ID CP21A_CANLF Reviewed; 492 AA.
AC Q8WNW0;
DT 26-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 27-MAR-2024, entry version 138.
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 Canis lupus familiaris (Dog) (Canis familiaris).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Canidae; Canis.
OX NCBI_TaxID=9615;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=Beagle; TISSUE=Adrenal gland;
RX PubMed=12204635; DOI=10.1016/s0034-5288(02)00070-x;
RA Takada K., Kitamura H., Takiguchi M., Saito M., Hashimoto A.;
RT "Cloning of canine 21-hydroxylase gene and its polymorphic analysis as a
RT candidate gene for congenital adrenal hyperplasia-like syndrome in
RT Pomeranians.";
RL Res. Vet. Sci. 73:159-163(2002).
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; AB052905; BAB79541.1; -; Genomic_DNA.
DR AlphaFoldDB; Q8WNW0; -.
DR SMR; Q8WNW0; -.
DR STRING; 9615.ENSCAFP00000001018; -.
DR PaxDb; 9612-ENSCAFP00000001018; -.
DR eggNOG; KOG0156; Eukaryota.
DR HOGENOM; CLU_001570_22_0_1; -.
DR InParanoid; Q8WNW0; -.
DR OMA; VQEFEWG; -.
DR TreeFam; TF105095; -.
DR Proteomes; UP000002254; Unplaced.
DR Proteomes; UP000694429; Unplaced.
DR Proteomes; UP000694542; Unplaced.
DR Proteomes; UP000805418; Unplaced.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IBA:GO_Central.
DR GO; GO:0103069; F:17-hydroxyprogesterone 21-hydroxylase activity; IEA:RHEA.
DR GO; GO:0020037; F:heme binding; IBA:GO_Central.
DR GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR GO; GO:0016712; F:oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen, reduced flavin or flavoprotein as one donor, and incorporation of one atom of oxygen; IBA:GO_Central.
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:0006082; P:organic acid metabolic process; IBA:GO_Central.
DR GO; GO:0006694; P:steroid biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:0008202; P:steroid metabolic process; ISS:UniProtKB.
DR GO; GO:0006805; P:xenobiotic metabolic process; IBA:GO_Central.
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; Reference proteome;
KW Steroid-binding; Steroidogenesis.
FT CHAIN 1..492
FT /note="Steroid 21-hydroxylase"
FT /id="PRO_0000051975"
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; 55366 MW; 8151F79FF0484A54 CRC64;
MLLLGVLLLT VLAGARLLWG KWKLRGLHLP PLVPGCLHLL QPDLPLHLLG LTQKLGPIYR
LRLGLQDVVV LNSKRTIEEA MVRKWVDFAG RPQTPSYKLV SLHHQDLSLG DYSLLWKAHK
KLTRSALLLG IRSSMEPLVE QLTQEFCERM RAQAGTPVAI QKEFSLLTCA IICHLTFGDK
EDTLVHTFHD CVQDLMRTWE HWSIQMLDII PFLRFFPNPG LWRLKRALEN RDHIVEKQLR
QHKESMVAGQ WRDMTDYMLQ RVGRLRAEEG CGQLLEGHVH MSVVDLFIGG TETTATTLSW
AVAFLLHHPE IQQRLQEELD RELGPGASGS RIPYRDPTRL PLLSATVAEV LRLRPVVPLA
LPHCTTRPSS ISGYDIPEGM VVIPNLQGAH LDETVWERPQ EFRPDRFLVP GASPRVLAFG
CGARVCLGEP LARLELLVVL AQLLRAFTLM PAAGTLPSLR PRARCGVNLS MQPFQVQLQP
RGAGVLGRGQ HP
//
