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 24-JAN-2024, entry version 156. 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}. 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; 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 iPTMnet; P20814; -. DR PhosphoSitePlus; P20814; -. DR PaxDb; 10116-ENSRNOP00000067531; -. DR GeneID; 171521; -. DR KEGG; rno:171521; -. DR AGR; RGD:620363; -. DR CTD; 171521; -. DR RGD; 620363; Cyp2c13. DR eggNOG; KOG0156; Eukaryota. DR InParanoid; P20814; -. DR OrthoDB; 2900138at2759; -. 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:0019373; P:epoxygenase P450 pathway; IBA:GO_Central. DR GO; GO:0006805; P:xenobiotic metabolic process; IBA:GO_Central. DR CDD; cd20665; CYP2C-like; 1. 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; PTHR24300:SF140; CYTOCHROME P450 2C40-RELATED; 1. DR PANTHER; PTHR24300; CYTOCHROME P450 508A4-RELATED; 1. DR Pfam; PF00067; p450; 1. DR PRINTS; PR00463; EP450I. DR PRINTS; PR00385; P450. DR SUPFAM; SSF48264; Cytochrome P450; 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 //