ID   B6VE01_HUMAN            Unreviewed;       104 AA.
AC   B6VE01;
DT   16-DEC-2008, integrated into UniProtKB/TrEMBL.
DT   16-DEC-2008, sequence version 1.
DT   27-MAR-2024, entry version 63.
DE   RecName: Full=Steroid 21-hydroxylase {ECO:0000256|ARBA:ARBA00044116};
DE            EC=1.14.14.16 {ECO:0000256|ARBA:ARBA00044040};
DE   AltName: Full=21-OHase {ECO:0000256|ARBA:ARBA00044304};
DE   AltName: Full=Cytochrome P-450c21 {ECO:0000256|ARBA:ARBA00044217};
DE   AltName: Full=Cytochrome P450 21 {ECO:0000256|ARBA:ARBA00044342};
DE   AltName: Full=Cytochrome P450 XXI {ECO:0000256|ARBA:ARBA00044282};
DE   AltName: Full=Cytochrome P450-C21 {ECO:0000256|ARBA:ARBA00044265};
DE   Flags: Fragment;
GN   Name=CYP21A2 {ECO:0000313|EMBL:ACJ09368.1};
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Homo.
OX   NCBI_TaxID=9606 {ECO:0000313|EMBL:ACJ09368.1};
RN   [1] {ECO:0000313|EMBL:ACJ09368.1}
RP   NUCLEOTIDE SEQUENCE.
RA   Maitra A., Ughale N., Menon P.;
RT   "Three novel missense mutations in CYP21A2 exon 10 observed in an Indian
RT   family.";
RL   Submitted (SEP-2008) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=heme b; Xref=ChEBI:CHEBI:60344;
CC         Evidence={ECO:0000256|ARBA:ARBA00001970};
CC   -!- SIMILARITY: Belongs to the cytochrome P450 family.
CC       {ECO:0000256|ARBA:ARBA00010617, ECO:0000256|RuleBase:RU000461}.
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; FJ376815; ACJ09368.1; -; Genomic_DNA.
DR   AlphaFoldDB; B6VE01; -.
DR   PeptideAtlas; B6VE01; -.
DR   ChiTaRS; CYP21A2; human.
DR   GO; GO:0020037; F:heme binding; IEA:InterPro.
DR   GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR   GO; GO:0004497; F:monooxygenase activity; IEA:UniProtKB-KW.
DR   GO; GO:0016705; F:oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen; IEA:InterPro.
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   SUPFAM; SSF48264; Cytochrome P450; 1.
DR   PROSITE; PS00086; CYTOCHROME_P450; 1.
PE   3: Inferred from homology;
KW   Heme {ECO:0000256|ARBA:ARBA00022617, ECO:0000256|RuleBase:RU000461};
KW   Iron {ECO:0000256|ARBA:ARBA00023004, ECO:0000256|RuleBase:RU000461};
KW   Lipid metabolism {ECO:0000256|ARBA:ARBA00023098};
KW   Lipid-binding {ECO:0000256|ARBA:ARBA00023121};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW   ECO:0000256|RuleBase:RU000461};
KW   Monooxygenase {ECO:0000256|RuleBase:RU000461};
KW   Oxidoreductase {ECO:0000256|RuleBase:RU000461};
KW   Steroid-binding {ECO:0000256|ARBA:ARBA00022665}.
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:ACJ09368.1"
SQ   SEQUENCE   104 AA;  11581 MW;  C6C04E22D1CCDC55 CRC64;
     AHLDETVWER PHEFWPDRFL EPGKNSRALA FGCGARVCLG EPLARLELFV VLTRLLQAFT
     LLPSGDALPS LQPLPHCSVI LKMQPFQVRL QPRGMGAHSP GQSQ
//