ID V8NL77_OPHHA Unreviewed; 509 AA.
AC V8NL77;
DT 19-FEB-2014, integrated into UniProtKB/TrEMBL.
DT 19-FEB-2014, sequence version 1.
DT 27-MAR-2024, entry version 39.
DE SubName: Full=5-beta-cholestane-3-alpha,7-alpha-diol 12-alpha-hydroxylase {ECO:0000313|EMBL:ETE62726.1};
DE Flags: Fragment;
GN Name=CYP8B1 {ECO:0000313|EMBL:ETE62726.1};
GN ORFNames=L345_11510 {ECO:0000313|EMBL:ETE62726.1};
OS Ophiophagus hannah (King cobra) (Naja hannah).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC Serpentes; Colubroidea; Elapidae; Elapinae; Ophiophagus.
OX NCBI_TaxID=8665 {ECO:0000313|EMBL:ETE62726.1, ECO:0000313|Proteomes:UP000018936};
RN [1] {ECO:0000313|EMBL:ETE62726.1, ECO:0000313|Proteomes:UP000018936}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Blood {ECO:0000313|EMBL:ETE62726.1};
RX PubMed=24297900; DOI=10.1073/pnas.1314702110;
RA Vonk F.J., Casewell N.R., Henkel C.V., Heimberg A.M., Jansen H.J.,
RA McCleary R.J., Kerkkamp H.M., Vos R.A., Guerreiro I., Calvete J.J.,
RA Wuster W., Woods A.E., Logan J.M., Harrison R.A., Castoe T.A.,
RA de Koning A.P., Pollock D.D., Yandell M., Calderon D., Renjifo C.,
RA Currier R.B., Salgado D., Pla D., Sanz L., Hyder A.S., Ribeiro J.M.,
RA Arntzen J.W., van den Thillart G.E., Boetzer M., Pirovano W., Dirks R.P.,
RA Spaink H.P., Duboule D., McGlinn E., Kini R.M., Richardson M.K.;
RT "The king cobra genome reveals dynamic gene evolution and adaptation in the
RT snake venom system.";
RL Proc. Natl. Acad. Sci. U.S.A. 110:20651-20656(2013).
CC -!- COFACTOR:
CC Name=heme; Xref=ChEBI:CHEBI:30413;
CC Evidence={ECO:0000256|ARBA:ARBA00001971,
CC ECO:0000256|PIRSR:PIRSR000047-1};
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000256|ARBA:ARBA00004389}; Single-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004389}. Membrane
CC {ECO:0000256|ARBA:ARBA00004167}; Single-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004167}.
CC -!- SIMILARITY: Belongs to the cytochrome P450 family.
CC {ECO:0000256|ARBA:ARBA00010617}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:ETE62726.1}.
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DR EMBL; AZIM01003097; ETE62726.1; -; Genomic_DNA.
DR AlphaFoldDB; V8NL77; -.
DR Proteomes; UP000018936; Unassembled WGS sequence.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0020037; F:heme binding; IEA:InterPro.
DR GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR GO; GO:0004497; F:monooxygenase activity; IEA:InterPro.
DR GO; GO:0016705; F:oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen; IEA:InterPro.
DR Gene3D; 1.10.630.10; Cytochrome P450; 1.
DR InterPro; IPR001128; Cyt_P450.
DR InterPro; IPR024204; Cyt_P450_CYP7A1-type.
DR InterPro; IPR002403; Cyt_P450_E_grp-IV.
DR InterPro; IPR036396; Cyt_P450_sf.
DR PANTHER; PTHR24306; -; 1.
DR PANTHER; PTHR24306:SF0; 7-ALPHA-HYDROXYCHOLEST-4-EN-3-ONE 12-ALPHA-HYDROXYLASE; 1.
DR Pfam; PF00067; p450; 1.
DR PIRSF; PIRSF000047; Cytochrome_CYPVIIA1; 1.
DR PRINTS; PR00465; EP450IV.
DR PRINTS; PR00385; P450.
DR SUPFAM; SSF48264; Cytochrome P450; 1.
PE 3: Inferred from homology;
KW Heme {ECO:0000256|ARBA:ARBA00022617, ECO:0000256|PIRSR:PIRSR000047-1};
KW Iron {ECO:0000256|ARBA:ARBA00023004, ECO:0000256|PIRSR:PIRSR000047-1};
KW Lipid biosynthesis {ECO:0000256|ARBA:ARBA00022516};
KW Lipid metabolism {ECO:0000256|ARBA:ARBA00022516};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|PIRSR:PIRSR000047-1};
KW Reference proteome {ECO:0000313|Proteomes:UP000018936};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 6..25
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT BINDING 109
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000047-2"
FT BINDING 294
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000047-2"
FT BINDING 392
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000047-2"
FT BINDING 450
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000256|PIRSR:PIRSR000047-1"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:ETE62726.1"
SQ SEQUENCE 509 AA; 59226 MW; DC87CEBE2310628A CRC64;
MSFWVTVAAA LGAGLLGVLY LMGFFRRRRP NEPPLDKGFI PWLGHALHFR NDNLNFLKTM
QKKHGDIFTT LIAGQYITFL MDPLSFGGIV KEARNKLDFI SFAAELVLRV FRFKATHETH
KIIETSSTRH LKGESLGVMT QAMMDALQTV LLRWQETSKE DPKSWKEDGL FHFCYNMVFR
AGFLALYGTK PSGKQKEKSE QKDKQHTEEV FIEFRKYDKL FPRLSYALLT PLEWGQVKKL
WNYFWQVLSV KNVYQKDNIS RWISDQSQQL AEIGMSEEMR DRFMFVLLWA AQGNTGPASF
WLLEFLMKHP KAMEEVRKEI EEVVKKSGQE VISRQKPLNI TKEMLSQMPV LDSAVEETLR
LVTAPLLVRL VLQDMEFKLH NGKSYLLRKG DKIGLFPFLS AHMDPEIHSE PQAFKYDRFL
SQNGSKKEFF KNGKKVKYFT MPWGAGTSMC PGRHFATNEI KLFTFLMLAC FDVELINQQE
EIPTINKSRY GFGVMQPMND VPFRYRCRC
//
