NOX3_RAT
ID NOX3_RAT Reviewed; 568 AA.
AC Q672K1;
DT 21-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2004, sequence version 1.
DT 03-AUG-2022, entry version 94.
DE RecName: Full=NADPH oxidase 3;
DE EC=1.6.3.-;
GN Name=Nox3;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RC STRAIN=Sprague-Dawley; TISSUE=Inner ear;
RX PubMed=15326186; DOI=10.1074/jbc.m403046200;
RA Banfi B., Malgrange B., Knisz J., Steger K., Dubois-Dauphin M.,
RA Krause K.-H.;
RT "NOX3, a superoxide-generating NADPH oxidase of the inner ear.";
RL J. Biol. Chem. 279:46065-46072(2004).
CC -!- FUNCTION: NADPH oxidase which constitutively produces superoxide upon
CC formation of a complex with CYBA/p22phox. Plays a role in the
CC biogenesis of otoconia/otolith, which are crystalline structures of the
CC inner ear involved in the perception of gravity (By similarity).
CC {ECO:0000250}.
CC -!- ACTIVITY REGULATION: Activated by the ototoxic drug cisplatin.
CC Activated by NOXO1. Cooperatively activated by NCF1 and NCF2 or NOXA1
CC in a phorbol 12-myristate 13-acetate (PMA)-dependent manner. Inhibited
CC by diphenyleneiodonium chloride (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Interacts with and stabilizes CYBA/p22phox. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane
CC protein {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Expressed in the inner ear by the spiral glanglia
CC and the organ of Corti. {ECO:0000269|PubMed:15326186}.
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DR EMBL; AY573239; AAT80343.1; -; mRNA.
DR RefSeq; NP_001004216.1; NM_001004216.1.
DR AlphaFoldDB; Q672K1; -.
DR SMR; Q672K1; -.
DR STRING; 10116.ENSRNOP00000022148; -.
DR PeroxiBase; 5407; RnoNOx03.
DR GlyGen; Q672K1; 1 site.
DR PaxDb; Q672K1; -.
DR Ensembl; ENSRNOT00000022148; ENSRNOP00000022148; ENSRNOG00000016490.
DR GeneID; 292279; -.
DR KEGG; rno:292279; -.
DR UCSC; RGD:1303190; rat.
DR CTD; 50508; -.
DR RGD; 1303190; Nox3.
DR eggNOG; KOG0039; Eukaryota.
DR GeneTree; ENSGT00940000160501; -.
DR HOGENOM; CLU_005646_3_1_1; -.
DR InParanoid; Q672K1; -.
DR OMA; MCRLYSS; -.
DR OrthoDB; 936110at2759; -.
DR PhylomeDB; Q672K1; -.
DR BRENDA; 1.6.3.1; 5301.
DR Reactome; R-RNO-5668599; RHO GTPases Activate NADPH Oxidases.
DR Reactome; R-RNO-9013149; RAC1 GTPase cycle.
DR Reactome; R-RNO-9013423; RAC3 GTPase cycle.
DR PRO; PR:Q672K1; -.
DR Proteomes; UP000002494; Chromosome 1.
DR Bgee; ENSRNOG00000016490; Expressed in frontal cortex.
DR GO; GO:0005737; C:cytoplasm; ISO:RGD.
DR GO; GO:0016020; C:membrane; TAS:RGD.
DR GO; GO:0043020; C:NADPH oxidase complex; ISO:RGD.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0016491; F:oxidoreductase activity; TAS:RGD.
DR GO; GO:0016175; F:superoxide-generating NAD(P)H oxidase activity; IBA:GO_Central.
DR GO; GO:0006952; P:defense response; IBA:GO_Central.
DR GO; GO:0009590; P:detection of gravity; ISO:RGD.
DR GO; GO:0048840; P:otolith development; ISO:RGD.
DR GO; GO:0009629; P:response to gravity; ISO:RGD.
DR GO; GO:0042554; P:superoxide anion generation; IBA:GO_Central.
DR GO; GO:0001659; P:temperature homeostasis; ISO:RGD.
DR Gene3D; 3.40.50.80; -; 1.
DR InterPro; IPR000778; Cyt_b245_heavy_chain.
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; IPR029653; NOX3.
DR InterPro; IPR017938; Riboflavin_synthase-like_b-brl.
DR PANTHER; PTHR11972:SF12; PTHR11972:SF12; 1.
DR Pfam; PF08022; FAD_binding_8; 1.
DR Pfam; PF01794; Ferric_reduct; 1.
DR Pfam; PF08030; NAD_binding_6; 1.
DR PRINTS; PR00466; GP91PHOX.
DR SUPFAM; SSF52343; SSF52343; 1.
DR SUPFAM; SSF63380; SSF63380; 1.
DR PROSITE; PS51384; FAD_FR; 1.
PE 2: Evidence at transcript level;
KW Glycoprotein; Membrane; Oxidoreductase; Reference proteome; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..568
FT /note="NADPH oxidase 3"
FT /id="PRO_0000227598"
FT TOPO_DOM 1..12
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 13..33
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 34..49
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 50..70
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 71..103
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 104..124
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 125..167
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 168..188
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 189..201
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 202..222
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 223..395
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 396..416
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 417..568
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 55..284
FT /note="Ferric oxidoreductase"
FT DOMAIN 285..395
FT /note="FAD-binding FR-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00716"
FT CARBOHYD 238
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 568 AA; 64416 MW; 1E19B013E7320EE2 CRC64;
MPTCWILNES VSFVVALLWL AINIYLFIDT FCWYAEEESF FYTRVILGSA LAWARASAVC
LNFNCMLILL PVSRNFVSLV RGTSVCCRGP WRRQLDKNLK FHKLVAYGIA VNSVIHIVAH
LFNLERYHLG QAKDAEGLLA ALSKLGNAPN ESYLNPVRTL YTGTTTQLLM TVSGITGLVI
SLALILIMTS STEFIRQSSY ELFWYTHHIF IFLFISLAIH GGGRIIRGQT PESLRLHNVT
FCRDHFDEWQ EAASCPVPQF SGKEPSAWKW TLGPVVLYAC EIIIRFWRSH QEVVITKVVS
HPSAVLELHM KKRDFKMAPG QYIFIQCPSI SPLEWHPFTL TSAPQEDFFS VHIRASGDWT
EALLKAFGAE GQAPSELCSM PRLAVDGPFG GSLADVFHYP VSVCIATGIG VTPFASLLKS
VWYKCCESQS LPGLSKVYFY WICRDAAAFE WFADLLLSLE TQMSEQGKAH LLSYHIYLTG
WDEYQAIHIA LHWDESLDVI TGLKQKTFYG RPNWNEEFKQ IAYNHPSSSI GVFFCGPKAM
SKTLQKMCRL YSSSDPRGVH FYYNKENF
