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RBOHB_ORYSI
ID   RBOHB_ORYSI             Reviewed;         905 AA.
AC   Q6J2K5;
DT   11-JAN-2011, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 117.
DE   RecName: Full=Respiratory burst oxidase homolog protein B;
DE            EC=1.11.1.-;
DE            EC=1.6.3.-;
DE   AltName: Full=NADPH oxidase RBOHB;
DE            Short=OsrbohB;
GN   Name=RBOHB; ORFNames=OsI_01895;
OS   Oryza sativa subsp. indica (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=39946;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Seedling;
RA   Ge X., Song F., Zheng Z.;
RT   "Identification of a benzothiadiazole-induced respiratory burst oxidase
RT   homolog B gene, OsrbohB.";
RL   Submitted (APR-2004) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. 93-11;
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: Calcium-dependent NADPH oxidase that generates superoxide.
CC       {ECO:0000250}.
CC   -!- SUBUNIT: Monomer and homodimer, stabilized by swapping the EF-hand
CC       motifs. Interacts with GTP-bound RAC1. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane
CC       protein {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the RBOH (TC 5.B.1.3) family. {ECO:0000305}.
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DR   EMBL; AY603975; AAT35117.1; -; mRNA.
DR   EMBL; CM000126; EEC70631.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q6J2K5; -.
DR   SMR; Q6J2K5; -.
DR   STRING; 39946.Q6J2K5; -.
DR   PRIDE; Q6J2K5; -.
DR   EnsemblPlants; BGIOSGA001663-TA; BGIOSGA001663-PA; BGIOSGA001663.
DR   Gramene; BGIOSGA001663-TA; BGIOSGA001663-PA; BGIOSGA001663.
DR   HOGENOM; CLU_005646_6_0_1; -.
DR   OMA; HKITANT; -.
DR   Proteomes; UP000007015; Chromosome 1.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005509; F:calcium ion binding; IEA:EnsemblPlants.
DR   GO; GO:0016174; F:NAD(P)H oxidase H2O2-forming activity; IEA:InterPro.
DR   GO; GO:0004601; F:peroxidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0043621; F:protein self-association; IEA:EnsemblPlants.
DR   Gene3D; 3.40.50.80; -; 1.
DR   InterPro; IPR000778; Cyt_b245_heavy_chain.
DR   InterPro; IPR011992; EF-hand-dom_pair.
DR   InterPro; IPR018247; EF_Hand_1_Ca_BS.
DR   InterPro; IPR002048; EF_hand_dom.
DR   InterPro; IPR013112; FAD-bd_8.
DR   InterPro; IPR017927; FAD-bd_FR_type.
DR   InterPro; IPR013130; Fe3_Rdtase_TM_dom.
DR   InterPro; IPR013121; Fe_red_NAD-bd_6.
DR   InterPro; IPR039261; FNR_nucleotide-bd.
DR   InterPro; IPR013623; NADPH_Ox.
DR   InterPro; IPR029654; RBOHB.
DR   InterPro; IPR017938; Riboflavin_synthase-like_b-brl.
DR   PANTHER; PTHR11972:SF141; PTHR11972:SF141; 1.
DR   Pfam; PF08022; FAD_binding_8; 1.
DR   Pfam; PF01794; Ferric_reduct; 1.
DR   Pfam; PF08030; NAD_binding_6; 1.
DR   Pfam; PF08414; NADPH_Ox; 1.
DR   PRINTS; PR00466; GP91PHOX.
DR   SUPFAM; SSF47473; SSF47473; 1.
DR   SUPFAM; SSF52343; SSF52343; 1.
DR   SUPFAM; SSF63380; SSF63380; 1.
DR   PROSITE; PS00018; EF_HAND_1; 1.
DR   PROSITE; PS50222; EF_HAND_2; 2.
DR   PROSITE; PS51384; FAD_FR; 1.
PE   2: Evidence at transcript level;
KW   Calcium; FAD; Flavoprotein; Membrane; Metal-binding; NADP; Oxidoreductase;
KW   Peroxidase; Reference proteome; Repeat; Transmembrane; Transmembrane helix.
FT   CHAIN           1..905
FT                   /note="Respiratory burst oxidase homolog protein B"
FT                   /id="PRO_0000403421"
FT   TOPO_DOM        1..355
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        356..376
FT                   /note="Helical; Name=1"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        377..440
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        441..461
FT                   /note="Helical; Name=2"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        462..496
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        497..517
FT                   /note="Helical; Name=3"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        518..539
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        540..560
FT                   /note="Helical; Name=4"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        561..568
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        569..586
FT                   /note="Helical; Name=5"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        587..717
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        718..738
FT                   /note="Helical; Name=6"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        739..905
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          229..264
FT                   /note="EF-hand 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   DOMAIN          273..308
FT                   /note="EF-hand 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   DOMAIN          395..551
FT                   /note="Ferric oxidoreductase"
FT   DOMAIN          587..715
FT                   /note="FAD-binding FR-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00716"
FT   REGION          1..46
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          69..134
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          172..180
FT                   /note="EF-hand-like 1"
FT                   /evidence="ECO:0000250"
FT   REGION          206..217
FT                   /note="EF-hand-like 2"
FT                   /evidence="ECO:0000250"
FT   COMPBIAS        12..42
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        93..128
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         242
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   BINDING         244
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   BINDING         246
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   BINDING         248
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   BINDING         253
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
SQ   SEQUENCE   905 AA;  101759 MW;  CF3187424F7BA16A CRC64;
     MADLEAGMVA AATDQGNSTR SQDDAATLIP NSGNLGSSNR STKTARFKDD DELVEITLDV
     QRDSVAIQEV RGVDEGGSGH GTGFDGLPLV SPSSKSGKLT SKLRQVTNGL KMKSSSRKAP
     SPQAQQSAKR VRKRLDRTKS SAAVALKGLQ FVTAKVGNDG WAAVEKRFNQ LQVDGVLLRS
     RFGKCIGMDG SDEFAVQMFD SLARKRGIVK QVLTKDELKD FYEQLTDQGF DNRLRTFFDM
     VDKNADGRLT AEEVKEIIAL SASANKLSKI KERADEYTAL IMEELDPTNL GYIEMEDLEA
     LLLQSPSEAA ARSTTTHSSK LSKALSMKLA SNKEMSPVRH YWQQFMYFLE ENWKRSWVMT
     LWISICIALF IWKFIQYRNR AVFGIMGYCV TTAKGAAETL KFNMALVLLP VCRNTITWIR
     SKTQVGAVVP FNDNINFHKV IAAGVAVGVA LHAGAHLTCD FPRLLHASDA QYELMKPFFG
     EKRPPNYWWF VKGTEGWTGV VMVVLMAIAF TLAQPWFRRN KLKDSNPLKK MTGFNAFWFT
     HHLFVIVYTL LFVHGTCLYL SRKWYKKTTW MYLAVPVVLY VSERILRLFR SHDAVGIQKV
     AVYPGNVLAL YMSKPPGFRY RSGQYIFIKC TAVSPYEWHP FSITSAPGDD YLSVHIRTRG
     DWTSRLRTVF SEACRPPTEG ESGLLRADLS KGITDEKARF PKLLVDGPYG APAQDYREYD
     VLLLIGLGIG ATPLISIVKD VLNHIQGEGS VGTTEPESSS KAKKKPFMTK RAYFYWVTRE
     EGSFEWFRGV MNEVSEKDKD GVIELHNHCS SVYQEGDARS ALIVMLQELQ HAKKGVDILS
     GTSVKTHFAR PNWRSVFKKV AVSHENQRVG VFYCGEPVLV PQLRQLSADF THKTNTRFDF
     HKENF
 
 
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