ID M3YLX9_MUSPF Unreviewed; 568 AA.
AC M3YLX9;
DT 01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 01-MAY-2013, sequence version 1.
DT 27-MAR-2024, entry version 60.
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};
GN Name=CYBB {ECO:0000313|Ensembl:ENSMPUP00000012336.1};
OS Mustela putorius furo (European domestic ferret) (Mustela furo).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Musteloidea; Mustelidae;
OC Mustelinae; Mustela.
OX NCBI_TaxID=9669 {ECO:0000313|Ensembl:ENSMPUP00000012336.1};
RN [1] {ECO:0000313|Ensembl:ENSMPUP00000012336.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (MAR-2023) to UniProtKB.
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; AEYP01038086; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AEYP01038087; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; M3YLX9; -.
DR STRING; 9669.ENSMPUP00000012336; -.
DR Ensembl; ENSMPUT00000012537.1; ENSMPUP00000012336.1; ENSMPUG00000012430.1.
DR eggNOG; KOG0039; Eukaryota.
DR GeneTree; ENSGT00940000160244; -.
DR HOGENOM; CLU_005646_3_1_1; -.
DR InParanoid; M3YLX9; -.
DR OMA; FTFAKEH; -.
DR GO; GO:0034702; C:monoatomic ion channel complex; IEA:UniProtKB-KW.
DR GO; GO:0043020; C:NADPH oxidase complex; IEA:Ensembl.
DR GO; GO:0009055; F:electron transfer activity; IEA:Ensembl.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:Ensembl.
DR GO; GO:0020037; F:heme binding; IEA:Ensembl.
DR GO; GO:0046982; F:protein heterodimerization activity; IEA:Ensembl.
DR GO; GO:0016175; F:superoxide-generating NAD(P)H oxidase activity; IEA:Ensembl.
DR GO; GO:0045087; P:innate immune response; IEA:Ensembl.
DR GO; GO:0034220; P:monoatomic ion transmembrane transport; IEA:UniProtKB-KW.
DR GO; GO:0045730; P:respiratory burst; IEA:Ensembl.
DR GO; GO:0042554; P:superoxide anion generation; IEA:Ensembl.
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 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 4: Predicted;
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..33
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 45..69
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 104..124
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 168..193
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 205..225
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 285..395
FT /note="FAD-binding FR-type"
FT /evidence="ECO:0000259|PROSITE:PS51384"
FT REGION 233..252
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 568 AA; 65505 MW; 82F468103D633EFF CRC64;
MGNWIENEGL SIFVVLVWLG MNVFLFIRFY RFYDIEPQYY YTRKLLGFAL PLARAPAACL
NFNCMLILLP VCRNLLSFLR GSSAKCCSTR IRRQLDRNLT FHKMVAWMIA LHTAIHTIAH
LFNVEWCVNA RVNKSDSYSI ALSRLGDKPG ETYLNFAREE IPQQSRGLYV AVTRVAGITG
IVITLCLILI ITSSAKTIRR SYFEVFWYTH HLFVIFFIGL AIHGAERIVR QQTQESLDKD
NPEKCDKDPS EWGKPGKCAI PQFAGNPPML WKARVKLPFF FFFLARALTF WRKNITKVVT
HPFKTIELQM KKKGFKMEVG QYIFVKCPKV SRLEWHPFTL TSAPEEDFFS IHIRIVGDWT
EGLFNACGCD KQEFQDAWKL PKIAVDGPFG TASEDVFSYE VVMLVGAGIG VTPFASILKS
VWYKYCNNAT NLRLKKIYFY WLCRDTHAFE WFADLLQLLE TQMQERNNAG FLSYNIYLTG
WDESQADHFA VHHDEEKDVI TGLKQKTLYG RPNWDNEFKT IASQHPNTRI GVFLCGPEAL
AETLSKQCIS NSESGPRGVH FIFNKENF
//
