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1.A.11.2.1
High-affinity electrogenic ammonia/methylammonia transporter (allosterically activated by the C-terminus (Loqué et al., 2009).  NH4+ is stable in the AmtB pore, reaching a binding site from which it can spontaneously transfer a proton to a pore-lining histidine residue (His168). The substrate diffuses down the pore in the form of NH3, while the proton is cotransported through a highly conserved hydrogen-bonded His168-His318 pair (Wang et al. 2012).

Accession Number:P54144
Protein Name:Ammonium transporter 1 member 1 aka Amt1.1
Length:501
Molecular Weight:53577.00
Species:Arabidopsis thaliana (Mouse-ear cress) [3702]
Number of TMSs:11
Location1 / Topology2 / Orientation3: Cell membrane1 / Multi-pass membrane protein2
Substrate ammonia, methylamine

Cross database links:

RefSeq: NP_193087.1   
Entrez Gene ID: 826983   
Pfam: PF00909   
BioCyc: MetaCyc:AT4G13510-MONOMER   
KEGG: ath:AT4G13510   

Gene Ontology

GO:0016021 C:integral to membrane
GO:0005634 C:nucleus
GO:0005886 C:plasma membrane
GO:0008519 F:ammonium transmembrane transporter activity
GO:0015696 P:ammonium transport
GO:0051258 P:protein polymerization
GO:0055085 P:transmembrane transport

References (17)

[1] “Identification of a high affinity NH4+ transporter from plants.”  Ninnemann O.et.al.   8062823
[2] “Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana.”  Mayer K.F.X.et.al.   10617198
[3] “Empirical analysis of transcriptional activity in the Arabidopsis genome.”  Yamada K.et.al.   14593172
[4] “Three functional transporters for constitutive, diurnally regulated, and starvation-induced uptake of ammonium into Arabidopsis roots.”  Gazzarrini S.et.al.   10330477
[5] “Functional analysis of an Arabidopsis T-DNA 'knockout' of the high-affinity NH4(+) transporter AtAMT1;1.”  Kaiser B.N.et.al.   12427993
[6] “Characterization of Arabidopsis AtAMT2, a high-affinity ammonium transporter of the plasma membrane.”  Sohlenkamp C.et.al.   12481062
[7] “Phosphoproteomics of the Arabidopsis plasma membrane and a new phosphorylation site database.”  Nuehse T.S.et.al.   15308754
[8] “Mechanisms of ammonium transport, accumulation, and retention in ooyctes and yeast cells expressing Arabidopsis AtAMT1;1.”  Wood C.C.et.al.   16806203
[9] “Role of AMT1;1 in NH4+ acquisition in Arabidopsis thaliana.”  Mayer M.et.al.   16917981
[10] “Additive contribution of AMT1;1 and AMT1;3 to high-affinity ammonium uptake across the plasma membrane of nitrogen-deficient Arabidopsis roots.”  Loque D.et.al.   17026539
[11] “Novel subsets of the Arabidopsis plasmalemma phosphoproteome identify phosphorylation sites in secondary active transporters.”  Hem S.et.al.   17869214
[12] “Quantitative phosphoproteomics of early elicitor signaling in Arabidopsis.”  Benschop J.J.et.al.   17317660
[13] “Reciprocal leaf and root expression of AtAmt1.1 and root architectural changes in response to nitrogen starvation.”  Engineer C.B.et.al.   17085512
[14] “Nitrogen-dependent posttranscriptional regulation of the ammonium transporter AtAMT1;1.”  Yuan L.et.al.   17172286
[15] “Site-specific phosphorylation profiling of Arabidopsis proteins by mass spectrometry and peptide chip analysis.”  de la Fuente van Bentem S.et.al.   18433157
[16] “Phosphoproteomic analysis of nuclei-enriched fractions from Arabidopsis thaliana.”  Jones A.M.E.et.al.   19245862
[17] “Large-scale Arabidopsis phosphoproteome profiling reveals novel chloroplast kinase substrates and phosphorylation networks.”  Reiland S.et.al.   19376835

External Searches:

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Predict TMSs (Predict number of transmembrane segments)
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FASTA formatted sequence
1:	MSCSATDLAV LLGPNATAAA NYICGQLGDV NNKFIDTAFA IDNTYLLFSA YLVFSMQLGF 
61:	AMLCAGSVRA KNTMNIMLTN VLDAAAGGLF YYLFGYAFAF GSPSNGFIGK HYFGLKDIPT 
121:	ASADYSNFLY QWAFAIAAAG ITSGSIAERT QFVAYLIYSS FLTGFVYPVV SHWFWSVDGW 
181:	ASPFRTDGDL LFSTGAIDFA GSGVVHMVGG IAGLWGALIE GPRLGRFDNG GRAIALRGHS 
241:	ASLVVLGTFL LWFGWYGFNP GSFNKILVTY ETGTYNGQWS AVGRTAVTTT LAGCTAALTT 
301:	LFGKRLLSGH WNVTDVCNGL LGGFAAITGG CSVVEPWAAI ICGFVAALVL LGCNKLAEKL 
361:	KYDDPLEAAQ LHGGCGAWGL IFTALFAQEK YLNQIYGNKP GRPHGLFMGG GGKLLGAQLI 
421:	QIIVITGWVS ATMGTLFFIL KKMKLLRISS EDEMAGMDMT RHGGFAYMYF DDDESHKAIQ 
481:	LRRVEPRSPS PSGANTTPTP V