ID DHCR7_MOUSE Reviewed; 471 AA. AC O88455; DT 31-JAN-2002, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1998, sequence version 1. DT 16-JUN-2009, entry version 67. DE RecName: Full=7-dehydrocholesterol reductase; DE Short=7-DHC reductase; DE EC=1.3.1.21; DE AltName: Full=Sterol Delta(7)-reductase; GN Name=Dhcr7; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RC STRAIN=C57BL/6J; RX MEDLINE=98318632; PubMed=9653161; DOI=10.1073/pnas.95.14.8181; RA Fitzky B.U., Witsch-Baumgartner M., Erdel M., Lee J.N., Paik Y.-K., RA Glossmann H., Utermann G., Moebius F.F.; RT "Mutations in the delta7-sterol reductase gene in patients with the RT Smith-Lemli-Opitz syndrome."; RL Proc. Natl. Acad. Sci. U.S.A. 95:8181-8186(1998). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). CC -!- FUNCTION: Production of cholesterol by reduction of C7-C8 double CC bond of 7-dehydrocholesterol (7-DHC). CC -!- CATALYTIC ACTIVITY: Cholesterol + NADP(+) = cholesta-5,7-dien-3- CC beta-ol + NADPH. CC -!- PATHWAY: Steroid biosynthesis; cholesterol biosynthesis. CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Multi-pass CC membrane protein. CC -!- SIMILARITY: Belongs to the ERG4/ERG24 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; AF057368; AAC40164.1; -; mRNA. DR EMBL; BC006854; AAH06854.1; -; mRNA. DR IPI; IPI00130988; -. DR RefSeq; NP_031882.1; -. DR UniGene; Mm.249342; -. DR PhosphoSite; O88455; -. DR PRIDE; O88455; -. DR Ensembl; ENSMUSG00000058454; Mus musculus. DR GeneID; 13360; -. DR KEGG; mmu:13360; -. DR MGI; MGI:1298378; Dhcr7. DR HOGENOM; O88455; -. DR HOVERGEN; O88455; -. DR OMA; O88455; WAKTPPV. DR BRENDA; 1.3.1.21; 244. DR NextBio; 283692; -. DR ArrayExpress; O88455; -. DR Bgee; O88455; -. DR CleanEx; MM_DHCR7; -. DR GermOnline; ENSMUSG00000058454; Mus musculus. DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell. DR GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW. DR GO; GO:0047598; F:7-dehydrocholesterol reductase activity; IDA:MGI. DR GO; GO:0001568; P:blood vessel development; IMP:MGI. DR GO; GO:0030154; P:cell differentiation; IMP:MGI. DR GO; GO:0006695; P:cholesterol biosynthetic process; IEA:UniProtKB-KW. DR GO; GO:0030324; P:lung development; IMP:MGI. DR GO; GO:0035264; P:multicellular organism growth; IMP:MGI. DR GO; GO:0055114; P:oxidation reduction; IEA:UniProtKB-KW. DR GO; GO:0009791; P:post-embryonic development; IMP:MGI. DR GO; GO:0042127; P:regulation of cell proliferation; IMP:MGI. DR InterPro; IPR001171; Ergosterol_biosynth_ERG4_ERG24. DR InterPro; IPR018083; Sterol_reductase_CS. DR Pfam; PF01222; ERG4_ERG24; 1. DR PROSITE; PS01017; STEROL_REDUCT_1; 1. DR PROSITE; PS01018; STEROL_REDUCT_2; 1. PE 2: Evidence at transcript level; KW Cholesterol biosynthesis; Endoplasmic reticulum; Lipid synthesis; KW Membrane; NADP; Oxidoreductase; Phosphoprotein; Steroid biosynthesis; KW Sterol biosynthesis; Transmembrane. FT CHAIN 1 471 7-dehydrocholesterol reductase. FT /FTId=PRO_0000207503. FT TRANSMEM 36 56 Potential. FT TRANSMEM 95 115 Potential. FT TRANSMEM 144 164 Potential. FT TRANSMEM 173 193 Potential. FT TRANSMEM 233 253 Potential. FT TRANSMEM 262 282 Potential. FT TRANSMEM 302 322 Potential. FT TRANSMEM 327 347 Potential. FT TRANSMEM 416 436 Potential. FT MOD_RES 14 14 Phosphoserine (By similarity). SQ SEQUENCE 471 AA; 53919 MW; 6B1BC356CC539290 CRC64; MASKSQHNAP KVKSPNGKAG SQGQWGRAWE VDWFSLASII FLLLFAPFIV YYFIMACDQY SCSLTAPALD IATGHASLAD IWAKTPPVTA KAAQLYALWV SFQVLLYSWL PDFCHRFLPG YVGGVQEGAI TPAGVVNKYE VNGLQAWLIT HILWFVNAYL LSWFSPTIIF DNWIPLLWCA NILGYAVSTF AMIKGYLFPT SAEDCKFTGN FFYNYMMGIE FNPRIGKWFD FKLFFNGRPG IVAWTLINLS FAAKQQELYG HVTNSMILVN VLQAIYVLDF FWNETWYLKT IDICHDHFGW YLGWGDCVWL PYLYTLQGLY LVYHPVQLST PNALGILLLG LVGYYIFRMT NHQKDLFRRT DGRCLIWGKK PKAIECSYTS ADGLKHHSKL LVSGFWGVAR HFNYTGDLMG SLAYCLACGG GHLLPYFYII YMTILLTHRC LRDEHRCANK YGRDWERYTA AVPYRLLPGI F //