MVQNHQTVLA VDMPQTGGSK YLDDDGKNKR TGSVWTASAH IITAVIGSGV LSLAWATAQL
GWLAGPVVML LFSAVTYFTS SLLAACYRSG DPISGKRNYT YMDAVRSNLG GVKVTLCGIV
QYLNIFGVAI GYTIASAISM MAIKRSNCFH KSGGKDPCHM NSNPYMIAFG LVQILFSQIP
DFDQLWWLSI LAAVMSFTYS SAGLALGIAQ VVVNGKVKGS LTGISIGAVT ETQKIWRTFQ
ALGDIAFAYS YSIILIEIQD TVKSPPSEEK TMKKATLVSV SVTTMFYMLC GCMGYAAFGD
LSPGNLLTGF GFYNPYWLLD IANAAIVIHL IGAYQVYCQP LFAFIEKQAS IQFPDSEFIA
KDIKIPIPGF KPLRLNVFRL IWRTVFVIIT TVISMLLPFF NDVVGLLGAL GFWPLTVYFP
VEMYIAQKKI PRWSTRWVCL QVFSLGCLVV SIAAAAGSIA GVLLDLKSYK PFRSEY
