GenomeNet

Database: UniProt
Entry: A0A2K6LQT6_RHIBE
LinkDB: A0A2K6LQT6_RHIBE
Original site: A0A2K6LQT6_RHIBE 
ID   A0A2K6LQT6_RHIBE        Unreviewed;       513 AA.
AC   A0A2K6LQT6;
DT   28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT   28-MAR-2018, sequence version 1.
DT   27-MAR-2024, entry version 27.
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:ENSRBIP00000025881.1};
OS   Rhinopithecus bieti (Black snub-nosed monkey) (Pygathrix bieti).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC   Cercopithecidae; Colobinae; Rhinopithecus.
OX   NCBI_TaxID=61621 {ECO:0000313|Ensembl:ENSRBIP00000025881.1, ECO:0000313|Proteomes:UP000233180};
RN   [1] {ECO:0000313|Ensembl:ENSRBIP00000025881.1, ECO:0000313|Proteomes:UP000233180}
RP   NUCLEOTIDE SEQUENCE.
RA   Wu, C.-I. and Zhang, Y.;
RT   "Genome of Rhinopithecus bieti.";
RL   Submitted (JUN-2016) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Ensembl:ENSRBIP00000025881.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (SEP-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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   AlphaFoldDB; A0A2K6LQT6; -.
DR   STRING; 61621.ENSRBIP00000025881; -.
DR   Ensembl; ENSRBIT00000049793.1; ENSRBIP00000025881.1; ENSRBIG00000036822.1.
DR   GeneTree; ENSGT00940000160244; -.
DR   OMA; FTFAKEH; -.
DR   Proteomes; UP000233180; Unplaced.
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   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:UP000233180};
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        152..177
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        189..209
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          272..380
FT                   /note="FAD-binding FR-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51384"
SQ   SEQUENCE   513 AA;  59459 MW;  436BFBEDDF394704 CRC64;
     LVWLGLNVFL FVWYYRVYDV PVKFFYTRKL LGSALALARA PAACLNFNCM LILLPVCRNL
     LSFLRGSSAC CSTRVRRQLD RNLTFHKMVA WMIALHSAIH TIAHLFNVEW CVNARVGNSD
     RYSVALSELG DRQNESYLNF ARDRIKNPEG GLYLAVTRVA GITGVVITLC LILIITSSTK
     TIRRSYFEVF WYTHHLFVIF FIGLAIHGVE RIVRGQTAES LVKHRPEVCE QKISEWGKIE
     DCPIPQFAGN PPMTWKWIVG PMFLYLCERL VRFWRSQQKV VITKVVTHPF KTIELQMKKK
     GFKMEVGQYI FVKCPKVSKL EWHPFTLTSA PEEDFFSIHI RIVGDWTEGL FNACGCDKQE
     FQDAWKLPKY CNNATNLRLK KIYFYWLCRD THAFEWFADL LQLLESQMQE RNNAGFLSYN
     IYLTGWDESQ ANHFAVHHDE EKDVITGLKQ KTLYGRPNWD NEFKTIASQH PNTRIGVFLC
     GPEALAKTLS KQSISNSESG PRGVHFIFNK ENF
//
DBGET integrated database retrieval system