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Database: UniProt
Entry: Q95MN3_RABIT
LinkDB: Q95MN3_RABIT
Original site: Q95MN3_RABIT 
ID   Q95MN3_RABIT            Unreviewed;       570 AA.
AC   Q95MN3;
DT   01-DEC-2001, integrated into UniProtKB/TrEMBL.
DT   01-DEC-2001, sequence version 1.
DT   27-MAR-2024, entry version 93.
DE   RecName: Full=Cytochrome b-245 heavy chain {ECO:0000256|ARBA:ARBA00039549};
DE   AltName: Full=CGD91-phox {ECO:0000256|ARBA:ARBA00043223};
DE   AltName: Full=Cytochrome b(558) subunit beta {ECO:0000256|ARBA:ARBA00042446};
DE   AltName: Full=Heme-binding membrane glycoprotein gp91phox {ECO:0000256|ARBA:ARBA00042961};
DE   AltName: Full=Neutrophil cytochrome b 91 kDa polypeptide {ECO:0000256|ARBA:ARBA00043221};
DE   AltName: Full=gp91-1 {ECO:0000256|ARBA:ARBA00042476};
DE   AltName: Full=gp91-phox {ECO:0000256|ARBA:ARBA00042502};
DE   AltName: Full=p22 phagocyte B-cytochrome {ECO:0000256|ARBA:ARBA00030106};
OS   Oryctolagus cuniculus (Rabbit).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Lagomorpha; Leporidae; Oryctolagus.
OX   NCBI_TaxID=9986 {ECO:0000313|EMBL:AAK60123.1};
RN   [1] {ECO:0000313|EMBL:AAK60123.1}
RP   NUCLEOTIDE SEQUENCE.
RX   PubMed=11818454;
RA   Gauss K.A., Mascolo P.L., Siemsen D.W., Nelson L.K., Bunger P.L.,
RA   Pagano P.J., Quinn M.T.;
RT   "Cloning and sequencing of rabbit leukocyte NADPH oxidase genes reveals a
RT   unique p67(phox) homolog.";
RL   J. Leukoc. Biol. 71:319-328(2002).
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000256|ARBA:ARBA00001974};
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC       pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
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DR   EMBL; AF323788; AAK60123.1; -; mRNA.
DR   RefSeq; NP_001075569.1; NM_001082100.1.
DR   AlphaFoldDB; Q95MN3; -.
DR   PeroxiBase; 4551; OcuNOx02.
DR   GeneID; 100008801; -.
DR   KEGG; ocu:100008801; -.
DR   CTD; 1536; -.
DR   OrthoDB; 367877at2759; -.
DR   GO; GO:0034702; C:monoatomic ion channel complex; IEA:UniProtKB-KW.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR   GO; GO:0034220; P:monoatomic ion transmembrane transport; IEA:UniProtKB-KW.
DR   CDD; cd06186; NOX_Duox_like_FAD_NADP; 1.
DR   Gene3D; 3.40.50.80; Nucleotide-binding domain of ferredoxin-NADP reductase (FNR) module; 1.
DR   Gene3D; 2.40.30.10; Translation factors; 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; IPR017938; Riboflavin_synthase-like_b-brl.
DR   PANTHER; PTHR11972:SF60; CYTOCHROME B-245 HEAVY CHAIN; 1.
DR   PANTHER; PTHR11972; NADPH OXIDASE; 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   SFLD; SFLDS00052; Ferric_Reductase_Domain; 1.
DR   SFLD; SFLDG01168; Ferric_reductase_subgroup_(FRE; 1.
DR   SFLD; SFLDG01169; NADPH_oxidase_subgroup_(NOX); 1.
DR   SUPFAM; SSF52343; Ferredoxin reductase-like, C-terminal NADP-linked domain; 1.
DR   SUPFAM; SSF63380; Riboflavin synthase domain-like; 1.
DR   PROSITE; PS51384; FAD_FR; 1.
PE   2: Evidence at transcript level;
KW   Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW   Ion channel {ECO:0000256|ARBA:ARBA00023303};
KW   Ion transport {ECO:0000256|ARBA:ARBA00022882};
KW   Iron {ECO:0000256|ARBA:ARBA00023004};
KW   Isopeptide bond {ECO:0000256|ARBA:ARBA00022499};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|SAM:Phobius}; Transport {ECO:0000256|ARBA:ARBA00022882};
KW   Ubl conjugation {ECO:0000256|ARBA:ARBA00022843};
KW   Voltage-gated channel {ECO:0000256|ARBA:ARBA00022882}.
FT   TRANSMEM        12..32
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        99..121
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        167..192
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        204..224
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          287..397
FT                   /note="FAD-binding FR-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51384"
SQ   SEQUENCE   570 AA;  65605 MW;  18E24CB6022C2776 CRC64;
     MGNWVENEGL SIFVIFVWLG LNVFLFVWYY WVYAFGKKYY YTTKLLGAAL PLARAPAACL
     NFNCLLILLP VCRNLLSFLR GSSACCSTRI RRQLDRNLTF HKMVAWMIAL HSAIHTIAHL
     FNVEWCVNAR VNNSDSYSIA LSEIGDKKNE TYLNFVRERI KNPEGGLLVA VTRLAGVTGI
     IITLCLILII TSSTKIIRRS YFEVFWYTHH LFVIFFIGLA IHGAERIVRG QTEESLKKHD
     PVMCEQHISD WGKIKDCPVP EFSGNPPMTW KWIVGPMFLY LCERLVRFWR SQQKVVITKV
     VTHPFKTIEL QMKKKGFKME VGQYIFVKCP TVSKLEWHPF TLTSAPEEDF FSIHIRIVGD
     WTEGLFNACG CDKQEFQDAW KLPKIAVDGP FGTASEDVFS YEVVMLVGAG IGVTPFASIL
     KSVWYKYCDN ATNLRLKKIY FYWLCRDTHA FEWFADLLQL LETQMQERNN AGFLSYNIYL
     TGWDESQANH FAVHHDEEKD VITGLKQKTL YGRPNWDNEF KTIASQHPNT RIGVFLCGPE
     ALAETLSKQS ISNSESGPRG VHFIFNKENF
//
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