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AMT12_ARATH
ID   AMT12_ARATH             Reviewed;         514 AA.
AC   Q9ZPJ8; Q9SQH8;
DT   26-JUL-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1999, sequence version 1.
DT   03-AUG-2022, entry version 142.
DE   RecName: Full=Ammonium transporter 1 member 2;
DE            Short=AtAMT1;2;
GN   Name=AMT1-2; OrderedLocusNames=At1g64780; ORFNames=F13O11.9;
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], FUNCTION, 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 [MRNA].
RC   STRAIN=cv. C24; TISSUE=Root;
RA   Shelden M.C., Howitt S.M., Udvardi M.K.;
RT   "Arabidopsis thaliana AtAMT1;2 from N-deprived roots.";
RL   Submitted (DEC-1998) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=11130712; DOI=10.1038/35048500;
RA   Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA   Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA   Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA   Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA   Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA   Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA   Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA   Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA   Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA   Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA   Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA   Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA   Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA   Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA   Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT   "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL   Nature 408:816-820(2000).
RN   [4]
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   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=14593172; DOI=10.1126/science.1088305;
RA   Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA   Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA   Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA   Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA   Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA   Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA   Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA   Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA   Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA   Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA   Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA   Ecker J.R.;
RT   "Empirical analysis of transcriptional activity in the Arabidopsis
RT   genome.";
RL   Science 302:842-846(2003).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-472, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   STRAIN=cv. Columbia;
RX   PubMed=19245862; DOI=10.1016/j.jprot.2009.02.004;
RA   Jones A.M.E., MacLean D., Studholme D.J., Serna-Sanz A., Andreasson E.,
RA   Rathjen J.P., Peck S.C.;
RT   "Phosphoproteomic analysis of nuclei-enriched fractions from Arabidopsis
RT   thaliana.";
RL   J. Proteomics 72:439-451(2009).
CC   -!- FUNCTION: Ammonium transporter probably involved in ammonium uptake
CC       from the soil. {ECO:0000269|PubMed:10330477}.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane
CC       protein {ECO:0000305}.
CC   -!- TISSUE SPECIFICITY: High expression in root.
CC       {ECO:0000269|PubMed:10330477}.
CC   -!- SIMILARITY: Belongs to the ammonia transporter channel (TC 1.A.11.2)
CC       family. {ECO:0000305}.
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DR   EMBL; AF083036; AAD54639.1; -; mRNA.
DR   EMBL; AF110771; AAD17001.1; -; mRNA.
DR   EMBL; AC006193; AAD38253.1; -; Genomic_DNA.
DR   EMBL; CP002684; AEE34288.1; -; Genomic_DNA.
DR   EMBL; AY062571; AAL32649.1; -; mRNA.
DR   EMBL; AY093374; AAM13373.1; -; mRNA.
DR   PIR; A96671; A96671.
DR   RefSeq; NP_176658.1; NM_105152.3.
DR   AlphaFoldDB; Q9ZPJ8; -.
DR   SMR; Q9ZPJ8; -.
DR   BioGRID; 28007; 8.
DR   IntAct; Q9ZPJ8; 1.
DR   STRING; 3702.AT1G64780.1; -.
DR   iPTMnet; Q9ZPJ8; -.
DR   PaxDb; Q9ZPJ8; -.
DR   PRIDE; Q9ZPJ8; -.
DR   ProteomicsDB; 240319; -.
DR   EnsemblPlants; AT1G64780.1; AT1G64780.1; AT1G64780.
DR   GeneID; 842786; -.
DR   Gramene; AT1G64780.1; AT1G64780.1; AT1G64780.
DR   KEGG; ath:AT1G64780; -.
DR   Araport; AT1G64780; -.
DR   TAIR; locus:2010791; AT1G64780.
DR   eggNOG; KOG0682; Eukaryota.
DR   HOGENOM; CLU_000445_33_1_1; -.
DR   InParanoid; Q9ZPJ8; -.
DR   OMA; MACWNSN; -.
DR   OrthoDB; 910733at2759; -.
DR   PhylomeDB; Q9ZPJ8; -.
DR   PRO; PR:Q9ZPJ8; -.
DR   Proteomes; UP000006548; Chromosome 1.
DR   ExpressionAtlas; Q9ZPJ8; baseline and differential.
DR   Genevisible; Q9ZPJ8; AT.
DR   GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR   GO; GO:0005886; C:plasma membrane; IDA:TAIR.
DR   GO; GO:0008519; F:ammonium transmembrane transporter activity; IBA:GO_Central.
DR   GO; GO:0097272; P:ammonium homeostasis; IBA:GO_Central.
DR   GO; GO:0072488; P:ammonium transmembrane transport; IBA:GO_Central.
DR   GO; GO:0015843; P:methylammonium transport; IMP:TAIR.
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   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; Membrane; Phosphoprotein; Reference proteome;
KW   Transmembrane; Transmembrane helix; Transport.
FT   CHAIN           1..514
FT                   /note="Ammonium transporter 1 member 2"
FT                   /id="PRO_0000139744"
FT   TRANSMEM        56..76
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        91..111
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        140..160
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        165..185
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        212..232
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        257..277
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        291..313
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        328..348
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        351..371
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        380..400
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        431..451
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   MOD_RES         472
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0007744|PubMed:19245862"
FT   CONFLICT        198
FT                   /note="R -> G (in Ref. 1; AAD54639)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        310
FT                   /note="A -> S (in Ref. 1; AAD54639)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        438
FT                   /note="V -> I (in Ref. 1; AAD54639)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   514 AA;  55014 MW;  86C3C61F044A0CC6 CRC64;
     MDTATTTCSA VDLSALLSSS SNSTSSLAAA TFLCSQISNI SNKLSDTTYA VDNTYLLFSA
     YLVFAMQLGF AMLCAGSVRA KNTMNIMLTN VLDAAAGAIS YYLFGFAFAF GTPSNGFIGR
     HHSFFALSSY PERPGSDFSF FLYQWAFAIA AAGITSGSIA ERTQFVAYLI YSTFLTGFVY
     PTVSHWFWSS DGWASASRSD NNLLFGSGAI DFAGSGVVHM VGGIAGLCGA LVEGPRIGRF
     DRSGRSVALR GHSASLVVLG TFLLWFGWYG FNPGSFLTIL KGYDKSRPYY GQWSAVGRTA
     VTTTLSGCTA ALTTLFSKRL LAGHWNVIDV CNGLLGGFAA ITSGCAVVEP WAAIVCGFVA
     SWVLIGFNLL AKKLKYDDPL EAAQLHGGCG AWGLIFTGLF ARKEYVNEIY SGDRPYGLFM
     GGGGKLLAAQ IVQIIVIVGW VTVTMGPLFY GLHKMNLLRI SAEDEMAGMD MTRHGGFAYA
     YNDEDDVSTK PWGHFAGRVE PTSRSSTPTP TLTV
 
 
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