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3 beta-hydroxysteroid dehydrogenase/Delta 5-->4-isomerase type 2 (3 beta-hydroxysteroid dehydrogenase/Delta 5-->4-isomerase type II) (3-beta-HSD II) (3-beta-HSD adrenal and gonadal type) [Includes: 3-beta-hydroxy-Delta(5)-steroid dehydrogenase (EC 1.1.1.145) (3-beta-hydroxy-5-ene steroid dehydrogenase) (Progesterone reductase); Steroid Delta-isomerase (EC 5.3.3.1) (Delta-5-3-ketosteroid isomerase)]

 3BHS2_HUMAN             Reviewed;         372 AA.
P26439; A2RRA5; Q16010; Q53GD4; Q6AI10; Q6LDB9; Q99890; Q9UD08;
01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
23-JAN-2007, sequence version 2.
28-FEB-2018, entry version 190.
RecName: Full=3 beta-hydroxysteroid dehydrogenase/Delta 5-->4-isomerase type 2;
AltName: Full=3 beta-hydroxysteroid dehydrogenase/Delta 5-->4-isomerase type II;
Short=3-beta-HSD II;
AltName: Full=3-beta-HSD adrenal and gonadal type;
Includes:
RecName: Full=3-beta-hydroxy-Delta(5)-steroid dehydrogenase;
EC=1.1.1.145;
AltName: Full=3-beta-hydroxy-5-ene steroid dehydrogenase;
AltName: Full=Progesterone reductase;
Includes:
RecName: Full=Steroid Delta-isomerase;
EC=5.3.3.1;
AltName: Full=Delta-5-3-ketosteroid isomerase;
Name=HSD3B2; Synonyms=HSDB3B;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=1741954; DOI=10.1089/dna.1991.10.701;
Lachance Y., Luu-The V., Verreault H., Dumont M., Rheaume E.,
Leblanc G., Labrie F.;
"Structure of the human type II 3 beta-hydroxysteroid
dehydrogenase/delta 5-delta 4 isomerase (3 beta-HSD) gene: adrenal and
gonadal specificity.";
DNA Cell Biol. 10:701-711(1991).
[2]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Adrenal gland;
PubMed=1944309; DOI=10.1210/mend-5-8-1147;
Rheaume E., Lachance Y., Zhao H.-F., Breton N., Dumont M.,
de Launoit Y., Trudel C., Luu-The V., Simard J., Labrie F.;
"Structure and expression of a new complementary DNA encoding the
almost exclusive 3 beta-hydroxysteroid dehydrogenase/delta 5-delta 4-
isomerase in human adrenals and gonads.";
Mol. Endocrinol. 5:1147-1157(1991).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), AND VARIANT
GLN-94.
TISSUE=Adrenal gland;
PubMed=17974005; DOI=10.1186/1471-2164-8-399;
Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H.,
Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K.,
Ottenwaelder B., Poustka A., Wiemann S., Schupp I.;
"The full-ORF clone resource of the German cDNA consortium.";
BMC Genomics 8:399-399(2007).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Small intestine;
Suzuki Y., Sugano S., Totoki Y., Toyoda A., Takeda T., Sakaki Y.,
Tanaka A., Yokoyama S.;
Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16710414; DOI=10.1038/nature04727;
Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D.,
Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A.,
Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F.,
McDonald L., Evans R., Phillips K., Atkinson A., Cooper R., Jones C.,
Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P.,
Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K.,
Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G.,
Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D.,
Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G.,
Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J.,
Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R.,
Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D.,
Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G.,
Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M.,
Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J.,
Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M.,
Loveland J., Lovell J., Lush M.J., Lyne R., Martin S.,
Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S.,
Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C.,
Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z.,
Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E.,
Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A.,
Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R.,
Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V.,
Beck S., Rogers J., Bentley D.R.;
"The DNA sequence and biological annotation of human chromosome 1.";
Nature 441:315-321(2006).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Brain;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[8]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 49-102.
PubMed=7588414; DOI=10.3109/07435809509030466;
Russell A.J., McCartin S., Corcao G., Burridge S.M., McBride M.W.,
McNicol A.M., Hawes C.S., Mason J.I., Sutcliffe R.G.;
"Variation in the expression of human 3 beta-hydroxysteroid
dehydrogenase.";
Endocr. Res. 21:485-494(1995).
[9]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 167-205.
PubMed=1363812; DOI=10.1038/ng0792-239;
Rheaume E., Simard J., Morel Y., Mebarki F., Zachmann M., Forest M.G.,
New M.I., Labrie F.;
"Congenital adrenal hyperplasia due to point mutations in the type II
3 beta-hydroxysteroid dehydrogenase gene.";
Nat. Genet. 1:239-245(1992).
[10]
POSSIBLE INVOLVEMENT IN INSULIN-RESISTANT POLYCYSTIC OVARY SYNDROME.
PubMed=14764797; DOI=10.1210/jc.2003-030934;
Carbunaru G., Prasad P., Scoccia B., Shea P., Hopwood N., Ziai F.,
Chang Y.T., Myers S.E., Mason J.I., Pang S.;
"The hormonal phenotype of nonclassic 3 beta-hydroxysteroid
dehydrogenase (HSD3B) deficiency in hyperandrogenic females is
associated with insulin-resistant polycystic ovary syndrome and is not
a variant of inherited HSD3B2 deficiency.";
J. Clin. Endocrinol. Metab. 89:783-794(2004).
[11]
VARIANTS AH2 LYS-142; PRO-245 AND ASN-253.
PubMed=8316254; DOI=10.1210/mend.7.5.8316254;
Simard J., Rheaume E., Sanchez R., Laflamme N., de Launoit Y.,
Luu-The V., van Seters A.P., Gordon R.D., Bettendorf M., Heinrich U.,
Moshang T., New M.I., Labrie F.;
"Molecular basis of congenital adrenal hyperplasia due to 3 beta-
hydroxysteroid dehydrogenase deficiency.";
Mol. Endocrinol. 7:716-728(1993).
[12]
VARIANTS AH2 TRP-108 AND LEU-186.
PubMed=7833923; DOI=10.1093/hmg/3.9.1639;
Sanchez R., Mebarki F., Rheaume E., Laflamme N., Forest M.G.,
Bey-Omar F., David M., Morel Y., Labrie F., Simard J.;
"Functional characterization of the novel L108W and P186L mutations
detected in the type II 3 beta-hydroxysteroid dehydrogenase gene of a
male pseudohermaphrodite with congenital adrenal hyperplasia.";
Hum. Mol. Genet. 3:1639-1645(1994).
[13]
VARIANT AH2 ASP-254.
PubMed=8126127; DOI=10.1210/jcem.78.3.8126127;
Sanchez R., Rheaume E., Laflamme N., Rosenfield R.L., Labrie F.,
Simard J.;
"Detection and functional characterization of the novel missense
mutation Y254D in type II 3 beta-hydroxysteroid dehydrogenase (3 beta
HSD) gene of a female patient with nonsalt-losing 3 beta HSD
deficiency.";
J. Clin. Endocrinol. Metab. 78:561-567(1994).
[14]
VARIANT AH2 ARG-129.
PubMed=7962268; DOI=10.1210/jcem.79.4.7962268;
Rheaume E., Sanchez R., Simard J., Chang Y.T., Wang J., Pang S.,
Labrie F.;
"Molecular basis of congenital adrenal hyperplasia in two siblings
with classical nonsalt-losing 3 beta-hydroxysteroid dehydrogenase
deficiency.";
J. Clin. Endocrinol. Metab. 79:1012-1018(1994).
[15]
VARIANT AH2 THR-82.
PubMed=8185809; DOI=10.1677/jme.0.0120119;
Mendonca B.B., Russell A.J., Vasconcelos-Leite M., Arnhold I.J.,
Bloise W., Wajchenberg B.L., Nicolau W., Sutcliffe R.G., Wallace A.M.;
"Mutation in 3 beta-hydroxysteroid dehydrogenase type II associated
with pseudohermaphroditism in males and premature pubarche or cryptic
expression in females.";
J. Mol. Endocrinol. 12:119-122(1994).
[16]
VARIANT AH2 ARG-173.
PubMed=8060486; DOI=10.1677/jme.0.0120225;
Russell A.J., Wallace A.M., Forest M.G., Donaldson M.D., Edwards C.R.,
Sutcliffe R.G.;
"Mutation in the human gene for 3 beta-hydroxysteroid dehydrogenase
type II leading to male pseudohermaphroditism without salt loss.";
J. Mol. Endocrinol. 12:225-237(1994).
[17]
VARIANT AH2 ASP-15.
PubMed=7893703; DOI=10.1021/bi00009a020;
Rheaume E., Sanchez R., Mebarki F., Gagnon E., Carel J.-C.,
Chaussain J.-L., Morel Y., Labrie F., Simard J.;
"Identification and characterization of the G15D mutation found in a
male patient with 3 beta-hydroxysteroid dehydrogenase (3 beta-HSD)
deficiency: alteration of the putative NAD-binding domain of type II 3
beta-HSD.";
Biochemistry 34:2893-2900(1995).
[18]
VARIANT AH2 PRO-205.
PubMed=7633426; DOI=10.1093/hmg/4.4.745;
Katsumata N., Tanae A., Yasunaga T., Horikawa R., Tanaka T., Hibi I.;
"A novel missense mutation in the type II 3 beta-hydroxysteroid
dehydrogenase gene in a family with classical salt-wasting congenital
adrenal hyperplasia due to 3 beta-hydroxysteroid dehydrogenase
deficiency.";
Hum. Mol. Genet. 4:745-746(1995).
[19]
VARIANT AH2 ARG-259.
PubMed=7633460; DOI=10.1093/hmg/4.5.969;
Tajima T., Fujieda K., Nakae J., Shinohara N., Yoshimoto M., Baba T.,
Kinoshita E., Igarashi Y., Oomura T.;
"Molecular analysis of type II 3 beta-hydroxysteroid dehydrogenase
gene in Japanese patients with classical 3 beta-hydroxysteroid
dehydrogenase deficiency.";
Hum. Mol. Genet. 4:969-971(1995).
[20]
VARIANT AH2 SER-100.
PubMed=7608265; DOI=10.1210/jcem.80.7.7608265;
Mebarki F., Sanchez R., Rheaume E., Laflamme N., Simard J.,
Forest M.G., Bey-Omar F., David M., Labrie F., Morel Y.;
"Nonsalt-losing male pseudohermaphroditism due to the novel homozygous
N100S mutation in the type II 3 beta-hydroxysteroid dehydrogenase
gene.";
J. Clin. Endocrinol. Metab. 80:2127-2134(1995).
[21]
VARIANT AH2 SER-236.
PubMed=9719627; DOI=10.1006/mgme.1998.2715;
Nayak S., Lee P.A., Witchel S.F.;
"Variants of the type II 3beta-hydroxysteroid dehydrogenase gene in
children with premature pubic hair and hyperandrogenic adolescents.";
Mol. Genet. Metab. 64:184-192(1998).
[22]
VARIANTS AH2 GLU-10; VAL-10; ASP-15; THR-82; SER-100; TRP-108;
ARG-129; LYS-142; LEU-155; VAL-167; ARG-173; LEU-186; PRO-205;
GLY-213; GLU-216; GLN-222; HIS-222; SER-236; PRO-245; ASN-253;
ASP-254; ARG-259; MET-259 AND VAL-294.
PubMed=10599696; DOI=10.1210/jcem.84.12.6288;
Moisan A.M., Ricketts M.L., Tardy V., Desrochers M., Mebarki F.,
Chaussain J.-L., Cabrol S., Raux-Demay M.C., Forest M.G.,
Sippell W.G., Peter M., Morel Y., Simard J.;
"New insight into the molecular basis of 3beta-hydroxysteroid
dehydrogenase deficiency: identification of eight mutations in the
HSD3B2 gene in eleven patients from seven new families and comparison
of the functional properties of twenty-five mutant enzymes.";
J. Clin. Endocrinol. Metab. 84:4410-4425(1999).
[23]
VARIANTS AH2 ARG-129; GLN-222 AND MET-259.
PubMed=10651755; DOI=10.1046/j.1365-2265.2000.00873.x;
Marui S., Castro M., Latronico A.C., Elias L.L., Arnhold I.J.,
Moreira A.C., Mendonca B.B.;
"Mutations in the type II 3beta-hydroxysteroid dehydrogenase (HSD3B2)
gene can cause premature pubarche in girls.";
Clin. Endocrinol. (Oxf.) 52:67-75(2000).
[24]
VARIANT AH2 GLU-10.
PubMed=10843183; DOI=10.1210/jcem.85.5.6581;
Alos N., Moisan A.M., Ward L., Desrochers M., Legault L., Leboeuf G.,
van Vliet G., Simard J.;
"A novel A10E homozygous mutation in the HSD3B2 gene causing severe
salt-wasting 3beta-hydroxysteroid dehydrogenase deficiency in 46,XX
and 46,XY French-Canadians: evaluation of gonadal function after
puberty.";
J. Clin. Endocrinol. Metab. 85:1968-1974(2000).
[25]
VARIANTS AH2 LYS-142 AND THR-222.
PubMed=12050213; DOI=10.1210/jcem.87.6.8559;
Pang S., Wang W., Rich B., David R., Chang Y.T., Carbunaru G.,
Myers S.E., Howie A.F., Smillie K.J., Mason J.I.;
"A novel nonstop mutation in the stop codon and a novel missense
mutation in the type II 3-beta-hydroxysteroid dehydrogenase (3-beta-
HSD) gene causing, respectively, nonclassic and classic 3-beta-HSD
deficiency congenital adrenal hyperplasia.";
J. Clin. Endocrinol. Metab. 87:2556-2563(2002).
[26]
VARIANT AH2 LEU-341, AND CHARACTERIZATION OF VARIANT AH2 LEU-341.
PubMed=18252794; DOI=10.1210/jc.2007-1874;
Welzel M., Wustemann N., Simic-Schleicher G., Dorr H.G., Schulze E.,
Shaikh G., Clayton P., Grotzinger J., Holterhus P.M., Riepe F.G.;
"Carboxyl-terminal mutations in 3beta-hydroxysteroid dehydrogenase
type II cause severe salt-wasting congenital adrenal hyperplasia.";
J. Clin. Endocrinol. Metab. 93:1418-1425(2008).
[27]
VARIANT AH2 PRO-82.
PubMed=22579964; DOI=10.1016/j.gene.2012.04.080;
Rabbani B., Mahdieh N., Haghi Ashtiani M.T., Setoodeh A., Rabbani A.;
"In silico structural, functional and pathogenicity evaluation of a
novel mutation: an overview of HSD3B2 gene mutations.";
Gene 503:215-221(2012).
-!- FUNCTION: 3-beta-HSD is a bifunctional enzyme, that catalyzes the
oxidative conversion of Delta(5)-ene-3-beta-hydroxy steroid, and
the oxidative conversion of ketosteroids. The 3-beta-HSD enzymatic
system plays a crucial role in the biosynthesis of all classes of
hormonal steroids.
-!- CATALYTIC ACTIVITY: A 3-beta-hydroxy-Delta(5)-steroid + NAD(+) = a
3-oxo-Delta(5)-steroid + NADH.
-!- CATALYTIC ACTIVITY: A 3-oxo-Delta(5)-steroid = a 3-oxo-Delta(4)-
steroid.
-!- PATHWAY: Lipid metabolism; steroid biosynthesis.
-!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Single-pass
membrane protein. Mitochondrion membrane; Single-pass membrane
protein.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=P26439-1; Sequence=Displayed;
Name=2;
IsoId=P26439-2; Sequence=VSP_037399, VSP_037400;
-!- TISSUE SPECIFICITY: Expressed in adrenal gland, testis and ovary.
-!- DISEASE: Adrenal hyperplasia 2 (AH2) [MIM:201810]: A form of
congenital adrenal hyperplasia, a common recessive disease due to
defective synthesis of cortisol. Congenital adrenal hyperplasia is
characterized by androgen excess leading to ambiguous genitalia in
affected females, rapid somatic growth during childhood in both
sexes with premature closure of the epiphyses and short adult
stature. Four clinical types: 'salt wasting' (SW, the most severe
type), 'simple virilizing' (SV, less severely affected patients),
with normal aldosterone biosynthesis, 'non-classic form' or late-
onset (NC or LOAH) and 'cryptic' (asymptomatic). In AH2,
virilization is much less marked or does not occur. AH2 is
frequently lethal in early life. {ECO:0000269|PubMed:10599696,
ECO:0000269|PubMed:10651755, ECO:0000269|PubMed:10843183,
ECO:0000269|PubMed:12050213, ECO:0000269|PubMed:18252794,
ECO:0000269|PubMed:22579964, ECO:0000269|PubMed:7608265,
ECO:0000269|PubMed:7633426, ECO:0000269|PubMed:7633460,
ECO:0000269|PubMed:7833923, ECO:0000269|PubMed:7893703,
ECO:0000269|PubMed:7962268, ECO:0000269|PubMed:8060486,
ECO:0000269|PubMed:8126127, ECO:0000269|PubMed:8185809,
ECO:0000269|PubMed:8316254, ECO:0000269|PubMed:9719627}. Note=The
disease is caused by mutations affecting the gene represented in
this entry.
-!- DISEASE: Note=Mild HSD3B2 deficiency in hyperandrogenic females is
associated with characteristic traits of polycystic ovary
syndrome, such as insulin resistance and luteinizing hormone
hypersecretion. {ECO:0000269|PubMed:14764797}.
-!- SIMILARITY: Belongs to the 3-beta-HSD family. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=AAC60600.1; Type=Frameshift; Positions=186; Note=The frameshift is caused by a single nucleotide insertion which is found in AH2.; Evidence={ECO:0000305};
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EMBL; M77144; AAA36014.1; -; Genomic_DNA.
EMBL; M67466; AAA36016.1; -; mRNA.
EMBL; CR627415; CAH10504.1; -; mRNA.
EMBL; AK222997; BAD96717.1; -; mRNA.
EMBL; AL359553; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471122; EAW56700.1; -; Genomic_DNA.
EMBL; BC038419; AAH38419.1; -; mRNA.
EMBL; BC131488; AAI31489.1; -; mRNA.
EMBL; S80140; AAD14329.1; -; Genomic_DNA.
EMBL; S60309; AAC60599.1; -; Genomic_DNA.
EMBL; S60310; AAC60600.1; ALT_FRAME; Genomic_DNA.
CCDS; CCDS902.1; -. [P26439-1]
PIR; A39488; DEHUH2.
RefSeq; NP_000189.1; NM_000198.3. [P26439-1]
RefSeq; NP_001159592.1; NM_001166120.1. [P26439-1]
UniGene; Hs.654399; -.
ProteinModelPortal; P26439; -.
BioGrid; 109517; 22.
CORUM; P26439; -.
STRING; 9606.ENSP00000358424; -.
BindingDB; P26439; -.
ChEMBL; CHEMBL3670; -.
DrugBank; DB01285; Corticotropin.
DrugBank; DB00603; Medroxyprogesterone acetate.
DrugBank; DB00157; NADH.
DrugBank; DB01108; Trilostane.
SwissLipids; SLP:000001296; -.
iPTMnet; P26439; -.
PhosphoSitePlus; P26439; -.
BioMuta; HSD3B2; -.
DMDM; 112770; -.
EPD; P26439; -.
PaxDb; P26439; -.
PeptideAtlas; P26439; -.
PRIDE; P26439; -.
DNASU; 3284; -.
Ensembl; ENST00000369416; ENSP00000358424; ENSG00000203859. [P26439-1]
Ensembl; ENST00000543831; ENSP00000445122; ENSG00000203859. [P26439-1]
GeneID; 3284; -.
KEGG; hsa:3284; -.
UCSC; uc001eht.4; human. [P26439-1]
CTD; 3284; -.
DisGeNET; 3284; -.
EuPathDB; HostDB:ENSG00000203859.9; -.
GeneCards; HSD3B2; -.
HGNC; HGNC:5218; HSD3B2.
HPA; HPA043261; -.
HPA; HPA043264; -.
HPA; HPA044028; -.
MalaCards; HSD3B2; -.
MIM; 201810; phenotype.
MIM; 613890; gene.
neXtProt; NX_P26439; -.
OpenTargets; ENSG00000203859; -.
Orphanet; 90791; Congenital adrenal hyperplasia due to 3-beta-hydroxysteroid dehydrogenase deficiency.
Orphanet; 3185; Polycystic ovary syndrome.
PharmGKB; PA29487; -.
eggNOG; KOG1430; Eukaryota.
eggNOG; COG0451; LUCA.
GeneTree; ENSGT00550000074557; -.
HOVERGEN; HBG000014; -.
KO; K00070; -.
OMA; YSYQPPF; -.
OrthoDB; EOG091G09QZ; -.
PhylomeDB; P26439; -.
TreeFam; TF343138; -.
BioCyc; MetaCyc:HS10943-MONOMER; -.
BRENDA; 1.1.1.145; 2681.
BRENDA; 5.3.3.1; 2681.
Reactome; R-HSA-193048; Androgen biosynthesis.
Reactome; R-HSA-193993; Mineralocorticoid biosynthesis.
Reactome; R-HSA-194002; Glucocorticoid biosynthesis.
SIGNOR; P26439; -.
UniPathway; UPA00062; -.
ChiTaRS; HSD3B2; human.
GeneWiki; HSD3B2; -.
GenomeRNAi; 3284; -.
PRO; PR:P26439; -.
Proteomes; UP000005640; Chromosome 1.
Bgee; ENSG00000203859; -.
CleanEx; HS_HSD3B2; -.
ExpressionAtlas; P26439; baseline and differential.
Genevisible; P26439; HS.
GO; GO:0005783; C:endoplasmic reticulum; NAS:UniProtKB.
GO; GO:0005789; C:endoplasmic reticulum membrane; TAS:Reactome.
GO; GO:0016021; C:integral component of membrane; NAS:UniProtKB.
GO; GO:0005743; C:mitochondrial inner membrane; ISS:UniProtKB.
GO; GO:0005758; C:mitochondrial intermembrane space; ISS:UniProtKB.
GO; GO:0031966; C:mitochondrial membrane; NAS:UniProtKB.
GO; GO:0030868; C:smooth endoplasmic reticulum membrane; ISS:UniProtKB.
GO; GO:0003854; F:3-beta-hydroxy-delta5-steroid dehydrogenase activity; IDA:UniProtKB.
GO; GO:0102294; F:cholesterol dehydrogenase activity; IEA:UniProtKB-EC.
GO; GO:0004769; F:steroid delta-isomerase activity; IDA:UniProtKB.
GO; GO:0006702; P:androgen biosynthetic process; TAS:Reactome.
GO; GO:0006704; P:glucocorticoid biosynthetic process; TAS:Reactome.
GO; GO:0006705; P:mineralocorticoid biosynthetic process; TAS:Reactome.
GO; GO:0006694; P:steroid biosynthetic process; IDA:UniProtKB.
InterPro; IPR002225; 3Beta_OHSteriod_DH/Estase.
InterPro; IPR036291; NAD(P)-bd_dom_sf.
Pfam; PF01073; 3Beta_HSD; 1.
SUPFAM; SSF51735; SSF51735; 2.
1: Evidence at protein level;
Alternative splicing; Complete proteome;
Congenital adrenal hyperplasia; Disease mutation;
Endoplasmic reticulum; Isomerase; Membrane; Mitochondrion;
Multifunctional enzyme; NAD; Oxidoreductase; Polymorphism;
Reference proteome; Steroidogenesis; Transmembrane;
Transmembrane helix.
CHAIN 1 372 3 beta-hydroxysteroid dehydrogenase/Delta
5-->4-isomerase type 2.
/FTId=PRO_0000087775.
TRANSMEM 287 307 Helical. {ECO:0000255}.
ACT_SITE 154 154 Proton acceptor. {ECO:0000250}.
BINDING 158 158 NAD. {ECO:0000250}.
VAR_SEQ 103 222 GTQLLLEACVQASVPVFIYTSSIEVAGPNSYKEIIQNGHEE
EPLENTWPTPYPYSKKLAEKAVLAANGWNLKNGDTLYTCAL
RPTYIYGEGGPFLSASINEALNNNGILSSVGKFSTVNP ->
ELQNKIKLTVLEGDILDEPFLKRACQDVSVVIHTACIIDVF
GVTHRQSIMNVNVKGRVAWGGDKARWGNEDQKEGQEGKRSL
SIEHLLCSGPSDFADHYQLGELKAAIFSFIDEKTRTEQ
(in isoform 2).
{ECO:0000303|PubMed:17974005}.
/FTId=VSP_037399.
VAR_SEQ 223 372 Missing (in isoform 2).
{ECO:0000303|PubMed:17974005}.
/FTId=VSP_037400.
VARIANT 10 10 A -> E (in AH2; activity abolished;
dbSNP:rs28934880).
{ECO:0000269|PubMed:10599696,
ECO:0000269|PubMed:10843183}.
/FTId=VAR_010517.
VARIANT 10 10 A -> V (in AH2; nonsalt-wasting form).
{ECO:0000269|PubMed:10599696}.
/FTId=VAR_010518.
VARIANT 15 15 G -> D (in AH2; activity abolished).
{ECO:0000269|PubMed:10599696,
ECO:0000269|PubMed:7893703}.
/FTId=VAR_010519.
VARIANT 74 74 D -> N (in dbSNP:rs4986954).
/FTId=VAR_048099.
VARIANT 82 82 A -> P (in AH2).
{ECO:0000269|PubMed:22579964}.
/FTId=VAR_070028.
VARIANT 82 82 A -> T (in AH2; dbSNP:rs757033996).
{ECO:0000269|PubMed:10599696,
ECO:0000269|PubMed:8185809}.
/FTId=VAR_010520.
VARIANT 94 94 E -> Q (in dbSNP:rs6211).
{ECO:0000269|PubMed:17974005}.
/FTId=VAR_014818.
VARIANT 100 100 N -> S (in AH2; nonsalt-wasting form).
{ECO:0000269|PubMed:10599696,
ECO:0000269|PubMed:7608265}.
/FTId=VAR_010521.
VARIANT 108 108 L -> W (in AH2; activity abolished).
{ECO:0000269|PubMed:10599696,
ECO:0000269|PubMed:7833923}.
/FTId=VAR_010522.
VARIANT 129 129 G -> R (in AH2; nonsalt-wasting form;
dbSNP:rs587628683).
{ECO:0000269|PubMed:10599696,
ECO:0000269|PubMed:10651755,
ECO:0000269|PubMed:7962268}.
/FTId=VAR_010523.
VARIANT 142 142 E -> K (in AH2; activity abolished;
dbSNP:rs80358219).
{ECO:0000269|PubMed:10599696,
ECO:0000269|PubMed:12050213,
ECO:0000269|PubMed:8316254}.
/FTId=VAR_000006.
VARIANT 155 155 P -> L (in AH2; nonsalt-wasting form;
dbSNP:rs779418168).
{ECO:0000269|PubMed:10599696}.
/FTId=VAR_010524.
VARIANT 167 167 A -> V (in AH2; late onset; almost normal
activity; dbSNP:rs35486059).
{ECO:0000269|PubMed:10599696}.
/FTId=VAR_010525.
VARIANT 173 173 L -> R (in AH2; nonsalt-wasting form;
dbSNP:rs762479018).
{ECO:0000269|PubMed:10599696,
ECO:0000269|PubMed:8060486}.
/FTId=VAR_010526.
VARIANT 186 186 P -> L (in AH2; activity abolished).
{ECO:0000269|PubMed:10599696,
ECO:0000269|PubMed:7833923}.
/FTId=VAR_010527.
VARIANT 205 205 L -> P (in AH2).
{ECO:0000269|PubMed:10599696,
ECO:0000269|PubMed:7633426}.
/FTId=VAR_000007.
VARIANT 213 213 S -> G (in AH2; late onset; partial loss
of activity; dbSNP:rs759422374).
{ECO:0000269|PubMed:10599696}.
/FTId=VAR_010528.
VARIANT 216 216 K -> E (in AH2; late onset; partial loss
of activity).
{ECO:0000269|PubMed:10599696}.
/FTId=VAR_010529.
VARIANT 222 222 P -> H (in AH2; nonsalt-wasting form;
activity abolished).
{ECO:0000269|PubMed:10599696}.
/FTId=VAR_010530.
VARIANT 222 222 P -> Q (in AH2; activity abolished;
dbSNP:rs765547422).
{ECO:0000269|PubMed:10599696,
ECO:0000269|PubMed:10651755}.
/FTId=VAR_010531.
VARIANT 222 222 P -> T (in AH2; dbSNP:rs80358220).
{ECO:0000269|PubMed:12050213}.
/FTId=VAR_015411.
VARIANT 231 238 Missing (in AH2; activity abolished).
/FTId=VAR_010532.
VARIANT 236 236 L -> S (in AH2; mild; 100% of activity;
dbSNP:rs35887327).
{ECO:0000269|PubMed:10599696,
ECO:0000269|PubMed:9719627}.
/FTId=VAR_010533.
VARIANT 245 245 A -> P (in AH2; loss of 88% of activity).
{ECO:0000269|PubMed:10599696,
ECO:0000269|PubMed:8316254}.
/FTId=VAR_000008.
VARIANT 253 253 Y -> N (in AH2; activity abolished).
{ECO:0000269|PubMed:10599696,
ECO:0000269|PubMed:8316254}.
/FTId=VAR_000009.
VARIANT 254 254 Y -> D (in AH2; activity abolished).
{ECO:0000269|PubMed:10599696,
ECO:0000269|PubMed:8126127}.
/FTId=VAR_000010.
VARIANT 259 259 T -> M (in AH2; activity abolished;
dbSNP:rs80358221).
{ECO:0000269|PubMed:10599696,
ECO:0000269|PubMed:10651755}.
/FTId=VAR_010534.
VARIANT 259 259 T -> R (in AH2; activity abolished).
{ECO:0000269|PubMed:10599696,
ECO:0000269|PubMed:7633460}.
/FTId=VAR_000011.
VARIANT 294 294 G -> V (in AH2; nonsalt-wasting form;
activity abolished).
{ECO:0000269|PubMed:10599696}.
/FTId=VAR_010535.
VARIANT 341 341 P -> L (in AH2; strongly reduced
activity; dbSNP:rs121964897).
{ECO:0000269|PubMed:18252794}.
/FTId=VAR_065665.
CONFLICT 52 53 RT -> KI (in Ref. 8; AAD14329).
{ECO:0000305}.
CONFLICT 92 94 HRE -> RRQ (in Ref. 8; AAD14329).
{ECO:0000305}.
CONFLICT 232 232 H -> L (in Ref. 4; BAD96717).
{ECO:0000305}.
SEQUENCE 372 AA; 42052 MW; 8E0D933488988451 CRC64;
MGWSCLVTGA GGLLGQRIVR LLVEEKELKE IRALDKAFRP ELREEFSKLQ NRTKLTVLEG
DILDEPFLKR ACQDVSVVIH TACIIDVFGV THRESIMNVN VKGTQLLLEA CVQASVPVFI
YTSSIEVAGP NSYKEIIQNG HEEEPLENTW PTPYPYSKKL AEKAVLAANG WNLKNGDTLY
TCALRPTYIY GEGGPFLSAS INEALNNNGI LSSVGKFSTV NPVYVGNVAW AHILALRALR
DPKKAPSVRG QFYYISDDTP HQSYDNLNYI LSKEFGLRLD SRWSLPLTLM YWIGFLLEVV
SFLLSPIYSY QPPFNRHTVT LSNSVFTFSY KKAQRDLAYK PLYSWEEAKQ KTVEWVGSLV
DRHKETLKSK TQ


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