ID 3BHS7_HUMAN Reviewed; 369 AA. AC Q9H2F3; Q96M28; Q9BSN9; DT 24-MAY-2004, integrated into UniProtKB/Swiss-Prot. DT 24-MAY-2004, sequence version 2. DT 27-MAR-2024, entry version 178. DE RecName: Full=3 beta-hydroxysteroid dehydrogenase type 7 {ECO:0000305}; DE AltName: Full=3 beta-hydroxysteroid dehydrogenase type VII; DE Short=3-beta-HSD VII; DE AltName: Full=3-beta-hydroxy-Delta(5)-C27 steroid oxidoreductase; DE Short=C(27) 3-beta-HSD; DE EC=1.1.1.-; DE AltName: Full=Cholest-5-ene-3-beta,7-alpha-diol 3-beta-dehydrogenase; DE EC=1.1.1.181 {ECO:0000269|PubMed:11067870}; GN Name=HSD3B7 {ECO:0000312|HGNC:HGNC:18324}; 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] (ISOFORM 1), FUNCTION, INVOLVEMENT IN CBAS1, RP VARIANT ALA-250, AND CATALYTIC ACTIVITY. RX PubMed=11067870; DOI=10.1172/jci10902; RA Schwarz M., Wright A.C., Davis D.L., Nazer H., Bjorkhem I., Russell D.W.; RT "The bile acid synthetic gene 3beta-hydroxy-delta(5)-C(27)-steroid RT oxidoreductase is mutated in progressive intrahepatic cholestasis."; RL J. Clin. Invest. 106:1175-1184(2000). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2). RC TISSUE=Stomach, and 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 [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=15616553; DOI=10.1038/nature03187; RA Martin J., Han C., Gordon L.A., Terry A., Prabhakar S., She X., Xie G., RA Hellsten U., Chan Y.M., Altherr M., Couronne O., Aerts A., Bajorek E., RA Black S., Blumer H., Branscomb E., Brown N.C., Bruno W.J., Buckingham J.M., RA Callen D.F., Campbell C.S., Campbell M.L., Campbell E.W., Caoile C., RA Challacombe J.F., Chasteen L.A., Chertkov O., Chi H.C., Christensen M., RA Clark L.M., Cohn J.D., Denys M., Detter J.C., Dickson M., RA Dimitrijevic-Bussod M., Escobar J., Fawcett J.J., Flowers D., Fotopulos D., RA Glavina T., Gomez M., Gonzales E., Goodstein D., Goodwin L.A., Grady D.L., RA Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Hildebrand C.E., RA Huang W., Israni S., Jett J., Jewett P.B., Kadner K., Kimball H., RA Kobayashi A., Krawczyk M.-C., Leyba T., Longmire J.L., Lopez F., Lou Y., RA Lowry S., Ludeman T., Manohar C.F., Mark G.A., McMurray K.L., Meincke L.J., RA Morgan J., Moyzis R.K., Mundt M.O., Munk A.C., Nandkeshwar R.D., RA Pitluck S., Pollard M., Predki P., Parson-Quintana B., Ramirez L., Rash S., RA Retterer J., Ricke D.O., Robinson D.L., Rodriguez A., Salamov A., RA Saunders E.H., Scott D., Shough T., Stallings R.L., Stalvey M., RA Sutherland R.D., Tapia R., Tesmer J.G., Thayer N., Thompson L.S., Tice H., RA Torney D.C., Tran-Gyamfi M., Tsai M., Ulanovsky L.E., Ustaszewska A., RA Vo N., White P.S., Williams A.L., Wills P.L., Wu J.-R., Wu K., Yang J., RA DeJong P., Bruce D., Doggett N.A., Deaven L., Schmutz J., Grimwood J., RA Richardson P., Rokhsar D.S., Eichler E.E., Gilna P., Lucas S.M., RA Myers R.M., Rubin E.M., Pennacchio L.A.; RT "The sequence and analysis of duplication-rich human chromosome 16."; RL Nature 432:988-994(2004). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Mural R.J., Istrail S., Sutton G., Florea L., Halpern A.L., Mobarry C.M., RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., RA Hunkapiller M.W., Myers E.W., Venter J.C.; RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases. RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC TISSUE=Uterus; 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 VARIANTS CBAS1 SER-19 AND LYS-147, AND CHARACTERIZATION OF VARIANT CBAS1 RP LYS-147. RX PubMed=12679481; DOI=10.1210/jc.2002-021580; RA Cheng J.B., Jacquemin E., Gerhardt M., Nazer H., Cresteil D., Heubi J.E., RA Setchell K.D., Russell D.W.; RT "Molecular genetics of 3beta-hydroxy-Delta5-C27-steroid oxidoreductase RT deficiency in 16 patients with loss of bile acid synthesis and liver RT disease."; RL J. Clin. Endocrinol. Metab. 88:1833-1841(2003). CC -!- FUNCTION: The 3-beta-HSD enzymatic system plays a crucial role in the CC biosynthesis of all classes of hormonal steroids. HSD VII is active CC against four 7-alpha-hydroxylated sterols. Does not metabolize several CC different C(19/21) steroids as substrates. Involved in bile acid CC synthesis (PubMed:11067870). Plays a key role in cell positioning and CC movement in lymphoid tissues by mediating degradation of 7-alpha,25- CC dihydroxycholesterol (7-alpha,25-OHC): 7-alpha,25-OHC acts as a ligand CC for the G protein-coupled receptor GPR183/EBI2, a chemotactic receptor CC for a number of lymphoid cells (By similarity). CC {ECO:0000250|UniProtKB:Q9EQC1, ECO:0000269|PubMed:11067870}. CC -!- CATALYTIC ACTIVITY: CC Reaction=7alpha-hydroxycholesterol + NAD(+) = 7alpha-hydroxycholest-4- CC en-3-one + H(+) + NADH; Xref=Rhea:RHEA:11896, ChEBI:CHEBI:15378, CC ChEBI:CHEBI:17500, ChEBI:CHEBI:17899, ChEBI:CHEBI:57540, CC ChEBI:CHEBI:57945; EC=1.1.1.181; CC Evidence={ECO:0000269|PubMed:11067870}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:11897; CC Evidence={ECO:0000305|PubMed:11067870}; CC -!- CATALYTIC ACTIVITY: CC Reaction=7alpha,25-dihydroxycholesterol + NAD(+) = 7alpha,25-dihydroxy- CC 4-cholesten-3-one + H(+) + NADH; Xref=Rhea:RHEA:47156, CC ChEBI:CHEBI:15378, ChEBI:CHEBI:37623, ChEBI:CHEBI:57540, CC ChEBI:CHEBI:57945, ChEBI:CHEBI:81013; CC Evidence={ECO:0000269|PubMed:11067870}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:47157; CC Evidence={ECO:0000305|PubMed:11067870}; CC -!- CATALYTIC ACTIVITY: CC Reaction=(25R)-cholest-5-en-3beta,7alpha,26-triol + NAD(+) = (25R)- CC 7alpha,26-dihydroxycholest-4-en-3-one + H(+) + NADH; CC Xref=Rhea:RHEA:47180, ChEBI:CHEBI:15378, ChEBI:CHEBI:57540, CC ChEBI:CHEBI:57945, ChEBI:CHEBI:76592, ChEBI:CHEBI:87476; CC Evidence={ECO:0000269|PubMed:11067870}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:47181; CC Evidence={ECO:0000305|PubMed:11067870}; CC -!- CATALYTIC ACTIVITY: CC Reaction=(24S)-7alpha-dihydroxycholesterol + NAD(+) = (24S)-7alpha,24- CC dihydroxycholest-4-en-3-one + H(+) + NADH; Xref=Rhea:RHEA:47200, CC ChEBI:CHEBI:15378, ChEBI:CHEBI:37640, ChEBI:CHEBI:57540, CC ChEBI:CHEBI:57945, ChEBI:CHEBI:63838; CC Evidence={ECO:0000269|PubMed:11067870}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:47201; CC Evidence={ECO:0000305|PubMed:11067870}; CC -!- PATHWAY: Lipid metabolism; steroid biosynthesis. CC {ECO:0000269|PubMed:11067870}. CC -!- INTERACTION: CC Q9H2F3; Q6UY14-3: ADAMTSL4; NbExp=3; IntAct=EBI-3918847, EBI-10173507; CC Q9H2F3; O95994: AGR2; NbExp=3; IntAct=EBI-3918847, EBI-712648; CC Q9H2F3; Q9NYG5-2: ANAPC11; NbExp=3; IntAct=EBI-3918847, EBI-12224467; CC Q9H2F3; Q92624: APPBP2; NbExp=3; IntAct=EBI-3918847, EBI-743771; CC Q9H2F3; Q03989: ARID5A; NbExp=3; IntAct=EBI-3918847, EBI-948603; CC Q9H2F3; Q8WXK4-2: ASB12; NbExp=3; IntAct=EBI-3918847, EBI-18394052; CC Q9H2F3; Q8WVV5: BTN2A2; NbExp=3; IntAct=EBI-3918847, EBI-8648738; CC Q9H2F3; Q6P5X5: C22orf39; NbExp=3; IntAct=EBI-3918847, EBI-7317823; CC Q9H2F3; P21964: COMT; NbExp=3; IntAct=EBI-3918847, EBI-372265; CC Q9H2F3; Q02930-3: CREB5; NbExp=3; IntAct=EBI-3918847, EBI-10192698; CC Q9H2F3; A8MQ03: CYSRT1; NbExp=3; IntAct=EBI-3918847, EBI-3867333; CC Q9H2F3; Q12805: EFEMP1; NbExp=3; IntAct=EBI-3918847, EBI-536772; CC Q9H2F3; O95967: EFEMP2; NbExp=3; IntAct=EBI-3918847, EBI-743414; CC Q9H2F3; Q9UHF1: EGFL7; NbExp=3; IntAct=EBI-3918847, EBI-949532; CC Q9H2F3; Q9GZR5: ELOVL4; NbExp=3; IntAct=EBI-3918847, EBI-18535450; CC Q9H2F3; Q92979: EMG1; NbExp=3; IntAct=EBI-3918847, EBI-718638; CC Q9H2F3; P98095: FBLN2; NbExp=3; IntAct=EBI-3918847, EBI-947973; CC Q9H2F3; O76003: GLRX3; NbExp=3; IntAct=EBI-3918847, EBI-374781; CC Q9H2F3; P49639: HOXA1; NbExp=3; IntAct=EBI-3918847, EBI-740785; CC Q9H2F3; Q7Z5P4: HSD17B13; NbExp=3; IntAct=EBI-3918847, EBI-18053395; CC Q9H2F3; O00629: KPNA4; NbExp=3; IntAct=EBI-3918847, EBI-396343; CC Q9H2F3; Q5T749: KPRP; NbExp=3; IntAct=EBI-3918847, EBI-10981970; CC Q9H2F3; Q15323: KRT31; NbExp=3; IntAct=EBI-3918847, EBI-948001; CC Q9H2F3; Q6A162: KRT40; NbExp=3; IntAct=EBI-3918847, EBI-10171697; CC Q9H2F3; O43790: KRT86; NbExp=3; IntAct=EBI-3918847, EBI-9996498; CC Q9H2F3; Q8IUG1: KRTAP1-3; NbExp=3; IntAct=EBI-3918847, EBI-11749135; CC Q9H2F3; P60409: KRTAP10-7; NbExp=3; IntAct=EBI-3918847, EBI-10172290; CC Q9H2F3; P60410: KRTAP10-8; NbExp=8; IntAct=EBI-3918847, EBI-10171774; CC Q9H2F3; P60411: KRTAP10-9; NbExp=3; IntAct=EBI-3918847, EBI-10172052; CC Q9H2F3; Q3SY46: KRTAP13-3; NbExp=3; IntAct=EBI-3918847, EBI-10241252; CC Q9H2F3; Q3LHN2: KRTAP19-2; NbExp=3; IntAct=EBI-3918847, EBI-12196745; CC Q9H2F3; Q9BYR5: KRTAP4-2; NbExp=3; IntAct=EBI-3918847, EBI-10172511; CC Q9H2F3; P26371: KRTAP5-9; NbExp=3; IntAct=EBI-3918847, EBI-3958099; CC Q9H2F3; Q5TA78: LCE4A; NbExp=3; IntAct=EBI-3918847, EBI-10246358; CC Q9H2F3; Q96FE5: LINGO1; NbExp=3; IntAct=EBI-3918847, EBI-719955; CC Q9H2F3; A8MW99: MEI4; NbExp=3; IntAct=EBI-3918847, EBI-19944212; CC Q9H2F3; Q6FHY5: MEOX2; NbExp=3; IntAct=EBI-3918847, EBI-16439278; CC Q9H2F3; Q7Z3S9: NOTCH2NLA; NbExp=3; IntAct=EBI-3918847, EBI-945833; CC Q9H2F3; Q92570: NR4A3; NbExp=3; IntAct=EBI-3918847, EBI-13644623; CC Q9H2F3; P32243-2: OTX2; NbExp=3; IntAct=EBI-3918847, EBI-9087860; CC Q9H2F3; P10745: RBP3; NbExp=3; IntAct=EBI-3918847, EBI-12806054; CC Q9H2F3; Q9H6H4: REEP4; NbExp=3; IntAct=EBI-3918847, EBI-7545592; CC Q9H2F3; Q9UGC6: RGS17; NbExp=3; IntAct=EBI-3918847, EBI-3918154; CC Q9H2F3; Q96GQ5: RUSF1; NbExp=3; IntAct=EBI-3918847, EBI-8636004; CC Q9H2F3; O43597: SPRY2; NbExp=3; IntAct=EBI-3918847, EBI-742487; CC Q9H2F3; Q9Y320: TMX2; NbExp=3; IntAct=EBI-3918847, EBI-6447886; CC Q9H2F3; Q8IWZ5: TRIM42; NbExp=5; IntAct=EBI-3918847, EBI-5235829; CC Q9H2F3; B2RXF5: ZBTB42; NbExp=3; IntAct=EBI-3918847, EBI-12287587; CC Q9H2F3; Q8N720: ZNF655; NbExp=3; IntAct=EBI-3918847, EBI-625509; CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Multi-pass CC membrane protein. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1; CC IsoId=Q9H2F3-1; Sequence=Displayed; CC Name=2; CC IsoId=Q9H2F3-2; Sequence=VSP_042658; CC -!- DISEASE: Congenital bile acid synthesis defect 1 (CBAS1) [MIM:607765]: CC A primary defect in bile synthesis leading to progressive liver CC disease. Clinical features include neonatal jaundice, severe CC intrahepatic cholestasis, cirrhosis. {ECO:0000269|PubMed:11067870, CC ECO:0000269|PubMed:12679481}. Note=The disease is caused by variants CC affecting the gene represented in this entry. CC -!- SIMILARITY: Belongs to the 3-beta-HSD 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; AF277719; AAG37824.1; -; mRNA. DR EMBL; AK057436; BAB71486.1; -; mRNA. DR EMBL; AK290950; BAF83639.1; -; mRNA. DR EMBL; AK292068; BAF84757.1; -; mRNA. DR EMBL; AC135048; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CH471192; EAW52183.1; -; Genomic_DNA. DR EMBL; BC004929; AAH04929.1; -; mRNA. DR CCDS; CCDS10698.1; -. [Q9H2F3-1] DR CCDS; CCDS45466.1; -. [Q9H2F3-2] DR RefSeq; NP_001136249.1; NM_001142777.1. [Q9H2F3-2] DR RefSeq; NP_001136250.1; NM_001142778.1. [Q9H2F3-2] DR RefSeq; NP_079469.2; NM_025193.3. [Q9H2F3-1] DR RefSeq; XP_005255658.2; XM_005255601.3. [Q9H2F3-1] DR RefSeq; XP_011544262.1; XM_011545960.2. [Q9H2F3-1] DR RefSeq; XP_011544263.1; XM_011545961.1. [Q9H2F3-1] DR RefSeq; XP_011544264.1; XM_011545962.2. [Q9H2F3-2] DR RefSeq; XP_016879221.1; XM_017023732.1. [Q9H2F3-2] DR AlphaFoldDB; Q9H2F3; -. DR BioGRID; 123208; 386. DR IntAct; Q9H2F3; 53. DR STRING; 9606.ENSP00000297679; -. DR SwissLipids; SLP:000001321; -. DR iPTMnet; Q9H2F3; -. DR PhosphoSitePlus; Q9H2F3; -. DR BioMuta; HSD3B7; -. DR DMDM; 47605550; -. DR EPD; Q9H2F3; -. DR jPOST; Q9H2F3; -. DR MassIVE; Q9H2F3; -. DR MaxQB; Q9H2F3; -. DR PaxDb; 9606-ENSP00000297679; -. DR PeptideAtlas; Q9H2F3; -. DR ProteomicsDB; 80538; -. [Q9H2F3-1] DR ProteomicsDB; 80539; -. [Q9H2F3-2] DR Pumba; Q9H2F3; -. DR Antibodypedia; 27526; 225 antibodies from 27 providers. DR DNASU; 80270; -. DR Ensembl; ENST00000262520.10; ENSP00000262520.6; ENSG00000099377.14. [Q9H2F3-2] DR Ensembl; ENST00000297679.10; ENSP00000297679.5; ENSG00000099377.14. [Q9H2F3-1] DR GeneID; 80270; -. DR KEGG; hsa:80270; -. DR MANE-Select; ENST00000297679.10; ENSP00000297679.5; NM_025193.4; NP_079469.2. DR UCSC; uc002eaf.3; human. [Q9H2F3-1] DR AGR; HGNC:18324; -. DR CTD; 80270; -. DR DisGeNET; 80270; -. DR GeneCards; HSD3B7; -. DR HGNC; HGNC:18324; HSD3B7. DR HPA; ENSG00000099377; Tissue enriched (liver). DR MalaCards; HSD3B7; -. DR MIM; 607764; gene. DR MIM; 607765; phenotype. DR neXtProt; NX_Q9H2F3; -. DR OpenTargets; ENSG00000099377; -. DR Orphanet; 79301; Congenital bile acid synthesis defect type 1. DR PharmGKB; PA134940289; -. DR VEuPathDB; HostDB:ENSG00000099377; -. DR eggNOG; KOG1430; Eukaryota. DR GeneTree; ENSGT00940000160236; -. DR HOGENOM; CLU_007383_6_3_1; -. DR InParanoid; Q9H2F3; -. DR OMA; GDHFKRG; -. DR OrthoDB; 3675908at2759; -. DR PhylomeDB; Q9H2F3; -. DR TreeFam; TF354279; -. DR PathwayCommons; Q9H2F3; -. DR Reactome; R-HSA-193368; Synthesis of bile acids and bile salts via 7alpha-hydroxycholesterol. DR Reactome; R-HSA-193775; Synthesis of bile acids and bile salts via 24-hydroxycholesterol. DR Reactome; R-HSA-193807; Synthesis of bile acids and bile salts via 27-hydroxycholesterol. DR SignaLink; Q9H2F3; -. DR UniPathway; UPA00062; -. DR BioGRID-ORCS; 80270; 10 hits in 1143 CRISPR screens. DR ChiTaRS; HSD3B7; human. DR GenomeRNAi; 80270; -. DR Pharos; Q9H2F3; Tbio. DR PRO; PR:Q9H2F3; -. DR Proteomes; UP000005640; Chromosome 16. DR RNAct; Q9H2F3; Protein. DR Bgee; ENSG00000099377; Expressed in right lobe of liver and 112 other cell types or tissues. DR ExpressionAtlas; Q9H2F3; baseline and differential. DR GO; GO:0005789; C:endoplasmic reticulum membrane; TAS:Reactome. DR GO; GO:0005811; C:lipid droplet; IDA:HPA. DR GO; GO:0003854; F:3-beta-hydroxy-delta5-steroid dehydrogenase activity; TAS:Reactome. DR GO; GO:0047016; F:cholest-5-ene-3-beta,7-alpha-diol 3-beta-dehydrogenase activity; ISS:UniProtKB. DR GO; GO:0016616; F:oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor; IBA:GO_Central. DR GO; GO:0035754; P:B cell chemotaxis; ISS:UniProtKB. DR GO; GO:0006699; P:bile acid biosynthetic process; TAS:UniProtKB. DR CDD; cd09811; 3b-HSD_HSDB1_like_SDR_e; 1. DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1. DR InterPro; IPR002225; 3Beta_OHSteriod_DH/Estase. DR InterPro; IPR036291; NAD(P)-bd_dom_sf. DR PANTHER; PTHR10366:SF835; 3 BETA-HYDROXYSTEROID DEHYDROGENASE TYPE 7; 1. DR PANTHER; PTHR10366; NAD DEPENDENT EPIMERASE/DEHYDRATASE; 1. DR Pfam; PF01073; 3Beta_HSD; 1. DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1. DR Genevisible; Q9H2F3; HS. PE 1: Evidence at protein level; KW Alternative splicing; Disease variant; Endoplasmic reticulum; KW Intrahepatic cholestasis; Lipid metabolism; Membrane; NAD; Oxidoreductase; KW Reference proteome; Steroidogenesis; Transmembrane; Transmembrane helix. FT CHAIN 1..369 FT /note="3 beta-hydroxysteroid dehydrogenase type 7" FT /id="PRO_0000087791" FT TRANSMEM 289..309 FT /note="Helical" FT /evidence="ECO:0000255" FT TRANSMEM 311..331 FT /note="Helical" FT /evidence="ECO:0000255" FT ACT_SITE 159 FT /note="Proton acceptor" FT /evidence="ECO:0000250" FT BINDING 163 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000250" FT VAR_SEQ 178..369 FT /note="VRGGLPLVTCALRPTGIYGEGHQIMRDFYRQGLRLGGWLFRAIPASVEHGRV FT YVGNVAWMHVLAARELEQRATLMGGQVYFCYDGSPYRSYEDFNMEFLGPCGLRLVGARP FT LLPYWLLVFLAALNALLQWLLRPLVLYAPLLNPYTLAVANTTFTVSTDKAQRHFGYEPL FT FSWEDSRTRTILWVQAATGSAQ -> AMLPGCTCWQPGSWSSGQP (in isoform FT 2)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_042658" FT VARIANT 19 FT /note="G -> S (in CBAS1)" FT /evidence="ECO:0000269|PubMed:12679481" FT /id="VAR_054775" FT VARIANT 147 FT /note="E -> K (in CBAS1; loss of activity; FT dbSNP:rs104894518)" FT /evidence="ECO:0000269|PubMed:12679481" FT /id="VAR_054776" FT VARIANT 250 FT /note="T -> A (in dbSNP:rs9938550)" FT /evidence="ECO:0000269|PubMed:11067870" FT /id="VAR_031040" FT VARIANT 347 FT /note="L -> P (in dbSNP:rs34212827)" FT /id="VAR_048100" FT CONFLICT 265 FT /note="Y -> H (in Ref. 1; AAG37824)" FT /evidence="ECO:0000305" FT CONFLICT 329 FT /note="T -> A (in Ref. 1; AAG37824)" FT /evidence="ECO:0000305" SQ SEQUENCE 369 AA; 41016 MW; 7254A5DAAFAC23E7 CRC64; MADSAQAQKL VYLVTGGCGF LGEHVVRMLL QREPRLGELR VFDQHLGPWL EELKTGPVRV TAIQGDVTQA HEVAAAVAGA HVVIHTAGLV DVFGRASPKT IHEVNVQGTR NVIEACVQTG TRFLVYTSSM EVVGPNTKGH PFYRGNEDTP YEAVHRHPYP CSKALAEWLV LEANGRKVRG GLPLVTCALR PTGIYGEGHQ IMRDFYRQGL RLGGWLFRAI PASVEHGRVY VGNVAWMHVL AARELEQRAT LMGGQVYFCY DGSPYRSYED FNMEFLGPCG LRLVGARPLL PYWLLVFLAA LNALLQWLLR PLVLYAPLLN PYTLAVANTT FTVSTDKAQR HFGYEPLFSW EDSRTRTILW VQAATGSAQ //