Ammonium transporter 1 member 1 - Arabidopsis thaliana (Mouse-ear cress)

Preferred order of sections

Names and origin

Protein names

Recommended name:
Ammonium transporter 1 member 1
Short name=AtAMT1;1

Gene names

Name:	AMT1-1
Ordered Locus Names:	At4g13510
ORF Names:	T6G15.60

Organism

Arabidopsis thaliana (Mouse-ear cress) [Reference proteome]

Taxonomic identifier

3702 [NCBI]

Taxonomic lineage

Eukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › rosids › malvids › Brassicales › Brassicaceae › Camelineae › Arabidopsis

Protein attributes

Sequence length	501 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	High affinity ammonium transporter probably involved in ammonium uptake from the soil, long-distance transport to the shoots and re-uptake of apoplastic ammonium that derives from photorespiration in shoots. Contributes with AMT1-3 to the overall ammonium uptake capacity in roots under nitrogen-deficiency conditions. Ref.7 Ref.9 Ref.10 Ref.11
Subcellular location	Cell membrane; Multi-pass membrane protein Ref.10 Ref.11.
Tissue specificity	Highly expressed in roots. Expressed in root tips, root hairs, root epidermis, rhizodermis, cortex and pericycle. Expressed in leaves epidermal and mesophyll cells. Ref.5 Ref.10 Ref.11 Ref.14
Induction	By nitrogen deprivation in roots and nitrogen supply in leaves. Ref.10 Ref.11 Ref.14 Ref.15
Post-translational modification	Phosphorylation level varies significantly during early response to general elicitors.
Disruption phenotype	No effect on ammonium uptake. Higher expression of AMT1-2; AMT1-3 and AMT2-1. Ref.6
Sequence similarities	Belongs to the ammonia transporter channel (TC 1.A.11.2) family. [View classification]
Biophysicochemical properties	Kinetic parameters: Measured in yeast knockout mutant YCW012. K_M=22 µM for ammonium chloride (at external pH 6.1) Ref.7 Ref.9
Sequence caution	The sequence AAK59819.1 differs from that shown. Reason: Frameshift at position 125. The sequence AAM47470.1 differs from that shown. Reason: Frameshift at position 125.

Ontologies

Keywords
Biological process	Ammonia transport Transport
Cellular component	Cell membrane Membrane
Domain	Transmembrane Transmembrane helix
PTM	Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	lateral root branching Inferred from mutant phenotype PubMed 21119058. Source: TAIR lateral root formation Inferred from mutant phenotype PubMed 21119058. Source: TAIR protein polymerization Inferred from direct assay PubMed 17293878. Source: TAIR response to abscisic acid stimulus Inferred from direct assay PubMed 20733066. Source: TAIR response to karrikin Inferred from expression pattern PubMed 20351290. Source: TAIR
Cellular_component	integral to membrane Inferred from electronic annotation. Source: UniProtKB-KW nucleus Inferred from direct assay Ref.16. Source: TAIR plasma membrane Inferred from direct assay PubMed 14506206 Ref.10 Ref.13 PubMed 22923678. Source: TAIR plasmodesma Inferred from direct assay PubMed 21533090. Source: TAIR
Molecular_function	ammonium transmembrane transporter activity Inferred from direct assay Ref.10. Source: TAIR
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 501

501

Ammonium transporter 1 member 1

PRO_0000224180

Regions

Transmembrane

8 – 28

21

Helical; Potential

Transmembrane

46 – 66

21

Helical; Potential

Transmembrane

81 – 101

21

Helical; Potential

Transmembrane

128 – 148

21

Helical; Potential

Transmembrane

152 – 172

21

Helical; Potential

Transmembrane

199 – 219

21

Helical; Potential

Transmembrane

243 – 263

21

Helical; Potential

Transmembrane

333 – 353

21

Helical; Potential

Transmembrane

366 – 386

21

Helical; Potential

Transmembrane

419 – 439

21

Helical; Potential

Compositional bias

409 – 412

4

Poly-Gly

Amino acid modifications

Modified residue

460

1

Phosphothreonine Ref.8 Ref.12 Ref.17

Modified residue

475

1

Phosphoserine Ref.13 Ref.16

Modified residue

488

1

Phosphoserine Ref.12 Ref.18

Modified residue

490

1

Phosphoserine Ref.12

Modified residue

492

1

Phosphoserine Ref.12

Sequences

Sequence

Length

Mass (Da)

Tools

P54144 [UniParc].

Last modified October 1, 1996. Version 1.
Checksum: 070BAF8228302BFF
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FASTA

501

53,577

        10         20         30         40         50         60 
MSCSATDLAV LLGPNATAAA NYICGQLGDV NNKFIDTAFA IDNTYLLFSA YLVFSMQLGF 

        70         80         90        100        110        120 
AMLCAGSVRA KNTMNIMLTN VLDAAAGGLF YYLFGYAFAF GSPSNGFIGK HYFGLKDIPT 

       130        140        150        160        170        180 
ASADYSNFLY QWAFAIAAAG ITSGSIAERT QFVAYLIYSS FLTGFVYPVV SHWFWSVDGW 

       190        200        210        220        230        240 
ASPFRTDGDL LFSTGAIDFA GSGVVHMVGG IAGLWGALIE GPRLGRFDNG GRAIALRGHS 

       250        260        270        280        290        300 
ASLVVLGTFL LWFGWYGFNP GSFNKILVTY ETGTYNGQWS AVGRTAVTTT LAGCTAALTT 

       310        320        330        340        350        360 
LFGKRLLSGH WNVTDVCNGL LGGFAAITGG CSVVEPWAAI ICGFVAALVL LGCNKLAEKL 

       370        380        390        400        410        420 
KYDDPLEAAQ LHGGCGAWGL IFTALFAQEK YLNQIYGNKP GRPHGLFMGG GGKLLGAQLI 

       430        440        450        460        470        480 
QIIVITGWVS ATMGTLFFIL KKMKLLRISS EDEMAGMDMT RHGGFAYMYF DDDESHKAIQ 

       490        500 
LRRVEPRSPS PSGANTTPTP V

« Hide

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Identification of a high affinity NH4+ transporter from plants." Ninnemann O., Janniaux J.-C., Frommer W.B. EMBO J. 13:3464-3471(1994) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Strain: cv. Landsberg erecta.
[2]	"Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana." Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T., Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B., Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M., de Simone V., Obermaier B. McCombie W.R. Nature 402:769-777(1999) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: cv. Columbia.
[3]	The Arabidopsis Information Resource (TAIR) Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases Cited for: GENOME REANNOTATION. Strain: cv. Columbia.
[4]	"Empirical analysis of transcriptional activity in the Arabidopsis genome." Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G. Ecker J.R. Science 302:842-846(2003) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: cv. Columbia.
[5]	"Three functional transporters for constitutive, diurnally regulated, and starvation-induced uptake of ammonium into Arabidopsis roots." Gazzarrini S., Lejay L., Gojon A., Ninnemann O., Frommer W.B., von Wiren N. Plant Cell 11:937-948(1999) [PubMed] [Europe PMC] [Abstract] Cited for: TISSUE SPECIFICITY. Strain: cv. C24.
[6]	"Functional analysis of an Arabidopsis T-DNA 'knockout' of the high-affinity NH4(+) transporter AtAMT1;1." Kaiser B.N., Rawat S.R., Siddiqi M.Y., Masle J., Glass A.D.M. Plant Physiol. 130:1263-1275(2002) [PubMed] [Europe PMC] [Abstract] Cited for: DISRUPTION PHENOTYPE.
[7]	"Characterization of Arabidopsis AtAMT2, a high-affinity ammonium transporter of the plasma membrane." Sohlenkamp C., Wood C.C., Roeb G.W., Udvardi M.K. Plant Physiol. 130:1788-1796(2002) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES.
[8]	"Phosphoproteomics of the Arabidopsis plasma membrane and a new phosphorylation site database." Nuehse T.S., Stensballe A., Jensen O.N., Peck S.C. Plant Cell 16:2394-2405(2004) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-460, SUBCELLULAR LOCATION, MASS SPECTROMETRY.
[9]	"Mechanisms of ammonium transport, accumulation, and retention in ooyctes and yeast cells expressing Arabidopsis AtAMT1;1." Wood C.C., Poree F., Dreyer I., Koehler G.J., Udvardi M.K. FEBS Lett. 580:3931-3936(2006) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES.
[10]	"Role of AMT1;1 in NH4+ acquisition in Arabidopsis thaliana." Mayer M., Ludewig U. Plant Biol. 8:522-528(2006) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, INDUCTION.
[11]	"Additive contribution of AMT1;1 and AMT1;3 to high-affinity ammonium uptake across the plasma membrane of nitrogen-deficient Arabidopsis roots." Loque D., Yuan L., Kojima S., Gojon A., Wirth J., Gazzarrini S., Ishiyama K., Takahashi H., von Wiren N. Plant J. 48:522-534(2006) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, INDUCTION.
[12]	"Novel subsets of the Arabidopsis plasmalemma phosphoproteome identify phosphorylation sites in secondary active transporters." Hem S., Rofidal V., Sommerer N., Rossignol M. Biochem. Biophys. Res. Commun. 363:375-380(2007) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-460; SER-488; SER-490 AND SER-492, MASS SPECTROMETRY.
[13]	"Quantitative phosphoproteomics of early elicitor signaling in Arabidopsis." Benschop J.J., Mohammed S., O'Flaherty M., Heck A.J.R., Slijper M., Menke F.L.H. Mol. Cell. Proteomics 6:1198-1214(2007) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-475, MASS SPECTROMETRY. Strain: cv. Columbia.
[14]	"Reciprocal leaf and root expression of AtAmt1.1 and root architectural changes in response to nitrogen starvation." Engineer C.B., Kranz R.G. Plant Physiol. 143:236-250(2007) [PubMed] [Europe PMC] [Abstract] Cited for: TISSUE SPECIFICITY, INDUCTION.
[15]	"Nitrogen-dependent posttranscriptional regulation of the ammonium transporter AtAMT1;1." Yuan L., Loque D., Ye F., Frommer W.B., von Wiren N. Plant Physiol. 143:732-744(2007) [PubMed] [Europe PMC] [Abstract] Cited for: INDUCTION.
[16]	"Site-specific phosphorylation profiling of Arabidopsis proteins by mass spectrometry and peptide chip analysis." de la Fuente van Bentem S., Anrather D., Dohnal I., Roitinger E., Csaszar E., Joore J., Buijnink J., Carreri A., Forzani C., Lorkovic Z.J., Barta A., Lecourieux D., Verhounig A., Jonak C., Hirt H. J. Proteome Res. 7:2458-2470(2008) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-475, MASS SPECTROMETRY. Tissue: Root.
[17]	"Phosphoproteomic analysis of nuclei-enriched fractions from Arabidopsis thaliana." Jones A.M.E., MacLean D., Studholme D.J., Serna-Sanz A., Andreasson E., Rathjen J.P., Peck S.C. J. Proteomics 72:439-451(2009) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-460, MASS SPECTROMETRY. Strain: cv. Columbia.
[18]	"Large-scale Arabidopsis phosphoproteome profiling reveals novel chloroplast kinase substrates and phosphorylation networks." Reiland S., Messerli G., Baerenfaller K., Gerrits B., Endler A., Grossmann J., Gruissem W., Baginsky S. Plant Physiol. 150:889-903(2009) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-488, MASS SPECTROMETRY. Strain: cv. Columbia. Tissue: Seedling.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	X75879 mRNA. Translation: CAA53473.1. AL049656 Genomic DNA. Translation: CAB41109.1. AL161536 Genomic DNA. Translation: CAB78393.1. CP002687 Genomic DNA. Translation: AEE83287.1. AY037219 mRNA. Translation: AAK59819.1. Frameshift. AY113167 mRNA. Translation: AAM47470.1. Frameshift.
IPI	IPI00547960.
PIR	T06653.
RefSeq	NP_193087.1. NM_117425.2.
UniGene	At.23790. At.33367. At.49725.
3D structure databases
ProteinModelPortal	P54144.
SMR	P54144. Positions 42-467.
ModBase	Search...
Protein-protein interaction databases
STRING	3702.AT4G13510.1-P.
Protein family/group databases
TCDB	1.A.11.2.1. ammonia transporter channel (Amt) family.
Proteomic databases
PaxDb	P54144.
PRIDE	P54144.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblPlants	AT4G13510.1; AT4G13510.1; AT4G13510.
GeneID	826983.
KEGG	ath:AT4G13510.
Organism-specific databases
TAIR	At4g13510.
Phylogenomic databases
eggNOG	COG0004.
HOGENOM	HOG000017735.
InParanoid	P54144.
KO	K03320.
OMA	SIGYIAV.
PhylomeDB	P54144.
ProtClustDB	CLSN2679335.
Enzyme and pathway databases
BioCyc	ARA:AT4G13510-MONOMER. MetaCyc:AT4G13510-MONOMER.
SABIO-RK	P54144.
Gene expression databases
Genevestigator	P54144.
GermOnline	AT4G13510. Arabidopsis thaliana.
Family and domain databases
InterPro	IPR001905. Ammonium_transpt. IPR018047. Ammonium_transpt_CS. IPR024041. NH4_transpt_AmtB-like_dom. [Graphical view]
PANTHER	PTHR11730. PTHR11730. 1 hit.
Pfam	PF00909. Ammonium_transp. 1 hit. [Graphical view]
SUPFAM	SSF111352. RH_like_transpt. 1 hit.
TIGRFAMs	TIGR00836. amt. 1 hit.
PROSITE	PS01219. AMMONIUM_TRANSP. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

AMT11_ARATH

Accession

Primary (citable) accession number: P54144
Secondary accession number(s): Q94C23

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1996
Last sequence update:	October 1, 1996
Last modified:	May 1, 2013
This is version 105 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Plant Protein Annotation Program

Relevant documents

Arabidopsis thaliana

Arabidopsis thaliana: entries and gene names

SIMILARITY comments

Index of protein domains and families

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Amino acid modifications

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Protein family/group databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Gene expression databases

Family and domain databases

Entry information

Relevant documents