HMA4_ORYSJ
ID HMA4_ORYSJ Reviewed; 978 AA.
AC Q6H7M3; A0A1B1ELV0;
DT 05-JUL-2017, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 167.
DE RecName: Full=Copper-transporting ATPase HMA4 {ECO:0000305};
DE EC=7.2.2.8 {ECO:0000269|PubMed:27387148};
DE AltName: Full=Protein HEAVY METAL ATPASE 4 {ECO:0000305};
DE Short=OsHMA4 {ECO:0000303|PubMed:27387148};
GN Name=HMA4 {ECO:0000303|PubMed:27387148};
GN OrderedLocusNames=Os02g0196600 {ECO:0000312|EMBL:BAF08107.1},
GN LOC_Os02g10290 {ECO:0000305};
GN ORFNames=OJ1225_F07.30 {ECO:0000312|EMBL:BAD25263.1},
GN OJ1524_D08.15 {ECO:0000312|EMBL:BAD25276.1},
GN OsJ_05752 {ECO:0000312|EMBL:EAZ22091.1};
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, POLYMORPHISM, VARIANT ALA-914, TISSUE SPECIFICITY, INDUCTION BY
RP COPPER, AND DISRUPTION PHENOTYPE.
RC STRAIN=cv. Lemont;
RX PubMed=27387148; DOI=10.1038/ncomms12138;
RA Huang X.-Y., Deng F., Yamaji N., Pinson S.R.M., Fujii-Kashino M., Danku J.,
RA Douglas A., Guerinot M.L., Salt D.E., Ma J.F.;
RT "A heavy metal P-type ATPase OsHMA4 prevents copper accumulation in rice
RT grain.";
RL Nat. Commun. 7:12138-12138(2016).
RN [2]
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 [3]
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 [4]
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 [5]
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).
CC -!- FUNCTION: Copper (Cu) transporter that mediates Cu transport in root
CC vacuoles. Involved in Cu detoxification by sequestrating Cu into root
CC vacuoles and limiting translocation of Cu from the roots to the shoots,
CC and accumulation in grains. {ECO:0000269|PubMed:27387148}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + Cu(+)(in) + H2O = ADP + Cu(+)(out) + H(+) + phosphate;
CC Xref=Rhea:RHEA:25792, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:49552,
CC ChEBI:CHEBI:456216; EC=7.2.2.8;
CC Evidence={ECO:0000269|PubMed:27387148};
CC -!- SUBCELLULAR LOCATION: Vacuole membrane {ECO:0000269|PubMed:27387148};
CC Multi-pass membrane protein {ECO:0000255}.
CC -!- TISSUE SPECIFICITY: Highly expressed in roots. Expressed in vascular
CC tissues of the stele, mainly in pericycle cells.
CC {ECO:0000269|PubMed:27387148}.
CC -!- INDUCTION: Induced by copper in roots, but not in shoots.
CC {ECO:0000269|PubMed:27387148}.
CC -!- POLYMORPHISM: A single amino acid substitution of Val-914 to Ala
CC increases HMA4 copper transport activity. This allele is found in a
CC number of rice cultivars, such as cv. Lemont, and is associated with
CC low accumulation of copper in rice grains. Identification of natural
CC allelic variation in HMA4 may facilitate the development of rice
CC varieties with grain copper concentrations adapted to dietary needs in
CC function of the copper concentration in soil.
CC {ECO:0000269|PubMed:27387148}.
CC -!- DISRUPTION PHENOTYPE: Reduced plant height and biomass. Reduced
CC fertility. Increased levels of copper in grain, leaf sheath and
CC internodes. {ECO:0000269|PubMed:27387148}.
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; KU168832; ANQ29703.1; -; mRNA.
DR EMBL; AP004184; BAD25263.1; -; Genomic_DNA.
DR EMBL; AP004191; BAD25276.1; -; Genomic_DNA.
DR EMBL; AP008208; BAF08107.1; -; Genomic_DNA.
DR EMBL; AP014958; BAS77458.1; -; Genomic_DNA.
DR EMBL; CM000139; EAZ22091.1; -; Genomic_DNA.
DR RefSeq; XP_015626172.1; XM_015770686.1.
DR AlphaFoldDB; Q6H7M3; -.
DR SMR; Q6H7M3; -.
DR STRING; 4530.OS02T0196600-01; -.
DR PaxDb; Q6H7M3; -.
DR PRIDE; Q6H7M3; -.
DR EnsemblPlants; Os02t0196600-01; Os02t0196600-01; Os02g0196600.
DR GeneID; 4328616; -.
DR Gramene; Os02t0196600-01; Os02t0196600-01; Os02g0196600.
DR KEGG; osa:4328616; -.
DR eggNOG; KOG0207; Eukaryota.
DR HOGENOM; CLU_001771_0_2_1; -.
DR InParanoid; Q6H7M3; -.
DR OMA; HWMLPAW; -.
DR OrthoDB; 649559at2759; -.
DR Proteomes; UP000000763; Chromosome 2.
DR Proteomes; UP000007752; Chromosome 2.
DR Proteomes; UP000059680; Chromosome 2.
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:0005507; F:copper ion binding; IEA:InterPro.
DR GO; GO:0140581; F:P-type monovalent copper transporter activity; IEA:UniProtKB-EC.
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; 3.
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 TIGRFAMs; TIGR00003; TIGR00003; 2.
DR PROSITE; PS00154; ATPASE_E1_E2; 1.
DR PROSITE; PS01047; HMA_1; 1.
DR PROSITE; PS50846; HMA_2; 3.
PE 1: Evidence at protein level;
KW ATP-binding; Copper; Ion transport; Membrane; Metal-binding;
KW Nucleotide-binding; Reference proteome; Repeat; Translocase; Transmembrane;
KW Transmembrane helix; Transport; Vacuole.
FT CHAIN 1..978
FT /note="Copper-transporting ATPase HMA4"
FT /id="PRO_0000440965"
FT TRANSMEM 280..300
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 315..335
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 352..372
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 385..405
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 545..565
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 584..604
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 907..927
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 935..955
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 37..103
FT /note="HMA 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00280"
FT DOMAIN 111..177
FT /note="HMA 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00280"
FT DOMAIN 186..252
FT /note="HMA 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00280"
FT REGION 1..35
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 48
FT /ligand="Cu(+)"
FT /ligand_id="ChEBI:CHEBI:49552"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00280"
FT BINDING 51
FT /ligand="Cu(+)"
FT /ligand_id="ChEBI:CHEBI:49552"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00280"
FT BINDING 122
FT /ligand="Cu(+)"
FT /ligand_id="ChEBI:CHEBI:49552"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00280"
FT BINDING 125
FT /ligand="Cu(+)"
FT /ligand_id="ChEBI:CHEBI:49552"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00280"
FT VARIANT 914
FT /note="V -> A (in strain: cv. Lemont; increases copper
FT transport activity)"
FT /evidence="ECO:0000269|PubMed:27387148"
SQ SEQUENCE 978 AA; 105130 MW; 33CBF467C48B91C5 CRC64;
MEQNGENHLK DPLLQADGGG SGASPAGASP RKERKTRKVM FNVRGISCAS CAVSIETVVA
GLKGVESVSV SPLQGQAVVQ YRPEEADART IKEAIEGLNF EVDELQEQEI AVCRLQIKGM
ACTSCSESVE RALQMVPGVK KAAVGLALEE AKVHFDPNIT SRDLIIEAIE DAGFGADLIS
SGDDVNKVHL KLEGVSSPED IKLIQSRLES VEGVNNVECD TAGQTIIVAY DPDVTGPRLL
IQCIQDAAQP PKYFNASLYS PPKQREAERH HEIRNYRNQF LWSCLFSVPV FMFSMVLPMI
SPFGDWLFYK VCNNMTIGML LRWLLCSPVQ FIIGWRFYVG AYHALKRGYS NMDVLVALGT
NAAYFYSVYI VLKALTSESF EGQDFFETSA MLISFILLGK YLEVVAKGKT SDALSKLTEL
APETACLLTL DKDGNAISET EISTQLLQRN DVIKIVPGEK VPVDGVVIKG QSHVNESMIT
GEARPIAKKP GDKVIGGTVN DNGCIIVKVT HVGSETALSQ IVQLVEAAQL ARAPVQKLAD
RISRFFVPTV VVAAFLTWLG WFVAGQFDIY PREWIPKAMD SFELALQFGI SVLVVACPCA
LGLATPTAVM VATGKGASQG VLIKGGNALE KAHKVKAIIF DKTGTLTVGK PSVVQTKVFS
KIPLLELCDL AAGAEANSEH PLSKAIVEYT KKLREQYGSH SDHIMESKDF EVHPGAGVSA
NVEGKLVLVG NKRLMQEFEV PISSEVEGHM SETEELARTC VLVAIDRTIC GALSVSDPLK
PEAGRAISYL SSMGISSIMV TGDNWATAKS IAKEVGIGTV FAEIDPVGKA EKIKDLQMKG
LTVAMVGDGI NDSPALAAAD VGLAIGAGTD VAIEAADIVL MRSSLEDVIT AIDLSRKTLS
RIRLNYVWAL GYNVLGMPVA AGVLFPFTGI RLPPWLAGAC MAASSVSVVC SSLLLQLYKK
PLHVEEVAAG PKNDPDLV
