ID G5BMP9_HETGA Unreviewed; 570 AA.
AC G5BMP9;
DT 14-DEC-2011, integrated into UniProtKB/TrEMBL.
DT 14-DEC-2011, sequence version 1.
DT 27-MAR-2024, entry version 53.
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|EMBL:JAO02703.1};
GN ORFNames=GW7_05813 {ECO:0000313|EMBL:EHB10560.1};
OS Heterocephalus glaber (Naked mole rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Hystricomorpha; Bathyergidae;
OC Heterocephalus.
OX NCBI_TaxID=10181 {ECO:0000313|EMBL:EHB10560.1, ECO:0000313|Proteomes:UP000006813};
RN [1] {ECO:0000313|EMBL:EHB10560.1, ECO:0000313|Proteomes:UP000006813}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=21993625; DOI=10.1038/nature10533;
RA Kim E.B., Fang X., Fushan A.A., Huang Z., Lobanov A.V., Han L.,
RA Marino S.M., Sun X., Turanov A.A., Yang P., Yim S.H., Zhao X.,
RA Kasaikina M.V., Stoletzki N., Peng C., Polak P., Xiong Z., Kiezun A.,
RA Zhu Y., Chen Y., Kryukov G.V., Zhang Q., Peshkin L., Yang L., Bronson R.T.,
RA Buffenstein R., Wang B., Han C., Li Q., Chen L., Zhao W., Sunyaev S.R.,
RA Park T.J., Zhang G., Wang J., Gladyshev V.N.;
RT "Genome sequencing reveals insights into physiology and longevity of the
RT naked mole rat.";
RL Nature 479:223-227(2011).
RN [2] {ECO:0000313|EMBL:JAO02703.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Skin {ECO:0000313|EMBL:JAO02703.1};
RA Bens M., Sahm A., Jahn N., Morhart M., Holtze S., Hildebrandt T.B.,
RA Platzer M., Szafranski K.;
RT "FRAMA: From RNA-seq data to annotated mRNA assemblies.";
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
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; JH171106; EHB10560.1; -; Genomic_DNA.
DR EMBL; GEBF01000930; JAO02703.1; -; Transcribed_RNA.
DR RefSeq; XP_004850091.1; XM_004850034.2.
DR AlphaFoldDB; G5BMP9; -.
DR STRING; 10181.G5BMP9; -.
DR Ensembl; ENSHGLT00000059455; ENSHGLP00000044791; ENSHGLG00000042638.
DR Ensembl; ENSHGLT00100043871; ENSHGLP00100033681; ENSHGLG00100037325.
DR GeneID; 101709509; -.
DR KEGG; hgl:101709509; -.
DR eggNOG; KOG0039; Eukaryota.
DR InParanoid; G5BMP9; -.
DR OMA; FTFAKEH; -.
DR OrthoDB; 367877at2759; -.
DR Proteomes; UP000006813; Unassembled WGS sequence.
DR Bgee; ENSHGLG00000013641; Expressed in liver and 4 other cell types or tissues.
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:0045335; C:phagocytic vesicle; IEA:Ensembl.
DR GO; GO:0016175; F:superoxide-generating NAD(P)H oxidase activity; IEA:Ensembl.
DR GO; GO:0050665; P:hydrogen peroxide biosynthetic process; IEA:Ensembl.
DR GO; GO:0006954; P:inflammatory response; 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:0006801; P:superoxide metabolic process; 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 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 Reference proteome {ECO:0000313|Proteomes:UP000006813};
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..30
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 51..71
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; 65604 MW; D10BCD485E17E6D9 CRC64;
MGNWAVNEGL SIFVILMWLG MNVFLFVYYY KVYDDEDKYF YTRKLLGKAL ALARAPAACL
NFNCMLILLP VCRNLLSFLR GSSACCSTRI RRQLDRNLTF HKMVAWMIAL HTAIHTIAHL
FNVEWCVDAR VNNSDPYSIA LSDIGDKENE DYLNFARKRI KNPEGGLYVA VTRLAGITGI
VITLCLILII TSSTKTIRRS YFEVFWYTHH LFVIFFIGLA IHGAEKIVRG QTTQSLKAHN
ITICNQNISQ WGKIENCPVP KFSGNPPMTW KWIVGPMFLY LCERLVRFWR SQQKVVITKV
VTHPFKTIEL QMKKKGFKME VGQYIFVKCP KVSKLEWHPF TLTSAPEEDF FSIHIRIVGD
WTEGLFNACG CDKQEFQDAW KLPKIAVDGP FGTASEDVFS YEVVMLVGAG IGVTPFASIL
KSVWYKYCNN ATNLKLKKIY FYWLCRDTHA FEWFADLLQL LETQMQERNN ADFLSYNIYL
TGWDESQANH FAVHHDEEKD VITGLKQKTL YGRPNWDNEF KTIASQHPNT RIGVFLCGPE
ALAETLNKQS ISNSDSGPRG VHFIFNKENF
//