HMA9_ORYSJ
ID HMA9_ORYSJ Reviewed; 1003 AA.
AC A0A0P0X004; Q0DAA4; Q655X4;
DT 05-JUL-2017, integrated into UniProtKB/Swiss-Prot.
DT 20-JAN-2016, sequence version 1.
DT 03-AUG-2022, entry version 46.
DE RecName: Full=Cation-transporting ATPase HMA5 {ECO:0000305};
DE EC=7.2.2.- {ECO:0000305};
DE AltName: Full=Protein HEAVY METAL ATPASE 5 {ECO:0000305};
DE Short=OsHMA5 {ECO:0000303|PubMed:17827266};
GN Name=HMA9 {ECO:0000303|PubMed:17827266};
GN OrderedLocusNames=Os06g0665800 {ECO:0000312|EMBL:BAS99032.1},
GN LOC_Os06g45500 {ECO:0000305};
GN ORFNames=P0473H04.28 {ECO:0000312|EMBL:BAD45393.1};
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 [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 [2]
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 [3]
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=12869764; DOI=10.1126/science.1081288;
RG The rice full-length cDNA consortium;
RT "Collection, mapping, and annotation of over 28,000 cDNA clones from
RT japonica rice.";
RL Science 301:376-379(2003).
RN [5]
RP FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, INDUCTION, AND
RP DISRUPTION PHENOTYPE.
RX PubMed=17827266; DOI=10.1104/pp.107.102236;
RA Lee S., Kim Y.Y., Lee Y., An G.;
RT "Rice P1B-type heavy-metal ATPase, OsHMA9, is a metal efflux protein.";
RL Plant Physiol. 145:831-842(2007).
CC -!- FUNCTION: Metal efflux transporter that may play a role in
CC detoxification of heavy metals, such as zinc, copper, lead and cadmium,
CC especially in the shoots. {ECO:0000269|PubMed:17827266}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:17827266}.
CC -!- TISSUE SPECIFICITY: Expressed in root vascular cylinder, vascular
CC bundles and mesophyll cells of leaf blades, and anther walls and
CC microspores of stamens. {ECO:0000269|PubMed:17827266}.
CC -!- INDUCTION: Induced by high concentrations of copper, zinc and cadmium.
CC {ECO:0000269|PubMed:17827266}.
CC -!- DISRUPTION PHENOTYPE: No visible phenotype under normal growth
CC conditions, but mutant plants exhibit increased sensitivity to elevated
CC levels of zinc, copper, lead, and to a lesser extent cadmium.
CC {ECO:0000269|PubMed:17827266}.
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=BAD45393.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=BAF20219.2; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AP003628; BAD45393.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AP008212; BAF20219.2; ALT_SEQ; Genomic_DNA.
DR EMBL; AP014962; BAS99032.1; -; Genomic_DNA.
DR EMBL; AK241795; -; NOT_ANNOTATED_CDS; mRNA.
DR RefSeq; XP_015643579.1; XM_015788093.1.
DR AlphaFoldDB; A0A0P0X004; -.
DR SMR; A0A0P0X004; -.
DR STRING; 4530.OS06T0665800-01; -.
DR PaxDb; A0A0P0X004; -.
DR EnsemblPlants; Os06t0665800-01; Os06t0665800-01; Os06g0665800.
DR GeneID; 4341778; -.
DR Gramene; Os06t0665800-01; Os06t0665800-01; Os06g0665800.
DR KEGG; osa:4341778; -.
DR eggNOG; KOG0207; Eukaryota.
DR OMA; NSWISGT; -.
DR OrthoDB; 649559at2759; -.
DR PlantReactome; R-OSA-5225756; Ethylene mediated signaling.
DR Proteomes; UP000000763; Chromosome 6.
DR Proteomes; UP000059680; Chromosome 6.
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; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0005507; F:copper ion binding; IBA:GO_Central.
DR GO; GO:0043682; F:P-type divalent copper transporter activity; IBA:GO_Central.
DR GO; GO:0055070; P:copper ion homeostasis; IBA:GO_Central.
DR GO; GO:0009636; P:response to toxic substance; IEA:UniProtKB-KW.
DR CDD; cd00371; HMA; 2.
DR Gene3D; 3.40.1110.10; -; 2.
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; IPR017969; Heavy-metal-associated_CS.
DR InterPro; IPR006122; HMA_Cu_ion-bd.
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; 2.
DR PRINTS; PR00120; HATPASE.
DR SFLD; SFLDF00027; p-type_atpase; 1.
DR SUPFAM; SSF55008; SSF55008; 2.
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; 2.
DR TIGRFAMs; TIGR00003; TIGR00003; 2.
DR PROSITE; PS00154; ATPASE_E1_E2; 1.
DR PROSITE; PS01047; HMA_1; 2.
DR PROSITE; PS50846; HMA_2; 3.
PE 2: Evidence at transcript level;
KW Cadmium; Cell membrane; Copper; Detoxification; Ion transport; Lead;
KW Membrane; Metal-binding; Reference proteome; Repeat; Translocase;
KW Transmembrane; Transmembrane helix; Transport; Zinc.
FT CHAIN 1..1003
FT /note="Cation-transporting ATPase HMA5"
FT /id="PRO_0000440967"
FT TRANSMEM 302..322
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 331..351
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 372..392
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 396..416
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 562..582
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 599..619
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 938..958
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 966..986
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 51..117
FT /note="HMA 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00280"
FT DOMAIN 133..199
FT /note="HMA 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00280"
FT DOMAIN 207..273
FT /note="HMA 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00280"
FT REGION 6..25
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 62
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00280"
FT BINDING 65
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00280"
FT BINDING 144
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00280"
FT BINDING 147
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00280"
SQ SEQUENCE 1003 AA; 107358 MW; 978BA8041B2D14E9 CRC64;
MAHLQLSAVA GGGRPAAAGG GGDEMEDVRL LDSYDEEMGG GAAAAAAGEE EEAHVRVTGM
TCSACTSAVE GAVSARRGVR RVAVSLLQNR AHVVFDPALL KVEDIIEAIE DAGFDAEIIP
DTAISQPKAQ KTLSAQFRIG GMTCANCVNS VEGILKRLSG VKGAVVALAT SLGEVEYDPS
VINKDEIVEA IEDAGFEAAF LQSSEQDKIL LGLTGLHTER DVNVLHDILK KMIGLRQFDV
NATVSEVEII FDPEAVGLRS IVDAIETGSN GRLKAHVQNP YARGASNDAH EAAKMLHLLR
SSLFLSIPVF FIRMVCPHIP FIRSILMMHC GPFHMGDLLK WILVSIVQFV VGKRFYIAAY
RALRHGSTNM DVLVVLGTTA SYVYSVCALL YGAFTGFHPP IYFETSAMII TFVLFGKYLE
VLAKGKTSDA IKKLVELVPA TALLLLKDKE GKYTEEREID ALLVQPGDIL KVLPGSKVPA
DGVVVWGTSH VNESMITGES APIPKEVSSA VIGGTMNLHG VLHIQANKVG SETVLSQIIS
LVETAQMSKA PIQKFADYVA SIFVPIVITL SMITFLVWFL CGWVGAYPNS WISGTSNCFV
FSLMFAIAVV VIACPCALGL ATPTAVMVAT GVGANHGVLV KGGDALERAQ NVNYVIFDKT
GTLTQGKAVV TTAKVFSGMD LGDFLTLVAS AEASSEHPLA KAIVEYAFHF HFFGKLPTSK
DGIEQRKEDR LSQLLLQVED FSALPGKGVQ CLINGKRVLV GNRTLVTENG VNVPPEAENF
LVDLELNAKT GILVSYDDDF VGLMGITDPL KREAAVVVEG LKKMGVHPVM LTGDNWRTAK
AVAKEVGIED VRAEVMPAGK ADVVRSLQKD GSIVAMVGDG INDSPALAAA DVGMAIGGGT
DIAIEAADYV LVRNNLEDVI TAIDLSRKTF SRIRWNYFFA MAYNVVAIPV AAGALFPFTR
LQMPPWLAGA CMAFSSVSVV CSSLLLRRYR KPRLTTVLQI TVE
