位置:首页 > 蛋白库 > APX3_ORYSJ
APX3_ORYSJ
ID   APX3_ORYSJ              Reviewed;         291 AA.
AC   Q0JEQ2; A0A0N7KIP4; Q6TY83; Q7XWZ7;
DT   11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT   03-OCT-2006, sequence version 1.
DT   03-AUG-2022, entry version 106.
DE   RecName: Full=Probable L-ascorbate peroxidase 3, peroxisomal {ECO:0000305};
DE            EC=1.11.1.11 {ECO:0000305};
DE   AltName: Full=OsAPx3 {ECO:0000303|PubMed:15599508};
GN   Name=APX3 {ECO:0000303|PubMed:15599508};
GN   OrderedLocusNames=Os04g0223300 {ECO:0000312|EMBL:BAS88185.1},
GN   LOC_Os04g14680 {ECO:0000305};
GN   ORFNames=OsJ_013310 {ECO:0000312|EMBL:EAZ29827.1},
GN   OSJNBb0072N21.2 {ECO:0000312|EMBL:CAD39836.2};
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 [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Nipponbare;
RX   PubMed=12447439; DOI=10.1038/nature01183;
RA   Feng Q., Zhang Y., Hao P., Wang S., Fu G., Huang Y., Li Y., Zhu J., Liu Y.,
RA   Hu X., Jia P., Zhang Y., Zhao Q., Ying K., Yu S., Tang Y., Weng Q.,
RA   Zhang L., Lu Y., Mu J., Lu Y., Zhang L.S., Yu Z., Fan D., Liu X., Lu T.,
RA   Li C., Wu Y., Sun T., Lei H., Li T., Hu H., Guan J., Wu M., Zhang R.,
RA   Zhou B., Chen Z., Chen L., Jin Z., Wang R., Yin H., Cai Z., Ren S., Lv G.,
RA   Gu W., Zhu G., Tu Y., Jia J., Zhang Y., Chen J., Kang H., Chen X., Shao C.,
RA   Sun Y., Hu Q., Zhang X., Zhang W., Wang L., Ding C., Sheng H., Gu J.,
RA   Chen S., Ni L., Zhu F., Chen W., Lan L., Lai Y., Cheng Z., Gu M., Jiang J.,
RA   Li J., Hong G., Xue Y., Han B.;
RT   "Sequence and analysis of rice chromosome 4.";
RL   Nature 420:316-320(2002).
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).
RN   [6]
RP   NOMENCLATURE.
RX   PubMed=15599508; DOI=10.1007/s00239-004-2666-z;
RA   Teixeira F.K., Menezes-Benavente L., Margis R., Margis-Pinheiro M.;
RT   "Analysis of the molecular evolutionary history of the ascorbate peroxidase
RT   gene family: inferences from the rice genome.";
RL   J. Mol. Evol. 59:761-770(2004).
RN   [7]
RP   SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX   PubMed=16397796; DOI=10.1007/s00425-005-0214-8;
RA   Teixeira F.K., Menezes-Benavente L., Galvao V.C., Margis R.,
RA   Margis-Pinheiro M.;
RT   "Rice ascorbate peroxidase gene family encodes functionally diverse
RT   isoforms localized in different subcellular compartments.";
RL   Planta 224:300-314(2006).
CC   -!- FUNCTION: Plays a key role in hydrogen peroxide removal. {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H2O2 + L-ascorbate = 2 H2O + L-dehydroascorbate;
CC         Xref=Rhea:RHEA:22996, ChEBI:CHEBI:15377, ChEBI:CHEBI:16240,
CC         ChEBI:CHEBI:38290, ChEBI:CHEBI:58539; EC=1.11.1.11;
CC         Evidence={ECO:0000305};
CC   -!- COFACTOR:
CC       Name=heme b; Xref=ChEBI:CHEBI:60344; Evidence={ECO:0000250};
CC       Note=Binds 1 heme b (iron(II)-protoporphyrin IX) group. {ECO:0000250};
CC   -!- SUBCELLULAR LOCATION: Peroxisome membrane
CC       {ECO:0000305|PubMed:16397796}; Single-pass membrane protein
CC       {ECO:0000255}. Note=Targets to peroxisomes and to a reticular
CC       compartment circulating the nucleus. {ECO:0000269|PubMed:16397796}.
CC   -!- TISSUE SPECIFICITY: Expressed in stems. {ECO:0000269|PubMed:16397796}.
CC   -!- MISCELLANEOUS: Binds one cation per subunit; probably K(+), but might
CC       also be Ca(2+). {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the peroxidase family. Ascorbate peroxidase
CC       subfamily. {ECO:0000305}.
CC   -!- CAUTION: According to PubMed:15599508, it may be peroxisomal. There is
CC       however no experimental evidence to prove this. {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; AL606634; CAD39836.2; -; Genomic_DNA.
DR   EMBL; AP008210; BAF14185.1; -; Genomic_DNA.
DR   EMBL; AP014960; BAS88185.1; -; Genomic_DNA.
DR   EMBL; CM000141; EAZ29827.1; -; Genomic_DNA.
DR   RefSeq; XP_015634435.1; XM_015778949.1.
DR   AlphaFoldDB; Q0JEQ2; -.
DR   SMR; Q0JEQ2; -.
DR   STRING; 4530.OS04T0223300-00; -.
DR   PeroxiBase; 1867; OsAPx03.
DR   PaxDb; Q0JEQ2; -.
DR   PRIDE; Q0JEQ2; -.
DR   EnsemblPlants; Os04t0223300-00; Os04t0223300-00; Os04g0223300.
DR   GeneID; 4335202; -.
DR   Gramene; Os04t0223300-00; Os04t0223300-00; Os04g0223300.
DR   KEGG; osa:4335202; -.
DR   eggNOG; ENOG502QR1E; Eukaryota.
DR   HOGENOM; CLU_036959_3_0_1; -.
DR   InParanoid; Q0JEQ2; -.
DR   OMA; DANQGAR; -.
DR   OrthoDB; 1228462at2759; -.
DR   BRENDA; 1.11.1.11; 4460.
DR   Proteomes; UP000000763; Chromosome 4.
DR   Proteomes; UP000007752; Chromosome 4.
DR   Proteomes; UP000059680; Chromosome 4.
DR   Genevisible; Q0JEQ2; OS.
DR   GO; GO:0009507; C:chloroplast; IBA:GO_Central.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005778; C:peroxisomal membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0020037; F:heme binding; IEA:InterPro.
DR   GO; GO:0016688; F:L-ascorbate peroxidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0004601; F:peroxidase activity; IBA:GO_Central.
DR   GO; GO:0034599; P:cellular response to oxidative stress; IBA:GO_Central.
DR   GO; GO:0042744; P:hydrogen peroxide catabolic process; IBA:GO_Central.
DR   GO; GO:0000302; P:response to reactive oxygen species; IBA:GO_Central.
DR   InterPro; IPR044831; Ccp1-like.
DR   InterPro; IPR002016; Haem_peroxidase.
DR   InterPro; IPR010255; Haem_peroxidase_sf.
DR   InterPro; IPR002207; Peroxidase_I.
DR   InterPro; IPR019794; Peroxidases_AS.
DR   InterPro; IPR019793; Peroxidases_heam-ligand_BS.
DR   PANTHER; PTHR31356; PTHR31356; 1.
DR   Pfam; PF00141; peroxidase; 1.
DR   PRINTS; PR00459; ASPEROXIDASE.
DR   PRINTS; PR00458; PEROXIDASE.
DR   SUPFAM; SSF48113; SSF48113; 1.
DR   PROSITE; PS00435; PEROXIDASE_1; 1.
DR   PROSITE; PS00436; PEROXIDASE_2; 1.
DR   PROSITE; PS50873; PEROXIDASE_4; 1.
PE   2: Evidence at transcript level;
KW   Calcium; Heme; Hydrogen peroxide; Iron; Membrane; Metal-binding;
KW   Oxidoreductase; Peroxidase; Peroxisome; Potassium; Reference proteome;
KW   Transmembrane; Transmembrane helix.
FT   CHAIN           1..291
FT                   /note="Probable L-ascorbate peroxidase 3, peroxisomal"
FT                   /id="PRO_0000055595"
FT   TRANSMEM        263..283
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   REGION          114..133
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        119..133
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        41
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00297,
FT                   ECO:0000255|PROSITE-ProRule:PRU10012"
FT   BINDING         161
FT                   /ligand="heme b"
FT                   /ligand_id="ChEBI:CHEBI:60344"
FT                   /ligand_part="Fe"
FT                   /ligand_part_id="ChEBI:CHEBI:18248"
FT                   /note="axial binding residue"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00297"
FT   BINDING         162
FT                   /ligand="K(+)"
FT                   /ligand_id="ChEBI:CHEBI:29103"
FT                   /evidence="ECO:0000250"
FT   BINDING         178
FT                   /ligand="K(+)"
FT                   /ligand_id="ChEBI:CHEBI:29103"
FT                   /evidence="ECO:0000250"
FT   BINDING         185
FT                   /ligand="K(+)"
FT                   /ligand_id="ChEBI:CHEBI:29103"
FT                   /evidence="ECO:0000250"
FT   SITE            37
FT                   /note="Transition state stabilizer"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00297"
SQ   SEQUENCE   291 AA;  32048 MW;  53CCEA0D39781236 CRC64;
     MSAAPVVDAE YMAEVERARR DLRALIASKS CAPIMLRLAW HDAGTYDKAT KTGGPNGSIR
     FPQEYSHAAN AGIKIAIDLL EPMKQKHPKI TYADLYQLAG VVAVEVTGGP TIDYVPGRRD
     SSDSPEEGRL PDAKKGAAHL REVFYRMGLS DKDIVALSGG HTLGKARPER SGFDGAWTKD
     PLKFDNSYFI ELLKENSEGL LKLPTDKALV EDPTFRRYVE LYAKDEDAFF RDYAESHKKL
     SELGFTPPRS AFIYKSCQKP KSLLMQTAAG VAVAAAVVAW AYLCESNKRL G
 
 
维奥蛋白资源库 - 中文蛋白资源 CopyRight © 2010-2024