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3 beta-hydroxysteroid dehydrogenase/Delta 5-->4-isomerase type 6 (EC 1.1.1.-) (3 beta-hydroxysteroid dehydrogenase/Delta 5-->4-isomerase type VI) (3-beta-HSD VI) [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)]

 3BHS6_MOUSE             Reviewed;         373 AA.
O35469; Q3UQN7;
15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
28-JUN-2011, sequence version 4.
05-DEC-2018, entry version 139.
RecName: Full=3 beta-hydroxysteroid dehydrogenase/Delta 5-->4-isomerase type 6;
EC=1.1.1.-;
AltName: Full=3 beta-hydroxysteroid dehydrogenase/Delta 5-->4-isomerase type VI;
Short=3-beta-HSD VI;
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=Hsd3b6;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
STRAIN=C57BL/6J;
PubMed=9075693; DOI=10.1210/endo.138.4.5042;
Abbaszade I.G., Arensburg J., Park C.-H.J., Kasa-Vubu J.Z., Orly J.,
Payne A.H.;
"Isolation of a new mouse 3beta-hydroxysteroid dehydrogenase isoform,
3beta-HSD VI, expressed during early pregnancy.";
Endocrinology 138:1392-1399(1997).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=C57BL/6J; TISSUE=Heart;
PubMed=16141072; DOI=10.1126/science.1112014;
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
Hayashizaki Y.;
"The transcriptional landscape of the mammalian genome.";
Science 309:1559-1563(2005).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=C57BL/6J;
PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
Lindblad-Toh K., Eichler E.E., Ponting C.P.;
"Lineage-specific biology revealed by a finished genome assembly of
the mouse.";
PLoS Biol. 7:E1000112-E1000112(2009).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[5]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Testis;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and
expression.";
Cell 143:1174-1189(2010).
-!- 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. May be involved in local production of
progesterone.
-!- CATALYTIC ACTIVITY:
Reaction=a 3beta-hydroxy-Delta(5)-steroid + NAD(+) = a 3-oxo-
Delta(5)-steroid + H(+) + NADH; Xref=Rhea:RHEA:24076,
ChEBI:CHEBI:1722, ChEBI:CHEBI:15378, ChEBI:CHEBI:47907,
ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=1.1.1.145;
-!- CATALYTIC ACTIVITY:
Reaction=a 3-oxo-Delta(5)-steroid = a 3-oxo-Delta(4)-steroid;
Xref=Rhea:RHEA:14709, ChEBI:CHEBI:47907, ChEBI:CHEBI:47909;
EC=5.3.3.1;
-!- PATHWAY: Lipid metabolism; steroid biosynthesis.
-!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Single-pass
membrane protein. Mitochondrion membrane; Single-pass membrane
protein.
-!- TISSUE SPECIFICITY: Expressed in skin and testis.
-!- DEVELOPMENTAL STAGE: Earliest isoform to be expressed during
embryogenesis in cells of embryonic origin at 7 and 9.5 dpc, and
is the major isoform expressed in uterine tissue at the time of
implantation (4.5 dpc) and continues to be expressed in uterine
tissue at 6.5, 7.5 and 9.5 dpc. It is expressed in giant
trophoblasts at 9.5 dpc and is expressed in the placenta through
15.5 dpc.
-!- SIMILARITY: Belongs to the 3-beta-HSD family. {ECO:0000305}.
-----------------------------------------------------------------------
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Distributed under the Creative Commons Attribution (CC BY 4.0) License
-----------------------------------------------------------------------
EMBL; AF031170; AAB84299.1; -; mRNA.
EMBL; AK142267; BAE25002.1; -; mRNA.
EMBL; AL606755; CAM13693.1; -; Genomic_DNA.
EMBL; CH466620; EDL38971.1; -; Genomic_DNA.
CCDS; CCDS17669.1; -.
RefSeq; NP_038849.2; NM_013821.3.
UniGene; Mm.14435; -.
ProteinModelPortal; O35469; -.
STRING; 10090.ENSMUSP00000029463; -.
iPTMnet; O35469; -.
PhosphoSitePlus; O35469; -.
MaxQB; O35469; -.
PaxDb; O35469; -.
PeptideAtlas; O35469; -.
PRIDE; O35469; -.
Ensembl; ENSMUST00000029463; ENSMUSP00000029463; ENSMUSG00000027869.
Ensembl; ENSMUST00000170847; ENSMUSP00000129911; ENSMUSG00000027869.
GeneID; 15497; -.
KEGG; mmu:15497; -.
UCSC; uc012cuq.1; mouse.
CTD; 15497; -.
MGI; MGI:109598; Hsd3b6.
eggNOG; KOG1430; Eukaryota.
eggNOG; COG0451; LUCA.
GeneTree; ENSGT00940000155444; -.
HOGENOM; HOG000167989; -.
HOVERGEN; HBG000014; -.
InParanoid; O35469; -.
KO; K00070; -.
OMA; YSYQPPF; -.
OrthoDB; EOG091G09QZ; -.
TreeFam; TF343138; -.
Reactome; R-MMU-193048; Androgen biosynthesis.
Reactome; R-MMU-193993; Mineralocorticoid biosynthesis.
Reactome; R-MMU-194002; Glucocorticoid biosynthesis.
UniPathway; UPA00062; -.
PRO; PR:O35469; -.
Proteomes; UP000000589; Chromosome 3.
Bgee; ENSMUSG00000027869; Expressed in 49 organ(s), highest expression level in testis.
Genevisible; O35469; MM.
GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0043231; C:intracellular membrane-bounded organelle; IBA:GO_Central.
GO; GO:0005743; C:mitochondrial inner membrane; ISO:MGI.
GO; GO:0005758; C:mitochondrial intermembrane space; ISO:MGI.
GO; GO:0003854; F:3-beta-hydroxy-delta5-steroid dehydrogenase activity; IBA:GO_Central.
GO; GO:0102294; F:cholesterol dehydrogenase activity; IEA:UniProtKB-EC.
GO; GO:0016491; F:oxidoreductase activity; IBA:GO_Central.
GO; GO:0016616; F:oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor; IBA:GO_Central.
GO; GO:0004769; F:steroid delta-isomerase activity; IEA:UniProtKB-EC.
GO; GO:0008207; P:C21-steroid hormone metabolic process; IBA:GO_Central.
GO; GO:0021766; P:hippocampus development; IBA:GO_Central.
GO; GO:0051412; P:response to corticosterone; IBA:GO_Central.
GO; GO:0006694; P:steroid biosynthetic process; IBA:GO_Central.
InterPro; IPR002225; 3Beta_OHSteriod_DH/Estase.
InterPro; IPR036291; NAD(P)-bd_dom_sf.
Pfam; PF01073; 3Beta_HSD; 1.
SUPFAM; SSF51735; SSF51735; 1.
1: Evidence at protein level;
Complete proteome; Endoplasmic reticulum; Isomerase; Membrane;
Mitochondrion; Multifunctional enzyme; NAD; Oxidoreductase;
Reference proteome; Steroidogenesis; Transmembrane;
Transmembrane helix.
CHAIN 1 373 3 beta-hydroxysteroid dehydrogenase/Delta
5-->4-isomerase type 6.
/FTId=PRO_0000087785.
TRANSMEM 288 308 Helical. {ECO:0000255}.
ACT_SITE 155 155 Proton acceptor. {ECO:0000250}.
BINDING 159 159 NAD. {ECO:0000250}.
CONFLICT 189 189 Y -> F (in Ref. 1; AAB84299).
{ECO:0000305}.
CONFLICT 366 366 E -> A (in Ref. 1; AAB84299).
{ECO:0000305}.
CONFLICT 371 371 K -> T (in Ref. 1; AAB84299).
{ECO:0000305}.
SEQUENCE 373 AA; 41977 MW; 10FE9278C5BDC534 CRC64;
MPGWSCLVTG AGGFLGQRIV QLLMQEKDLE EIRVLDKFFR PETREQFFNL DTNIKVTVLE
GDILDTQYLR KACQGISVVI HTAAVIDVTG VIPRQTILDV NLKGTQNLLE ACIQASVPAF
IFSSSVDVAG PNSYKEIILN GNEEEHHESI WSDPYPYSKK MAEKAVLAAN GSMLKIGGTL
HTCALRPMYI YGERSPFISN TIITALKNKN ILGCTGKFST ANPVYVGNVA WAHILAARGL
RDPKKSPNIQ GEFYYISDDT PHQSYDDLNY TLSKEWGFCP DSSWSLPVPL LYWLAFMLET
VSFLLSPIYR FIPPFNRHLV TLTGSTFTFS YKKAQRDLGY EPLVSWEEAK QKTSEWIGTL
VEQHRETLDT KSQ


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