CP2CP_MESAU
ID CP2CP_MESAU Reviewed; 490 AA.
AC Q08078;
DT 15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 107.
DE RecName: Full=Cytochrome P450 2C25;
DE EC=1.14.14.1;
DE AltName: Full=CYPIIC25;
DE AltName: Full=Cytochrome P450 HSM1;
GN Name=CYP2C25;
OS Mesocricetus auratus (Golden hamster).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea;
OC Cricetidae; Cricetinae; Mesocricetus.
OX NCBI_TaxID=10036;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Liver;
RX PubMed=8114672;
RA Sakuma T., Masaki K., Itoh S., Yokoi T., Kamataki T.;
RT "Sex-related differences in the expression of cytochrome P450 in hamsters:
RT cDNA cloning and examination of the expression of three distinct CYP2C
RT cDNAs.";
RL Mol. Pharmacol. 45:228-236(1994).
CC -!- FUNCTION: Catalyzes the hydroxylation of tolbutamide and the N-
CC demethylation of aminopyrine and benzphetamine. Also has testosterone
CC hydroxylase (16 beta) 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 -!- 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 -!- SIMILARITY: Belongs to the cytochrome P450 family. {ECO:0000305}.
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DR EMBL; X63022; CAA44753.1; -; mRNA.
DR PIR; I48189; I48189.
DR RefSeq; NP_001268615.1; NM_001281686.1.
DR AlphaFoldDB; Q08078; -.
DR SMR; Q08078; -.
DR STRING; 10036.XP_005063675.1; -.
DR GeneID; 101823450; -.
DR KEGG; ag:CAA44753; -.
DR eggNOG; KOG0156; Eukaryota.
DR OrthoDB; 702827at2759; -.
DR Proteomes; UP000189706; Unplaced.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0070330; F:aromatase activity; IEA:UniProtKB-EC.
DR GO; GO:0020037; F:heme binding; IEA:InterPro.
DR GO; GO:0005506; F:iron ion binding; IEA:InterPro.
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..490
FT /note="Cytochrome P450 2C25"
FT /id="PRO_0000051713"
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 /evidence="ECO:0000250"
SQ SEQUENCE 490 AA; 55967 MW; AB040B2ECAB80453 CRC64;
MDAVLVLVFI LSSLVFLSLW RQSSERRKLP PGPTPLPIIG NFLQIDVKNI SGSLTNFSKV
YGPVFTLYLG MKPTVVLHGY ETVKEALIDH GEEFAGRGDF PMAERINKGL GIVFSNGNRW
KEIRRFSLMT LRNLGMGKRN IEDRVQEEAQ CLVEELRKTN GSPCDPTFIL SCAPCNVICS
IIFQNRFDYK DQDFLTFMKK VNENVRILSS PWLQVCNNFP SLIDYCPGSH HKITKNVNYL
KKYILEKIEE HQESLDIENP RDFIDYYLIK LKQANHNQQS EFSLENLTTT VSDLFGAGTE
TTSTTLRYAL LLLLKHPHVT AKVQEEIDQV VGRHRKPCMQ DRSHMPYTDA MIHEVQRFID
LIPISLPHAV TCDIKFRDYF IPKGTTVITS LSSVLHDNKE FPNPEVFDPG HFLDKNGNFK
KSDYFMPFSA GKRICAGEGL ARMELFLFLT TILQNFKLKS MIHPKDIDTT PVVNGFASLP
PSYQLCFIPV