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Ammonium transporter 1 member 1 (AtAMT1;1)

 AMT11_ARATH             Reviewed;         501 AA.
P54144; Q94C23;
01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
01-OCT-1996, sequence version 1.
25-OCT-2017, entry version 136.
RecName: Full=Ammonium transporter 1 member 1;
Short=AtAMT1;1;
Name=AMT1-1; OrderedLocusNames=At4g13510; ORFNames=T6G15.60;
Arabidopsis thaliana (Mouse-ear cress).
Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
Spermatophyta; Magnoliophyta; eudicotyledons; Gunneridae;
Pentapetalae; rosids; malvids; Brassicales; Brassicaceae; Camelineae;
Arabidopsis.
NCBI_TaxID=3702;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
STRAIN=cv. Landsberg erecta;
PubMed=8062823;
Ninnemann O., Janniaux J.-C., Frommer W.B.;
"Identification of a high affinity NH4+ transporter from plants.";
EMBO J. 13:3464-3471(1994).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=cv. Columbia;
PubMed=10617198; DOI=10.1038/47134;
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., Mache R., Mueller M.,
Kreis M., Delseny M., Puigdomenech P., Watson M., Schmidtheini T.,
Reichert B., Portetelle D., Perez-Alonso M., Boutry M., Bancroft I.,
Vos P., Hoheisel J., Zimmermann W., Wedler H., Ridley P.,
Langham S.-A., McCullagh B., Bilham L., Robben J.,
van der Schueren J., Grymonprez B., Chuang Y.-J., Vandenbussche F.,
Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R., Defoor E.,
Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M.,
Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W.,
Mooijman P., Klein Lankhorst R., Rose M., Hauf J., Koetter P.,
Berneiser S., Hempel S., Feldpausch M., Lamberth S., Van den Daele H.,
De Keyser A., Buysshaert C., Gielen J., Villarroel R., De Clercq R.,
van Montagu M., Rogers J., Cronin A., Quail M.A., Bray-Allen S.,
Clark L., Doggett J., Hall S., Kay M., Lennard N., McLay K., Mayes R.,
Pettett A., Rajandream M.A., Lyne M., Benes V., Rechmann S.,
Borkova D., Bloecker H., Scharfe M., Grimm M., Loehnert T.-H.,
Dose S., de Haan M., Maarse A.C., Schaefer M., Mueller-Auer S.,
Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D., Herzl A.,
Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E.,
Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R.,
Schnabl S., Hiller R., Schmidt W., Lecharny A., Aubourg S.,
Chefdor F., Cooke R., Berger C., Monfort A., Casacuberta E.,
Gibbons T., Weber N., Vandenbol M., Bargues M., Terol J., Torres A.,
Perez-Perez A., Purnelle B., Bent E., Johnson S., Tacon D., Jesse T.,
Heijnen L., Schwarz S., Scholler P., Heber S., Francs P., Bielke C.,
Frishman D., Haase D., Lemcke K., Mewes H.-W., Stocker S.,
Zaccaria P., Bevan M., Wilson R.K., de la Bastide M., Habermann K.,
Parnell L., Dedhia N., Gnoj L., Schutz K., Huang E., Spiegel L.,
Sekhon M., Murray J., Sheet P., Cordes M., Abu-Threideh J.,
Stoneking T., Kalicki J., Graves T., Harmon G., Edwards J.,
Latreille P., Courtney L., Cloud J., Abbott A., Scott K., Johnson D.,
Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K.,
Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W.,
Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D.,
Du H., Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C.,
Antonoiu B., Zidanic M., Strong C., Sun H., Lamar B., Yordan C.,
Ma P., Zhong J., Preston R., Vil D., Shekher M., Matero A., Shah R.,
Swaby I.K., O'Shaughnessy A., Rodriguez M., Hoffman J., Till S.,
Granat S., Shohdy N., Hasegawa A., Hameed A., Lodhi M., Johnson A.,
Chen E., Marra M.A., Martienssen R., McCombie W.R.;
"Sequence and analysis of chromosome 4 of the plant Arabidopsis
thaliana.";
Nature 402:769-777(1999).
[3]
GENOME REANNOTATION.
STRAIN=cv. Columbia;
The Arabidopsis Information Portal (Araport);
Submitted (MAY-2016) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=cv. Columbia;
PubMed=14593172; DOI=10.1126/science.1088305;
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.,
Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J.,
Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y.,
Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P.,
Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F.,
Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M.,
Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J.,
Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T.,
Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y.,
Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R.;
"Empirical analysis of transcriptional activity in the Arabidopsis
genome.";
Science 302:842-846(2003).
[5]
TISSUE SPECIFICITY.
STRAIN=cv. C24;
PubMed=10330477; DOI=10.1105/tpc.11.5.937;
Gazzarrini S., Lejay L., Gojon A., Ninnemann O., Frommer W.B.,
von Wiren N.;
"Three functional transporters for constitutive, diurnally regulated,
and starvation-induced uptake of ammonium into Arabidopsis roots.";
Plant Cell 11:937-948(1999).
[6]
DISRUPTION PHENOTYPE.
PubMed=12427993; DOI=10.1104/pp.102.010843;
Kaiser B.N., Rawat S.R., Siddiqi M.Y., Masle J., Glass A.D.M.;
"Functional analysis of an Arabidopsis T-DNA 'knockout' of the high-
affinity NH4(+) transporter AtAMT1;1.";
Plant Physiol. 130:1263-1275(2002).
[7]
FUNCTION, AND BIOPHYSICOCHEMICAL PROPERTIES.
PubMed=12481062; DOI=10.1104/pp.008599;
Sohlenkamp C., Wood C.C., Roeb G.W., Udvardi M.K.;
"Characterization of Arabidopsis AtAMT2, a high-affinity ammonium
transporter of the plasma membrane.";
Plant Physiol. 130:1788-1796(2002).
[8]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-460, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
STRAIN=cv. La-0;
PubMed=14506206; DOI=10.1074/mcp.T300006-MCP200;
Nuehse T.S., Stensballe A., Jensen O.N., Peck S.C.;
"Large-scale analysis of in vivo phosphorylated membrane proteins by
immobilized metal ion affinity chromatography and mass spectrometry.";
Mol. Cell. Proteomics 2:1234-1243(2003).
[9]
SUBCELLULAR LOCATION, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT
THR-460, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
PubMed=15308754; DOI=10.1105/tpc.104.023150;
Nuehse T.S., Stensballe A., Jensen O.N., Peck S.C.;
"Phosphoproteomics of the Arabidopsis plasma membrane and a new
phosphorylation site database.";
Plant Cell 16:2394-2405(2004).
[10]
FUNCTION, AND BIOPHYSICOCHEMICAL PROPERTIES.
PubMed=16806203; DOI=10.1016/j.febslet.2006.06.026;
Wood C.C., Poree F., Dreyer I., Koehler G.J., Udvardi M.K.;
"Mechanisms of ammonium transport, accumulation, and retention in
ooyctes and yeast cells expressing Arabidopsis AtAMT1;1.";
FEBS Lett. 580:3931-3936(2006).
[11]
FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND INDUCTION.
PubMed=16917981; DOI=10.1055/s-2006-923877;
Mayer M., Ludewig U.;
"Role of AMT1;1 in NH4+ acquisition in Arabidopsis thaliana.";
Plant Biol. 8:522-528(2006).
[12]
FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND INDUCTION.
PubMed=17026539; DOI=10.1111/j.1365-313X.2006.02887.x;
Loque D., Yuan L., Kojima S., Gojon A., Wirth J., Gazzarrini S.,
Ishiyama K., Takahashi H., von Wiren N.;
"Additive contribution of AMT1;1 and AMT1;3 to high-affinity ammonium
uptake across the plasma membrane of nitrogen-deficient Arabidopsis
roots.";
Plant J. 48:522-534(2006).
[13]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-460; SER-490 AND
SER-492, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
PubMed=17869214; DOI=10.1016/j.bbrc.2007.08.177;
Hem S., Rofidal V., Sommerer N., Rossignol M.;
"Novel subsets of the Arabidopsis plasmalemma phosphoproteome identify
phosphorylation sites in secondary active transporters.";
Biochem. Biophys. Res. Commun. 363:375-380(2007).
[14]
TISSUE SPECIFICITY, AND INDUCTION.
PubMed=17085512; DOI=10.1104/pp.106.088500;
Engineer C.B., Kranz R.G.;
"Reciprocal leaf and root expression of AtAmt1.1 and root
architectural changes in response to nitrogen starvation.";
Plant Physiol. 143:236-250(2007).
[15]
INDUCTION.
PubMed=17172286; DOI=10.1104/pp.106.093237;
Yuan L., Loque D., Ye F., Frommer W.B., von Wiren N.;
"Nitrogen-dependent posttranscriptional regulation of the ammonium
transporter AtAMT1;1.";
Plant Physiol. 143:732-744(2007).
[16]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-475, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Root;
PubMed=18433157; DOI=10.1021/pr8000173;
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.;
"Site-specific phosphorylation profiling of Arabidopsis proteins by
mass spectrometry and peptide chip analysis.";
J. Proteome Res. 7:2458-2470(2008).
[17]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-460, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
STRAIN=cv. Columbia;
PubMed=19245862; DOI=10.1016/j.jprot.2009.02.004;
Jones A.M.E., MacLean D., Studholme D.J., Serna-Sanz A.,
Andreasson E., Rathjen J.P., Peck S.C.;
"Phosphoproteomic analysis of nuclei-enriched fractions from
Arabidopsis thaliana.";
J. Proteomics 72:439-451(2009).
[18]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-488, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19376835; DOI=10.1104/pp.109.138677;
Reiland S., Messerli G., Baerenfaller K., Gerrits B., Endler A.,
Grossmann J., Gruissem W., Baginsky S.;
"Large-scale Arabidopsis phosphoproteome profiling reveals novel
chloroplast kinase substrates and phosphorylation networks.";
Plant Physiol. 150:889-903(2009).
[19]
SUBUNIT, AND INTERACTION WITH CEPR2; AT2G28990 AND PAM74.
PubMed=21423366; DOI=10.3389/fphys.2010.00024;
Lalonde S., Sero A., Pratelli R., Pilot G., Chen J., Sardi M.I.,
Parsa S.A., Kim D.Y., Acharya B.R., Stein E.V., Hu H.C., Villiers F.,
Takeda K., Yang Y., Han Y.S., Schwacke R., Chiang W., Kato N.,
Loque D., Assmann S.M., Kwak J.M., Schroeder J.I., Rhee S.Y.,
Frommer W.B.;
"A membrane protein/signaling protein interaction network for
Arabidopsis version AMPv2.";
Front. Physiol. 1:24-24(2010).
-!- 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. {ECO:0000269|PubMed:12481062,
ECO:0000269|PubMed:16806203, ECO:0000269|PubMed:16917981,
ECO:0000269|PubMed:17026539}.
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Kinetic parameters:
KM=22 uM for ammonium chloride (at external pH 6.1)
{ECO:0000269|PubMed:12481062, ECO:0000269|PubMed:16806203};
Note=Measured in yeast knockout mutant YCW012.;
-!- SUBUNIT: Self interacts. Interacts with the receptor protein
kinases CEPR2, At2g28990 and PAM74. {ECO:0000269|PubMed:21423366}.
-!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:15308754,
ECO:0000269|PubMed:16917981, ECO:0000269|PubMed:17026539}; Multi-
pass membrane protein {ECO:0000269|PubMed:15308754,
ECO:0000269|PubMed:16917981, ECO:0000269|PubMed:17026539}.
-!- 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.
{ECO:0000269|PubMed:10330477, ECO:0000269|PubMed:16917981,
ECO:0000269|PubMed:17026539, ECO:0000269|PubMed:17085512}.
-!- INDUCTION: By nitrogen deprivation in roots and nitrogen supply in
leaves. {ECO:0000269|PubMed:16917981, ECO:0000269|PubMed:17026539,
ECO:0000269|PubMed:17085512, ECO:0000269|PubMed:17172286}.
-!- DISRUPTION PHENOTYPE: No effect on ammonium uptake. Higher
expression of AMT1-2; AMT1-3 and AMT2-1.
{ECO:0000269|PubMed:12427993}.
-!- SIMILARITY: Belongs to the ammonia transporter channel (TC
1.A.11.2) family. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=AAK59819.1; Type=Frameshift; Positions=125; Evidence={ECO:0000305};
Sequence=AAM47470.1; Type=Frameshift; Positions=125; Evidence={ECO:0000305};
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EMBL; X75879; CAA53473.1; -; mRNA.
EMBL; AL049656; CAB41109.1; -; Genomic_DNA.
EMBL; AL161536; CAB78393.1; -; Genomic_DNA.
EMBL; CP002687; AEE83287.1; -; Genomic_DNA.
EMBL; AY037219; AAK59819.1; ALT_FRAME; mRNA.
EMBL; AY113167; AAM47470.1; ALT_FRAME; mRNA.
PIR; T06653; T06653.
RefSeq; NP_193087.1; NM_117425.2.
UniGene; At.23790; -.
UniGene; At.33367; -.
UniGene; At.49725; -.
ProteinModelPortal; P54144; -.
BioGrid; 12280; 46.
MINT; MINT-8061187; -.
STRING; 3702.AT4G13510.1; -.
TCDB; 1.A.11.2.1; the ammonium transporter channel (amt) family.
iPTMnet; P54144; -.
PaxDb; P54144; -.
PRIDE; P54144; -.
EnsemblPlants; AT4G13510.1; AT4G13510.1; AT4G13510.
GeneID; 826983; -.
Gramene; AT4G13510.1; AT4G13510.1; AT4G13510.
KEGG; ath:AT4G13510; -.
Araport; AT4G13510; -.
TAIR; locus:2140877; AT4G13510.
eggNOG; KOG0682; Eukaryota.
eggNOG; COG0004; LUCA.
HOGENOM; HOG000017735; -.
InParanoid; P54144; -.
KO; K03320; -.
OMA; KFFFLMT; -.
OrthoDB; EOG093609QB; -.
PhylomeDB; P54144; -.
BioCyc; ARA:AT4G13510-MONOMER; -.
BioCyc; MetaCyc:AT4G13510-MONOMER; -.
SABIO-RK; P54144; -.
PRO; PR:P54144; -.
Proteomes; UP000006548; Chromosome 4.
ExpressionAtlas; P54144; baseline and differential.
Genevisible; P54144; AT.
GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
GO; GO:0005634; C:nucleus; IDA:TAIR.
GO; GO:0005886; C:plasma membrane; IDA:TAIR.
GO; GO:0009506; C:plasmodesma; IDA:TAIR.
GO; GO:0008519; F:ammonium transmembrane transporter activity; IDA:TAIR.
GO; GO:0043621; F:protein self-association; IDA:UniProtKB.
GO; GO:0015696; P:ammonium transport; IDA:TAIR.
GO; GO:0080181; P:lateral root branching; IMP:TAIR.
GO; GO:0010311; P:lateral root formation; IMP:TAIR.
GO; GO:0015695; P:organic cation transport; IBA:GO_Central.
GO; GO:0051258; P:protein polymerization; IDA:TAIR.
GO; GO:0009737; P:response to abscisic acid; IDA:TAIR.
GO; GO:0080167; P:response to karrikin; IEP:TAIR.
Gene3D; 1.10.3430.10; -; 1.
InterPro; IPR029020; Ammonium/urea_transptr.
InterPro; IPR001905; Ammonium_transpt.
InterPro; IPR018047; Ammonium_transpt_CS.
InterPro; IPR024041; NH4_transpt_AmtB-like_dom.
Pfam; PF00909; Ammonium_transp; 1.
SUPFAM; SSF111352; SSF111352; 1.
TIGRFAMs; TIGR00836; amt; 1.
PROSITE; PS01219; AMMONIUM_TRANSP; 1.
1: Evidence at protein level;
Ammonia transport; Cell membrane; Complete proteome; Membrane;
Phosphoprotein; Reference proteome; Transmembrane;
Transmembrane helix; Transport.
CHAIN 1 501 Ammonium transporter 1 member 1.
/FTId=PRO_0000224180.
TRANSMEM 8 28 Helical. {ECO:0000255}.
TRANSMEM 46 66 Helical. {ECO:0000255}.
TRANSMEM 81 101 Helical. {ECO:0000255}.
TRANSMEM 128 148 Helical. {ECO:0000255}.
TRANSMEM 152 172 Helical. {ECO:0000255}.
TRANSMEM 199 219 Helical. {ECO:0000255}.
TRANSMEM 243 263 Helical. {ECO:0000255}.
TRANSMEM 333 353 Helical. {ECO:0000255}.
TRANSMEM 366 386 Helical. {ECO:0000255}.
TRANSMEM 419 439 Helical. {ECO:0000255}.
COMPBIAS 409 412 Poly-Gly.
MOD_RES 460 460 Phosphothreonine.
{ECO:0000244|PubMed:14506206,
ECO:0000244|PubMed:15308754,
ECO:0000244|PubMed:17869214,
ECO:0000244|PubMed:19245862}.
MOD_RES 475 475 Phosphoserine.
{ECO:0000244|PubMed:18433157}.
MOD_RES 488 488 Phosphoserine.
{ECO:0000244|PubMed:19376835}.
MOD_RES 490 490 Phosphoserine.
{ECO:0000244|PubMed:17869214}.
MOD_RES 492 492 Phosphoserine.
{ECO:0000244|PubMed:17869214}.
SEQUENCE 501 AA; 53577 MW; 070BAF8228302BFF CRC64;
MSCSATDLAV LLGPNATAAA NYICGQLGDV NNKFIDTAFA IDNTYLLFSA YLVFSMQLGF
AMLCAGSVRA KNTMNIMLTN VLDAAAGGLF YYLFGYAFAF GSPSNGFIGK HYFGLKDIPT
ASADYSNFLY QWAFAIAAAG ITSGSIAERT QFVAYLIYSS FLTGFVYPVV SHWFWSVDGW
ASPFRTDGDL LFSTGAIDFA GSGVVHMVGG IAGLWGALIE GPRLGRFDNG GRAIALRGHS
ASLVVLGTFL LWFGWYGFNP GSFNKILVTY ETGTYNGQWS AVGRTAVTTT LAGCTAALTT
LFGKRLLSGH WNVTDVCNGL LGGFAAITGG CSVVEPWAAI ICGFVAALVL LGCNKLAEKL
KYDDPLEAAQ LHGGCGAWGL IFTALFAQEK YLNQIYGNKP GRPHGLFMGG GGKLLGAQLI
QIIVITGWVS ATMGTLFFIL KKMKLLRISS EDEMAGMDMT RHGGFAYMYF DDDESHKAIQ
LRRVEPRSPS PSGANTTPTP V


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EIAAB45843 Bos taurus,Bovine,Monoamine transporter,SLC18A2,Solute carrier family 18 member 2,Synaptic vesicular amine transporter,VAT2,Vesicular amine transporter 2,VMAT2
EIAAB25184 Aromatic amino acid transporter 1,MCT 10,Mct10,Monocarboxylate transporter 10,Rat,Rattus norvegicus,Slc16a10,Solute carrier family 16 member 10,Tat1,T-type amino acid transporter 1
EIAAB25183 Aromatic amino acid transporter 1,MCT 10,Mct10,Monocarboxylate transporter 10,Mouse,Mus musculus,Slc16a10,Solute carrier family 16 member 10,Tat1,T-type amino acid transporter 1
EIAAB45846 Monoamine transporter,Rat,Rattus norvegicus,Slc18a2,Solute carrier family 18 member 2,Svat,Synaptic vesicular amine transporter,VAT2,Vesicular amine transporter 2,Vmat2
EIAAB45845 Homo sapiens,Human,Monoamine transporter,SLC18A2,Solute carrier family 18 member 2,SVMT,Synaptic vesicular amine transporter,VAT2,Vesicular amine transporter 2,VMAT2
EIAAB25185 Aromatic amino acid transporter 1,Homo sapiens,Human,MCT 10,MCT10,Monocarboxylate transporter 10,SLC16A10,Solute carrier family 16 member 10,TAT1,T-type amino acid transporter 1
EIAAB36713 hOAT1,Homo sapiens,hPAHT,hROAT1,Human,OAT1,Organic anion transporter 1,PAH transporter,PAHT,Renal organic anion transporter 1,SLC22A6,Solute carrier family 22 member 6


 

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