ID A0A2Y9R7F5_TRIMA Unreviewed; 558 AA.
AC A0A2Y9R7F5;
DT 12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT 12-SEP-2018, sequence version 1.
DT 27-MAR-2024, entry version 17.
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=LOC101344219 {ECO:0000313|RefSeq:XP_023587699.1};
OS Trichechus manatus latirostris (Florida manatee).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Afrotheria; Sirenia; Trichechidae; Trichechus.
OX NCBI_TaxID=127582 {ECO:0000313|Proteomes:UP000248480, ECO:0000313|RefSeq:XP_023587699.1};
RN [1] {ECO:0000313|RefSeq:XP_023587699.1}
RP IDENTIFICATION.
RG RefSeq;
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 RefSeq; XP_023587699.1; XM_023731931.1.
DR AlphaFoldDB; A0A2Y9R7F5; -.
DR Proteomes; UP000248480; Unplaced.
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; 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 Reference proteome {ECO:0000313|Proteomes:UP000248480};
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..31
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..221
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 275..385
FT /note="FAD-binding FR-type"
FT /evidence="ECO:0000259|PROSITE:PS51384"
SQ SEQUENCE 558 AA; 64027 MW; AFD8642CBDD5E3DD CRC64;
MANWFVNEGL SIFVILVWLG MNVFLFVWYY LVYDVPVKFF YTRKLLGSAL AFARAPAACL
NFNCMLILLP VCRNLLSFLR GSSACCSTRI RRQLDRNLTF HKMVAWMIAL HTAIHTIAHL
FNVEWCVNAR VNNSDPYSIA LSNIGDKPGE TYLNFARKRI KNPEGGLYVA VTLLAGITGI
VITLCLILII TSSTKTIRRS YFEVFWYTHH LFVIFFIGLA IHGAQRIVRG QTADSLKVHD
PKVCSQNISD WGKIKECPIP EFAGNPPMTW KWIVGPMFLY LCERLVRFWR SQQKVVITKM
KKKGFKMEVG QYIFVKCPKV SKLEWHPFTL TSAPEEDFFS IHIRIVGDWT EGLFKACGCD
KQEFQDAWKL PKIAVDGPFG TASEDVFSYE VVMLVGAGIG VTPFASILKS VWYKYCNNAT
SLRLKKIYFY WLCRDTHAFE WFADLLQLLE TQMQERDNAD FLSYNIYLTG WDESQANHFA
VHHDEEKDVI TGLKQKTLYG RPNWDNEFKT IASQHPNTRI GVFLCGPEAL AETLSKQSIS
NSESGPRGVH FIFNKENF
//
