ID G3UWE4_MOUSE Unreviewed; 502 AA. AC G3UWE4; DT 16-NOV-2011, integrated into UniProtKB/TrEMBL. DT 16-NOV-2011, sequence version 1. DT 27-MAR-2024, entry version 78. DE RecName: Full=steroid 11beta-monooxygenase {ECO:0000256|ARBA:ARBA00012767}; DE EC=1.14.15.4 {ECO:0000256|ARBA:ARBA00012767}; GN Name=Cyp11b2 {ECO:0000313|Ensembl:ENSMUSP00000131503.2, GN ECO:0000313|MGI:MGI:88584}; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae; OC Murinae; Mus; Mus. OX NCBI_TaxID=10090 {ECO:0000313|Ensembl:ENSMUSP00000131503.2, ECO:0000313|Proteomes:UP000000589}; RN [1] {ECO:0000313|Ensembl:ENSMUSP00000131503.2, ECO:0000313|Proteomes:UP000000589} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=C57BL/6J {ECO:0000313|Ensembl:ENSMUSP00000131503.2, RC ECO:0000313|Proteomes:UP000000589}; RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112; RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X., RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y., RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S., RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R., RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K., RA Eichler E.E., Ponting C.P.; RT "Lineage-specific biology revealed by a finished genome assembly of the RT mouse."; RL PLoS Biol. 7:E1000112-E1000112(2009). RN [2] {ECO:0000313|Ensembl:ENSMUSP00000131503.2} RP IDENTIFICATION. RC STRAIN=C57BL/6J {ECO:0000313|Ensembl:ENSMUSP00000131503.2}; RG Ensembl; RL Submitted (NOV-2023) to UniProtKB. CC -!- CATALYTIC ACTIVITY: CC Reaction=21-hydroxyprogesterone + 2 H(+) + O2 + 2 reduced [adrenodoxin] CC = 18-hydroxy-11-deoxycorticosterone + H2O + 2 oxidized [adrenodoxin]; CC Xref=Rhea:RHEA:76151, Rhea:RHEA-COMP:9998, Rhea:RHEA-COMP:9999, CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, CC ChEBI:CHEBI:16973, ChEBI:CHEBI:33737, ChEBI:CHEBI:33738, CC ChEBI:CHEBI:195166; Evidence={ECO:0000256|ARBA:ARBA00035593}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:76152; CC Evidence={ECO:0000256|ARBA:ARBA00035593}; 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 ECO:0000256|PIRSR:PIRSR602399-1}; CC -!- SIMILARITY: Belongs to the cytochrome P450 family. CC {ECO:0000256|ARBA:ARBA00010617, ECO:0000256|RuleBase:RU000461}. 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 RefSeq; NP_034121.3; NM_009991.3. DR AlphaFoldDB; G3UWE4; -. DR SMR; G3UWE4; -. DR MaxQB; G3UWE4; -. DR ProteomicsDB; 339292; -. DR DNASU; 13072; -. DR Ensembl; ENSMUST00000167634.2; ENSMUSP00000131503.2; ENSMUSG00000022589.9. DR GeneID; 13072; -. DR KEGG; mmu:13072; -. DR UCSC; uc007wgf.2; mouse. DR AGR; MGI:88584; -. DR CTD; 1585; -. DR MGI; MGI:88584; Cyp11b2. DR VEuPathDB; HostDB:ENSMUSG00000022589; -. DR GeneTree; ENSGT00940000161506; -. DR HOGENOM; CLU_001570_28_4_1; -. DR OMA; RNHKCGV; -. DR OrthoDB; 2658719at2759; -. DR PhylomeDB; G3UWE4; -. DR TreeFam; TF105094; -. DR BioGRID-ORCS; 13072; 9 hits in 79 CRISPR screens. DR Proteomes; UP000000589; Chromosome 15. DR Bgee; ENSMUSG00000022589; Expressed in adrenal gland and 20 other cell types or tissues. DR ExpressionAtlas; G3UWE4; baseline and differential. DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW. DR GO; GO:0005739; C:mitochondrion; IEA:InterPro. DR GO; GO:0020037; F:heme binding; IEA:InterPro. DR GO; GO:0005506; F:iron ion binding; IEA:InterPro. DR GO; GO:0004507; F:steroid 11-beta-monooxygenase activity; IEA:UniProtKB-EC. DR GO; GO:0006694; P:steroid biosynthetic process; IEA:UniProtKB-KW. DR Gene3D; 1.10.630.10; Cytochrome P450; 1. DR InterPro; IPR001128; Cyt_P450. DR InterPro; IPR017972; Cyt_P450_CS. 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 PRINTS; PR00385; P450. DR SUPFAM; SSF48264; Cytochrome P450; 1. DR PROSITE; PS00086; CYTOCHROME_P450; 1. PE 1: Evidence at protein level; KW Heme {ECO:0000256|ARBA:ARBA00022617, ECO:0000256|PIRSR:PIRSR602399-1}; KW Iron {ECO:0000256|ARBA:ARBA00023004, ECO:0000256|PIRSR:PIRSR602399-1}; KW Membrane {ECO:0000256|ARBA:ARBA00023136}; KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, KW ECO:0000256|PIRSR:PIRSR602399-1}; KW Monooxygenase {ECO:0000256|ARBA:ARBA00023033, KW ECO:0000256|RuleBase:RU000461}; KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002, KW ECO:0000256|RuleBase:RU000461}; KW Proteomics identification {ECO:0007829|MaxQB:G3UWE4, KW ECO:0007829|ProteomicsDB:G3UWE4}; KW Reference proteome {ECO:0000313|Proteomes:UP000000589}; KW Steroidogenesis {ECO:0000256|ARBA:ARBA00023250}; KW Transit peptide {ECO:0000256|ARBA:ARBA00022946}. FT BINDING 383 FT /ligand="21-hydroxyprogesterone" FT /ligand_id="ChEBI:CHEBI:16973" FT /evidence="ECO:0000256|PIRSR:PIRSR602399-1" FT BINDING 449 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:PIRSR602399-1" SQ SEQUENCE 502 AA; 57575 MW; BCAFFF3EE471ED37 CRC64; MAMALRVTAD VWLARPWQCL HRTRALGTTA TLAPKTLQPF EAIPQYSRNK WLKMIQILRE QGQENLHLEM HQVFRELGPI FRHSVGKTQI VSVMLPEDAE KLHQVESMLP RRMHLEPWVA HRELRGLRRG VFLLNGPEWR LNRLRLNRNV LSPKAVQKFV PMVDMVARDF LETLKEKVLQ NARGSLTMDV QQSLFNYTIE ASNFALFGER LGLLGHDLSP GSLKFIHALH SMFKSTSQLL FLPKSLTRWT STRVWKEHFD AWDVISEYAN RCIWKVHQEL RLGSSQTYSG IVAELISQGS LPLDAIKANS MELTAGSVDT TAIPLVMTLF ELARNPDVQK ALRQESLAAE ASIAANPQKA MSDLPLLRAA LKETLRLYPV GGFLERILSS DLVLQNYHVP AGTLVLLYLY SMGRNPAVFP RPERYMPQRW LERKRSFQHL AFGFGVRQCL GRRLAEVEMM LLLHHILKTF QVETLRQEDV QMAYRFVLMP SSSPVLTFRP VS //