ID DHCR7_HUMAN Reviewed; 475 AA. AC Q9UBM7; B2R6Z2; O60492; O60717; DT 31-JAN-2002, integrated into UniProtKB/Swiss-Prot. DT 01-MAY-2000, sequence version 1. DT 17-JUN-2020, entry version 190. DE RecName: Full=7-dehydrocholesterol reductase {ECO:0000303|PubMed:9683613}; DE Short=7-DHC reductase; DE EC=1.3.1.21 {ECO:0000269|PubMed:25637936, ECO:0000269|PubMed:9465114, ECO:0000269|PubMed:9634533}; DE AltName: Full=Delta7-sterol reductase {ECO:0000303|PubMed:9465114}; DE AltName: Full=Sterol Delta(7)-reductase; DE AltName: Full=Sterol reductase SR-2; GN Name=DHCR7; Synonyms=D7SR; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; OC Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA], AND VARIANTS SLOS LEU-119; ARG-244 AND CYS-248. RX PubMed=9683613; DOI=10.1086/301982; RA Waterham H.R., Wijburg F.A., Hennekam R.C.M., Vreken P., Poll-The B.T., RA Dorland L., Duran M., Jira P.E., Smeitink J.A.M., Wevers R.A., RA Wanders R.J.A.; RT "Smith-Lemli-Opitz syndrome is caused by mutations in the 7- RT dehydrocholesterol reductase gene."; RL Am. J. Hum. Genet. 63:329-338(1998). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA], VARIANT LEU-5, CATALYTIC ACTIVITY, TISSUE RP SPECIFICITY, AND FUNCTION. RC TISSUE=Liver; RX PubMed=9465114; DOI=10.1073/pnas.95.4.1899; RA Moebius F.F., Fitzky B.U., Lee J.N., Paik Y.K., Glossmann H.; RT "Molecular cloning and expression of the human delta7-sterol reductase."; RL Proc. Natl. Acad. Sci. U.S.A. 95:1899-1902(1998). RN [3] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], SUBCELLULAR LOCATION, AND TISSUE RP SPECIFICITY. RX PubMed=9878250; DOI=10.1006/geno.1998.5615; RA Holmer L., Pezhman A., Worman H.J.; RT "The human lamin B receptor/sterol reductase multigene family."; RL Genomics 54:469-476(1998). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT LEU-5. RC TISSUE=Testis; RX PubMed=14702039; DOI=10.1038/ng1285; RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S., RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., RA Isogai T., Sugano S.; RT "Complete sequencing and characterization of 21,243 full-length human RT cDNAs."; RL Nat. Genet. 36:40-45(2004). RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Brain; 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 project: RT the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [6] RP NUCLEOTIDE SEQUENCE [MRNA] OF 14-475, CATALYTIC ACTIVITY, AND FUNCTION. RC TISSUE=Liver; RX PubMed=9634533; DOI=10.1086/301936; RA Wassif C.A., Maslen C., Kachilele-Linjewile S., Lin D., Linck L.M., RA Conner W.E., Steiner R.D., Porter F.D.; RT "Mutations in the human sterol delta 7-reductase gene at 11q12-13 cause RT Smith-Lemli-Opitz syndrome."; RL Am. J. Hum. Genet. 63:55-62(1998). RN [7] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-14, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007; RA Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., RA Greff Z., Keri G., Stemmann O., Mann M.; RT "Kinase-selective enrichment enables quantitative phosphoproteomics of the RT kinome across the cell cycle."; RL Mol. Cell 31:438-448(2008). RN [8] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-14, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=19369195; DOI=10.1074/mcp.m800588-mcp200; RA Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G., RA Mann M., Daub H.; RT "Large-scale proteomics analysis of the human kinome."; RL Mol. Cell. Proteomics 8:1751-1764(2009). RN [9] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-14, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Leukemic T-cell; RX PubMed=19690332; DOI=10.1126/scisignal.2000007; RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., RA Rodionov V., Han D.K.; RT "Quantitative phosphoproteomic analysis of T cell receptor signaling RT reveals system-wide modulation of protein-protein interactions."; RL Sci. Signal. 2:RA46-RA46(2009). RN [10] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-14, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=20068231; DOI=10.1126/scisignal.2000475; RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.; RT "Quantitative phosphoproteomics reveals widespread full phosphorylation RT site occupancy during mitosis."; RL Sci. Signal. 3:RA3-RA3(2010). RN [11] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21269460; DOI=10.1186/1752-0509-5-17; RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., RA Bennett K.L., Superti-Furga G., Colinge J.; RT "Initial characterization of the human central proteome."; RL BMC Syst. Biol. 5:17-17(2011). RN [12] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-14, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21406692; DOI=10.1126/scisignal.2001570; RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.; RT "System-wide temporal characterization of the proteome and phosphoproteome RT of human embryonic stem cell differentiation."; RL Sci. Signal. 4:RS3-RS3(2011). RN [13] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=22814378; DOI=10.1073/pnas.1210303109; RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.; RT "N-terminal acetylome analyses and functional insights of the N-terminal RT acetyltransferase NatB."; RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012). RN [14] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-14, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Erythroleukemia; RX PubMed=23186163; DOI=10.1021/pr300630k; RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J., RA Mohammed S.; RT "Toward a comprehensive characterization of a human cancer cell RT phosphoproteome."; RL J. Proteome Res. 12:260-271(2013). RN [15] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-14, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Liver; RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014; RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., RA Ye M., Zou H.; RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver RT phosphoproteome."; RL J. Proteomics 96:253-262(2014). RN [16] RP INTERACTION WITH DHCR24, CATALYTIC ACTIVITY, AND FUNCTION. RX PubMed=25637936; DOI=10.1194/jlr.m056986; RA Luu W., Hart-Smith G., Sharpe L.J., Brown A.J.; RT "The terminal enzymes of cholesterol synthesis, DHCR24 and DHCR7, interact RT physically and functionally."; RL J. Lipid Res. 56:888-897(2015). RN [17] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=25944712; DOI=10.1002/pmic.201400617; RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D., RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.; RT "N-terminome analysis of the human mitochondrial proteome."; RL Proteomics 15:2519-2524(2015). RN [18] RP VARIANTS SLOS SER-51; MET-93; PRO-99; PRO-157; VAL-247; LEU-326; TRP-352; RP SER-380; CYS-404 AND SER-410. RX 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 Smith- RT Lemli-Opitz syndrome."; RL Proc. Natl. Acad. Sci. U.S.A. 95:8181-8186(1998). RN [19] RP VARIANTS SLOS SER-51; MET-93; PRO-99; HIS-107; PRO-109; ASP-147; MET-154; RP PRO-157; LEU-169; CYS-182; CYS-242; VAL-247; MET-281; ILE-289; GLY-311; RP TYR-311; HIS-324; LEU-326; GLN-352; TRP-352; ALA-353; CYS-362; TYR-380; RP ARG-380; SER-380; LEU-397; CYS-404; SER-404; HIS-408; SER-410; ARG-410; RP CYS-443; GLN-446; GLN-448; LYS-448 AND LEU-450. RX PubMed=10677299; DOI=10.1086/302760; RA Witsch-Baumgartner M., Fitzky B.U., Ogorelkova M., Kraft H.G., RA Moebius F.F., Glossmann H., Seedorf U., Gillessen-Kaesbach G., RA Hoffmann G.F., Clayton P., Kelley R.I., Utermann G.; RT "Mutational spectrum in the Delta7-sterol reductase gene and genotype- RT phenotype correlation in 84 patients with Smith-Lemli-Opitz syndrome."; RL Am. J. Hum. Genet. 66:402-412(2000). RN [20] RP VARIANT SLOS ILE-289. RX PubMed=10995508; RX DOI=10.1002/1096-8628(20000918)94:3<214::aid-ajmg7>3.0.co;2-r; RA Krakowiak P.A., Nwokoro N.A., Wassif C.A., Battaile K.P., Nowaczyk M.J.M., RA Connor W.E., Maslen C., Steiner R.D., Porter F.D.; RT "Mutation analysis and description of sixteen RSH/Smith-Lemli-Opitz RT syndrome patients: polymerase chain reaction-based assays to simplify RT genotyping."; RL Am. J. Med. Genet. 94:214-227(2000). RN [21] RP VARIANTS SLOS MET-93; PRO-109; LEU-119; MET-154; LEU-182; TYR-183; GLU-198; RP HIS-242; ARG-244; CYS-248 AND LEU-255. RX PubMed=11427181; DOI=10.1017/s0003480001008600; RA Jira P.E., Wanders R.J.A., Smeitink J.A.M., De Jong J., Wevers R.A., RA Oostheim W., Tuerlings J.H.A.M., Hennekam R.C.M., Sengers R.C.A., RA Waterham H.R.; RT "Novel mutations in the 7-dehydrocholesterol reductase gene of 13 patients RT with Smith-Lemli-Opitz syndrome."; RL Ann. Hum. Genet. 65:229-236(2001). RN [22] RP VARIANTS SLOS MET-93; LEU-326; TRP-352 AND CYS-404. RX PubMed=11175299; DOI=10.1038/sj.ejhg.5200579; RA Witsch-Baumgartner M., Ciara E., Loffler J., Menzel H.J., Seedorf U., RA Burn J., Gillessen-Kaesbach G., Hoffmann G.F., Fitzky B.U., Mundy H., RA Clayton P., Kelley R.I., Krajewska-Walasek M., Utermann G.; RT "Frequency gradients of DHCR7 mutations in patients with Smith-Lemli-Opitz RT syndrome in Europe: evidence for different origins of common mutations."; RL Eur. J. Hum. Genet. 9:45-50(2001). RN [23] RP VARIANT SLOS LYS-448. RX PubMed=12949967; DOI=10.1002/ajmg.a.20207; RA Langius F.A., Waterham H.R., Romeijn G.J., Oostheim W., de Barse M.M., RA Dorland L., Duran M., Beemer F.A., Wanders R.J., Poll-The B.T.; RT "Identification of three patients with a very mild form of Smith-Lemli- RT Opitz syndrome."; RL Am. J. Med. Genet. A 122:24-29(2003). RN [24] RP VARIANTS SLOS PRO-68; CYS-113; VAL-138; LEU-145; SER-235; CYS-242; THR-297; RP ARG-344; CYS-404; TYR-405; HIS-408 AND PRO-426. RX PubMed=15954111; DOI=10.1002/humu.9346; RA Waye J.S., Krakowiak P.A., Wassif C.A., Sterner A.L., Eng B., RA Nakamura L.M., Nowaczyk M.J.M., Porter F.D.; RT "Identification of nine novel DHCR7 missense mutations in patients with RT Smith-Lemli-Opitz syndrome (SLOS)."; RL Hum. Mutat. 26:59-59(2005). RN [25] RP VARIANT ARG-118. RX PubMed=25787250; DOI=10.1073/pnas.1503696112; RA Cromer M.K., Choi M., Nelson-Williams C., Fonseca A.L., Kunstman J.W., RA Korah R.M., Overton J.D., Mane S., Kenney B., Malchoff C.D., Stalberg P., RA Akerstroem G., Westin G., Hellman P., Carling T., Bjoerklund P., RA Lifton R.P.; RT "Neomorphic effects of recurrent somatic mutations in Yin Yang 1 in RT insulin-producing adenomas."; RL Proc. Natl. Acad. Sci. U.S.A. 112:4062-4067(2015). CC -!- FUNCTION: Production of cholesterol by reduction of C7-C8 double bond CC of 7-dehydrocholesterol (7-DHC). {ECO:0000269|PubMed:25637936, CC ECO:0000269|PubMed:9465114, ECO:0000269|PubMed:9634533}. CC -!- CATALYTIC ACTIVITY: CC Reaction=cholesterol + NADP(+) = cholesta-5,7-dien-3beta-ol + H(+) + CC NADPH; Xref=Rhea:RHEA:23984, ChEBI:CHEBI:15378, ChEBI:CHEBI:16113, CC ChEBI:CHEBI:17759, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.3.1.21; CC Evidence={ECO:0000269|PubMed:25637936, ECO:0000269|PubMed:9465114, CC ECO:0000269|PubMed:9634533}; CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:23986; CC Evidence={ECO:0000305|PubMed:9634533}; CC -!- CATALYTIC ACTIVITY: CC Reaction=cholesta-5,7,24-trien-3beta-ol + H(+) + NADPH = cholesta-5,24- CC dien-3beta-ol + NADP(+); Xref=Rhea:RHEA:46740, ChEBI:CHEBI:15378, CC ChEBI:CHEBI:17737, ChEBI:CHEBI:27910, ChEBI:CHEBI:57783, CC ChEBI:CHEBI:58349; Evidence={ECO:0000250|UniProtKB:O88455}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:46741; CC Evidence={ECO:0000250|UniProtKB:O88455}; CC -!- PATHWAY: Steroid biosynthesis; cholesterol biosynthesis. CC {ECO:0000269|PubMed:25637936, ECO:0000269|PubMed:9634533}. CC -!- SUBUNIT: Interacts with DHCR24; this interaction regulates DHCR7 CC activity. {ECO:0000269|PubMed:25637936}. CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane CC {ECO:0000269|PubMed:9878250}; Multi-pass membrane protein CC {ECO:0000255}. CC -!- TISSUE SPECIFICITY: Widely expressed. Most abundant in adrenal gland, CC liver, testis, and brain. {ECO:0000269|PubMed:9465114, CC ECO:0000269|PubMed:9878250}. CC -!- DISEASE: Smith-Lemli-Opitz syndrome (SLOS) [MIM:270400]: An autosomal CC recessive frequent inborn disorder of sterol metabolism with CC characteristic congenital malformations and mental retardation. CC Children with SLOS have elevated serum 7-dehydrocholesterol (7-DHC) CC levels and low serum cholesterol levels. SLOS occurs in relatively high CC frequency: approximately 1 in 20,000 to 30,000 births in populations of CC northern and central European background. Historically, a clinical CC distinction often was made between classic ('type I') SLOS and the more CC severely affected ('type II') patients. There is, in reality, a CC clinical and biochemical continuum from mild to severe SLOS. CC {ECO:0000269|PubMed:10677299, ECO:0000269|PubMed:10995508, CC ECO:0000269|PubMed:11175299, ECO:0000269|PubMed:11427181, CC ECO:0000269|PubMed:12949967, ECO:0000269|PubMed:15954111, CC ECO:0000269|PubMed:25637936, ECO:0000269|PubMed:9653161, CC ECO:0000269|PubMed:9683613}. Note=The disease is caused by mutations CC affecting the gene represented in this entry. CC -!- SIMILARITY: Belongs to the ERG4/ERG24 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; AF096305; AAD09766.1; -; mRNA. DR EMBL; AF034544; AAC05086.1; -; mRNA. DR EMBL; AF110060; AAD24762.1; -; Genomic_DNA. DR EMBL; AF067127; AAD02816.1; -; mRNA. DR EMBL; AK312775; BAG35639.1; -; mRNA. DR EMBL; BC000054; AAH00054.1; -; mRNA. DR EMBL; AF062481; AAC18345.1; -; mRNA. DR CCDS; CCDS8200.1; -. DR RefSeq; NP_001157289.1; NM_001163817.1. DR RefSeq; NP_001351.2; NM_001360.2. DR BioGRID; 108063; 43. DR IntAct; Q9UBM7; 30. DR MINT; Q9UBM7; -. DR STRING; 9606.ENSP00000347717; -. DR BindingDB; Q9UBM7; -. DR ChEMBL; CHEMBL2169735; -. DR DrugBank; DB00157; NADH. DR DrugCentral; Q9UBM7; -. DR SwissLipids; SLP:000001078; -. DR iPTMnet; Q9UBM7; -. DR PhosphoSitePlus; Q9UBM7; -. DR SwissPalm; Q9UBM7; -. DR BioMuta; DHCR7; -. DR DMDM; 20138066; -. DR CPTAC; CPTAC-353; -. DR CPTAC; CPTAC-354; -. DR EPD; Q9UBM7; -. DR jPOST; Q9UBM7; -. DR MassIVE; Q9UBM7; -. DR MaxQB; Q9UBM7; -. DR PaxDb; Q9UBM7; -. DR PeptideAtlas; Q9UBM7; -. DR PRIDE; Q9UBM7; -. DR ProteomicsDB; 84009; -. DR Antibodypedia; 30720; 159 antibodies. DR DNASU; 1717; -. DR Ensembl; ENST00000355527; ENSP00000347717; ENSG00000172893. DR Ensembl; ENST00000407721; ENSP00000384739; ENSG00000172893. DR GeneID; 1717; -. DR KEGG; hsa:1717; -. DR UCSC; uc001oqk.4; human. DR CTD; 1717; -. DR DisGeNET; 1717; -. DR EuPathDB; HostDB:ENSG00000172893.15; -. DR GeneCards; DHCR7; -. DR GeneReviews; DHCR7; -. DR HGNC; HGNC:2860; DHCR7. DR HPA; ENSG00000172893; Tissue enhanced (liver). DR MalaCards; DHCR7; -. DR MIM; 270400; phenotype. DR MIM; 602858; gene. DR neXtProt; NX_Q9UBM7; -. DR OpenTargets; ENSG00000172893; -. DR Orphanet; 818; Smith-Lemli-Opitz syndrome. DR PharmGKB; PA27321; -. DR eggNOG; KOG1435; Eukaryota. DR eggNOG; ENOG410XP67; LUCA. DR GeneTree; ENSGT00390000000417; -. DR HOGENOM; CLU_015631_0_0_1; -. DR InParanoid; Q9UBM7; -. DR KO; K00213; -. DR OMA; THRCIRD; -. DR OrthoDB; 532774at2759; -. DR PhylomeDB; Q9UBM7; -. DR TreeFam; TF101180; -. DR BioCyc; MetaCyc:HS10588-MONOMER; -. DR BRENDA; 1.3.1.21; 2681. DR Reactome; R-HSA-2426168; Activation of gene expression by SREBF (SREBP). DR Reactome; R-HSA-6807047; Cholesterol biosynthesis via desmosterol. DR Reactome; R-HSA-6807062; Cholesterol biosynthesis via lathosterol. DR SABIO-RK; Q9UBM7; -. DR UniPathway; UPA00063; -. DR BioGRID-ORCS; 1717; 3 hits in 791 CRISPR screens. DR ChiTaRS; DHCR7; human. DR GeneWiki; 7-Dehydrocholesterol_reductase; -. DR GenomeRNAi; 1717; -. DR Pharos; Q9UBM7; Tchem. DR PRO; PR:Q9UBM7; -. DR Proteomes; UP000005640; Chromosome 11. DR RNAct; Q9UBM7; protein. DR Bgee; ENSG00000172893; Expressed in adrenal tissue and 201 other tissues. DR ExpressionAtlas; Q9UBM7; baseline and differential. DR Genevisible; Q9UBM7; HS. DR GO; GO:0005829; C:cytosol; IDA:HPA. DR GO; GO:0005783; C:endoplasmic reticulum; IDA:UniProtKB. DR GO; GO:0005789; C:endoplasmic reticulum membrane; TAS:Reactome. DR GO; GO:0030176; C:integral component of endoplasmic reticulum membrane; IBA:GO_Central. DR GO; GO:0016020; C:membrane; HDA:UniProtKB. DR GO; GO:0005640; C:nuclear outer membrane; IDA:UniProtKB. DR GO; GO:0047598; F:7-dehydrocholesterol reductase activity; IDA:UniProtKB. DR GO; GO:0050661; F:NADP binding; ISS:UniProtKB. DR GO; GO:0016627; F:oxidoreductase activity, acting on the CH-CH group of donors; IBA:GO_Central. DR GO; GO:0009918; F:sterol delta7 reductase activity; IBA:GO_Central. DR GO; GO:0001568; P:blood vessel development; IEA:Ensembl. DR GO; GO:0016132; P:brassinosteroid biosynthetic process; IBA:GO_Central. DR GO; GO:0030154; P:cell differentiation; IEA:Ensembl. DR GO; GO:0006695; P:cholesterol biosynthetic process; IMP:UniProtKB. DR GO; GO:0033489; P:cholesterol biosynthetic process via desmosterol; TAS:Reactome. DR GO; GO:0033490; P:cholesterol biosynthetic process via lathosterol; TAS:Reactome. DR GO; GO:0030324; P:lung development; IEA:Ensembl. DR GO; GO:0035264; P:multicellular organism growth; IEA:Ensembl. DR GO; GO:0009791; P:post-embryonic development; IEA:Ensembl. DR GO; GO:0042127; P:regulation of cell population proliferation; IEA:Ensembl. DR GO; GO:0045540; P:regulation of cholesterol biosynthetic process; TAS:Reactome. DR GO; GO:0016126; P:sterol biosynthetic process; IBA:GO_Central. 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 1: Evidence at protein level; KW Cholesterol biosynthesis; Cholesterol metabolism; Disease mutation; KW Endoplasmic reticulum; Lipid biosynthesis; Lipid metabolism; Membrane; KW NADP; Oxidoreductase; Phosphoprotein; Polymorphism; Reference proteome; KW Steroid biosynthesis; Steroid metabolism; Sterol biosynthesis; KW Sterol metabolism; Transmembrane; Transmembrane helix. FT CHAIN 1..475 FT /note="7-dehydrocholesterol reductase" FT /id="PRO_0000207502" FT TRANSMEM 40..60 FT /note="Helical" FT /evidence="ECO:0000255" FT TRANSMEM 154..174 FT /note="Helical" FT /evidence="ECO:0000255" FT TRANSMEM 177..197 FT /note="Helical" FT /evidence="ECO:0000255" FT TRANSMEM 266..286 FT /note="Helical" FT /evidence="ECO:0000255" FT TRANSMEM 306..326 FT /note="Helical" FT /evidence="ECO:0000255" FT TRANSMEM 331..351 FT /note="Helical" FT /evidence="ECO:0000255" FT TRANSMEM 420..440 FT /note="Helical" FT /evidence="ECO:0000255" FT NP_BIND 407..408 FT /note="NADP" FT /evidence="ECO:0000250|UniProtKB:G4SW86" FT NP_BIND 451..455 FT /note="NADP" FT /evidence="ECO:0000250|UniProtKB:G4SW86" FT BINDING 358 FT /note="NADP" FT /evidence="ECO:0000250|UniProtKB:G4SW86" FT BINDING 362 FT /note="NADP" FT /evidence="ECO:0000250|UniProtKB:G4SW86" FT BINDING 395 FT /note="NADP; via amide nitrogen and carbonyl oxygen" FT /evidence="ECO:0000250|UniProtKB:G4SW86" FT BINDING 400 FT /note="NADP" FT /evidence="ECO:0000250|UniProtKB:G4SW86" FT BINDING 447 FT /note="NADP" FT /evidence="ECO:0000250|UniProtKB:G4SW86" FT BINDING 462 FT /note="NADP" FT /evidence="ECO:0000250|UniProtKB:G4SW86" FT MOD_RES 14 FT /note="Phosphoserine" FT /evidence="ECO:0000244|PubMed:18691976, FT ECO:0000244|PubMed:19369195, ECO:0000244|PubMed:19690332, FT ECO:0000244|PubMed:20068231, ECO:0000244|PubMed:21406692, FT ECO:0000244|PubMed:23186163, ECO:0000244|PubMed:24275569" FT VARIANT 5 FT /note="S -> L (in dbSNP:rs1127869)" FT /evidence="ECO:0000269|PubMed:14702039, FT ECO:0000269|PubMed:9465114" FT /id="VAR_067456" FT VARIANT 51 FT /note="P -> S (in SLOS; dbSNP:rs104886035)" FT /evidence="ECO:0000269|PubMed:10677299, FT ECO:0000269|PubMed:9653161" FT /id="VAR_012717" FT VARIANT 68 FT /note="L -> P (in SLOS; dbSNP:rs104886038)" FT /evidence="ECO:0000269|PubMed:15954111" FT /id="VAR_023148" FT VARIANT 93 FT /note="T -> M (in SLOS; dbSNP:rs80338853)" FT /evidence="ECO:0000269|PubMed:10677299, FT ECO:0000269|PubMed:11175299, ECO:0000269|PubMed:11427181, FT ECO:0000269|PubMed:9653161" FT /id="VAR_012718" FT VARIANT 99 FT /note="L -> P (in SLOS; dbSNP:rs104886041)" FT /evidence="ECO:0000269|PubMed:10677299, FT ECO:0000269|PubMed:9653161" FT /id="VAR_012719" FT VARIANT 107 FT /note="Q -> H (in SLOS; dbSNP:rs104886040)" FT /evidence="ECO:0000269|PubMed:10677299" FT /id="VAR_023149" FT VARIANT 109 FT /note="L -> P (in SLOS; dbSNP:rs121912195)" FT /evidence="ECO:0000269|PubMed:10677299, FT ECO:0000269|PubMed:11427181" FT /id="VAR_023150" FT VARIANT 113 FT /note="S -> C (in SLOS)" FT /evidence="ECO:0000269|PubMed:15954111" FT /id="VAR_023151" FT VARIANT 118 FT /note="C -> R" FT /evidence="ECO:0000269|PubMed:25787250" FT /id="VAR_074180" FT VARIANT 119 FT /note="H -> L (in SLOS; dbSNP:rs28938174)" FT /evidence="ECO:0000269|PubMed:11427181, FT ECO:0000269|PubMed:9683613" FT /id="VAR_012720" FT VARIANT 138 FT /note="G -> V (in SLOS)" FT /evidence="ECO:0000269|PubMed:15954111" FT /id="VAR_023152" FT VARIANT 145 FT /note="I -> L (in SLOS; dbSNP:rs1555146475)" FT /evidence="ECO:0000269|PubMed:15954111" FT /id="VAR_023153" FT VARIANT 147 FT /note="G -> D (in SLOS; dbSNP:rs777425801)" FT /evidence="ECO:0000269|PubMed:10677299" FT /id="VAR_023154" FT VARIANT 154 FT /note="T -> M (in SLOS; dbSNP:rs143312232)" FT /evidence="ECO:0000269|PubMed:10677299, FT ECO:0000269|PubMed:11427181" FT /id="VAR_023155" FT VARIANT 157 FT /note="L -> P (in SLOS; dbSNP:rs753960624)" FT /evidence="ECO:0000269|PubMed:10677299, FT ECO:0000269|PubMed:9653161" FT /id="VAR_012721" FT VARIANT 169 FT /note="S -> L (in SLOS; dbSNP:rs80338855)" FT /evidence="ECO:0000269|PubMed:10677299" FT /id="VAR_023156" FT VARIANT 182 FT /note="W -> C (in SLOS)" FT /evidence="ECO:0000269|PubMed:10677299" FT /id="VAR_023157" FT VARIANT 182 FT /note="W -> L (in SLOS; dbSNP:rs536394774)" FT /evidence="ECO:0000269|PubMed:11427181" FT /id="VAR_023158" FT VARIANT 183 FT /note="C -> Y (in SLOS)" FT /evidence="ECO:0000269|PubMed:11427181" FT /id="VAR_023159" FT VARIANT 198 FT /note="K -> E (in SLOS)" FT /evidence="ECO:0000269|PubMed:11427181" FT /id="VAR_023160" FT VARIANT 235 FT /note="F -> S (in SLOS; dbSNP:rs1555146061)" FT /evidence="ECO:0000269|PubMed:15954111" FT /id="VAR_023161" FT VARIANT 242 FT /note="R -> C (in SLOS; dbSNP:rs80338856)" FT /evidence="ECO:0000269|PubMed:10677299, FT ECO:0000269|PubMed:15954111" FT /id="VAR_023162" FT VARIANT 242 FT /note="R -> H (in SLOS; dbSNP:rs80338857)" FT /evidence="ECO:0000269|PubMed:11427181" FT /id="VAR_023163" FT VARIANT 244 FT /note="G -> R (in SLOS; dbSNP:rs121909764)" FT /evidence="ECO:0000269|PubMed:11427181, FT ECO:0000269|PubMed:9683613" FT /id="VAR_012722" FT VARIANT 247 FT /note="A -> V (in SLOS; dbSNP:rs886041354)" FT /evidence="ECO:0000269|PubMed:10677299, FT ECO:0000269|PubMed:9653161" FT /id="VAR_012723" FT VARIANT 248 FT /note="W -> C (in SLOS; dbSNP:rs104894212)" FT /evidence="ECO:0000269|PubMed:11427181, FT ECO:0000269|PubMed:9683613" FT /id="VAR_012724" FT VARIANT 255 FT /note="F -> L (in SLOS)" FT /evidence="ECO:0000269|PubMed:11427181" FT /id="VAR_023164" FT VARIANT 281 FT /note="V -> M (in SLOS; dbSNP:rs398123607)" FT /evidence="ECO:0000269|PubMed:10677299" FT /id="VAR_023165" FT VARIANT 289 FT /note="T -> I (in SLOS; dbSNP:rs121909765)" FT /evidence="ECO:0000269|PubMed:10677299, FT ECO:0000269|PubMed:10995508" FT /id="VAR_012725" FT VARIANT 297 FT /note="I -> T (in SLOS)" FT /evidence="ECO:0000269|PubMed:15954111" FT /id="VAR_023166" FT VARIANT 311 FT /note="C -> G (in SLOS)" FT /evidence="ECO:0000269|PubMed:10677299" FT /id="VAR_023167" FT VARIANT 311 FT /note="C -> Y (in SLOS)" FT /evidence="ECO:0000269|PubMed:10677299" FT /id="VAR_023168" FT VARIANT 324 FT /note="Y -> H (in SLOS; dbSNP:rs1173707321)" FT /evidence="ECO:0000269|PubMed:10677299" FT /id="VAR_023169" FT VARIANT 326 FT /note="V -> L (in SLOS; dbSNP:rs80338859)" FT /evidence="ECO:0000269|PubMed:10677299, FT ECO:0000269|PubMed:11175299, ECO:0000269|PubMed:9653161" FT /id="VAR_012726" FT VARIANT 344 FT /note="G -> R (in SLOS)" FT /evidence="ECO:0000269|PubMed:15954111" FT /id="VAR_023170" FT VARIANT 352 FT /note="R -> Q (in SLOS; dbSNP:rs121909768)" FT /evidence="ECO:0000269|PubMed:10677299" FT /id="VAR_023171" FT VARIANT 352 FT /note="R -> W (in SLOS; dbSNP:rs80338860)" FT /evidence="ECO:0000269|PubMed:10677299, FT ECO:0000269|PubMed:11175299, ECO:0000269|PubMed:9653161" FT /id="VAR_012727" FT VARIANT 353 FT /note="V -> A (in SLOS)" FT /evidence="ECO:0000269|PubMed:10677299" FT /id="VAR_023172" FT VARIANT 362 FT /note="R -> C (in SLOS; dbSNP:rs371302153)" FT /evidence="ECO:0000269|PubMed:10677299" FT /id="VAR_023173" FT VARIANT 380 FT /note="C -> R (in SLOS; dbSNP:rs373306653)" FT /evidence="ECO:0000269|PubMed:10677299" FT /id="VAR_023174" FT VARIANT 380 FT /note="C -> S (in SLOS)" FT /evidence="ECO:0000269|PubMed:10677299, FT ECO:0000269|PubMed:9653161" FT /id="VAR_012728" FT VARIANT 380 FT /note="C -> Y (in SLOS; dbSNP:rs779709646)" FT /evidence="ECO:0000269|PubMed:10677299" FT /id="VAR_023175" FT VARIANT 397 FT /note="S -> L (in SLOS; dbSNP:rs773134475)" FT /evidence="ECO:0000269|PubMed:10677299" FT /id="VAR_023176" FT VARIANT 404 FT /note="R -> C (in SLOS; dbSNP:rs61757582)" FT /evidence="ECO:0000269|PubMed:10677299, FT ECO:0000269|PubMed:11175299, ECO:0000269|PubMed:15954111, FT ECO:0000269|PubMed:9653161" FT /id="VAR_012729" FT VARIANT 404 FT /note="R -> S (in SLOS; dbSNP:rs61757582)" FT /evidence="ECO:0000269|PubMed:10677299" FT /id="VAR_023177" FT VARIANT 405 FT /note="H -> Y (in SLOS)" FT /evidence="ECO:0000269|PubMed:15954111" FT /id="VAR_023178" FT VARIANT 408 FT /note="Y -> H (in SLOS; dbSNP:rs1046560765)" FT /evidence="ECO:0000269|PubMed:10677299, FT ECO:0000269|PubMed:15954111" FT /id="VAR_023179" FT VARIANT 410 FT /note="G -> R (in SLOS; dbSNP:rs80338862)" FT /evidence="ECO:0000269|PubMed:10677299" FT /id="VAR_023180" FT VARIANT 410 FT /note="G -> S (in SLOS; dbSNP:rs80338862)" FT /evidence="ECO:0000269|PubMed:10677299, FT ECO:0000269|PubMed:9653161" FT /id="VAR_012730" FT VARIANT 425 FT /note="G -> S (in dbSNP:rs760242)" FT /id="VAR_052154" FT VARIANT 426 FT /note="H -> P (in SLOS; dbSNP:rs1354718634)" FT /evidence="ECO:0000269|PubMed:15954111" FT /id="VAR_023181" FT VARIANT 443 FT /note="R -> C (in SLOS; dbSNP:rs535561852)" FT /evidence="ECO:0000269|PubMed:10677299" FT /id="VAR_023182" FT VARIANT 446 FT /note="R -> Q (in SLOS; dbSNP:rs751604696)" FT /evidence="ECO:0000269|PubMed:10677299" FT /id="VAR_023183" FT VARIANT 448 FT /note="E -> K (in SLOS; mild; dbSNP:rs80338864)" FT /evidence="ECO:0000269|PubMed:10677299, FT ECO:0000269|PubMed:12949967" FT /id="VAR_016975" FT VARIANT 448 FT /note="E -> Q (in SLOS; dbSNP:rs80338864)" FT /evidence="ECO:0000269|PubMed:10677299" FT /id="VAR_023184" FT VARIANT 450 FT /note="R -> L (in SLOS; dbSNP:rs542266962)" FT /evidence="ECO:0000269|PubMed:10677299" FT /id="VAR_023185" FT CONFLICT 14 FT /note="S -> A (in Ref. 6; AAC18345)" FT /evidence="ECO:0000305" SQ SEQUENCE 475 AA; 54489 MW; 7D726443834C4EEB CRC64; MAAKSQPNIP KAKSLDGVTN DRTASQGQWG RAWEVDWFSL ASVIFLLLFA PFIVYYFIMA CDQYSCALTG PVVDIVTGHA RLSDIWAKTP PITRKAAQLY TLWVTFQVLL YTSLPDFCHK FLPGYVGGIQ EGAVTPAGVV NKYQINGLQA WLLTHLLWFA NAHLLSWFSP TIIFDNWIPL LWCANILGYA VSTFAMVKGY FFPTSARDCK FTGNFFYNYM MGIEFNPRIG KWFDFKLFFN GRPGIVAWTL INLSFAAKQR ELHSHVTNAM VLVNVLQAIY VIDFFWNETW YLKTIDICHD HFGWYLGWGD CVWLPYLYTL QGLYLVYHPV QLSTPHAVGV LLLGLVGYYI FRVANHQKDL FRRTDGRCLI WGRKPKVIEC SYTSADGQRH HSKLLVSGFW GVARHFNYVG DLMGSLAYCL ACGGGHLLPY FYIIYMAILL THRCLRDEHR CASKYGRDWE RYTAAVPYRL LPGIF //