ID CP2DP_PIG Reviewed; 500 AA. AC O46658; DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2007, sequence version 3. DT 25-NOV-2008, entry version 59. DE RecName: Full=Vitamin D(3) 25-hydroxylase; DE EC=1.14.13.15; DE AltName: Full=Cytochrome P450 2D25; DE AltName: Full=CYPIID25; GN Name=CYP2D25; OS Sus scrofa (Pig). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Suina; Suidae; OC Sus. OX NCBI_TaxID=9823; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA], AND PROTEIN SEQUENCE OF 2-57; 249-273 AND RP 408-430. RC TISSUE=Liver; RX MEDLINE=98086378; PubMed=9425298; DOI=10.1006/bbrc.1997.7551; RA Postlind H., Axen E., Bergman T., Wikvall K.; RT "Cloning, structure, and expression of a cDNA encoding vitamin D3 25- RT hydroxylase."; RL Biochem. Biophys. Res. Commun. 241:491-497(1997). RN [2] RP PROTEIN SEQUENCE OF 2-17. RC TISSUE=Liver; RX MEDLINE=93075023; PubMed=1445236; RA Axen E., Bergman T., Wikvall K.; RT "Purification and characterization of a vitamin D3 25-hydroxylase from RT pig liver microsomes."; RL Biochem. J. 287:725-731(1992). RN [3] RP PROTEIN SEQUENCE OF 2-11. RC TISSUE=Liver; RX MEDLINE=91316123; PubMed=1859829; DOI=10.1016/0167-4838(91)90161-R; RA Sono H., Sonoda Y., Sato Y.; RT "Purification and characterization of cytochrome P-45014DM (lanosterol RT 14 alpha-demethylase) from pig liver microsomes."; RL Biochim. Biophys. Acta 1078:388-394(1991). CC -!- FUNCTION: Catalyzes the first step in the metabolic activation of CC vitamin D(3) into 1-alpha,25-dihydroxyvitamin D(3), its active, CC hormonal form. CC -!- CATALYTIC ACTIVITY: 5-beta-cholestane-3-alpha,7-alpha,12-alpha- CC triol + NADPH + O(2) = (25R)-5-beta-cholestane-3-alpha,7-alpha,12- CC alpha,26-tetraol + NADP(+) + H(2)O. CC -!- COFACTOR: Heme group (By similarity). CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Peripheral CC membrane protein. Microsome membrane; Peripheral membrane protein. CC -!- TISSUE SPECIFICITY: Found in liver and kidney. CC -!- SIMILARITY: Belongs to the cytochrome P450 family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; Y16417; CAA76205.1; -; mRNA. DR PIR; JC5819; JC5819. DR RefSeq; NP_999559.1; -. DR UniGene; Ssc.55051; -. DR HSSP; P00179; 1DT6. DR GeneID; 397687; -. DR KEGG; ssc:397687; -. DR HOVERGEN; O46658; -. DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell. DR GO; GO:0005792; C:microsome; IEA:UniProtKB-KW. DR GO; GO:0047749; F:cholestanetriol 26-monooxygenase activity; IEA:EC. DR GO; GO:0009055; F:electron carrier activity; IEA:InterPro. DR GO; GO:0020037; F:heme binding; IEA:InterPro. DR GO; GO:0005506; F:iron ion binding; IEA:InterPro. DR GO; GO:0016712; F:oxidoreductase activity, acting on paired d...; IEA:InterPro. DR GO; GO:0055114; P:oxidation reduction; IEA:UniProtKB-KW. DR InterPro; IPR001128; Cyt_P450. DR InterPro; IPR002401; Cyt_P450_E_grp-I. DR InterPro; IPR008069; Cyt_P450_E_grp-I_CYP2D-like. DR Gene3D; G3DSA:1.10.630.10; Cyt_P450; 1. DR PANTHER; PTHR19383; Cyt_P450; 1. DR Pfam; PF00067; p450; 1. DR PRINTS; PR00463; EP450I. DR PRINTS; PR01686; EP450ICYP2D. DR PRINTS; PR00385; P450. DR PROSITE; PS00086; CYTOCHROME_P450; 1. PE 1: Evidence at protein level; KW Direct protein sequencing; Endoplasmic reticulum; Heme; Iron; KW Membrane; Metal-binding; Microsome; Monooxygenase; NADP; KW Oxidoreductase. FT INIT_MET 1 1 Removed. FT CHAIN 2 500 Vitamin D(3) 25-hydroxylase. FT /FTId=PRO_0000051745. FT METAL 446 446 Iron (heme axial ligand) (By similarity). SQ SEQUENCE 500 AA; 56512 MW; F1C878A02C44503D CRC64; MGLLTGDLLG ILALAMVIFL LLVDLMHRRS RWAPRYPPGP MPLPGLGNLL QVNFQDPRLS FIQLRRRFGD VFSLQQIWRP VVVLNGLAAV REALVSHSHE TSDRPPVFIL EHLGYGPRSE GVILARYGKA WREQRRFSVS TLRNFGLGKK SLEEWVTQEA SCLCAAFADQ AGRPFSPNNL LNKAVSNVIA SLTFARRFEY NDPRMLKLLD LVLEGLKEEV GLMRQVLEAM PVLRHIPGLC AKLFPRQKAF LVMIDELITE HKMTRDLAQP PRDLTDAFLD EMKEAKGNPE SSFNDENLRL VVAHLFSAGM ITTSTTLAWA LLLMILHPDV QRRVQQEIDE VIGHVRQPEI KDQALMPFTL AVLHEVQRFG DIVPLGVAHM TSCDIEVQGF LIPKGTTLIT NLTSVLKDET VWKKPFRFYP EHFLDAQGRF TKQEAFMPFS AGRRSCLGEP LARMELFLFF TTLLQAFSFS VPTGQPCPSD HGVFAFLLFP SPYQLCAVPR //