3BHS1_HUMAN
ID 3BHS1_HUMAN Reviewed; 373 AA.
AC P14060; A8K691; Q14545; Q8IV65;
DT 01-JAN-1990, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 210.
DE RecName: Full=3 beta-hydroxysteroid dehydrogenase/Delta 5-->4-isomerase type 1;
DE AltName: Full=3 beta-hydroxysteroid dehydrogenase/Delta 5-->4-isomerase type I {ECO:0000303|PubMed:1401999};
DE Short=3-beta-HSD I;
DE AltName: Full=3-beta-hydroxy-5-ene steroid dehydrogenase {ECO:0000303|PubMed:1920284};
DE AltName: Full=3-beta-hydroxy-Delta(5)-steroid dehydrogenase {ECO:0000305|PubMed:1401999};
DE EC=1.1.1.145 {ECO:0000269|PubMed:1401999};
DE AltName: Full=3-beta-hydroxysteroid 3-dehydrogenase {ECO:0000305|PubMed:1401999};
DE EC=1.1.1.270 {ECO:0000269|PubMed:1401999};
DE AltName: Full=Delta-5-3-ketosteroid isomerase;
DE AltName: Full=Dihydrotestosterone oxidoreductase;
DE EC=1.1.1.210 {ECO:0000269|PubMed:1401999};
DE AltName: Full=Steroid Delta-isomerase {ECO:0000305|PubMed:1401999};
DE EC=5.3.3.1 {ECO:0000269|PubMed:1401999};
DE AltName: Full=Trophoblast antigen FDO161G {ECO:0000303|PubMed:1920284};
GN Name=HSD3B1 {ECO:0000312|HGNC:HGNC:5217}; Synonyms=3BH, HSDB3A;
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 PROTEIN SEQUENCE OF 2-30.
RX PubMed=2779585; DOI=10.1210/mend-3-8-1310;
RA Luu-The V., Lachance Y., Labrie F., Leblanc G., Thomas J.L.,
RA Strickler R.C., Labrie C.;
RT "Full length cDNA structure and deduced amino acid sequence of human 3
RT beta-hydroxy-5-ene steroid dehydrogenase.";
RL Mol. Endocrinol. 3:1310-1312(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], AND FUNCTION.
RC TISSUE=Placenta;
RX PubMed=2139411; DOI=10.1210/endo-126-5-2493;
RA Lorence M.C., Murry B.A., Trant J.M., Mason J.I.;
RT "Human 3 beta-hydroxysteroid dehydrogenase/delta 5-->4-isomerase from
RT placenta: expression in nonsteroidogenic cells of a protein that catalyzes
RT the dehydrogenation/isomerization of C21 and C19 steroids.";
RL Endocrinology 126:2493-2498(1990).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2082186; DOI=10.1210/mend-4-12-1850;
RA Lorence M.C., Corbin C.J., Kamimura N., Mahendroo M.S., Mason J.I.;
RT "Structural analysis of the gene encoding human 3 beta-hydroxysteroid
RT dehydrogenase/delta 5-->4-isomerase.";
RL Mol. Endocrinol. 4:1850-1855(1990).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANT ASN-367.
RX PubMed=2243100; DOI=10.1016/s0021-9258(17)30528-8;
RA Lachance Y., Luu-The V., Labrie C., Simard J., Dumont M., Launoit Y.D.,
RA Guerin S., Leblanc G., Labrie F.;
RT "Characterization of human 3 beta-hydroxysteroid dehydrogenase/delta 5-
RT delta 4-isomerase gene and its expression in mammalian cells.";
RL J. Biol. Chem. 265:20469-20475(1990).
RN [5]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Placenta;
RX PubMed=1920284; DOI=10.1530/jrf.0.0930149;
RA Nickson D.A., McBride M.W., Zeinali S., Hawes C.S., Petropoulos A.,
RA Mueller U.W., Sutcliffe R.G.;
RT "Molecular cloning and expression of human trophoblast antigen FDO161G and
RT its identification as 3 beta-hydroxy-5-ene steroid dehydrogenase.";
RL J. Reprod. Fertil. 93:149-156(1991).
RN [6]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES,
RP SUBSTRATE SPECIFICITY, TISSUE SPECIFICITY, CATALYTIC ACTIVITY, AND PATHWAY.
RX PubMed=1401999; DOI=10.1111/1523-1747.ep12616131;
RA Dumont M., Van L.T., Dupont E., Pelletier G., Labrie F.;
RT "Characterization, expression, and immunohistochemical localization of 3
RT beta-hydroxysteroid dehydrogenase/delta 5-delta 4 isomerase in human
RT skin.";
RL J. Invest. Dermatol. 99:415-421(1992).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Placenta;
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 [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT ASN-367.
RC TISSUE=Skin;
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 [9]
RP VARIANTS VAL-79 AND LEU-286.
RX PubMed=10391209; DOI=10.1038/10290;
RA Cargill M., Altshuler D., Ireland J., Sklar P., Ardlie K., Patil N.,
RA Shaw N., Lane C.R., Lim E.P., Kalyanaraman N., Nemesh J., Ziaugra L.,
RA Friedland L., Rolfe A., Warrington J., Lipshutz R., Daley G.Q.,
RA Lander E.S.;
RT "Characterization of single-nucleotide polymorphisms in coding regions of
RT human genes.";
RL Nat. Genet. 22:231-238(1999).
RN [10]
RP ERRATUM OF PUBMED:10391209.
RA Cargill M., Altshuler D., Ireland J., Sklar P., Ardlie K., Patil N.,
RA Shaw N., Lane C.R., Lim E.P., Kalyanaraman N., Nemesh J., Ziaugra L.,
RA Friedland L., Rolfe A., Warrington J., Lipshutz R., Daley G.Q.,
RA Lander E.S.;
RL Nat. Genet. 23:373-373(1999).
CC -!- FUNCTION: A bifunctional enzyme responsible for the oxidation and
CC isomerization of 3beta-hydroxy-Delta(5)-steroid precursors to 3-oxo-
CC Delta(4)-steroids, an essential step in steroid hormone biosynthesis.
CC Specifically catalyzes the conversion of pregnenolone to progesterone,
CC 17alpha-hydroxypregnenolone to 17alpha-hydroxyprogesterone,
CC dehydroepiandrosterone (DHEA) to 4-androstenedione, and androstenediol
CC to testosterone. Additionally, catalyzes the interconversion between
CC 3beta-hydroxy and 3-oxo-5alpha-androstane steroids controlling the
CC bioavalability of the active forms. Specifically converts
CC dihydrotestosterone to its inactive form 5alpha-androstanediol, that
CC does not bind androgen receptor/AR. Also converts androstanedione, a
CC precursor of testosterone and estrone, to epiandrosterone
CC (PubMed:1401999, PubMed:2139411). Expected to use NAD(+) as preferred
CC electron donor for the 3beta-hydroxy-steroid dehydrogenase activity and
CC NADPH for the 3-ketosteroid reductase activity (Probable).
CC {ECO:0000269|PubMed:1401999, ECO:0000269|PubMed:2139411,
CC ECO:0000305|PubMed:1401999}.
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; EC=1.1.1.145;
CC Evidence={ECO:0000269|PubMed:1401999};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=NAD(+) + pregnenolone = H(+) + NADH + pregn-5-ene-3,20-dione;
CC Xref=Rhea:RHEA:43924, ChEBI:CHEBI:15378, ChEBI:CHEBI:16581,
CC ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:63837;
CC Evidence={ECO:0000269|PubMed:1401999};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=3beta-hydroxyandrost-5-en-17-one + NAD(+) = androst-5-ene-
CC 3,17-dione + H(+) + NADH; Xref=Rhea:RHEA:43932, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:28689, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945,
CC ChEBI:CHEBI:83865; EC=1.1.1.145;
CC Evidence={ECO:0000269|PubMed:1401999};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=androst-5-en-3beta,17beta-diol + NAD(+) = 17beta-hydroxy-
CC androst-5-en-3-one + H(+) + NADH; Xref=Rhea:RHEA:56932,
CC ChEBI:CHEBI:2710, ChEBI:CHEBI:15378, ChEBI:CHEBI:57540,
CC ChEBI:CHEBI:57945, ChEBI:CHEBI:141179;
CC Evidence={ECO:0000250|UniProtKB:P22071};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 3beta-hydroxysteroid + NADP(+) = a 3-oxosteroid + H(+) +
CC NADPH; Xref=Rhea:RHEA:34787, ChEBI:CHEBI:15378, ChEBI:CHEBI:36836,
CC ChEBI:CHEBI:47788, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349;
CC EC=1.1.1.270; Evidence={ECO:0000269|PubMed:1401999};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=5alpha-androstane-3beta,17beta-diol + NADP(+) = 17beta-
CC hydroxy-5alpha-androstan-3-one + H(+) + NADPH; Xref=Rhea:RHEA:16297,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:16330, ChEBI:CHEBI:18329,
CC ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.1.1.210;
CC Evidence={ECO:0000269|PubMed:1401999};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=3beta-hydroxy-5alpha-androstan-17-one + NADP(+) = 5alpha-
CC androstan-3,17-dione + H(+) + NADPH; Xref=Rhea:RHEA:56916,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:15994, ChEBI:CHEBI:57783,
CC ChEBI:CHEBI:58349, ChEBI:CHEBI:541975;
CC Evidence={ECO:0000250|UniProtKB:P22071};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 3-oxo-Delta(5)-steroid = a 3-oxo-Delta(4)-steroid;
CC Xref=Rhea:RHEA:14709, ChEBI:CHEBI:47907, ChEBI:CHEBI:47909;
CC EC=5.3.3.1; Evidence={ECO:0000269|PubMed:1401999};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=pregn-5-ene-3,20-dione = progesterone; Xref=Rhea:RHEA:43928,
CC ChEBI:CHEBI:17026, ChEBI:CHEBI:63837;
CC Evidence={ECO:0000269|PubMed:1401999};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=androst-5-ene-3,17-dione = androst-4-ene-3,17-dione;
CC Xref=Rhea:RHEA:43936, ChEBI:CHEBI:16422, ChEBI:CHEBI:83865;
CC Evidence={ECO:0000269|PubMed:1401999};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=17beta-hydroxy-androst-5-en-3-one = testosterone;
CC Xref=Rhea:RHEA:56936, ChEBI:CHEBI:17347, ChEBI:CHEBI:141179;
CC Evidence={ECO:0000250|UniProtKB:P22071};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=5alpha-androstane-3beta,17beta-diol + NAD(+) = 17beta-hydroxy-
CC 5alpha-androstan-3-one + H(+) + NADH; Xref=Rhea:RHEA:42184,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:16330, ChEBI:CHEBI:18329,
CC ChEBI:CHEBI:57540, ChEBI:CHEBI:57945;
CC Evidence={ECO:0000269|PubMed:1401999};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.13 uM for dehydroepiandrosterone (in the presence of NAD(+))
CC {ECO:0000269|PubMed:1401999};
CC KM=0.33 uM for pregnenolone (in the presence of NAD(+))
CC {ECO:0000269|PubMed:1401999};
CC KM=2.1 uM for dihydrotestosterone (in the presence of NADH)
CC {ECO:0000269|PubMed:1401999};
CC Vmax=0.93 nmol/min/mg enzyme for dehydroepiandrosterone oxidation in
CC the presence of NAD(+) {ECO:0000269|PubMed:1401999};
CC Vmax=2.43 nmol/min/mg enzyme for pregnenolone oxidation in the
CC presence of NAD(+) {ECO:0000269|PubMed:1401999};
CC Vmax=14.12 nmol/min/mg enzyme for dihydrotestosterone reduction in
CC the presence of NADH {ECO:0000269|PubMed:1401999};
CC -!- PATHWAY: Steroid hormone biosynthesis. {ECO:0000269|PubMed:1401999}.
CC -!- PATHWAY: Steroid metabolism. {ECO:0000269|PubMed:1401999}.
CC -!- INTERACTION:
CC P14060; Q13520: AQP6; NbExp=3; IntAct=EBI-17426018, EBI-13059134;
CC P14060; P27797: CALR; NbExp=3; IntAct=EBI-17426018, EBI-1049597;
CC P14060; P36957: DLST; NbExp=3; IntAct=EBI-17426018, EBI-351007;
CC P14060; P22607: FGFR3; NbExp=3; IntAct=EBI-17426018, EBI-348399;
CC P14060; P06396: GSN; NbExp=3; IntAct=EBI-17426018, EBI-351506;
CC P14060; Q8TDX7: NEK7; NbExp=3; IntAct=EBI-17426018, EBI-1055945;
CC P14060; Q7RTY0: SLC16A13; NbExp=3; IntAct=EBI-17426018, EBI-12243266;
CC P14060; Q9NUH8: TMEM14B; NbExp=3; IntAct=EBI-17426018, EBI-8638294;
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Single-pass
CC membrane protein. Mitochondrion membrane; Single-pass membrane protein.
CC -!- TISSUE SPECIFICITY: Placenta and skin (PubMed:1401999). Predominantly
CC expressed in mammary gland tissue. {ECO:0000269|PubMed:1401999}.
CC -!- SIMILARITY: Belongs to the 3-beta-HSD family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA36001.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; M27137; AAA36015.1; -; mRNA.
DR EMBL; M28392; AAA36001.1; ALT_SEQ; Genomic_DNA.
DR EMBL; M28162; AAA36001.1; JOINED; Genomic_DNA.
DR EMBL; M28391; AAA36001.1; JOINED; Genomic_DNA.
DR EMBL; X53321; CAA37408.1; -; mRNA.
DR EMBL; M35493; AAA51538.1; -; mRNA.
DR EMBL; M63397; AAA51662.1; -; Genomic_DNA.
DR EMBL; M63395; AAA51662.1; JOINED; Genomic_DNA.
DR EMBL; M63396; AAA51662.1; JOINED; Genomic_DNA.
DR EMBL; M38180; AAA51831.1; -; Genomic_DNA.
DR EMBL; X55997; CAA39469.1; -; mRNA.
DR EMBL; S45679; AAB23543.1; -; mRNA.
DR EMBL; AK291556; BAF84245.1; -; mRNA.
DR EMBL; BC031999; AAH31999.1; -; mRNA.
DR CCDS; CCDS903.1; -.
DR PIR; A36551; DEHUHS.
DR RefSeq; NP_000853.1; NM_000862.2.
DR RefSeq; NP_001315544.1; NM_001328615.1.
DR AlphaFoldDB; P14060; -.
DR SMR; P14060; -.
DR BioGRID; 109516; 6.
DR IntAct; P14060; 11.
DR STRING; 9606.ENSP00000358421; -.
DR BindingDB; P14060; -.
DR ChEMBL; CHEMBL1958; -.
DR DrugBank; DB01536; Androstenedione.
DR DrugBank; DB14538; Hydrocortisone aceponate.
DR DrugBank; DB14539; Hydrocortisone acetate.
DR DrugBank; DB14540; Hydrocortisone butyrate.
DR DrugBank; DB14541; Hydrocortisone cypionate.
DR DrugBank; DB14542; Hydrocortisone phosphate.
DR DrugBank; DB14543; Hydrocortisone probutate.
DR DrugBank; DB14544; Hydrocortisone valerate.
DR DrugBank; DB00157; NADH.
DR DrugBank; DB01708; Prasterone.
DR DrugBank; DB09070; Tibolone.
DR DrugBank; DB01108; Trilostane.
DR DrugCentral; P14060; -.
DR SwissLipids; SLP:000001297; -.
DR iPTMnet; P14060; -.
DR PhosphoSitePlus; P14060; -.
DR BioMuta; HSD3B1; -.
DR DMDM; 112767; -.
DR MassIVE; P14060; -.
DR PaxDb; P14060; -.
DR PeptideAtlas; P14060; -.
DR PRIDE; P14060; -.
DR ProteomicsDB; 53017; -.
DR Antibodypedia; 33912; 378 antibodies from 31 providers.
DR DNASU; 3283; -.
DR Ensembl; ENST00000369413.8; ENSP00000358421.3; ENSG00000203857.10.
DR Ensembl; ENST00000528909.1; ENSP00000432268.1; ENSG00000203857.10.
DR GeneID; 3283; -.
DR KEGG; hsa:3283; -.
DR MANE-Select; ENST00000369413.8; ENSP00000358421.3; NM_000862.3; NP_000853.1.
DR UCSC; uc001ehv.2; human.
DR CTD; 3283; -.
DR DisGeNET; 3283; -.
DR GeneCards; HSD3B1; -.
DR HGNC; HGNC:5217; HSD3B1.
DR HPA; ENSG00000203857; Tissue enriched (placenta).
DR MIM; 109715; gene.
DR neXtProt; NX_P14060; -.
DR OpenTargets; ENSG00000203857; -.
DR PharmGKB; PA29486; -.
DR VEuPathDB; HostDB:ENSG00000203857; -.
DR eggNOG; KOG1430; Eukaryota.
DR GeneTree; ENSGT00940000161374; -.
DR HOGENOM; CLU_007383_6_3_1; -.
DR OMA; PFNRHRV; -.
DR OrthoDB; 930591at2759; -.
DR PhylomeDB; P14060; -.
DR TreeFam; TF343138; -.
DR BioCyc; MetaCyc:HS08829-MON; -.
DR BRENDA; 1.1.1.145; 2681.
DR BRENDA; 5.3.3.1; 2681.
DR PathwayCommons; P14060; -.
DR Reactome; R-HSA-193048; Androgen biosynthesis.
DR Reactome; R-HSA-193993; Mineralocorticoid biosynthesis.
DR Reactome; R-HSA-194002; Glucocorticoid biosynthesis.
DR SABIO-RK; P14060; -.
DR SignaLink; P14060; -.
DR SIGNOR; P14060; -.
DR BioGRID-ORCS; 3283; 24 hits in 1026 CRISPR screens.
DR GeneWiki; HSD3B1; -.
DR GenomeRNAi; 3283; -.
DR Pharos; P14060; Tchem.
DR PRO; PR:P14060; -.
DR Proteomes; UP000005640; Chromosome 1.
DR RNAct; P14060; protein.
DR Bgee; ENSG00000203857; Expressed in placenta and 97 other tissues.
DR ExpressionAtlas; P14060; baseline and differential.
DR Genevisible; P14060; HS.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:HPA.
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:0045171; C:intercellular bridge; IDA:HPA.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IBA:GO_Central.
DR GO; GO:0005743; C:mitochondrial inner membrane; IDA:UniProtKB.
DR GO; GO:0005758; C:mitochondrial intermembrane space; IDA:UniProtKB.
DR GO; GO:0005730; C:nucleolus; IDA:HPA.
DR GO; GO:0030868; C:smooth endoplasmic reticulum membrane; ISS:UniProtKB.
DR GO; GO:0003854; F:3-beta-hydroxy-delta5-steroid dehydrogenase activity; ISS:UniProtKB.
DR GO; GO:0000253; F:3-keto sterol reductase activity; IEA:UniProtKB-EC.
DR GO; GO:0047024; F:5alpha-androstane-3beta,17beta-diol dehydrogenase activity; IEA:UniProtKB-EC.
DR GO; GO:0102294; F:cholesterol dehydrogenase activity; IEA:UniProtKB-EC.
DR GO; GO:0102176; F:cycloeucalenone reductase activity; IEA:UniProtKB-EC.
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:0004769; F:steroid delta-isomerase activity; ISS:UniProtKB.
DR GO; GO:0006702; P:androgen biosynthetic process; TAS:UniProtKB.
DR GO; GO:0008207; P:C21-steroid hormone metabolic process; IBA:GO_Central.
DR GO; GO:0006703; P:estrogen biosynthetic process; TAS:UniProtKB.
DR GO; GO:0021766; P:hippocampus development; IBA:GO_Central.
DR GO; GO:0051412; P:response to corticosterone; IBA:GO_Central.
DR GO; GO:0006694; P:steroid biosynthetic process; ISS: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 Direct protein sequencing; Endoplasmic reticulum; Isomerase;
KW Lipid metabolism; Membrane; Mitochondrion; Multifunctional enzyme; NAD;
KW NADP; Oxidoreductase; Reference proteome; Steroid metabolism;
KW Steroidogenesis; Transmembrane; Transmembrane helix.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:2779585"
FT CHAIN 2..373
FT /note="3 beta-hydroxysteroid dehydrogenase/Delta 5-->4-
FT isomerase type 1"
FT /id="PRO_0000087774"
FT TRANSMEM 288..308
FT /note="Helical"
FT /evidence="ECO:0000255"
FT ACT_SITE 159
FT /note="Proton donor"
FT /evidence="ECO:0000250|UniProtKB:Q12068"
FT BINDING 10..15
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:Q12068"
FT BINDING 155
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:Q12068"
FT BINDING 159
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:Q12068"
FT VARIANT 54
FT /note="T -> I (in dbSNP:rs3088283)"
FT /id="VAR_048096"
FT VARIANT 71
FT /note="R -> I (in dbSNP:rs4986952)"
FT /id="VAR_048097"
FT VARIANT 79
FT /note="I -> V (in dbSNP:rs6201)"
FT /evidence="ECO:0000269|PubMed:10391209"
FT /id="VAR_014174"
FT VARIANT 90
FT /note="G -> S (in dbSNP:rs6684974)"
FT /id="VAR_048098"
FT VARIANT 286
FT /note="F -> L (in dbSNP:rs6205)"
FT /evidence="ECO:0000269|PubMed:10391209"
FT /id="VAR_014175"
FT VARIANT 367
FT /note="T -> N (in dbSNP:rs1047303)"
FT /evidence="ECO:0000269|PubMed:15489334,
FT ECO:0000269|PubMed:2243100"
FT /id="VAR_000005"
SQ SEQUENCE 373 AA; 42252 MW; 2C76616E7EA7433A CRC64;
MTGWSCLVTG AGGFLGQRII RLLVKEKELK EIRVLDKAFG PELREEFSKL QNKTKLTVLE
GDILDEPFLK RACQDVSVII HTACIIDVFG VTHRESIMNV NVKGTQLLLE ACVQASVPVF
IYTSSIEVAG PNSYKEIIQN GHEEEPLENT WPAPYPHSKK LAEKAVLAAN GWNLKNGGTL
YTCALRPMYI YGEGSRFLSA SINEALNNNG ILSSVGKFST VNPVYVGNVA WAHILALRAL
QDPKKAPSIR GQFYYISDDT PHQSYDNLNY TLSKEFGLRL DSRWSFPLSL MYWIGFLLEI
VSFLLRPIYT YRPPFNRHIV TLSNSVFTFS YKKAQRDLAY KPLYSWEEAK QKTVEWVGSL
VDRHKETLKS KTQ
