CP21A_FELCA
ID CP21A_FELCA Reviewed; 492 AA.
AC Q2LA60;
DT 09-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT 21-FEB-2006, sequence version 1.
DT 03-AUG-2022, entry version 96.
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 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;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=Birman;
RA Brzezinska K., Kosowska B., Dobosz T., Moska M., Strzala T., Marszalek B.;
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; DQ341429; ABC69211.1; -; Genomic_DNA.
DR RefSeq; XP_003986007.1; XM_003985958.4.
DR AlphaFoldDB; Q2LA60; -.
DR SMR; Q2LA60; -.
DR STRING; 9685.ENSFCAP00000004176; -.
DR GeneID; 101094596; -.
DR KEGG; fca:101094596; -.
DR CTD; 1589; -.
DR eggNOG; KOG0156; Eukaryota.
DR HOGENOM; CLU_001570_22_0_1; -.
DR InParanoid; Q2LA60; -.
DR OrthoDB; 702827at2759; -.
DR TreeFam; TF105095; -.
DR Proteomes; UP000011712; Unplaced.
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; IBA:GO_Central.
DR GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR GO; GO:0106309; F:progesterone 21-hydroxylase activity; IEA:RHEA.
DR GO; GO:0004509; F:steroid 21-monooxygenase activity; IBA:GO_Central.
DR GO; GO:0005496; F:steroid binding; IEA:UniProtKB-KW.
DR GO; GO:0008395; F:steroid hydroxylase activity; ISS:UniProtKB.
DR GO; GO:0006704; P:glucocorticoid biosynthetic process; IBA:GO_Central.
DR GO; GO:0006694; P:steroid biosynthetic process; IBA:GO_Central.
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; Reference proteome;
KW Steroid-binding; Steroidogenesis.
FT CHAIN 1..492
FT /note="Steroid 21-hydroxylase"
FT /id="PRO_0000269710"
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; 55476 MW; 3BFA53788469E510 CRC64;
MLLLGLLLLT ALAGARLLWN KWKYRSLHLP PLAPGFLHLL QPDLPIYLLG LTQKLGPVYR
LRLGLQDVVV LNSKRTIEEA LIRRWVDFAG RPQMPSYKLV SQHYQDLSLG DYSLLWKAHK
KLTRSALLLG IRNSMEPLVE QLTQEFCERM RAQAGTPVAI QKEFSFLTCS VICCLTFGDK
EDTLVHAFHD CVEDLMKSWE HWSIQVLDIV PFLRFFPNPG LRRLKQALEN RDRIVEKQLR
QHKDSMVAGQ WRDMTDYMLQ GMGKPKVEKG HGRLLEGHVH MSVVDLFIGG TETTATTLSW
AVAFLLHHPE IQQRLQEELD CELGPGASGS RVPLKDPSRL PLLTATIAEV LRLRPVVPLA
LPHRTTRHSS ILGYDIPEGT VVIPNLQGAH LDDTVWEQPH EFRPDRFLVP GASPRVLAFG
CGARVCLGEP LARLELFVVL ARLLHAFTLL PPTGPLPSLR PRSHCGINLT MQPFQVRLQP
RGAVAPGPSQ HQ
