HMA5_ORYSJ
ID HMA5_ORYSJ Reviewed; 1002 AA.
AC A3AWA4; Q0JB51; Q7XU05;
DT 05-JUL-2017, integrated into UniProtKB/Swiss-Prot.
DT 20-MAR-2007, sequence version 1.
DT 03-AUG-2022, entry version 116.
DE RecName: Full=Copper-transporting ATPase HMA5 {ECO:0000305};
DE EC=7.2.2.8 {ECO:0000269|PubMed:24064929};
DE AltName: Full=Protein HEAVY METAL ATPASE 5 {ECO:0000305};
DE Short=OsHMA5 {ECO:0000303|PubMed:24064929};
GN Name=HMA5 {ECO:0000303|PubMed:24064929};
GN OrderedLocusNames=Os04g0556000 {ECO:0000312|EMBL:BAS90429.1},
GN LOC_Os04g46940 {ECO:0000305};
GN ORFNames=OsJ_15734 {ECO:0000312|EMBL:EAZ31593.1},
GN OSJNBb0012E24.8 {ECO:0000312|EMBL:CAD41643.2};
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, SUBCELLULAR LOCATION, TISSUE
RP SPECIFICITY, INDUCTION BY COPPER, AND DISRUPTION PHENOTYPE.
RX PubMed=24064929; DOI=10.1104/pp.113.226225;
RA Deng F., Yamaji N., Xia J., Ma J.F.;
RT "A member of the heavy metal P-type ATPase OsHMA5 is involved in xylem
RT loading of copper in rice.";
RL Plant Physiol. 163:1353-1362(2013).
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 plays an essential role in
CC promoting translocation of Cu from roots to shoots. Involved in loading
CC Cu to the xylem of the roots and other organs, including panicles.
CC {ECO:0000269|PubMed:24064929}.
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:24064929};
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:24064929};
CC Multi-pass membrane protein {ECO:0000255}.
CC -!- TISSUE SPECIFICITY: Expressed in root pericycle cells, xylem region of
CC diffuse vascular bundles in the first node, and vascular tissues of
CC peduncle, rachis and husk. {ECO:0000269|PubMed:24064929}.
CC -!- INDUCTION: Weakly induced by high copper concentration.
CC {ECO:0000269|PubMed:24064929}.
CC -!- DISRUPTION PHENOTYPE: Reduced grain yield. Increased levels of copper
CC in roots. Decreased levels of copper in shoots and grains.
CC {ECO:0000269|PubMed:24064929}.
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=BAF15436.2; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=CAD41643.2; Type=Erroneous gene model prediction; Evidence={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; AB840272; BAO05266.1; -; mRNA.
DR EMBL; AL606647; CAD41643.2; ALT_SEQ; Genomic_DNA.
DR EMBL; AP008210; BAF15436.2; ALT_SEQ; Genomic_DNA.
DR EMBL; AP014960; BAS90429.1; -; Genomic_DNA.
DR EMBL; CM000141; EAZ31593.1; -; Genomic_DNA.
DR RefSeq; XP_015635938.1; XM_015780452.1.
DR AlphaFoldDB; A3AWA4; -.
DR SMR; A3AWA4; -.
DR STRING; 4530.OS04T0556000-01; -.
DR PaxDb; A3AWA4; -.
DR PRIDE; A3AWA4; -.
DR EnsemblPlants; Os04t0556000-01; Os04t0556000-01; Os04g0556000.
DR GeneID; 4336625; -.
DR Gramene; Os04t0556000-01; Os04t0556000-01; Os04g0556000.
DR KEGG; osa:4336625; -.
DR eggNOG; KOG0207; Eukaryota.
DR HOGENOM; CLU_001771_0_2_1; -.
DR OMA; IEKTGYE; -.
DR OrthoDB; 649559at2759; -.
DR Proteomes; UP000000763; Chromosome 4.
DR Proteomes; UP000007752; Chromosome 4.
DR Proteomes; UP000059680; Chromosome 4.
DR ExpressionAtlas; A3AWA4; 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: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; 3.
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; 3.
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; 2.
DR PROSITE; PS50846; HMA_2; 3.
PE 2: Evidence at transcript level;
KW ATP-binding; Cell membrane; Copper; Ion transport; Membrane; Metal-binding;
KW Nucleotide-binding; Reference proteome; Repeat; Translocase; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..1002
FT /note="Copper-transporting ATPase HMA5"
FT /id="PRO_0000440966"
FT TRANSMEM 320..340
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 354..374
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 392..412
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 425..445
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 585..605
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 624..644
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 943..963
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 972..992
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 75..141
FT /note="HMA 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00280"
FT DOMAIN 153..219
FT /note="HMA 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00280"
FT DOMAIN 228..294
FT /note="HMA 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00280"
FT REGION 32..63
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 86
FT /ligand="Cu(+)"
FT /ligand_id="ChEBI:CHEBI:49552"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00280"
FT BINDING 89
FT /ligand="Cu(+)"
FT /ligand_id="ChEBI:CHEBI:49552"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00280"
FT BINDING 164
FT /ligand="Cu(+)"
FT /ligand_id="ChEBI:CHEBI:49552"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00280"
FT BINDING 167
FT /ligand="Cu(+)"
FT /ligand_id="ChEBI:CHEBI:49552"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00280"
SQ SEQUENCE 1002 AA; 107987 MW; A7F1E574DE4CCEBF CRC64;
MAASTRALFL SCFHGSGGGG GTSEVSRRLV LRPRYPSMPR RPRSAAVAGE GGEGGGGGGD
GDLEAAAVGA EEEEKVAVFE VSGMTCAACA GSVEKAVKRL QGIHDAAVDV LGGRAQVVFY
PAFVSEEKIR ETIQDVGFEA KLIDEEVKEK NILVCRLHIK GMTCTSCAST VESILQVVPG
VQRASVALAT EEAEIRYDRR IVTASQLTHA VEETGFEAIL ITTGDDQSRI DLKVDGTLNE
RSIMIVKSSV QALPGVEDIK VDPELHKITI SYKPDQTGPR DLIEVIESAA SGDLTVSIYP
EADGRQQHRH GEIKRYRQSF LWSLVFTIPV FLTSMVFMYI PGLKDGLEKK VINMMSIGEL
LRWILSTPVQ FVIGRRFYTG AYKALSHGSS NMDVLIALGT NTAYFYSVYS ILRAASSHNY
MATDFFETSS MLISFILLGK YLEILAKGKT SEAIAKLMDL APETATMLIY DHEGNVVGEK
EIDSRLIQKN DVIKVVPGGK VASDGFVIWG QSHVNESMIT GESRPVAKRK GDTVIGGTVN
ENGVLHVRAT FVGSESALAQ IVRLVESAQM AKAPVQKFAD QISRVFVPLV IILSLLTWLA
WFLAGRLHGY PNSWIPSSMD SFQLALQFGI SVMVIACPCA LGLATPTAVM VATGVGASQG
VLIKGGQALE SAQKVDCIVF DKTGTLTIGK PVVVNTRLLK NMVLREFYAY VAAAEVNSEH
PLGKAVVEHA KKFHSEESHV WTEARDFISV TGHGVKAKIS GRAVMVGNKS FMLTSGIDIP
VEALEILTEE EEKAQTAIIV AMDQEVVGII SVSDPIKPNA REVISYLKSM KVESIMVTGD
NWGTANAISK EVGIENTVAE AKPEQKAEKV KELQSAGRTV AMVGDGINDS PALVSADVGL
AIGAGTDVAI EAADIVLMKS NLEDVITAID LSRKTFFRIR MNYVWALGYN IIGIPIAAGV
LFPSTRFRLP PWVAGAAMAA SSVSVVCWSL LLRYYKSPKL GR