3BHS7_HUMAN
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 03-AUG-2022, entry version 170.
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. {ECO:0000250|UniProtKB:Q9EQC1,
CC ECO:0000269|PubMed:11067870}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 3beta-hydroxy-Delta(5)-steroid + NAD(+) = a 3-oxo-Delta(5)-
CC steroid + H(+) + NADH; Xref=Rhea:RHEA:24076, ChEBI:CHEBI:1722,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:47907, ChEBI:CHEBI:57540,
CC ChEBI:CHEBI:57945;
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}.
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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; Q9H2F3; -.
DR PeptideAtlas; Q9H2F3; -.
DR PRIDE; Q9H2F3; -.
DR ProteomicsDB; 80538; -. [Q9H2F3-1]
DR ProteomicsDB; 80539; -. [Q9H2F3-2]
DR Antibodypedia; 27526; 198 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 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; 930591at2759; -.
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; 9 hits in 1063 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 111 other tissues.
DR ExpressionAtlas; Q9H2F3; baseline and differential.
DR Genevisible; Q9H2F3; HS.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; TAS:Reactome.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
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 InterPro; IPR002225; 3Beta_OHSteriod_DH/Estase.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR Pfam; PF01073; 3Beta_HSD; 1.
DR SUPFAM; SSF51735; SSF51735; 1.
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
