ID K7FK13_PELSI Unreviewed; 572 AA.
AC K7FK13;
DT 09-JAN-2013, integrated into UniProtKB/TrEMBL.
DT 09-JAN-2013, sequence version 1.
DT 27-MAR-2024, entry version 63.
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:ENSPSIP00000008373.1};
OS Pelodiscus sinensis (Chinese softshell turtle) (Trionyx sinensis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Testudinata; Testudines; Cryptodira; Trionychia;
OC Trionychidae; Pelodiscus.
OX NCBI_TaxID=13735 {ECO:0000313|Ensembl:ENSPSIP00000008373.1, ECO:0000313|Proteomes:UP000007267};
RN [1] {ECO:0000313|Proteomes:UP000007267}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Daiwa-1 {ECO:0000313|Proteomes:UP000007267};
RG Soft-shell Turtle Genome Consortium;
RL Submitted (OCT-2011) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Proteomes:UP000007267}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Daiwa-1 {ECO:0000313|Proteomes:UP000007267};
RX PubMed=23624526; DOI=10.1038/ng.2615;
RA Wang Z., Pascual-Anaya J., Zadissa A., Li W., Niimura Y., Huang Z., Li C.,
RA White S., Xiong Z., Fang D., Wang B., Ming Y., Chen Y., Zheng Y.,
RA Kuraku S., Pignatelli M., Herrero J., Beal K., Nozawa M., Li Q., Wang J.,
RA Zhang H., Yu L., Shigenobu S., Wang J., Liu J., Flicek P., Searle S.,
RA Wang J., Kuratani S., Yin Y., Aken B., Zhang G., Irie N.;
RT "The draft genomes of soft-shell turtle and green sea turtle yield insights
RT into the development and evolution of the turtle-specific body plan.";
RL Nat. Genet. 45:701-706(2013).
RN [3] {ECO:0000313|Ensembl:ENSPSIP00000008373.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-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; AGCU01157650; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AGCU01157651; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; K7FK13; -.
DR STRING; 13735.ENSPSIP00000008373; -.
DR Ensembl; ENSPSIT00000008416.1; ENSPSIP00000008373.1; ENSPSIG00000007475.1.
DR eggNOG; KOG0039; Eukaryota.
DR GeneTree; ENSGT00940000160244; -.
DR HOGENOM; CLU_005646_3_1_1; -.
DR OMA; FTFAKEH; -.
DR TreeFam; TF105354; -.
DR Proteomes; UP000007267; Unassembled WGS sequence.
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 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 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 Reference proteome {ECO:0000313|Proteomes:UP000007267};
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 169..192
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 212..230
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 289..399
FT /note="FAD-binding FR-type"
FT /evidence="ECO:0000259|PROSITE:PS51384"
SQ SEQUENCE 572 AA; 65982 MW; BE7A459083D13B96 CRC64;
MGNWVVNEGL SIFVILVWLG LNAFLFWWYY RVYDVPKKFY YSRELLGSAL PWARAPAACL
NFNCLLILLP VCRNLLSFLR GSSAPKCCST RIRRQLDRNL TFHKMVAWMI ALHTAIHTVA
HLFNVERCVD ARVEANGTIQ AVLSKLGDKE DESYLNFVRK KFKNPEGGLY VAFTYLAGLS
GVIITLALIL IITSSTKTIR RSYFEVFWFT HHLFVIFFIG LVIHGAGRIV RGQTEESLKQ
HDPEKCAKHF MQWGIKSECP IPQFAGNPPM TWKWVIVPMI LYFFERMVRF WRSQQKVVIT
KVVNHPFKTF ELQMMKKGFK MEVGQYIFVK CPAVSHLEWH PFTLTSAPEE DYFSIHIRIV
GDWTEGLANV CGCDKQEFQE AWKLPKIAVD GPFGTASEDV FSYETVMLVG AGIGVTPFAS
ILKSVWYKYC NDATNLKLKK IYFYWLCRDT HAFEWFADLL QSLEIQMQER DNADFLSYNI
YLTGWDESQA THFTVHHDEE KDVITGLKQK TLYGRPNWDN EFKTIASQHP SSRVGVFLCG
PEALAETLNK QCISNSAADP RGVHFIFNKE NF
//
