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   27-MAR-2024, entry version 102.
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
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; DQ341429; ABC69211.1; -; Genomic_DNA.
DR   RefSeq; XP_003986007.1; XM_003985958.4.
DR   AlphaFoldDB; Q2LA60; -.
DR   SMR; Q2LA60; -.
DR   STRING; 9685.ENSFCAP00000004176; -.
DR   PaxDb; 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; 2900138at2759; -.
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: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; 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
//