DHCR7_HUMAN
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 03-AUG-2022, entry version 200.
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: 7-dehydrocholesterol reductase of the cholesterol
CC biosynthetic pathway reducing the C7-C8 double bond of cholesta-5,7-
CC dien-3beta-ol (7-dehydrocholesterol/7-DHC) and cholesta-5,7,24-trien-
CC 3beta-ol, two intermediates in that pathway.
CC {ECO:0000269|PubMed:25637936, ECO:0000269|PubMed:9465114,
CC ECO:0000269|PubMed:9634533}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=cholesterol + NADP(+) = 7-dehydrocholesterol + H(+) + NADPH;
CC 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=7-dehydrodesmosterol + H(+) + NADPH = desmosterol + NADP(+);
CC Xref=Rhea:RHEA:46740, ChEBI:CHEBI:15378, ChEBI:CHEBI:17737,
CC ChEBI:CHEBI:27910, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349;
CC 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 intellectual disability.
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 variants
CC affecting the gene represented in this entry.
CC -!- SIMILARITY: Belongs to the ERG4/ERG24 family. {ECO:0000305}.
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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 AlphaFoldDB; Q9UBM7; -.
DR SMR; Q9UBM7; -.
DR BioGRID; 108063; 162.
DR IntAct; Q9UBM7; 42.
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 GlyGen; Q9UBM7; 1 site, 1 O-linked glycan (1 site).
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; 176 antibodies from 25 providers.
DR DNASU; 1717; -.
DR Ensembl; ENST00000355527.8; ENSP00000347717.4; ENSG00000172893.18.
DR Ensembl; ENST00000407721.6; ENSP00000384739.2; ENSG00000172893.18.
DR Ensembl; ENST00000525346.6; ENSP00000435707.3; ENSG00000172893.18.
DR Ensembl; ENST00000526780.6; ENSP00000435668.2; ENSG00000172893.18.
DR GeneID; 1717; -.
DR KEGG; hsa:1717; -.
DR MANE-Select; ENST00000355527.8; ENSP00000347717.4; NM_001360.3; NP_001351.2.
DR UCSC; uc001oqk.4; human.
DR CTD; 1717; -.
DR DisGeNET; 1717; -.
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 VEuPathDB; HostDB:ENSG00000172893; -.
DR eggNOG; KOG1435; Eukaryota.
DR GeneTree; ENSGT00390000000417; -.
DR HOGENOM; CLU_015631_0_0_1; -.
DR InParanoid; Q9UBM7; -.
DR OMA; TSGFWGW; -.
DR OrthoDB; 532774at2759; -.
DR PhylomeDB; Q9UBM7; -.
DR TreeFam; TF101180; -.
DR BioCyc; MetaCyc:HS10588-MON; -.
DR BRENDA; 1.3.1.21; 2681.
DR PathwayCommons; Q9UBM7; -.
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 SignaLink; Q9UBM7; -.
DR SIGNOR; Q9UBM7; -.
DR UniPathway; UPA00063; -.
DR BioGRID-ORCS; 1717; 13 hits in 1086 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 172 other tissues.
DR ExpressionAtlas; Q9UBM7; baseline and differential.
DR Genevisible; Q9UBM7; HS.
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:0016132; P:brassinosteroid biosynthetic process; IBA:GO_Central.
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:0045540; P:regulation of cholesterol biosynthetic process; IEA:Ensembl.
DR GO; GO:0016126; P:sterol biosynthetic process; IBA:GO_Central.
DR InterPro; IPR001171; ERG24_DHCR-like.
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 variant;
KW Endoplasmic reticulum; Lipid biosynthesis; Lipid metabolism; Membrane;
KW NADP; Oxidoreductase; Phosphoprotein; 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 REGION 1..21
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 358
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:G4SW86"
FT BINDING 362
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:G4SW86"
FT BINDING 395
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:G4SW86"
FT BINDING 400
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:G4SW86"
FT BINDING 407..408
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:G4SW86"
FT BINDING 447
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:G4SW86"
FT BINDING 451..455
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:G4SW86"
FT BINDING 462
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:G4SW86"
FT MOD_RES 14
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18691976,
FT ECO:0007744|PubMed:19369195, ECO:0007744|PubMed:19690332,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163, ECO:0007744|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
