CP2CD_RAT
ID CP2CD_RAT Reviewed; 490 AA.
AC P20814; P22693; Q64587;
DT 01-FEB-1991, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1991, sequence version 1.
DT 03-AUG-2022, entry version 150.
DE RecName: Full=Cytochrome P450 2C13, male-specific;
DE EC=1.14.14.1;
DE AltName: Full=CYPIIC13;
DE AltName: Full=Cytochrome P-450g;
DE AltName: Full=Cytochrome P450-G;
DE AltName: Full=Cytochrome P450-UT-5;
GN Name=Cyp2c13; Synonyms=Cyp2c-13;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (G+).
RC STRAIN=Sprague-Dawley; TISSUE=Liver;
RX PubMed=2775738; DOI=10.1021/bi00440a020;
RA McClellan-Green P.D., Negishi M., Goldstein J.A.;
RT "Characterization of a cDNA for rat P-450g, a highly polymorphic, male-
RT specific cytochrome in the P-450IIC subfamily.";
RL Biochemistry 28:5832-5839(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (G-).
RC STRAIN=Sprague-Dawley; TISSUE=Liver;
RX PubMed=2325668; DOI=10.1210/mend-4-1-53;
RA Zaphiropoulos P.G., Stroem A., Robertson J.A., Gustafsson J.-A.;
RT "Structural and regulatory analysis of the male-specific rat liver
RT cytochrome P-450 g: repression by continuous growth hormone
RT administration.";
RL Mol. Endocrinol. 4:53-58(1990).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Eguchi H., Westin S., Stroem A., Gustafsson J.-A., Zaphiropolos P.G.;
RT "Gene structure and expression of the rat cytochrome P450IIC13, a
RT polymorphic male-specific cytochrome in the P450IIC subfamily.";
RL Submitted (DEC-1991) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 19-468 (G-).
RC STRAIN=Sprague-Dawley; TISSUE=Liver;
RX PubMed=2337591; DOI=10.1021/bi00455a018;
RA Yeowell H.N., McClellan-Green P.D., Negishi M., Goldstein J.A.;
RT "Characterization of a cDNA for the unexpressed form of cytochrome P-450g
RT from the (-g) rat and differentiation of its mRNA from that of the (+g)
RT phenotype using specific oligoprobes.";
RL Biochemistry 29:713-718(1990).
RN [5]
RP PROTEIN SEQUENCE OF 1-30 (G+).
RX PubMed=2434473; DOI=10.1093/oxfordjournals.jbchem.a121842;
RA Matsumoto T., Emi Y., Kawabata S., Omura T.;
RT "Purification and characterization of three male-specific and one female-
RT specific forms of cytochrome P-450 from rat liver microsomes.";
RL J. Biochem. 100:1359-1371(1986).
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 -!- 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, and to a lesser extent in prostate, kidney,
CC heart and brain.
CC -!- INDUCTION: P450 can be induced to high levels in liver and other
CC tissues by various foreign compounds, including drugs, pesticides, and
CC carcinogens.
CC -!- MISCELLANEOUS: The G(-) form of this protein is thought to be
CC unexpressed.
CC -!- SIMILARITY: Belongs to the cytochrome P450 family. {ECO:0000305}.
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DR EMBL; J02861; AAA41785.1; -; mRNA.
DR EMBL; M33994; AAA41063.1; -; mRNA.
DR EMBL; M82855; AAA41059.1; -; Genomic_DNA.
DR EMBL; M82849; AAA41059.1; JOINED; Genomic_DNA.
DR EMBL; M82850; AAA41059.1; JOINED; Genomic_DNA.
DR EMBL; M82846; AAA41059.1; JOINED; Genomic_DNA.
DR EMBL; M82848; AAA41059.1; JOINED; Genomic_DNA.
DR EMBL; M82853; AAA41059.1; JOINED; Genomic_DNA.
DR EMBL; M82851; AAA41059.1; JOINED; Genomic_DNA.
DR EMBL; M82852; AAA41059.1; JOINED; Genomic_DNA.
DR EMBL; M32277; AAA41031.1; -; mRNA.
DR PIR; A36122; A36122.
DR PIR; I52410; I52410.
DR RefSeq; NP_612523.1; NM_138514.1.
DR AlphaFoldDB; P20814; -.
DR SMR; P20814; -.
DR STRING; 10116.ENSRNOP00000067531; -.
DR ChEMBL; CHEMBL3509596; -.
DR PaxDb; P20814; -.
DR PRIDE; P20814; -.
DR GeneID; 171521; -.
DR KEGG; rno:171521; -.
DR CTD; 171521; -.
DR RGD; 620363; Cyp2c13.
DR eggNOG; KOG0156; Eukaryota.
DR InParanoid; P20814; -.
DR OrthoDB; 702827at2759; -.
DR PhylomeDB; P20814; -.
DR PRO; PR:P20814; -.
DR Proteomes; UP000002494; 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:0004497; F:monooxygenase activity; TAS:RGD.
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 1: Evidence at protein level;
KW Direct protein sequencing; Endoplasmic reticulum; Heme; Iron; Membrane;
KW Metal-binding; Microsome; Monooxygenase; Oxidoreductase;
KW Reference proteome.
FT CHAIN 1..490
FT /note="Cytochrome P450 2C13, male-specific"
FT /id="PRO_0000051703"
FT BINDING 435
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 VARIANT 22
FT /note="P -> L (in G- phenotype)"
FT VARIANT 180
FT /note="S -> C (in G- phenotype)"
FT VARIANT 234
FT /note="F -> L (in G- phenotype)"
FT VARIANT 237
FT /note="H -> Y (in G- phenotype)"
FT VARIANT 240
FT /note="L -> V (in G- phenotype)"
FT VARIANT 338
FT /note="C -> S (in G- phenotype)"
FT VARIANT 369
FT /note="E -> D (in G- phenotype)"
FT CONFLICT 353
FT /note="H -> Q (in Ref. 3; AAA41059)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 490 AA; 55860 MW; F585891A7BB9F536 CRC64;
MDPVVVLLLS LFFLLFLSLW RPSSGRGKLP PGPTPLPIIG NFFQVDMKDI RQSLTNFSKT
YGPVYTLYVG SQPTVVLHGY EALKEALVDH GEEFSGRGRL PICEKVAKGQ GIAFSHGNVW
KATRHFTVKT LRNLGMGKGT IEDKVQEEAK WLVKELKKTN GSPCDPQFIM GCAPGNVICS
IILQNRFDYE DKDFLNLIEK VNEAVKIISS PGIQVFNIFP ILLDYCPGNH NIYFKNHTWL
KSYLLEKIKE HEESLDVSNP RDFIDYFLIE RNQENANQWM NYTLEHLAIM VTDLFFAGIE
TVSSTMRFAL LLLMKYPHVT AKVQEEIDHV IGRHRSPCMQ DRSHMPYTNA MVHEVQRYID
IGPNGLLHEV TCDTKFRNYF IPKGTAVLTS LTSVLHDSKE FPNPEMFDPG HFLDENGNFK
KSDYFIPFSA GKRMCLGESL ARMELFLFLT TILQNFKLKS LVDPKDINTT PICSSLSSVP
PTFQMRFIPL
