ID   CP2CL_CANLF             Reviewed;         487 AA.
AC   P56594; O62734;
DT   15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT   15-JUL-1999, sequence version 2.
DT   03-AUG-2022, entry version 126.
DE   RecName: Full=Cytochrome P450 2C21;
DE            EC=1.14.14.1;
DE   AltName: Full=CYPIIC21;
DE   AltName: Full=Cytochrome P450 DM1-1;
DE   Flags: Fragment;
GN   Name=CYP2C21;
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 [MRNA].
RC   STRAIN=Beagle; TISSUE=Liver;
RX   PubMed=9492393;
RA   Blaisdell J., Goldstein J.A., Bai S.A.;
RT   "Isolation of a new canine cytochrome P450 cDNA from the cytochrome P450 2C
RT   subfamily (CYP2C41) and evidence for polymorphic differences in its
RT   expression.";
RL   Drug Metab. Dispos. 26:278-283(1998).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 25-487.
RC   STRAIN=Beagle; TISSUE=Liver;
RX   PubMed=2122230;
RA   Uchida T., Komori M., Kitada M., Kamataki T.;
RT   "Isolation of cDNAs coding for three different forms of liver microsomal
RT   cytochrome P-450 from polychlorinated biphenyl-treated beagle dogs.";
RL   Mol. Pharmacol. 38:644-651(1990).
CC   -!- FUNCTION: Cytochromes P450 are a group of heme-thiolate monooxygenases.
CC       In liver microsomes, this enzyme is involved in an NADPH-dependent
CC       electron transport pathway. It oxidizes a variety of structurally
CC       unrelated compounds, including steroids, fatty acids, and xenobiotics.
CC       Showed testosterone hydrolase activity.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=an organic molecule + O2 + reduced [NADPH--hemoprotein
CC         reductase] = an alcohol + H(+) + H2O + oxidized [NADPH--hemoprotein
CC         reductase]; Xref=Rhea:RHEA:17149, Rhea:RHEA-COMP:11964, Rhea:RHEA-
CC         COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379,
CC         ChEBI:CHEBI:30879, ChEBI:CHEBI:57618, ChEBI:CHEBI:58210,
CC         ChEBI:CHEBI:142491; EC=1.14.14.1;
CC   -!- COFACTOR:
CC       Name=heme; Xref=ChEBI:CHEBI:30413; Evidence={ECO:0000250};
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Peripheral
CC       membrane protein. Microsome membrane; Peripheral membrane protein.
CC   -!- TISSUE SPECIFICITY: Liver.
CC   -!- SIMILARITY: Belongs to the cytochrome P450 family. {ECO:0000305}.
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DR   EMBL; AF049909; AAC05209.1; -; mRNA.
DR   AlphaFoldDB; P56594; -.
DR   SMR; P56594; -.
DR   STRING; 9615.ENSCAFP00000011937; -.
DR   PaxDb; P56594; -.
DR   PRIDE; P56594; -.
DR   eggNOG; KOG0156; Eukaryota.
DR   InParanoid; P56594; -.
DR   Proteomes; UP000002254; 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:0008392; F:arachidonic acid epoxygenase activity; IBA:GO_Central.
DR   GO; GO:0070330; F:aromatase activity; IEA:UniProtKB-EC.
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:0008395; F:steroid hydroxylase activity; IBA:GO_Central.
DR   GO; GO:0019373; P:epoxygenase P450 pathway; IBA:GO_Central.
DR   GO; GO:0006082; P:organic acid metabolic process; IBA:GO_Central.
DR   GO; GO:0006805; P:xenobiotic metabolic process; IBA:GO_Central.
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   2: Evidence at transcript level;
KW   Endoplasmic reticulum; Heme; Iron; Membrane; Metal-binding; Microsome;
KW   Monooxygenase; Oxidoreductase; Reference proteome.
FT   CHAIN           <1..487
FT                   /note="Cytochrome P450 2C21"
FT                   /id="PRO_0000051710"
FT   BINDING         432
FT                   /ligand="heme"
FT                   /ligand_id="ChEBI:CHEBI:30413"
FT                   /ligand_part="Fe"
FT                   /ligand_part_id="ChEBI:CHEBI:18248"
FT                   /note="axial binding residue"
FT                   /evidence="ECO:0000250"
FT   CONFLICT        337..342
FT                   /note="Missing (in Ref. 2; no nucleotide entry)"
FT                   /evidence="ECO:0000305"
FT   NON_TER         1
SQ   SEQUENCE   487 AA;  55531 MW;  E1390CACC7DD577D CRC64;
     FIVLVICLSC LISFFLWNQN RAKGKLPPGP TPLPIIGNIL QINTKNVSKS LSKLAENYGP
     VFTVYFGMKP TVVLYGYEAV KEALIDRSEE FSGRGHFPLL DWTIQGLGIV FSNGEKWKQT
     RRFSLTVLRN MGMGKKTVED RIQEEALYLV EALKKTNASP CDPTFLLGCA PCNVICSIIF
     QNRFEYDDKD FLTLLEYFHE NLLISSTSWI QLYNAFPLLI HYLPGSHHVL FKNIANQFKF
     ISEKIKEHEE SLNFSNPRDF IDYFLIKIEK EKHNKQSEFT MDNLIITIWD VFSAGTETTS
     TTLRYGLLVL LKHPDVTAKV QEEIHRVVGR HRSPCMQDRS CMPYTDAVVH EIQRYIDLVP
     NNLPHSVTQD IKFREYLIPK GTTILTSLTS VLHDEKGFPN PDQFDPGHFL DENGSFKKSD
     YFMAFSAGKR VCVGEGLARM ELFLLLTNIL QHFTLKPLVD PKDIDTTPIA NGLGATPPSY
     KLCFVPV