ID A0A337SXY0_FELCA Unreviewed; 437 AA.
AC A0A337SXY0;
DT 10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT 10-OCT-2018, sequence version 1.
DT 27-MAR-2024, entry version 17.
DE SubName: Full=Cytochrome P450 family 11 subfamily B member 1 {ECO:0000313|Ensembl:ENSFCAP00000051461.1};
GN Name=CYP11B1 {ECO:0000313|Ensembl:ENSFCAP00000051461.1,
GN ECO:0000313|VGNC:VGNC:103333};
OS Felis catus (Cat) (Felis silvestris catus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Feliformia; Felidae; Felinae; Felis.
OX NCBI_TaxID=9685 {ECO:0000313|Ensembl:ENSFCAP00000051461.1, ECO:0000313|Proteomes:UP000011712};
RN [1] {ECO:0000313|Ensembl:ENSFCAP00000051461.1, ECO:0000313|Proteomes:UP000011712}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Abyssinian {ECO:0000313|Ensembl:ENSFCAP00000051461.1,
RC ECO:0000313|Proteomes:UP000011712};
RX PubMed=17975172; DOI=10.1101/gr.6380007;
RA Pontius J.U., Mullikin J.C., Smith D.R., Lindblad-Toh K., Gnerre S.,
RA Clamp M., Chang J., Stephens R., Neelam B., Volfovsky N., Schaffer A.A.,
RA Agarwala R., Narfstrom K., Murphy W.J., Giger U., Roca A.L., Antunes A.,
RA Menotti-Raymond M., Yuhki N., Pecon-Slattery J., Johnson W.E., Bourque G.,
RA Tesler G., O'Brien S.J.;
RT "Initial sequence and comparative analysis of the cat genome.";
RL Genome Res. 17:1675-1689(2007).
RN [2] {ECO:0000313|Ensembl:ENSFCAP00000051461.1, ECO:0000313|Proteomes:UP000011712}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Abyssinian {ECO:0000313|Ensembl:ENSFCAP00000051461.1,
RC ECO:0000313|Proteomes:UP000011712};
RA Hillier L.W., Warren W., Obrien S., Wilson R.K.;
RT "Sequence assembly of the Felis catus genome version 6.2.";
RL Submitted (SEP-2011) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|Ensembl:ENSFCAP00000051461.1}
RP IDENTIFICATION.
RC STRAIN=breed Abyssinian {ECO:0000313|Ensembl:ENSFCAP00000051461.1};
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=21-hydroxyprogesterone + 2 H(+) + O2 + 2 reduced [adrenodoxin]
CC = corticosterone + H2O + 2 oxidized [adrenodoxin];
CC Xref=Rhea:RHEA:46104, Rhea:RHEA-COMP:9998, Rhea:RHEA-COMP:9999,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:16827, ChEBI:CHEBI:16973, ChEBI:CHEBI:33737,
CC ChEBI:CHEBI:33738; Evidence={ECO:0000256|ARBA:ARBA00035574};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:46105;
CC Evidence={ECO:0000256|ARBA:ARBA00035574};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a steroid + 2 H(+) + O2 + 2 reduced [adrenodoxin] = an 11beta-
CC hydroxysteroid + H2O + 2 oxidized [adrenodoxin];
CC Xref=Rhea:RHEA:15629, Rhea:RHEA-COMP:9998, Rhea:RHEA-COMP:9999,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:33737, ChEBI:CHEBI:33738, ChEBI:CHEBI:35341,
CC ChEBI:CHEBI:35346; EC=1.14.15.4;
CC Evidence={ECO:0000256|ARBA:ARBA00035575};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:15630;
CC Evidence={ECO:0000256|ARBA:ARBA00035575};
CC -!- COFACTOR:
CC Name=heme; Xref=ChEBI:CHEBI:30413;
CC Evidence={ECO:0000256|ARBA:ARBA00001971};
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004170};
CC Peripheral membrane protein {ECO:0000256|ARBA:ARBA00004170}.
CC Mitochondrion inner membrane {ECO:0000256|ARBA:ARBA00004637};
CC Peripheral membrane protein {ECO:0000256|ARBA:ARBA00004637}.
CC -!- SIMILARITY: Belongs to the cytochrome P450 family.
CC {ECO:0000256|ARBA:ARBA00010617}.
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 EMBL; AANG04003518; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; XP_004000204.1; XM_004000155.2.
DR AlphaFoldDB; A0A337SXY0; -.
DR SMR; A0A337SXY0; -.
DR Ensembl; ENSFCAT00000055331.1; ENSFCAP00000051461.1; ENSFCAG00000018677.5.
DR VGNC; VGNC:103333; CYP11B1.
DR GeneTree; ENSGT00940000163354; -.
DR Proteomes; UP000011712; Chromosome F2.
DR GO; GO:0005743; C:mitochondrial inner 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:UniProtKB-KW.
DR GO; GO:0016705; F:oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen; IEA:InterPro.
DR GO; GO:0006629; P:lipid metabolic process; IEA:UniProt.
DR Gene3D; 1.10.630.10; Cytochrome P450; 1.
DR InterPro; IPR001128; Cyt_P450.
DR InterPro; IPR002399; Cyt_P450_mitochondrial.
DR InterPro; IPR036396; Cyt_P450_sf.
DR PANTHER; PTHR24279; -; 1.
DR PANTHER; PTHR24279:SF1; CYTOCHROME P450 11B2, MITOCHONDRIAL; 1.
DR Pfam; PF00067; p450; 1.
DR PRINTS; PR00408; MITP450.
DR SUPFAM; SSF48264; Cytochrome P450; 1.
PE 3: Inferred from homology;
KW Membrane {ECO:0000256|ARBA:ARBA00023136};
KW Reference proteome {ECO:0000313|Proteomes:UP000011712};
KW Steroidogenesis {ECO:0000256|ARBA:ARBA00023250};
KW Transit peptide {ECO:0000256|ARBA:ARBA00022946}.
SQ SEQUENCE 437 AA; 49500 MW; 752986F9EC2E7BE5 CRC64;
MAFGAKARVW LAGPWPSPGR ARAPGAGAAP APKAVLPFEA IPRCPGNKWM RLLQIWKEQR
LENLHLEVHQ LFQELGPILR YDVGGTRMVL LMLPEDVQRI QQVDGHQPWR PLLDPWLAYR
QHRGHKCGVF LLNGPEWRMN RLKLNPDLLS PQAVQKYLPM VDCVARDFSK ALKSRVLQNA
RGSLTVDIQP SILYYTIEAS NLALFGERLG LLGHSPSPAS LNFLRALKVM LKSTAQLMFM
PRVLSRWTST QLWKEHFESW DYIFQYANNA IQKIYQEVAL SRPEHYSGIV GELLTHADLS
LEAIRANSIE LTTGSVDTTA YPLLMTLFEL ARNPDVQQAL RQESLGAEAR ISQDPQSATS
ELPLLRAALK ETLRLYPVGM SVDRKVASDV VLQNYHIPAG VLKSFLVETL RQEDVKMTYQ
FVFMPSTYPL LTFRAIN
//
