RBOHA_ARATH
ID RBOHA_ARATH Reviewed; 902 AA.
AC O81209; Q9LY21;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 15-JAN-2008, sequence version 2.
DT 03-AUG-2022, entry version 141.
DE RecName: Full=Respiratory burst oxidase homolog protein A;
DE EC=1.11.1.-;
DE EC=1.6.3.-;
DE AltName: Full=NADPH oxidase RBOHA;
DE Short=AtRBOHA;
GN Name=RBOHA; OrderedLocusNames=At5g07390; ORFNames=T2I1.100;
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND TISSUE SPECIFICITY.
RC STRAIN=cv. Landsberg erecta;
RX PubMed=9628030; DOI=10.1046/j.1365-313x.1998.00136.x;
RA Torres M.A., Onouchi H., Hamada S., Machida C., Hammond-Kosack K.E.,
RA Jones J.D.G.;
RT "Six Arabidopsis thaliana homologues of the human respiratory burst oxidase
RT (gp91phox).";
RL Plant J. 14:365-370(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130714; DOI=10.1038/35048507;
RA Tabata S., Kaneko T., Nakamura Y., Kotani H., Kato T., Asamizu E.,
RA Miyajima N., Sasamoto S., Kimura T., Hosouchi T., Kawashima K., Kohara M.,
RA Matsumoto M., Matsuno A., Muraki A., Nakayama S., Nakazaki N., Naruo K.,
RA Okumura S., Shinpo S., Takeuchi C., Wada T., Watanabe A., Yamada M.,
RA Yasuda M., Sato S., de la Bastide M., Huang E., Spiegel L., Gnoj L.,
RA O'Shaughnessy A., Preston R., Habermann K., Murray J., Johnson D.,
RA Rohlfing T., Nelson J., Stoneking T., Pepin K., Spieth J., Sekhon M.,
RA Armstrong J., Becker M., Belter E., Cordum H., Cordes M., Courtney L.,
RA Courtney W., Dante M., Du H., Edwards J., Fryman J., Haakensen B.,
RA Lamar E., Latreille P., Leonard S., Meyer R., Mulvaney E., Ozersky P.,
RA Riley A., Strowmatt C., Wagner-McPherson C., Wollam A., Yoakum M., Bell M.,
RA Dedhia N., Parnell L., Shah R., Rodriguez M., Hoon See L., Vil D.,
RA Baker J., Kirchoff K., Toth K., King L., Bahret A., Miller B., Marra M.A.,
RA Martienssen R., McCombie W.R., Wilson R.K., Murphy G., Bancroft I.,
RA Volckaert G., Wambutt R., Duesterhoeft A., Stiekema W., Pohl T.,
RA Entian K.-D., Terryn N., Hartley N., Bent E., Johnson S., Langham S.-A.,
RA McCullagh B., Robben J., Grymonprez B., Zimmermann W., Ramsperger U.,
RA Wedler H., Balke K., Wedler E., Peters S., van Staveren M., Dirkse W.,
RA Mooijman P., Klein Lankhorst R., Weitzenegger T., Bothe G., Rose M.,
RA Hauf J., Berneiser S., Hempel S., Feldpausch M., Lamberth S.,
RA Villarroel R., Gielen J., Ardiles W., Bents O., Lemcke K., Kolesov G.,
RA Mayer K.F.X., Rudd S., Schoof H., Schueller C., Zaccaria P., Mewes H.-W.,
RA Bevan M., Fransz P.F.;
RT "Sequence and analysis of chromosome 5 of the plant Arabidopsis thaliana.";
RL Nature 408:823-826(2000).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
RN [5]
RP GENE FAMILY, AND NOMENCLATURE.
RX PubMed=16760484; DOI=10.1104/pp.106.078089;
RA Sagi M., Fluhr R.;
RT "Production of reactive oxygen species by plant NADPH oxidases.";
RL Plant Physiol. 141:336-340(2006).
CC -!- FUNCTION: Calcium-dependent NADPH oxidase that generates superoxide.
CC -!- SUBUNIT: Monomer and homodimer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane
CC protein {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=1;
CC Comment=A number of isoforms are produced. According to EST
CC sequences.;
CC Name=1;
CC IsoId=O81209-1; Sequence=Displayed;
CC -!- SIMILARITY: Belongs to the RBOH (TC 5.B.1.3) family. {ECO:0000305}.
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DR EMBL; AF055353; AAC39475.1; -; Genomic_DNA.
DR EMBL; AL163912; CAB87928.1; -; Genomic_DNA.
DR EMBL; CP002688; AED91151.1; -; Genomic_DNA.
DR EMBL; BT003857; AAO41907.1; -; mRNA.
DR PIR; T49878; T49878.
DR RefSeq; NP_196356.1; NM_120821.2. [O81209-1]
DR AlphaFoldDB; O81209; -.
DR SMR; O81209; -.
DR STRING; 3702.AT5G07390.1; -.
DR PeroxiBase; 3282; AtRboh01.
DR TCDB; 5.B.1.1.8; the phagocyte (gp91(phox)) nadph oxidase family.
DR PaxDb; O81209; -.
DR PRIDE; O81209; -.
DR ProteomicsDB; 225940; -. [O81209-1]
DR EnsemblPlants; AT5G07390.1; AT5G07390.1; AT5G07390. [O81209-1]
DR GeneID; 830630; -.
DR Gramene; AT5G07390.1; AT5G07390.1; AT5G07390. [O81209-1]
DR KEGG; ath:AT5G07390; -.
DR Araport; AT5G07390; -.
DR TAIR; locus:2183309; AT5G07390.
DR eggNOG; KOG0039; Eukaryota.
DR InParanoid; O81209; -.
DR OMA; SEVCNPR; -.
DR OrthoDB; 936110at2759; -.
DR PhylomeDB; O81209; -.
DR BioCyc; ARA:AT5G07390-MON; -.
DR PRO; PR:O81209; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; O81209; baseline and differential.
DR Genevisible; O81209; AT.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0031226; C:intrinsic component of plasma membrane; IDA:TAIR.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0005509; F:calcium ion binding; IDA:TAIR.
DR GO; GO:0000293; F:ferric-chelate reductase activity; IBA:GO_Central.
DR GO; GO:0016174; F:NAD(P)H oxidase H2O2-forming activity; IBA:GO_Central.
DR GO; GO:0004601; F:peroxidase activity; IEA:UniProtKB-KW.
DR CDD; cd00051; EFh; 1.
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; IPR017938; Riboflavin_synthase-like_b-brl.
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; 1.
DR PROSITE; PS51384; FAD_FR; 1.
PE 2: Evidence at transcript level;
KW Alternative splicing; Calcium; FAD; Flavoprotein; Membrane; Metal-binding;
KW NADP; Oxidoreductase; Peroxidase; Phosphoprotein; Reference proteome;
KW Repeat; Transmembrane; Transmembrane helix.
FT CHAIN 1..902
FT /note="Respiratory burst oxidase homolog protein A"
FT /id="PRO_0000313753"
FT TOPO_DOM 1..344
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 345..365
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 366..380
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 381..401
FT /note="Helical; Name=2"
FT /evidence="ECO:0000250"
FT TOPO_DOM 402..428
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 429..449
FT /note="Helical; Name=3"
FT /evidence="ECO:0000250"
FT TOPO_DOM 450..484
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 485..505
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 506..529
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 530..550
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 551..709
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 710..730
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 731..902
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 221..256
FT /note="EF-hand 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 265..300
FT /note="EF-hand 2"
FT /evidence="ECO:0000305"
FT DOMAIN 383..540
FT /note="Ferric oxidoreductase"
FT DOMAIN 575..703
FT /note="FAD-binding FR-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00716"
FT REGION 63..87
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 107..130
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 163..173
FT /note="EF-hand-like 1"
FT /evidence="ECO:0000250"
FT REGION 198..209
FT /note="EF-hand-like 2"
FT /evidence="ECO:0000250"
FT REGION 738..760
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 70..87
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 234
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 236
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 238
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 240
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250, ECO:0000255|PROSITE-
FT ProRule:PRU00448"
FT BINDING 245
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT MOD_RES 311
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9FIJ0"
FT MOD_RES 315
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9FIJ0"
FT CONFLICT 166
FT /note="T -> N (in Ref. 1; AAC39475)"
FT /evidence="ECO:0000305"
FT CONFLICT 207
FT /note="I -> M (in Ref. 1; AAC39475)"
FT /evidence="ECO:0000305"
FT CONFLICT 307
FT /note="G -> S (in Ref. 1; AAC39475)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 902 AA; 102935 MW; E43286CAD4F857B2 CRC64;
MMNRSEMQKL GFEHVRYYTE SPYNRGESSA NVATTSNYYG EDEPYVEITL DIHDDSVSVY
GLKSPNHRGA GSNYEDQSLL RQGRSGRSNS VLKRLASSVS TGITRVASSV SSSSARKPPR
PQLAKLRRSK SRAELALKGL KFITKTDGVT GWPEVEKRFY VMTMTTNGLL HRSRFGECIG
MKSTEFALAL FDALARRENV SGDSININEL KEFWKQITDQ DFDSRLRTFF AMVDKDSDGR
LNEAEVREII TLSASANELD NIRRQADEYA ALIMEELDPY HYGYIMIENL EILLLQAPMQ
DVRDGEGKKL SKMLSQNLMV PQSRNLGARF CRGMKYFLFD NWKRVWVMAL WIGAMAGLFT
WKFMEYRKRS AYEVMGVCVC IAKGAAETLK LNMAMILLPV CRNTITWLRT KTKLSAIVPF
DDSLNFHKVI AIGISVGVGI HATSHLACDF PRLIAADEDQ YEPMEKYFGP QTKRYLDFVQ
SVEGVTGIGM VVLMTIAFTL ATTWFRRNKL NLPGPLKKIT GFNAFWYSHH LFVIVYSLLV
VHGFYVYLII EPWYKKTTWM YLMVPVVLYL CERLIRAFRS SVEAVSVLKV AVLPGNVLSL
HLSRPSNFRY KSGQYMYLNC SAVSTLEWHP FSITSAPGDD YLSVHIRVLG DWTKQLRSLF
SEVCKPRPPD EHRLNRADSK HWDYIPDFPR ILIDGPYGAP AQDYKKFEVV LLVGLGIGAT
PMISIVSDII NNLKGVEEGS NRRQSPIHNM VTPPVSPSRK SETFRTKRAY FYWVTREQGS
FDWFKNVMDE VTETDRKNVI ELHNYCTSVY EEGDARSALI TMLQSLNHAK HGVDVVSGTR
VMSHFARPNW RSVFKRIAVN HPKTRVGVFY CGAAGLVKEL RHLSLDFSHK TSTKFIFHKE
NF
