AMT13_ARATH
ID AMT13_ARATH Reviewed; 498 AA.
AC Q9SQH9; Q0WSW8; Q9LK15;
DT 26-JUL-2002, integrated into UniProtKB/Swiss-Prot.
DT 26-JUN-2007, sequence version 2.
DT 03-AUG-2022, entry version 138.
DE RecName: Full=Ammonium transporter 1 member 3;
DE Short=AtAMT1;3;
GN Name=AMT1-3; OrderedLocusNames=At3g24300; ORFNames=K7M2.7;
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], AND TISSUE SPECIFICITY.
RC STRAIN=cv. C24; TISSUE=Seed;
RX PubMed=10330477; DOI=10.2307/3870826;
RA Gazzarrini S., Lejay L., Gojon A., Ninnemann O., Frommer W.B.,
RA von Wiren N.;
RT "Three functional transporters for constitutive, diurnally regulated, and
RT starvation-induced uptake of ammonium into Arabidopsis roots.";
RL Plant Cell 11:937-948(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10907853; DOI=10.1093/dnares/7.3.217;
RA Kaneko T., Katoh T., Sato S., Nakamura Y., Asamizu E., Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 3. II. Sequence
RT features of the 4,251,695 bp regions covered by 90 P1, TAC and BAC
RT clones.";
RL DNA Res. 7:217-221(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;
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 [5]
RP FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND INDUCTION.
RX PubMed=17026539; DOI=10.1111/j.1365-313x.2006.02887.x;
RA Loque D., Yuan L., Kojima S., Gojon A., Wirth J., Gazzarrini S.,
RA Ishiyama K., Takahashi H., von Wiren N.;
RT "Additive contribution of AMT1;1 and AMT1;3 to high-affinity ammonium
RT uptake across the plasma membrane of nitrogen-deficient Arabidopsis
RT roots.";
RL Plant J. 48:522-534(2006).
CC -!- FUNCTION: Ammonium transporter probably involved in ammonium uptake
CC from the soil. Contributes with AMT1-1 to the overall ammonium uptake
CC capacity in roots under nitrogen-deficiency conditions.
CC {ECO:0000269|PubMed:17026539}.
CC -!- INTERACTION:
CC Q9SQH9; P54144: AMT1-1; NbExp=3; IntAct=EBI-16716530, EBI-16426081;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:17026539};
CC Multi-pass membrane protein {ECO:0000269|PubMed:17026539}.
CC -!- TISSUE SPECIFICITY: Highly expressed in roots. Expressed in root tips,
CC root hairs, root epidermis, rhizodermis and cortex.
CC {ECO:0000269|PubMed:10330477, ECO:0000269|PubMed:17026539}.
CC -!- INDUCTION: By nitrogen deprivation. Highest expression at the end of
CC the light period. {ECO:0000269|PubMed:17026539}.
CC -!- SIMILARITY: Belongs to the ammonia transporter channel (TC 1.A.11.2)
CC family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAD54638.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AF083035; AAD54638.1; ALT_FRAME; mRNA.
DR EMBL; AP000382; BAB02929.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE76886.1; -; Genomic_DNA.
DR EMBL; AK227798; BAE99780.1; -; mRNA.
DR RefSeq; NP_189073.1; NM_113336.3.
DR AlphaFoldDB; Q9SQH9; -.
DR SMR; Q9SQH9; -.
DR BioGRID; 7350; 229.
DR ComplexPortal; CPX-3581; AMT1-3 homotrimer.
DR ComplexPortal; CPX-3582; AMT1-1 - AMT1-3 heterotrimer, variant 1.
DR ComplexPortal; CPX-3583; AMT1-1 - AMT1-3 heterotrimer, variant 2.
DR IntAct; Q9SQH9; 1.
DR STRING; 3702.AT3G24300.1; -.
DR TCDB; 1.A.11.2.13; the ammonium transporter channel (amt) family.
DR iPTMnet; Q9SQH9; -.
DR PaxDb; Q9SQH9; -.
DR PRIDE; Q9SQH9; -.
DR ProteomicsDB; 245002; -.
DR EnsemblPlants; AT3G24300.1; AT3G24300.1; AT3G24300.
DR GeneID; 822018; -.
DR Gramene; AT3G24300.1; AT3G24300.1; AT3G24300.
DR KEGG; ath:AT3G24300; -.
DR Araport; AT3G24300; -.
DR TAIR; locus:2087173; AT3G24300.
DR eggNOG; KOG0682; Eukaryota.
DR HOGENOM; CLU_000445_33_1_1; -.
DR InParanoid; Q9SQH9; -.
DR OMA; HNFALRD; -.
DR OrthoDB; 910733at2759; -.
DR PhylomeDB; Q9SQH9; -.
DR BioCyc; ARA:AT3G24300-MON; -.
DR BioCyc; MetaCyc:AT3G24300-MON; -.
DR SABIO-RK; Q9SQH9; -.
DR PRO; PR:Q9SQH9; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q9SQH9; baseline and differential.
DR Genevisible; Q9SQH9; AT.
DR GO; GO:0110067; C:ammonium transmembrane transporter complex; IDA:ComplexPortal.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; IDA:ComplexPortal.
DR GO; GO:0008519; F:ammonium transmembrane transporter activity; IMP:TAIR.
DR GO; GO:0097272; P:ammonium homeostasis; IBA:GO_Central.
DR GO; GO:0072488; P:ammonium transmembrane transport; IMP:ComplexPortal.
DR GO; GO:0080181; P:lateral root branching; IMP:TAIR.
DR GO; GO:0010311; P:lateral root formation; IMP: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 Pfam; PF00909; Ammonium_transp; 1.
DR TIGRFAMs; TIGR00836; amt; 1.
DR PROSITE; PS01219; AMMONIUM_TRANSP; 1.
PE 1: Evidence at protein level;
KW Ammonia transport; Cell membrane; Membrane; Phosphoprotein;
KW Reference proteome; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..498
FT /note="Ammonium transporter 1 member 3"
FT /id="PRO_0000139745"
FT TRANSMEM 50..70
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 85..105
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 131..151
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 156..176
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 203..223
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 247..267
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 315..335
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 337..357
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 370..390
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 423..443
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 479..498
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 464
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P54144"
FT MOD_RES 487
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P54144"
SQ SEQUENCE 498 AA; 53298 MW; 551067158A7590F0 CRC64;
MSGAITCSAA DLATLLGPNA TAAADYICGQ LGTVNNKFTD AAFAIDNTYL LFSAYLVFAM
QLGFAMLCAG SVRAKNTMNI MLTNVLDAAA GGLFYYLFGY AFAFGGSSEG FIGRHNFALR
DFPTPTADYS FFLYQWAFAI AAAGITSGSI AERTQFVAYL IYSSFLTGFV YPVVSHWFWS
PDGWASPFRS ADDRLFSTGA IDFAGSGVVH MVGGIAGLWG ALIEGPRRGR FEKGGRAIAL
RGHSASLVVL GTFLLWFGWY GFNPGSFTKI LVPYNSGSNY GQWSGIGRTA VNTTLSGCTA
ALTTLFGKRL LSGHWNVTDV CNGLLGGFAA ITAGCSVVEP WAAIVCGFMA SVVLIGCNKL
AELVQYDDPL EAAQLHGGCG AWGLIFVGLF AKEKYLNEVY GATPGRPYGL FMGGGGKLLG
AQLVQILVIV GWVSATMGTL FFILKRLNLL RISEQHEMQG MDMTRHGGFA YIYHDNDDES
HRVDPGSPFP RSATPPRV
