位置:首页 > 蛋白库 > HMA3_ORYSJ
HMA3_ORYSJ
ID   HMA3_ORYSJ              Reviewed;        1004 AA.
AC   Q8H384; E3WCP0; Q0D7L9;
DT   05-JUL-2017, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   03-AUG-2022, entry version 158.
DE   RecName: Full=Cadmium/zinc-transporting ATPase HMA3 {ECO:0000305};
DE            EC=7.2.2.12 {ECO:0000305|PubMed:20823253};
DE            EC=7.2.2.21 {ECO:0000269|PubMed:20823253};
DE   AltName: Full=Protein HEAVY METAL ATPASE 3 {ECO:0000305};
DE            Short=OsHMA3 {ECO:0000303|PubMed:20823253};
GN   Name=HMA3 {ECO:0000303|PubMed:20823253}; Synonyms=CASTLE1n;
GN   OrderedLocusNames=Os07g0232900 {ECO:0000312|EMBL:BAF21154.2},
GN   LOC_Os07g12900 {ECO:0000305};
GN   ORFNames=OSJNBa0061L20.105 {ECO:0000312|EMBL:BAC21509.1};
OS   Oryza sativa subsp. japonica (Rice).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC   Oryzoideae; Oryzeae; Oryzinae; Oryza; Oryza sativa.
OX   NCBI_TaxID=39947;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR
RP   LOCATION, TISSUE SPECIFICITY, POLYMORPHISM, AND MUTAGENESIS OF ARG-80.
RC   STRAIN=cv. Nipponbare;
RX   PubMed=20823253; DOI=10.1073/pnas.1005396107;
RA   Ueno D., Yamaji N., Kono I., Huang C.F., Ando T., Yano M., Ma J.F.;
RT   "Gene limiting cadmium accumulation in rice.";
RL   Proc. Natl. Acad. Sci. U.S.A. 107:16500-16505(2010).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=cv. Akita 63;
RX   PubMed=20840506; DOI=10.1111/j.1469-8137.2010.03459.x;
RA   Miyadate H., Adachi S., Hiraizumi A., Tezuka K., Nakazawa N., Kawamoto T.,
RA   Katou K., Kodama I., Sakurai K., Takahashi H., Satoh-Nagasawa N.,
RA   Watanabe A., Fujimura T., Akagi H.;
RT   "OsHMA3, a P1B-type of ATPase affects root-to-shoot cadmium translocation
RT   in rice by mediating efflux into vacuoles.";
RL   New Phytol. 189:190-199(2011).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Nipponbare;
RX   PubMed=16100779; DOI=10.1038/nature03895;
RG   International rice genome sequencing project (IRGSP);
RT   "The map-based sequence of the rice genome.";
RL   Nature 436:793-800(2005).
RN   [4]
RP   GENOME REANNOTATION.
RC   STRAIN=cv. Nipponbare;
RX   PubMed=18089549; DOI=10.1093/nar/gkm978;
RG   The rice annotation project (RAP);
RT   "The rice annotation project database (RAP-DB): 2008 update.";
RL   Nucleic Acids Res. 36:D1028-D1033(2008).
RN   [5]
RP   GENOME REANNOTATION.
RC   STRAIN=cv. Nipponbare;
RX   PubMed=24280374; DOI=10.1186/1939-8433-6-4;
RA   Kawahara Y., de la Bastide M., Hamilton J.P., Kanamori H., McCombie W.R.,
RA   Ouyang S., Schwartz D.C., Tanaka T., Wu J., Zhou S., Childs K.L.,
RA   Davidson R.M., Lin H., Quesada-Ocampo L., Vaillancourt B., Sakai H.,
RA   Lee S.S., Kim J., Numa H., Itoh T., Buell C.R., Matsumoto T.;
RT   "Improvement of the Oryza sativa Nipponbare reference genome using next
RT   generation sequence and optical map data.";
RL   Rice 6:4-4(2013).
RN   [6]
RP   FUNCTION, AND BIOTECHNOLOGY.
RX   PubMed=25151617; DOI=10.1093/jxb/eru340;
RA   Sasaki A., Yamaji N., Ma J.F.;
RT   "Overexpression of OsHMA3 enhances Cd tolerance and expression of Zn
RT   transporter genes in rice.";
RL   J. Exp. Bot. 65:6013-6021(2014).
CC   -!- FUNCTION: Root-specific cadmium (Cd) transporter that mediates Cd
CC       efflux in root vacuoles. Involved in Cd detoxification by sequestrating
CC       Cd into root vacuoles and limiting translocation of Cd from the roots
CC       to the shoots, and accumulation in grains.
CC       {ECO:0000269|PubMed:20823253, ECO:0000269|PubMed:20840506,
CC       ECO:0000269|PubMed:25151617}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + H2O + Zn(2+)(in) = ADP + H(+) + phosphate + Zn(2+)(out);
CC         Xref=Rhea:RHEA:20621, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:29105, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474,
CC         ChEBI:CHEBI:456216; EC=7.2.2.12;
CC         Evidence={ECO:0000305|PubMed:20823253};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + Cd(2+)(in) + H2O = ADP + Cd(2+)(out) + H(+) + phosphate;
CC         Xref=Rhea:RHEA:12132, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:48775,
CC         ChEBI:CHEBI:456216; EC=7.2.2.21;
CC         Evidence={ECO:0000269|PubMed:20823253};
CC   -!- SUBCELLULAR LOCATION: Vacuole membrane {ECO:0000269|PubMed:20823253,
CC       ECO:0000269|PubMed:20840506}; Multi-pass membrane protein
CC       {ECO:0000255}. Note=Localizes to the tonoplast of root cells.
CC       {ECO:0000269|PubMed:20823253, ECO:0000269|PubMed:20840506}.
CC   -!- TISSUE SPECIFICITY: Specifically expressed in roots.
CC       {ECO:0000269|PubMed:20823253, ECO:0000269|PubMed:20840506}.
CC   -!- POLYMORPHISM: A single amino acid substitution of Arg-80 to His
CC       abolishes HMA3 cadmium transport activity through the tonoplast in root
CC       cells. This allele is found in a number of rice cultivars, and is
CC       associated with high accumulation of cadmium in rice grains.
CC       Identification of natural allelic variation in HMA3 may facilitate the
CC       development of rice varieties with grain cadmium concentrations adapted
CC       to dietary needs in function of the cadmium concentration in soil.
CC       {ECO:0000269|PubMed:20823253}.
CC   -!- BIOTECHNOLOGY: Over-expression of HMA3 allows to reduce efficiently
CC       cadmium accumulation in the grain and to enhance cadmium tolerance in
CC       rice. {ECO:0000269|PubMed:25151617}.
CC   -!- SIMILARITY: Belongs to the cation transport ATPase (P-type) (TC 3.A.3)
CC       family. Type IB subfamily. {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AB557931; BAJ23048.1; -; mRNA.
DR   EMBL; AB559519; BAJ25742.1; -; mRNA.
DR   EMBL; AB559522; BAJ25745.1; -; Genomic_DNA.
DR   EMBL; AP005246; BAC21509.1; -; Genomic_DNA.
DR   EMBL; AP008213; BAF21154.2; -; Genomic_DNA.
DR   EMBL; AP014963; BAT00724.1; -; Genomic_DNA.
DR   RefSeq; XP_015647368.1; XM_015791882.1.
DR   AlphaFoldDB; Q8H384; -.
DR   SMR; Q8H384; -.
DR   STRING; 4530.OS07T0232900-01; -.
DR   TCDB; 3.A.3.6.17; the p-type atpase (p-atpase) superfamily.
DR   PaxDb; Q8H384; -.
DR   PRIDE; Q8H384; -.
DR   EnsemblPlants; Os07t0232900-01; Os07t0232900-01; Os07g0232900.
DR   GeneID; 4342783; -.
DR   Gramene; Os07t0232900-01; Os07t0232900-01; Os07g0232900.
DR   KEGG; osa:4342783; -.
DR   eggNOG; KOG0207; Eukaryota.
DR   HOGENOM; CLU_001771_6_1_1; -.
DR   InParanoid; Q8H384; -.
DR   OMA; FAQPWET; -.
DR   OrthoDB; 649559at2759; -.
DR   BRENDA; 7.2.2.2; 4460.
DR   Proteomes; UP000000763; Chromosome 7.
DR   Proteomes; UP000059680; Chromosome 7.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005774; C:vacuolar membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR   GO; GO:0015086; F:cadmium ion transmembrane transporter activity; IBA:GO_Central.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0008551; F:P-type cadmium transporter activity; IEA:UniProtKB-EC.
DR   GO; GO:0016463; F:P-type zinc transporter activity; IEA:UniProtKB-EC.
DR   GO; GO:0005385; F:zinc ion transmembrane transporter activity; IBA:GO_Central.
DR   Gene3D; 3.40.1110.10; -; 1.
DR   Gene3D; 3.40.50.1000; -; 1.
DR   InterPro; IPR023299; ATPase_P-typ_cyto_dom_N.
DR   InterPro; IPR018303; ATPase_P-typ_P_site.
DR   InterPro; IPR023298; ATPase_P-typ_TM_dom_sf.
DR   InterPro; IPR008250; ATPase_P-typ_transduc_dom_A_sf.
DR   InterPro; IPR036412; HAD-like_sf.
DR   InterPro; IPR023214; HAD_sf.
DR   InterPro; IPR006121; HMA_dom.
DR   InterPro; IPR036163; HMA_dom_sf.
DR   InterPro; IPR027256; P-typ_ATPase_IB.
DR   InterPro; IPR001757; P_typ_ATPase.
DR   InterPro; IPR044492; P_typ_ATPase_HD_dom.
DR   Pfam; PF00403; HMA; 1.
DR   SFLD; SFLDF00027; p-type_atpase; 1.
DR   SUPFAM; SSF55008; SSF55008; 1.
DR   SUPFAM; SSF56784; SSF56784; 1.
DR   SUPFAM; SSF81653; SSF81653; 1.
DR   SUPFAM; SSF81665; SSF81665; 1.
DR   TIGRFAMs; TIGR01525; ATPase-IB_hvy; 1.
DR   TIGRFAMs; TIGR01494; ATPase_P-type; 1.
DR   PROSITE; PS00154; ATPASE_E1_E2; 1.
DR   PROSITE; PS50846; HMA_2; 1.
PE   1: Evidence at protein level;
KW   ATP-binding; Cadmium; Ion transport; Membrane; Metal-binding;
KW   Nucleotide-binding; Reference proteome; Translocase; Transmembrane;
KW   Transmembrane helix; Transport; Vacuole; Zinc.
FT   CHAIN           1..1004
FT                   /note="Cadmium/zinc-transporting ATPase HMA3"
FT                   /id="PRO_0000440963"
FT   TRANSMEM        120..140
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        144..164
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        171..191
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        193..213
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        340..360
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        371..391
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        683..703
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        707..727
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          42..108
FT                   /note="HMA"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00280"
FT   REGION          931..952
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MUTAGEN         80
FT                   /note="R->H: Abolishes HMA3 cadmium transport activity
FT                   through the tonoplast in root cells."
FT                   /evidence="ECO:0000269|PubMed:20823253"
FT   CONFLICT        713
FT                   /note="L -> F (in Ref. 2; BAJ25745)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        853
FT                   /note="G -> A (in Ref. 2; BAJ25745)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   1004 AA;  102664 MW;  610C1303317657F3 CRC64;
     MAGKDEAEGL EARLLLLPPE AAAEEPTRCG GGDGGGGGRK RKKTYLDVLG VCCSAEVALV
     ERLLAPLDGV RVVSVVVASR TVVVEHDPAA APESAIVKAL NKAGLEASVR AYGSSGVVSR
     WPSPYIVASG VLLTASFFEW LFPPLQCLAV AAVVAGAPPM VRRGFAAASR LSLDINVLML
     IAVAGALCLG DYTEAGAIVF LFTTAEWLET LACTKASAGM SSLMGMLPVK AVIATTGEVV
     SVRDVRVGDV VAVRAGEIVP VDGVVVDGQS EVDERSLTGE SFPVPKQPHS EVWAGTMNFD
     GYIAVRTTAL AENSTVAKME RLVEAAQNSR SKTQRLIDSC AKYYTPAVVV VAAGVALIPA
     LLGADGLEQW WKLALVMLVS ACPCALVLST PVASFCAMLR AARMGIFIKG GDVLESLGEI
     RAVAFDKTGT ITRGEFSIDS FHLVGDHKVE MDHLLYWIAS IESKSSHPMA AALVEYAQSK
     SIQPNPENVG DFRIYPGEGI YGEIHGKHIY IGNRRTLARA SSPQSTQEMG EMIKGVSIGY
     VICDGELAGV FSLSDDCRTG AAEAIRELGS LGIKSVMLTG DSSAAATHAQ GQLGGVMEEL
     HSELLPEDKV RLVSGLKARF GPTMMVGDGM NDAAALAAAD VGVSMGISGS AAAMETSHAT
     LMSSDVLRVP EAVRLGRCAR RTIAVNVAGS VAVKAAVLAL AAAWRPVLWA AVLADVGTCL
     LVVLNSMTLL REEWKGGAKE DGACRATARS LVMRSQLAAD SQAPNAADAG AAGREQTNGC
     RCCPKPGMSP EHSVVIDIRA DGERQEERPA EAAVVAKCCG GGGGEGIRCG ASKKPTATVV
     VAKCCGGGGG GEGTRCGASK NPATAAVVAK CCSGGGGEGI GCGASKKPTA TAVVAKCCGG
     GGEGTRCAAS KKPATAAVVA KCCGGDGGEG TGCGASKRSP PAEGSCSGGE GGTNGVGRCC
     TSVKRPTCCD MGAAEVSDSS PETAKDCRNG RCCAKTMNSG EVKG
 
 
维奥蛋白资源库 - 中文蛋白资源 CopyRight © 2010-2024