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Cytochrome P450 1A2 (EC 1.14.14.1) (CYPIA2) (Cholesterol 25-hydroxylase) (Cytochrome P450-D2) (DAH2)

 CP1A2_CANLF             Reviewed;         512 AA.
P56592;
15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
23-JAN-2007, sequence version 2.
25-OCT-2017, entry version 105.
RecName: Full=Cytochrome P450 1A2;
EC=1.14.14.1 {ECO:0000250|UniProtKB:P05177};
AltName: Full=CYPIA2;
AltName: Full=Cholesterol 25-hydroxylase {ECO:0000250|UniProtKB:P05177};
AltName: Full=Cytochrome P450-D2;
AltName: Full=DAH2;
Name=CYP1A2;
Canis lupus familiaris (Dog) (Canis familiaris).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Laurasiatheria; Carnivora; Caniformia; Canidae;
Canis.
NCBI_TaxID=9615;
[1]
PROTEIN SEQUENCE OF 2-17.
STRAIN=Beagle; TISSUE=Liver;
PubMed=2910310; DOI=10.1016/0006-2952(89)90154-8;
Ohta K., Motoya M., Komori M., Miura T., Kitada M., Kamataki T.;
"A novel form of cytochrome P-450 in beagle dogs. P-450-D3 is a low
spin form of cytochrome P-450 but with catalytic and structural
properties similar to P-450d.";
Biochem. Pharmacol. 38:91-96(1989).
[2]
NUCLEOTIDE SEQUENCE [MRNA] OF 10-512.
STRAIN=Beagle; TISSUE=Liver;
PubMed=2122230;
Uchida T., Komori M., Kitada M., Kamataki T.;
"Isolation of cDNAs coding for three different forms of liver
microsomal cytochrome P-450 from polychlorinated biphenyl-treated
beagle dogs.";
Mol. Pharmacol. 38:644-651(1990).
-!- FUNCTION: Cytochromes P450 are a group of heme-thiolate
monooxygenases. In liver microsomes, this enzyme is involved in an
NADPH-dependent electron transport pathway. It oxidizes a variety
of structurally unrelated compounds, including steroids, fatty
acids, and xenobiotics. Most active in catalyzing 2-hydroxylation.
{ECO:0000250|UniProtKB:P05177}.
-!- CATALYTIC ACTIVITY: RH + [reduced NADPH--hemoprotein reductase] +
O(2) = ROH + [oxidized NADPH--hemoprotein reductase] + H(2)O.
{ECO:0000250|UniProtKB:P05177}.
-!- COFACTOR:
Name=heme; Xref=ChEBI:CHEBI:30413; Evidence={ECO:0000250};
-!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Peripheral
membrane protein. Microsome membrane
{ECO:0000250|UniProtKB:P05177}; Peripheral membrane protein.
-!- TISSUE SPECIFICITY: Constitutively expressed in liver.
-!- INDUCTION: By polychlorinated biphenyl (PCB) in liver and kidney.
-!- SIMILARITY: Belongs to the cytochrome P450 family. {ECO:0000305}.
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PIR; B37222; B37222.
UniGene; Cfa.14521; -.
ProteinModelPortal; P56592; -.
SMR; P56592; -.
STRING; 9615.ENSCAFP00000035314; -.
PaxDb; P56592; -.
PRIDE; P56592; -.
eggNOG; KOG0156; Eukaryota.
eggNOG; COG2124; LUCA.
HOVERGEN; HBG106944; -.
InParanoid; P56592; -.
Proteomes; UP000002254; Unplaced.
GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
GO; GO:0043231; C:intracellular membrane-bounded organelle; IBA:GO_Central.
GO; GO:0031090; C:organelle membrane; IEA:UniProtKB-SubCell.
GO; GO:0070330; F:aromatase activity; IEA:UniProtKB-EC.
GO; GO:0020037; F:heme binding; ISS:UniProtKB.
GO; GO:0005506; F:iron ion binding; IEA:InterPro.
GO; GO:0004497; F:monooxygenase activity; IBA:GO_Central.
GO; GO:0008202; P:steroid metabolic process; IEA:UniProtKB-KW.
Gene3D; 1.10.630.10; -; 1.
InterPro; IPR001128; Cyt_P450.
InterPro; IPR017972; Cyt_P450_CS.
InterPro; IPR002401; Cyt_P450_E_grp-I.
InterPro; IPR008066; Cyt_P450_E_grp-I_CYP1.
InterPro; IPR036396; Cyt_P450_sf.
Pfam; PF00067; p450; 1.
PRINTS; PR00463; EP450I.
PRINTS; PR01683; EP450ICYP1A.
PRINTS; PR00385; P450.
SUPFAM; SSF48264; SSF48264; 1.
PROSITE; PS00086; CYTOCHROME_P450; 1.
1: Evidence at protein level;
Complete proteome; Direct protein sequencing; Endoplasmic reticulum;
Glycoprotein; Heme; Iron; Lipid metabolism; Membrane; Metal-binding;
Microsome; Monooxygenase; Oxidoreductase; Reference proteome;
Steroid metabolism; Sterol metabolism.
INIT_MET 1 1 Removed. {ECO:0000269|PubMed:2910310}.
CHAIN 2 512 Cytochrome P450 1A2.
/FTId=PRO_0000051649.
METAL 454 454 Iron (heme axial ligand). {ECO:0000250}.
BINDING 222 222 Substrate. {ECO:0000250}.
CARBOHYD 65 65 O-linked (GlcNAc) serine. {ECO:0000250}.
SEQUENCE 512 AA; 57637 MW; E49DF4C54F4B3CFB CRC64;
MALSQMATGL LLASTIFCLI LWVVKAWQPR LPKGLKSPPG PWGWPLLGNV LTLGKSPHLA
LSRLSQRYGD VLQIRIGSTP VLVLSGLDTI RQALVRQGDD FKGRPDLYSL SLITDSQSMS
FSPDSGPVWA AGRRLAQNAL NTFSIASDPA SSCSCYLEEH VSKEAEALLS RLQEQMAEVG
RFDPYNQVLL SVANVIGAMC FGHHFSQRSE EMLPLLMSSS DFVETVSSGN PLDFFPILQY
MPNSALQRFK NFNQTFVQSL QKIVQEHYQD FDERSVQDIT GALLKHNEKS SRASDGHIPQ
EKIVNLINDI FGAGFDTVTT AISWSLMYLV ANPEIQRQIQ KELDTVIGRA RQPRLSDRPQ
LPLMEAFILE IFRHTSFVPF TIPHSTTKDT TLKGFYIPKE CCVFINQWQV NHDQQVWGDP
FAFRPERFLT ADGTTINKTL SEKVMLFGMG KRRCIGEVLA KWEIFLFLAI LLQRLEFSVP
AGVKVDLTPI YGLTMKHTRC EHVQARPRFS IK


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