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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};
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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
 
 
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