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ZIP9_ARATH
ID   ZIP9_ARATH              Reviewed;         344 AA.
AC   O82643;
DT   26-SEP-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1998, sequence version 1.
DT   03-AUG-2022, entry version 133.
DE   RecName: Full=Zinc transporter 9;
DE   AltName: Full=ZRT/IRT-like protein 9;
GN   Name=ZIP9; OrderedLocusNames=At4g33020; ORFNames=F26P21.140;
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 [GENOMIC DNA].
RX   PubMed=11500563; DOI=10.1104/pp.126.4.1646;
RA   Maeser P., Thomine S., Schroeder J.I., Ward J.M., Hirschi K., Sze H.,
RA   Talke I.N., Amtmann A., Maathuis F.J.M., Sanders D., Harper J.F.,
RA   Tchieu J., Gribskov M., Persans M.W., Salt D.E., Kim S.A., Guerinot M.L.;
RT   "Phylogenetic relationships within cation transporter families of
RT   Arabidopsis.";
RL   Plant Physiol. 126:1646-1667(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=10617198; DOI=10.1038/47134;
RA   Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T.,
RA   Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B.,
RA   Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M.,
RA   de Simone V., Obermaier B., Mache R., Mueller M., Kreis M., Delseny M.,
RA   Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D.,
RA   Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J.,
RA   Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B.,
RA   Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J.,
RA   Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R.,
RA   Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M.,
RA   Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P.,
RA   Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S.,
RA   Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C.,
RA   Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J.,
RA   Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S.,
RA   Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A.,
RA   Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M.,
RA   Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M.,
RA   Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D.,
RA   Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E.,
RA   Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S.,
RA   Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R.,
RA   Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M.,
RA   Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E.,
RA   Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P.,
RA   Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K.,
RA   Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K.,
RA   de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K.,
RA   Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M.,
RA   Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G.,
RA   Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K.,
RA   Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K.,
RA   Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W.,
RA   Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H.,
RA   Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B.,
RA   Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J.,
RA   Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K.,
RA   O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N.,
RA   Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A.,
RA   Martienssen R., McCombie W.R.;
RT   "Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana.";
RL   Nature 402:769-777(1999).
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   INDUCTION.
RX   PubMed=13129917; DOI=10.1074/jbc.m309338200;
RA   Wintz H., Fox T., Wu Y.-Y., Feng V., Chen W., Chang H.-S., Zhu T.,
RA   Vulpe C.D.;
RT   "Expression profiles of Arabidopsis thaliana in mineral deficiencies reveal
RT   novel transporters involved in metal homeostasis.";
RL   J. Biol. Chem. 278:47644-47653(2003).
RN   [5]
RP   FUNCTION, AND INDUCTION.
RX   PubMed=26306426; DOI=10.1111/tpj.12996;
RA   Inaba S., Kurata R., Kobayashi M., Yamagishi Y., Mori I., Ogata Y.,
RA   Fukao Y.;
RT   "Identification of putative target genes of bZIP19, a transcription factor
RT   essential for Arabidopsis adaptation to Zn deficiency in roots.";
RL   Plant J. 84:323-334(2015).
CC   -!- FUNCTION: Zinc transporter involved in zinc uptake in roots. Targeted
CC       by BZIP19 transcription factor in response to zinc-deficient
CC       conditions. {ECO:0000269|PubMed:26306426}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass membrane
CC       protein {ECO:0000305}.
CC   -!- INDUCTION: In shoots and roots by zinc starvation.
CC       {ECO:0000269|PubMed:13129917, ECO:0000269|PubMed:26306426}.
CC   -!- SIMILARITY: Belongs to the ZIP transporter (TC 2.A.5) family.
CC       {ECO:0000305}.
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DR   EMBL; AF369912; AAL38435.1; -; Genomic_DNA.
DR   EMBL; AL031804; CAA21211.1; -; Genomic_DNA.
DR   EMBL; AL161582; CAB80019.1; -; Genomic_DNA.
DR   EMBL; CP002687; AEE86161.1; -; Genomic_DNA.
DR   PIR; T05310; T05310.
DR   RefSeq; NP_195028.1; NM_119456.2.
DR   AlphaFoldDB; O82643; -.
DR   STRING; 3702.AT4G33020.1; -.
DR   PaxDb; O82643; -.
DR   ProteomicsDB; 232336; -.
DR   EnsemblPlants; AT4G33020.1; AT4G33020.1; AT4G33020.
DR   GeneID; 829439; -.
DR   Gramene; AT4G33020.1; AT4G33020.1; AT4G33020.
DR   KEGG; ath:AT4G33020; -.
DR   Araport; AT4G33020; -.
DR   TAIR; locus:2123787; AT4G33020.
DR   eggNOG; KOG1558; Eukaryota.
DR   HOGENOM; CLU_027089_3_0_1; -.
DR   InParanoid; O82643; -.
DR   OMA; PSNGGLM; -.
DR   PhylomeDB; O82643; -.
DR   PRO; PR:O82643; -.
DR   Proteomes; UP000006548; Chromosome 4.
DR   ExpressionAtlas; O82643; baseline and differential.
DR   Genevisible; O82643; AT.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0016020; C:membrane; IBA:GO_Central.
DR   GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR   GO; GO:0005385; F:zinc ion transmembrane transporter activity; IBA:GO_Central.
DR   GO; GO:0010043; P:response to zinc ion; IEP:TAIR.
DR   GO; GO:0071577; P:zinc ion transmembrane transport; IMP:UniProtKB.
DR   InterPro; IPR003689; ZIP.
DR   InterPro; IPR004698; Zn/Fe_permease_fun/pln.
DR   Pfam; PF02535; Zip; 1.
DR   TIGRFAMs; TIGR00820; zip; 1.
PE   2: Evidence at transcript level;
KW   Cell membrane; Ion transport; Membrane; Reference proteome; Transmembrane;
KW   Transmembrane helix; Transport; Zinc; Zinc transport.
FT   CHAIN           1..344
FT                   /note="Zinc transporter 9"
FT                   /id="PRO_0000068762"
FT   TRANSMEM        1..21
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        22..30
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        31..51
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        52..72
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        73..93
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        94..188
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        189..209
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        210..221
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        222..242
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        243..251
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        252..272
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        273..291
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        292..312
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        313..323
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        324..344
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   344 AA;  36151 MW;  AABCA10526EA88C5 CRC64;
     MASILISGAA GVSIPLVGTL LPLNGGLMRG AKAFAAGVIL ATGFVHMLSG GSKALSDPCL
     PEFPWKMFPF PEFFAMVAAL LTLLADFMIT GYYERKQEKM MNQSVESLGT QVSVMSDPGL
     ESGFLRDQED GGALHIVGMR AHAEHHRHSL SMGAEGFEAL SKRSGVSGHG HGHSHGHGDV
     GLDSGVRHVV VSQILEMGIV SHSIIIGISL GVSHSPCTIR PLLLALSFHQ FFEGFALGGC
     VAEARLTPRG SAMMAFFFAI TTPIGVAVGT AIASSYNSYS VAALVAEGVL DSLSAGILVY
     MALVDLIAAD FLSKKMSVDF RVQVVSYCFL FLGAGMMSAL AIWA
 
 
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