HMA2_ORYSJ
ID HMA2_ORYSJ Reviewed; 1067 AA.
AC A3BF39; C7J449; E7EC32;
DT 05-JUL-2017, integrated into UniProtKB/Swiss-Prot.
DT 20-MAR-2007, sequence version 1.
DT 03-AUG-2022, entry version 108.
DE RecName: Full=Cadmium/zinc-transporting ATPase HMA2 {ECO:0000305};
DE EC=7.2.2.12 {ECO:0000269|PubMed:22123790};
DE EC=7.2.2.21 {ECO:0000269|PubMed:22123790};
DE AltName: Full=Protein HEAVY METAL ATPASE 2 {ECO:0000305};
DE Short=OsHMA2 {ECO:0000303|PubMed:22123790};
GN Name=HMA2 {ECO:0000303|PubMed:22123790};
GN OrderedLocusNames=Os06g0700700 {ECO:0000312|EMBL:BAS99337.1},
GN LOC_Os06g48720 {ECO:0000305};
GN ORFNames=OsJ_22530 {ECO:0000312|EMBL:EAZ38178.1};
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], AND FUNCTION.
RC STRAIN=cv. Volano; TISSUE=Root;
RX PubMed=21388416; DOI=10.1111/j.1365-3040.2011.02299.x;
RA Nocito F.F., Lancilli C., Dendena B., Lucchini G., Sacchi G.A.;
RT "Cadmium retention in rice roots is influenced by cadmium availability,
RT chelation and translocation.";
RL Plant Cell Environ. 34:994-1008(2011).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR
RP LOCATION, TISSUE SPECIFICITY, AND DISRUPTION PHENOTYPE.
RC STRAIN=cv. Nipponbare;
RX PubMed=22123790; DOI=10.1093/pcp/pcr166;
RA Satoh-Nagasawa N., Mori M., Nakazawa N., Kawamoto T., Nagato Y.,
RA Sakurai K., Takahashi H., Watanabe A., Akagi H.;
RT "Mutations in rice (Oryza sativa) heavy metal ATPase 2 (OsHMA2) restrict
RT the translocation of zinc and cadmium.";
RL Plant Cell Physiol. 53:213-224(2012).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, AND TISSUE
RP SPECIFICITY.
RC STRAIN=cv. Nipponbare;
RX PubMed=23575418; DOI=10.1104/pp.113.216564;
RA Yamaji N., Xia J., Mitani-Ueno N., Yokosho K., Feng Ma J.;
RT "Preferential delivery of zinc to developing tissues in rice is mediated by
RT P-type heavy metal ATPase OsHMA2.";
RL Plant Physiol. 162:927-939(2013).
RN [4]
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 [5]
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 [6]
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 [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=15685292; DOI=10.1371/journal.pbio.0030038;
RA Yu J., Wang J., Lin W., Li S., Li H., Zhou J., Ni P., Dong W., Hu S.,
RA Zeng C., Zhang J., Zhang Y., Li R., Xu Z., Li S., Li X., Zheng H., Cong L.,
RA Lin L., Yin J., Geng J., Li G., Shi J., Liu J., Lv H., Li J., Wang J.,
RA Deng Y., Ran L., Shi X., Wang X., Wu Q., Li C., Ren X., Wang J., Wang X.,
RA Li D., Liu D., Zhang X., Ji Z., Zhao W., Sun Y., Zhang Z., Bao J., Han Y.,
RA Dong L., Ji J., Chen P., Wu S., Liu J., Xiao Y., Bu D., Tan J., Yang L.,
RA Ye C., Zhang J., Xu J., Zhou Y., Yu Y., Zhang B., Zhuang S., Wei H.,
RA Liu B., Lei M., Yu H., Li Y., Xu H., Wei S., He X., Fang L., Zhang Z.,
RA Zhang Y., Huang X., Su Z., Tong W., Li J., Tong Z., Li S., Ye J., Wang L.,
RA Fang L., Lei T., Chen C.-S., Chen H.-C., Xu Z., Li H., Huang H., Zhang F.,
RA Xu H., Li N., Zhao C., Li S., Dong L., Huang Y., Li L., Xi Y., Qi Q.,
RA Li W., Zhang B., Hu W., Zhang Y., Tian X., Jiao Y., Liang X., Jin J.,
RA Gao L., Zheng W., Hao B., Liu S.-M., Wang W., Yuan L., Cao M.,
RA McDermott J., Samudrala R., Wang J., Wong G.K.-S., Yang H.;
RT "The genomes of Oryza sativa: a history of duplications.";
RL PLoS Biol. 3:266-281(2005).
RN [8]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=22548273; DOI=10.1111/j.1365-3040.2012.02527.x;
RA Takahashi R., Ishimaru Y., Shimo H., Ogo Y., Senoura T., Nishizawa N.K.,
RA Nakanishi H.;
RT "The OsHMA2 transporter is involved in root-to-shoot translocation of Zn
RT and Cd in rice.";
RL Plant Cell Environ. 35:1948-1957(2012).
CC -!- FUNCTION: Zinc/cadmium transporter that plays an essential role in
CC promoting translocation of zinc and cadmium from roots to shoots
CC (PubMed:21388416, PubMed:22123790, PubMed:23575418, PubMed:22548273).
CC May control cadmium loading into xylem (PubMed:21388416). In roots,
CC transports zinc and cadmium from the apoplast to the symplast to
CC facilitate translocation via the phloem. In nodes, functions to load
CC zinc and cadmium to the phloem for the preferential distribution to the
CC upper nodes and panicles (PubMed:23575418).
CC {ECO:0000269|PubMed:21388416, ECO:0000269|PubMed:22123790,
CC ECO:0000269|PubMed:22548273, ECO:0000269|PubMed:23575418}.
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:0000269|PubMed:22123790};
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:22123790};
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:22123790,
CC ECO:0000269|PubMed:22548273, ECO:0000269|PubMed:23575418}; Multi-pass
CC membrane protein {ECO:0000255}.
CC -!- TISSUE SPECIFICITY: In roots, localizes at the pericycle cells. In
CC nodes, localizes in the phloem parenchyma and companion cells of both
CC enlarged and diffuse vascular bundles. {ECO:0000269|PubMed:23575418}.
CC -!- DISRUPTION PHENOTYPE: Reduced plant height and biomass. Reduced grain
CC yield. Decreased levels of zinc an cadmium in grain, rachis, husk and
CC nodes. {ECO:0000269|PubMed:22123790, ECO:0000269|PubMed:23575418}.
CC -!- SIMILARITY: Belongs to the cation transport ATPase (P-type) (TC 3.A.3)
CC family. Type IB subfamily. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAH93709.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; HQ646362; ADU53143.1; -; mRNA.
DR EMBL; AB661672; BAM36049.1; -; mRNA.
DR EMBL; AB697186; BAN45659.1; -; mRNA.
DR EMBL; AP005966; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AP008212; BAH93709.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AP014962; BAS99337.1; -; Genomic_DNA.
DR EMBL; CM000143; EAZ38178.1; -; Genomic_DNA.
DR RefSeq; XP_015643659.1; XM_015788173.1.
DR AlphaFoldDB; A3BF39; -.
DR SMR; A3BF39; -.
DR STRING; 4530.OS06T0700700-01; -.
DR TCDB; 3.A.3.6.19; the p-type atpase (p-atpase) superfamily.
DR PRIDE; A3BF39; -.
DR EnsemblPlants; Os06t0700700-02; Os06t0700700-02; Os06g0700700.
DR GeneID; 4341965; -.
DR Gramene; Os06t0700700-02; Os06t0700700-02; Os06g0700700.
DR KEGG; osa:4341965; -.
DR eggNOG; KOG0207; Eukaryota.
DR OrthoDB; 649559at2759; -.
DR BRENDA; 7.2.2.12; 4460.
DR Proteomes; UP000000763; Chromosome 6.
DR Proteomes; UP000007752; Chromosome 6.
DR Proteomes; UP000059680; Chromosome 6.
DR ExpressionAtlas; A3BF39; baseline and differential.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma 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 CDD; cd00371; HMA; 1.
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 PRINTS; PR00120; HATPASE.
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; Cell membrane; Ion transport; Membrane;
KW Metal-binding; Nucleotide-binding; Reference proteome; Translocase;
KW Transmembrane; Transmembrane helix; Transport; Zinc.
FT CHAIN 1..1067
FT /note="Cadmium/zinc-transporting ATPase HMA2"
FT /id="PRO_0000440964"
FT TRANSMEM 94..114
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 117..137
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 140..160
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 162..182
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 313..333
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 342..362
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 649..669
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 673..693
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 9..75
FT /note="HMA"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00280"
FT REGION 711..739
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 760..790
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 960..996
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 70
FT /note="A -> T (in Ref. 1; ADU53143)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1067 AA; 115973 MW; 2D0C023B9E56E634 CRC64;
MAAEGGRCQK SYFDVLGICC PSEVPLVEKL LQPLEGVQKV TVIVPSRTVI VVHDVDAISQ
SQIVKALNQA RLEASVRAYG NGSEKITNKW PSPYVLLCGL LLVVSLFEHF WHPLKWFALV
AAAAGLPPIV LRSIAAIRRL TLDVNILMLI AVAGAIALKD YSEAGFIVFL FTTAEWLETR
ASHKATAGMS ALMSMAPQKA ILAETGEVVA ARDVKVNTVI AVKAGEVIPI DGVVVDGRSE
VDESTLTGES FPVSKQPDSQ VWAGTLNIDG YIAVRTTAMA DNSAVAKMAR LVEEAQNSRS
STQRLIDTCA KYYTPAVVVM AGSVAAIPAI AKAHNLKHWF QLALVLLVSA CPCALVLSTP
IATFCALLRA ARTGLLIKGG DVLESLASIK VAAFDKTGTI TRGEFSVEEF QPVGERVSLQ
QLLYWVSSVE SRSSHPMASV LVDYAQSKSV EPKSENVSEF QIYPGEGIYG EIDGAGIYIG
NKRILSRASC ETVPDMKDMK GVTIGYVACN NELIGVFTLS DACRTGSAEA IKELRSLGIK
SVMLTGDSSA AATYAQNQLG NILAEVHAEL LPEDKVRIVG ELKEKDGPTL MVGDGMNDAP
ALAKADVGVS MGVSGSAVAM ETSHVALMSN DIRRIPKAVR LARRTHRTII VNIIFSVITK
LAIVGLAFAG HPLIWAAVLA DVGTCLLVIM YSMLLLREKD SRKAKKCAAS HHGSPKKCCS
SSHHGSHAKK NHGVSHHCSD GPCKSMVSCK ESSVAKNACH DHHHEHNHHE EPAHKHSSNQ
HGCHDHSHGH SNCKEPSNQL ITNKHACHDG HNHCADTSNL HDTKKHDCHG HEHSTCKEEL
NALPPTNDHA CHGHEHSHCE EPVALHSTGE HACHEHEHEH IHCDEPIGSH CADKHACHDH
EQVHEHHCCD EQQTPHTADL HPCHDHDHDN LEVEEVKDCH AEPPHHHNHC CHEPHDQVKN
DTHPVQEHSI SIEESSDHHE HHHNEEHKAE DCGHHPKPKD CAPPPTDCIS RNCCSNTSKG
KDICSSLHRD HHTSQASRCC RSYVKCSRPS RSCCSHSIVK LPEIVVE
