AAP1_ARATH
ID AAP1_ARATH Reviewed; 485 AA.
AC Q42400; O48546;
DT 03-NOV-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 128.
DE RecName: Full=Amino acid permease 1;
DE AltName: Full=Amino acid transporter AAP1;
DE AltName: Full=Neutral amino acid transporter II;
GN Name=AAP1; Synonyms=NAT2; OrderedLocusNames=At1g58360;
GN ORFNames=F19C14.3, ZCF54;
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 [GENOMIC DNA / MRNA], FUNCTION, AND BIOPHYSICOCHEMICAL
RP PROPERTIES.
RX PubMed=8356039; DOI=10.1073/pnas.90.16.7441;
RA Hsu L.-C., Chiou T.-J., Chen L., Bush D.R.;
RT "Cloning a plant amino acid transporter by functional complementation of a
RT yeast amino acid transport mutant.";
RL Proc. Natl. Acad. Sci. U.S.A. 90:7441-7445(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=8327465; DOI=10.1073/pnas.90.13.5944;
RA Frommer W.B., Hummel S., Riesmeier J.W.;
RT "Expression cloning in yeast of a cDNA encoding a broad specificity amino
RT acid permease from Arabidopsis thaliana.";
RL Proc. Natl. Acad. Sci. U.S.A. 90:5944-5948(1993).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=10548732; DOI=10.1016/s0378-1119(99)00403-5;
RA Kato A., Suzuki M., Kuwahara A., Ooe H., Higano-Inaba K., Komeda Y.;
RT "Isolation and analysis of cDNA within a 300 kb Arabidopsis thaliana
RT genomic region located around the 100 map unit of chromosome 1.";
RL Gene 239:309-316(1999).
RN [4]
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 [5]
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 [6]
RP FUNCTION, 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 CHARACTERIZATION.
RX PubMed=8567681; DOI=10.1074/jbc.271.4.2213;
RA Boorer K.J., Frommer W.B., Bush D.R., Kreman M., Loo D.D.F., Wright E.M.;
RT "Kinetics and specificity of a H+/amino acid transporter from Arabidopsis
RT thaliana.";
RL J. Biol. Chem. 271:2213-2220(1996).
RN [9]
RP TOPOLOGY.
RX PubMed=9374550; DOI=10.1074/jbc.272.48.30552;
RA Chang H.-C., Bush D.R.;
RT "Topology of NAT2, a prototypical example of a new family of amino acid
RT transporters.";
RL J. Biol. Chem. 272:30552-30557(1997).
RN [10]
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 [11]
RP BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=12244056; DOI=10.1074/jbc.m207730200;
RA Okumoto S., Schmidt R., Tegeder M., Fischer W.-N., Rentsch D.,
RA Frommer W.B., Koch W.;
RT "High affinity amino acid transporters specifically expressed in xylem
RT parenchyma and developing seeds of Arabidopsis.";
RL J. Biol. Chem. 277:45338-45346(2002).
RN [12]
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 [13]
RP FUNCTION, TISSUE SPECIFICITY, AND SUBCELLULAR LOCATION.
RX PubMed=17419840; DOI=10.1111/j.1365-313x.2007.03045.x;
RA Lee Y.-H., Foster J., Chen J., Voll L.M., Weber A.P.M., Tegeder M.;
RT "AAP1 transports uncharged amino acids into roots of Arabidopsis.";
RL Plant J. 50:305-319(2007).
RN [14]
RP FUNCTION, TISSUE SPECIFICITY, AND DISRUPTION PHENOTYPE.
RX PubMed=19392706; DOI=10.1111/j.1365-313x.2009.03890.x;
RA Sanders A., Collier R., Trethewy A., Gould G., Sieker R., Tegeder M.;
RT "AAP1 regulates import of amino acids into developing Arabidopsis
RT embryos.";
RL Plant J. 59:540-552(2009).
CC -!- FUNCTION: Amino acid-proton symporter. Stereospecific transporter with
CC a broad specificity for histidine, glutamate and neutral amino acids.
CC Reduced affinities for asparagine and valine. Involved in amino acid
CC uptake from the apoplastic cavity into the embryo cells for storage
CC protein accumulation and in root amino acid uptake.
CC {ECO:0000269|PubMed:17419840, ECO:0000269|PubMed:19392706,
CC ECO:0000269|PubMed:7608199, ECO:0000269|PubMed:8281191,
CC ECO:0000269|PubMed:8327465, ECO:0000269|PubMed:8356039}.
CC -!- ACTIVITY REGULATION: Inhibited by carbonylcyanide m-
CC chlorophenylhydrazone and diethylpyrocarbonate (DEPC).
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=292 uM for alanine {ECO:0000269|PubMed:12244056,
CC ECO:0000269|PubMed:8327465, ECO:0000269|PubMed:8356039};
CC KM=60 uM for L-proline {ECO:0000269|PubMed:12244056,
CC ECO:0000269|PubMed:8327465, ECO:0000269|PubMed:8356039};
CC KM=774 uM for aspartate {ECO:0000269|PubMed:12244056,
CC ECO:0000269|PubMed:8327465, ECO:0000269|PubMed:8356039};
CC Vmax=0.644 nmol/min/mg enzyme toward aspartate
CC {ECO:0000269|PubMed:12244056, ECO:0000269|PubMed:8327465,
CC ECO:0000269|PubMed:8356039};
CC pH dependence:
CC Optimum pH is acidic. {ECO:0000269|PubMed:12244056,
CC ECO:0000269|PubMed:8327465, ECO:0000269|PubMed:8356039};
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:17419840};
CC Multi-pass membrane protein {ECO:0000269|PubMed:17419840}.
CC -!- TISSUE SPECIFICITY: Highly expressed in developing pods. Found in the
CC endosperm and in the storage parenchyma and the outer epidermis cells
CC of the developing embryo. Lower levels of expression in flowers, in the
CC vascular system of the cotyledon and in the root epidermal cells,
CC including root hairs and throughout the root tip.
CC {ECO:0000269|PubMed:17419840, ECO:0000269|PubMed:19392706,
CC ECO:0000269|PubMed:7608199, ECO:0000269|PubMed:8281191,
CC ECO:0000269|PubMed:9675899}.
CC -!- DEVELOPMENTAL STAGE: Expressed in endosperm during early stages of seed
CC development. Strongly induced at heart stage of embryogenesis.
CC {ECO:0000269|PubMed:9675899}.
CC -!- DISRUPTION PHENOTYPE: No effect on plant growth or seed germination,
CC but reduced seed weight and total seed yield. Resistant to toxic
CC concentrations of amino acids in the growth medium.
CC {ECO:0000269|PubMed:19392706}.
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; L16240; AAA32726.1; -; mRNA.
DR EMBL; AF031649; AAB87674.1; -; Genomic_DNA.
DR EMBL; X67124; CAA47603.1; -; mRNA.
DR EMBL; AB077822; BAB83868.1; -; Genomic_DNA.
DR EMBL; AC008051; AAF82252.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE33541.1; -; Genomic_DNA.
DR PIR; A48187; A48187.
DR RefSeq; NP_176132.1; NM_104616.5.
DR AlphaFoldDB; Q42400; -.
DR STRING; 3702.AT1G58360.1; -.
DR TCDB; 2.A.18.2.1; the amino acid/auxin permease (aaap) family.
DR PaxDb; Q42400; -.
DR PRIDE; Q42400; -.
DR ProteomicsDB; 244335; -.
DR EnsemblPlants; AT1G58360.1; AT1G58360.1; AT1G58360.
DR GeneID; 842205; -.
DR Gramene; AT1G58360.1; AT1G58360.1; AT1G58360.
DR KEGG; ath:AT1G58360; -.
DR Araport; AT1G58360; -.
DR TAIR; locus:2016600; AT1G58360.
DR eggNOG; KOG1303; Eukaryota.
DR HOGENOM; CLU_031247_4_1_1; -.
DR InParanoid; Q42400; -.
DR OMA; AVGKSNC; -.
DR OrthoDB; 570025at2759; -.
DR PhylomeDB; Q42400; -.
DR BioCyc; MetaCyc:AT1G58360-MON; -.
DR SABIO-RK; Q42400; -.
DR PRO; PR:Q42400; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q42400; baseline and differential.
DR Genevisible; Q42400; 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; IDA:TAIR.
DR GO; GO:0015172; F:acidic amino acid transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0015171; F:amino acid transmembrane transporter activity; IMP:TAIR.
DR GO; GO:0015180; F:L-alanine transmembrane transporter activity; IMP:TAIR.
DR GO; GO:0005313; F:L-glutamate transmembrane transporter activity; IMP:TAIR.
DR GO; GO:0015186; F:L-glutamine transmembrane transporter activity; IMP:TAIR.
DR GO; GO:0015193; F:L-proline transmembrane transporter activity; IMP:TAIR.
DR GO; GO:0015194; F:L-serine transmembrane transporter activity; IMP:TAIR.
DR GO; GO:0015175; F:neutral 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; IBA:GO_Central.
DR GO; GO:0043090; P:amino acid import; IMP:TAIR.
DR GO; GO:0003333; P:amino acid transmembrane transport; IBA:GO_Central.
DR GO; GO:0015808; P:L-alanine transport; IMP:TAIR.
DR GO; GO:0098712; P:L-glutamate import across plasma membrane; IMP:TAIR.
DR GO; GO:0015804; P:neutral amino acid transport; IBA:GO_Central.
DR GO; GO:0009624; P:response to nematode; HEP: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..485
FT /note="Amino acid permease 1"
FT /id="PRO_0000387499"
FT TOPO_DOM 1..40
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:9374550"
FT TRANSMEM 41..61
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 62..82
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 83..129
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305|PubMed:9374550"
FT TRANSMEM 130..150
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 151..166
FT /note="Extracellular"
FT /evidence="ECO:0000305|PubMed:9374550"
FT TRANSMEM 167..187
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 188..194
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305|PubMed:9374550"
FT TRANSMEM 195..215
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 216..245
FT /note="Extracellular"
FT /evidence="ECO:0000305|PubMed:9374550"
FT TRANSMEM 246..266
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 267..285
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305|PubMed:9374550"
FT TRANSMEM 286..306
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 307..318
FT /note="Extracellular"
FT /evidence="ECO:0000305|PubMed:9374550"
FT TRANSMEM 319..339
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 340..394
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305|PubMed:9374550"
FT TRANSMEM 395..415
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 416..436
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 437..450
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305|PubMed:9374550"
FT TRANSMEM 451..471
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 472..485
FT /note="Extracellular"
FT /evidence="ECO:0000269|PubMed:9374550"
FT REGION 1..35
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..23
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 252
FT /note="D -> Y (in Ref. 1; AAB87674)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 485 AA; 52895 MW; 722E3895937CCC5B CRC64;
MKSFNTEGHN HSTAESGDAY TVSDPTKNVD EDGREKRTGT WLTASAHIIT AVIGSGVLSL
AWAIAQLGWI AGTSILLIFS FITYFTSTML ADCYRAPDPV TGKRNYTYMD VVRSYLGGRK
VQLCGVAQYG NLIGVTVGYT ITASISLVAV GKSNCFHDKG HTADCTISNY PYMAVFGIIQ
VILSQIPNFH KLSFLSIMAA VMSFTYATIG IGLAIATVAG GKVGKTSMTG TAVGVDVTAA
QKIWRSFQAV GDIAFAYAYA TVLIEIQDTL RSSPAENKAM KRASLVGVST TTFFYILCGC
IGYAAFGNNA PGDFLTDFGF FEPFWLIDFA NACIAVHLIG AYQVFAQPIF QFVEKKCNRN
YPDNKFITSE YSVNVPFLGK FNISLFRLVW RTAYVVITTV VAMIFPFFNA ILGLIGAASF
WPLTVYFPVE MHIAQTKIKK YSARWIALKT MCYVCLIVSL LAAAGSIAGL ISSVKTYKPF
RTMHE
