ID CP21A_LYNLY Reviewed; 492 AA. AC Q2LA59; DT 09-JAN-2007, integrated into UniProtKB/Swiss-Prot. DT 21-FEB-2006, sequence version 1. DT 27-MAR-2024, entry version 80. DE RecName: Full=Steroid 21-hydroxylase; DE EC=1.14.14.16 {ECO:0000250|UniProtKB:P00191}; DE AltName: Full=21-OHase; DE AltName: Full=Cytochrome P-450c21; DE AltName: Full=Cytochrome P450 21; DE AltName: Full=Cytochrome P450 XXI; DE AltName: Full=Cytochrome P450-C21; GN Name=CYP21; OS Lynx lynx (Eurasian lynx) (Felis lynx). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Laurasiatheria; Carnivora; Feliformia; Felidae; Felinae; Lynx. OX NCBI_TaxID=13125; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC TISSUE=Muscle; RA Kosowska B., Brzezinska K., Dobosz T., Moska M., Strzala T., Marszalek B., RA Schmidt K.; RT "Phylogenetic analysis of a steroid 21-hydroxylase gene in some species of RT animals and a man."; RL Submitted (DEC-2005) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Specifically catalyzes the 21-hydroxylation of steroids. CC Required for the adrenal synthesis of mineralocorticoids and CC glucocorticoids. {ECO:0000250|UniProtKB:P00191}. CC -!- CATALYTIC ACTIVITY: CC Reaction=17alpha-hydroxyprogesterone + O2 + reduced [NADPH--hemoprotein CC reductase] = 11-deoxycortisol + H(+) + H2O + oxidized CC [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:50308, Rhea:RHEA- CC COMP:11964, Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377, CC ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:17252, CC ChEBI:CHEBI:28324, ChEBI:CHEBI:57618, ChEBI:CHEBI:58210; CC EC=1.14.14.16; Evidence={ECO:0000250|UniProtKB:P00191}; CC -!- CATALYTIC ACTIVITY: CC Reaction=O2 + progesterone + reduced [NADPH--hemoprotein reductase] = CC 21-hydroxyprogesterone + H(+) + H2O + oxidized [NADPH--hemoprotein CC reductase]; Xref=Rhea:RHEA:50304, Rhea:RHEA-COMP:11964, Rhea:RHEA- CC COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, CC ChEBI:CHEBI:16973, ChEBI:CHEBI:17026, ChEBI:CHEBI:57618, CC ChEBI:CHEBI:58210; EC=1.14.14.16; CC Evidence={ECO:0000250|UniProtKB:P00191}; CC -!- COFACTOR: CC Name=heme b; Xref=ChEBI:CHEBI:60344; CC Evidence={ECO:0000250|UniProtKB:P00191}; CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Peripheral CC membrane protein. Microsome membrane; Peripheral membrane protein. CC -!- DOMAIN: The leucine-rich hydrophobic amino acid N-terminal region CC probably helps to anchor the protein to the microsomal membrane. CC -!- SIMILARITY: Belongs to the cytochrome P450 family. {ECO:0000305}. 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; DQ341430; ABC69212.1; -; Genomic_DNA. DR AlphaFoldDB; Q2LA59; -. DR SMR; Q2LA59; -. DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell. DR GO; GO:0103069; F:17-hydroxyprogesterone 21-hydroxylase activity; IEA:RHEA. DR GO; GO:0020037; F:heme binding; IEA:InterPro. DR GO; GO:0005506; F:iron ion binding; IEA:InterPro. DR GO; GO:0106309; F:progesterone 21-hydroxylase activity; IEA:RHEA. DR GO; GO:0005496; F:steroid binding; IEA:UniProtKB-KW. DR GO; GO:0008395; F:steroid hydroxylase activity; ISS:UniProtKB. DR GO; GO:0006694; P:steroid biosynthetic process; IEA:UniProtKB-KW. DR GO; GO:0008202; P:steroid metabolic process; ISS:UniProtKB. DR CDD; cd20674; CYP21; 1. DR Gene3D; 1.10.630.10; Cytochrome P450; 1. DR InterPro; IPR001128; Cyt_P450. DR InterPro; IPR017972; Cyt_P450_CS. DR InterPro; IPR002401; Cyt_P450_E_grp-I. DR InterPro; IPR036396; Cyt_P450_sf. DR PANTHER; PTHR24289; STEROID 17-ALPHA-HYDROXYLASE/17,20 LYASE; 1. DR PANTHER; PTHR24289:SF14; STEROID 21-HYDROXYLASE-LIKE; 1. DR Pfam; PF00067; p450; 1. DR PRINTS; PR00463; EP450I. DR PRINTS; PR00385; P450. DR SUPFAM; SSF48264; Cytochrome P450; 1. DR PROSITE; PS00086; CYTOCHROME_P450; 1. PE 3: Inferred from homology; KW Endoplasmic reticulum; Heme; Iron; Lipid-binding; Membrane; Metal-binding; KW Microsome; Monooxygenase; Oxidoreductase; Steroid-binding; Steroidogenesis. FT CHAIN 1..492 FT /note="Steroid 21-hydroxylase" FT /id="PRO_0000269711" FT BINDING 91 FT /ligand="heme b" FT /ligand_id="ChEBI:CHEBI:60344" FT /evidence="ECO:0000250|UniProtKB:P08686" FT BINDING 120 FT /ligand="heme b" FT /ligand_id="ChEBI:CHEBI:60344" FT /evidence="ECO:0000250|UniProtKB:P08686" FT BINDING 231 FT /ligand="17alpha-hydroxyprogesterone" FT /ligand_id="ChEBI:CHEBI:17252" FT /evidence="ECO:0000250|UniProtKB:P00191" FT BINDING 231 FT /ligand="progesterone" FT /ligand_id="ChEBI:CHEBI:17026" FT /evidence="ECO:0000250|UniProtKB:P08686" FT BINDING 363 FT /ligand="heme b" FT /ligand_id="ChEBI:CHEBI:60344" FT /evidence="ECO:0000250|UniProtKB:P08686" FT BINDING 424 FT /ligand="heme b" FT /ligand_id="ChEBI:CHEBI:60344" FT /evidence="ECO:0000250|UniProtKB:P08686" FT BINDING 426 FT /ligand="heme b" FT /ligand_id="ChEBI:CHEBI:60344" FT /ligand_part="Fe" FT /ligand_part_id="ChEBI:CHEBI:18248" FT /note="axial binding residue" FT /evidence="ECO:0000250|UniProtKB:P08686" SQ SEQUENCE 492 AA; 55397 MW; AA148E9CB122C05D CRC64; MLLLGLLLLT ALAGARLLWN KWKYRSLHLP PLAPGFLHLL QPDLPIYLLG LTQKLGPVYR LRLGLQDVVV LNSKRTIEEA MIRRWVDFAG RPQMPSYKLV SQPYQDLSLG DYSLLWKAHK KLTRSALLLG IRNSMEPLVE QLTQEFCERM RAQAGTPVAI QKEFSFLTCS VICCLTFGDK EDTLVHAFHD CVQDLMKSWE HWSIQVLDIV PFLRFFPNPG LQRLKQALEN RDRIVEKQLR QHKDSMVAGQ WRDMTDYMLQ GMGKPRAEKG HGRLLEGHVH MSVVDLFIGG TETTATTLSW AVAFLLHHPE IQQRLQEELD CELGPGASGS RVPLKDPSRL PLLTATIAEV LRLRPVVPLA LPHRTTRHSS ILGYDIPEGT VVIPNLQGAH LDDTVWEQPH EFRPDRFLVP GASPRVLAFG CGARVCLGEP LARLELFVVL ARLLHAFTLL PPTGPLPSLR PRSHCGINLT MQPFQVQLQP RGAVAPGPSQ HQ //