AMT2_ARATH
ID AMT2_ARATH Reviewed; 475 AA.
AC Q9M6N7; Q1JPN2;
DT 26-JUL-2002, integrated into UniProtKB/Swiss-Prot.
DT 24-MAY-2004, sequence version 2.
DT 03-AUG-2022, entry version 140.
DE RecName: Full=Ammonium transporter 2;
DE Short=AtAMT2;
GN Name=AMT2; OrderedLocusNames=At2g38290; ORFNames=F16M14.22;
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] (ISOFORM 1), AND CHARACTERIZATION.
RC STRAIN=cv. C24; TISSUE=Root;
RX PubMed=10675553; DOI=10.1016/s0014-5793(00)01153-4;
RA Sohlenkamp C., Shelden M.C., Howitt S.M., Udvardi M.K.;
RT "Characterization of Arabidopsis AtAMT2, a novel ammonium transporter in
RT plants.";
RL FEBS Lett. 467:273-278(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10617197; DOI=10.1038/45471;
RA Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D.,
RA Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V.,
RA Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S.,
RA Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J.,
RA Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M.,
RA Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O.,
RA Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.;
RT "Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana.";
RL Nature 402:761-768(1999).
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] (ISOFORM 1).
RC STRAIN=cv. Columbia;
RA Shinn P., Chen H., Kim C.J., Quinitio C., Ecker J.R.;
RT "Arabidopsis ORF clones.";
RL Submitted (MAY-2006) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=cv. Columbia;
RA Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
RA Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
RA Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
RA Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y.,
RA Shinozaki K.;
RT "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC STRAIN=cv. Columbia;
RX PubMed=14993207; DOI=10.1101/gr.1515604;
RA Castelli V., Aury J.-M., Jaillon O., Wincker P., Clepet C., Menard M.,
RA Cruaud C., Quetier F., Scarpelli C., Schaechter V., Temple G., Caboche M.,
RA Weissenbach J., Salanoubat M.;
RT "Whole genome sequence comparisons and 'full-length' cDNA sequences: a
RT combined approach to evaluate and improve Arabidopsis genome annotation.";
RL Genome Res. 14:406-413(2004).
RN [7]
RP FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, SUBCELLULAR LOCATION, TISSUE
RP SPECIFICITY, AND INDUCTION.
RX PubMed=12481062; DOI=10.1104/pp.008599;
RA Sohlenkamp C., Wood C.C., Roeb G.W., Udvardi M.K.;
RT "Characterization of Arabidopsis AtAMT2, a high-affinity ammonium
RT transporter of the plasma membrane.";
RL Plant Physiol. 130:1788-1796(2002).
CC -!- FUNCTION: High affinity ammonium transporter that may play an important
CC role in moving ammonium between the apoplast and symplast of cells
CC throughout the plant. Does not transport methylammonium.
CC {ECO:0000269|PubMed:12481062}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=21 uM for ammonium chloride (at external pH 6.1)
CC {ECO:0000269|PubMed:12481062};
CC Note=Measured in yeast knockout mutant YCW012.;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:12481062};
CC Multi-pass membrane protein {ECO:0000269|PubMed:12481062}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9M6N7-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9M6N7-2; Sequence=VSP_038202;
CC -!- TISSUE SPECIFICITY: Higher expression in shoots than roots.
CC {ECO:0000269|PubMed:12481062}.
CC -!- INDUCTION: By nitrogen deprivation in roots.
CC {ECO:0000269|PubMed:12481062}.
CC -!- SIMILARITY: Belongs to the ammonia transporter channel (TC 1.A.11.2)
CC family. {ECO:0000305}.
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DR EMBL; AF182039; AAF37192.1; -; mRNA.
DR EMBL; AC003028; AAM14857.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC09518.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC09519.1; -; Genomic_DNA.
DR EMBL; BT025321; ABF57277.1; -; mRNA.
DR EMBL; AK226212; BAE98377.1; -; mRNA.
DR EMBL; BX819203; -; NOT_ANNOTATED_CDS; mRNA.
DR PIR; T01260; T01260.
DR RefSeq; NP_181363.1; NM_129385.5. [Q9M6N7-1]
DR RefSeq; NP_973634.1; NM_201905.1. [Q9M6N7-2]
DR AlphaFoldDB; Q9M6N7; -.
DR SMR; Q9M6N7; -.
DR BioGRID; 3751; 4.
DR IntAct; Q9M6N7; 4.
DR STRING; 3702.AT2G38290.1; -.
DR TCDB; 1.A.11.2.2; the ammonium transporter channel (amt) family.
DR PaxDb; Q9M6N7; -.
DR PRIDE; Q9M6N7; -.
DR ProteomicsDB; 245053; -. [Q9M6N7-1]
DR EnsemblPlants; AT2G38290.1; AT2G38290.1; AT2G38290. [Q9M6N7-1]
DR EnsemblPlants; AT2G38290.2; AT2G38290.2; AT2G38290. [Q9M6N7-2]
DR GeneID; 818409; -.
DR Gramene; AT2G38290.1; AT2G38290.1; AT2G38290. [Q9M6N7-1]
DR Gramene; AT2G38290.2; AT2G38290.2; AT2G38290. [Q9M6N7-2]
DR KEGG; ath:AT2G38290; -.
DR Araport; AT2G38290; -.
DR TAIR; locus:2042917; AT2G38290.
DR eggNOG; KOG0682; Eukaryota.
DR InParanoid; Q9M6N7; -.
DR OMA; IESPMHE; -.
DR OrthoDB; 910733at2759; -.
DR PhylomeDB; Q9M6N7; -.
DR SABIO-RK; Q9M6N7; -.
DR PRO; PR:Q9M6N7; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; Q9M6N7; baseline and differential.
DR Genevisible; Q9M6N7; AT.
DR GO; GO:0005887; C:integral component of plasma membrane; IEA:InterPro.
DR GO; GO:0005886; C:plasma membrane; IDA:TAIR.
DR GO; GO:0009506; C:plasmodesma; HDA:TAIR.
DR GO; GO:0008519; F:ammonium transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0015398; F:high-affinity secondary active ammonium transmembrane transporter activity; IDA:TAIR.
DR GO; GO:0072488; P:ammonium transmembrane transport; IBA:GO_Central.
DR GO; GO:0009624; P:response to nematode; HEP:TAIR.
DR Gene3D; 1.10.3430.10; -; 1.
DR InterPro; IPR029020; Ammonium/urea_transptr.
DR InterPro; IPR001905; Ammonium_transpt.
DR InterPro; IPR018047; Ammonium_transpt_CS.
DR InterPro; IPR024041; NH4_transpt_AmtB-like_dom.
DR InterPro; IPR002229; RhesusRHD.
DR PANTHER; PTHR43029; PTHR43029; 1.
DR Pfam; PF00909; Ammonium_transp; 1.
DR PRINTS; PR00342; RHESUSRHD.
DR TIGRFAMs; TIGR00836; amt; 1.
DR PROSITE; PS01219; AMMONIUM_TRANSP; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Ammonia transport; Cell membrane; Membrane;
KW Reference proteome; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..475
FT /note="Ammonium transporter 2"
FT /id="PRO_0000139747"
FT TRANSMEM 27..47
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 55..75
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 120..140
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 148..168
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 183..203
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 218..238
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 254..274
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 279..299
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 302..322
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 336..356
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 389..409
FT /note="Helical"
FT /evidence="ECO:0000255"
FT VAR_SEQ 1..116
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14993207"
FT /id="VSP_038202"
FT VARIANT 95
FT /note="D -> N (in strain: cv. C24)"
FT CONFLICT 369
FT /note="P -> L (in Ref. 6; BX819203)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 475 AA; 50768 MW; A4958B0A8D2CAE60 CRC64;
MAGAYDPSLP EVPEWLNKGD NAWQLTAATL VGLQSMPGLV ILYASIVKKK WAVNSAFMAL
YAFAAVLLCW VLLCYKMAFG EELLPFWGKG GPAFDQGYLK GQAKIPNSNV AAPYFPMATL
VYFQFTFAAI TTILVAGSVL GRMNIKAWMA FVPLWLIFSY TVGAYSIWGG GFLYQWGVID
YSGGYVIHLS SGVAGFVAAY WVGPRPKADR ERFPPNNVLL MLAGAGLLWM GWSGFNGGAP
YAANLTSSIA VLNTNLSAAT SLLVWTTLDV IFFGKPSVIG AIQGMVTGLA GVTPGAGLIQ
TWAAIIIGVV SGTAPWASMM IIHKKSALLQ KVDDTLAVFY THAVAGLLGG IMTGLFAHPD
LCVLVLPLPA TRGAFYGGNG GKQLLKQLAG AAFIAVWNVV STTIILLAIR VFIPLRMAEE
ELGIGDDAAH GEEAYALWGD GEKFDATRHV QQFERDQEAA HPSYVHGARG VTIVL
