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Cytochrome P450 2C11 (EC 1.14.14.1) (CYPIIC11) (Cytochrome P-450(M-1)) (Cytochrome P450-UT-2) (Cytochrome P450-UT-A) (Cytochrome P450H)

 CP2CB_RAT               Reviewed;         500 AA.
P08683; Q63141; Q64554;
01-JAN-1988, integrated into UniProtKB/Swiss-Prot.
01-JAN-1988, sequence version 1.
05-DEC-2018, entry version 165.
RecName: Full=Cytochrome P450 2C11;
EC=1.14.14.1;
AltName: Full=CYPIIC11;
AltName: Full=Cytochrome P-450(M-1);
AltName: Full=Cytochrome P450-UT-2;
AltName: Full=Cytochrome P450-UT-A;
AltName: Full=Cytochrome P450H;
Name=Cyp2c11; Synonyms=Cyp2c, Cyp2c-11;
Rattus norvegicus (Rat).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Rattus.
NCBI_TaxID=10116;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=3805049;
Yoshioka H., Morohashi K., Sogawa K., Miyata T., Kawajiri K.,
Hirose T., Inayama S., Fujii-Kuriyama Y., Omura T.;
"Structural analysis and specific expression of microsomal cytochrome
P-450(M-1) mRNA in male rat livers.";
J. Biol. Chem. 262:1706-1711(1987).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=2894840; DOI=10.1021/bi00399a039;
Morishima N., Yoshioka H., Higashi Y., Sogawa K., Fujii-Kuriyama Y.;
"Gene structure of cytochrome P-450(M-1) specifically expressed in
male rat liver.";
Biochemistry 26:8279-8285(1987).
[3]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Liver;
PubMed=2455430;
Stroem A., Mode A., Zaphiropoulos P.G., Nilsson A.G., Morgan E.,
Gustafsson J.-A.;
"Cloning and pretranslational hormonal regulation of testosterone 16
alpha-hydroxylase (P-45016 alpha) in male rat liver.";
Acta Endocrinol. 118:314-320(1988).
[4]
NUCLEOTIDE SEQUENCE [MRNA].
STRAIN=Wistar Gunn; TISSUE=Liver;
PubMed=8611037; DOI=10.1006/abbi.1996.0079;
Biagini C., Celier C.;
"cDNA-directed expression of two allelic variants of cytochrome P450
2C11 using COS1 and SF21 insect cells.";
Arch. Biochem. Biophys. 326:298-305(1996).
[5]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=3164963;
Zaphiropoulos P.G., Mode A., Stroem A., Husman B., Andersson G.,
Gustafsson J.-A.;
"Sequence and regulation of two growth-hormone-controlled, sex-
specific isozymes of cytochrome P-450 in rat liver, P-450(15)beta and
P-450(16)alpha.";
Acta Med. Scand. Suppl. 723:161-167(1988).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Liver;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[7]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-56.
STRAIN=Sprague-Dawley; TISSUE=Liver;
PubMed=8068205; DOI=10.1089/dna.1994.13.805;
Stroem A., Eguchi H., Mode A., Legraverend C., Tollet P.,
Stroemstedt P.-E., Gustafsson J.-A.;
"Characterization of the proximal promoter and two silencer elements
in the CYP2C11 gene expressed in rat liver.";
DNA Cell Biol. 13:805-819(1994).
[8]
SEQUENCE REVISION TO 12.
Stroem A.;
Submitted (JUL-1999) to the EMBL/GenBank/DDBJ databases.
[9]
PROTEIN SEQUENCE OF 1-30.
PubMed=2434473;
Matsumoto T., Emi Y., Kawabata S., Omura T.;
"Purification and characterization of three male-specific and one
female-specific forms of cytochrome P-450 from rat liver microsomes.";
J. Biochem. 100:1359-1371(1986).
-!- FUNCTION: Metabolizes testosterone mainly in positions 2 alpha and
16 alpha.
-!- CATALYTIC ACTIVITY:
Reaction=an alkane + O2 + reduced [NADPH--hemoprotein reductase] =
a primary alcohol + H(+) + H2O + oxidized [NADPH--hemoprotein
reductase]; Xref=Rhea:RHEA:17149, Rhea:RHEA-COMP:11964,
Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
ChEBI:CHEBI:15379, ChEBI:CHEBI:15734, ChEBI:CHEBI:18310,
ChEBI:CHEBI:57618, ChEBI:CHEBI:58210; EC=1.14.14.1;
-!- COFACTOR:
Name=heme; Xref=ChEBI:CHEBI:30413; Evidence={ECO:0000250};
-!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Peripheral
membrane protein. Microsome membrane; Peripheral membrane protein.
-!- TISSUE SPECIFICITY: Liver; male-specific.
-!- INDUCTION: Constitutively expressed.
-!- SIMILARITY: Belongs to the cytochrome P450 family. {ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; J02657; AAA41062.1; -; mRNA.
EMBL; M18363; AAA41007.1; -; Genomic_DNA.
EMBL; M18356; AAA41007.1; JOINED; Genomic_DNA.
EMBL; M18357; AAA41007.1; JOINED; Genomic_DNA.
EMBL; M18359; AAA41007.1; JOINED; Genomic_DNA.
EMBL; M18360; AAA41007.1; JOINED; Genomic_DNA.
EMBL; M18361; AAA41007.1; JOINED; Genomic_DNA.
EMBL; M18362; AAA41007.1; JOINED; Genomic_DNA.
EMBL; U33173; AAB02144.1; -; mRNA.
EMBL; BC088146; AAH88146.1; -; mRNA.
EMBL; X79081; CAA55686.3; -; Genomic_DNA.
PIR; A26685; A26685.
PIR; S62785; S62785.
RefSeq; NP_062057.2; NM_019184.2.
UniGene; Rn.10870; -.
ProteinModelPortal; P08683; -.
SMR; P08683; -.
STRING; 10116.ENSRNOP00000017310; -.
BindingDB; P08683; -.
ChEMBL; CHEMBL4971; -.
SwissLipids; SLP:000001687; -.
iPTMnet; P08683; -.
PhosphoSitePlus; P08683; -.
PaxDb; P08683; -.
PRIDE; P08683; -.
GeneID; 29277; -.
KEGG; rno:29277; -.
CTD; 29277; -.
RGD; 2469; Cyp2c11.
eggNOG; KOG0156; Eukaryota.
eggNOG; COG2124; LUCA.
HOGENOM; HOG000036992; -.
HOVERGEN; HBG015789; -.
InParanoid; P08683; -.
KO; K07413; -.
PhylomeDB; P08683; -.
TreeFam; TF352043; -.
BRENDA; 1.14.13.159; 5301.
BRENDA; 1.14.14.1; 5301.
SABIO-RK; P08683; -.
PRO; PR:P08683; -.
Proteomes; UP000002494; Unplaced.
GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
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:0008392; F:arachidonic acid epoxygenase activity; IBA:GO_Central.
GO; GO:0070330; F:aromatase activity; IEA:UniProtKB-EC.
GO; GO:0020037; F:heme binding; IBA:GO_Central.
GO; GO:0005506; F:iron ion binding; IEA:InterPro.
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.
GO; GO:0008395; F:steroid hydroxylase activity; IBA:GO_Central.
GO; GO:0008390; F:testosterone 16-alpha-hydroxylase activity; IMP:RGD.
GO; GO:0019373; P:epoxygenase P450 pathway; IBA:GO_Central.
GO; GO:0042738; P:exogenous drug catabolic process; IBA:GO_Central.
GO; GO:0006082; P:organic acid metabolic process; IBA:GO_Central.
GO; GO:0055114; P:oxidation-reduction process; IBA:GO_Central.
GO; GO:0006805; P:xenobiotic metabolic process; IBA:GO_Central.
Gene3D; 1.10.630.10; -; 1.
InterPro; IPR001128; Cyt_P450.
InterPro; IPR017972; Cyt_P450_CS.
InterPro; IPR002401; Cyt_P450_E_grp-I.
InterPro; IPR008068; Cyt_P450_E_grp-I_CYP2B-like.
InterPro; IPR036396; Cyt_P450_sf.
Pfam; PF00067; p450; 1.
PRINTS; PR00463; EP450I.
PRINTS; PR01685; EP450ICYP2B.
PRINTS; PR00385; P450.
SUPFAM; SSF48264; SSF48264; 1.
PROSITE; PS00086; CYTOCHROME_P450; 1.
1: Evidence at protein level;
Complete proteome; Direct protein sequencing; Endoplasmic reticulum;
Heme; Iron; Membrane; Metal-binding; Microsome; Monooxygenase;
Oxidoreductase; Polymorphism; Reference proteome.
CHAIN 1 500 Cytochrome P450 2C11.
/FTId=PRO_0000051701.
METAL 435 435 Iron (heme axial ligand). {ECO:0000250}.
VARIANT 4 4 V -> A (in strain: Wistar Gunn).
VARIANT 116 116 N -> S (in strain: Wistar Gunn).
VARIANT 187 187 F -> L (in strain: Wistar Gunn).
CONFLICT 329 329 R -> H (in Ref. 2; AAA41007).
{ECO:0000305}.
SEQUENCE 500 AA; 57181 MW; 8DCE0E356D8A5AC3 CRC64;
MDPVLVLVLT LSSLLLLSLW RQSFGRGKLP PGPTPLPIIG NTLQIYMKDI GQSIKKFSKV
YGPIFTLYLG MKPFVVLHGY EAVKEALVDL GEEFSGRGSF PVSERVNKGL GVIFSNGMQW
KEIRRFSIMT LRTFGMGKRT IEDRIQEEAQ CLVEELRKSK GAPFDPTFIL GCAPCNVICS
IIFQNRFDYK DPTFLNLMHR FNENFRLFSS PWLQVCNTFP AIIDYFPGSH NQVLKNFFYI
KNYVLEKVKE HQESLDKDNP RDFIDCFLNK MEQEKHNPQS EFTLESLVAT VTDMFGAGTE
TTSTTLRYGL LLLLKHVDVT AKVQEEIERV IGRNRSPCMK DRSQMPYTDA VVHEIQRYID
LVPTNLPHLV TRDIKFRNYF IPKGTNVIVS LSSILHDDKE FPNPEKFDPG HFLDERGNFK
KSDYFMPFSA GKRICAGEAL ARTELFLFFT TILQNFNLKS LVDVKDIDTT PAISGFGHLP
PFYEACFIPV QRADSLSSHL


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