CP21A_LYNLY
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 03-AUG-2022, entry version 76.
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 [NADPH--
CC hemoprotein reductase]; Xref=Rhea:RHEA:50308, Rhea:RHEA-COMP:11964,
CC Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:15379, ChEBI:CHEBI:17252, ChEBI:CHEBI:28324,
CC ChEBI:CHEBI:57618, ChEBI:CHEBI:58210; EC=1.14.14.16;
CC 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}.
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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 Gene3D; 1.10.630.10; -; 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 Pfam; PF00067; p450; 1.
DR PRINTS; PR00463; EP450I.
DR PRINTS; PR00385; P450.
DR SUPFAM; SSF48264; SSF48264; 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
