Did you know ? If you order before Friday 14h we deliver 90PCT of the the time next Tuesday, GENTAUR another in time delivery

3-hydroxyacyl-CoA dehydrogenase type-2 (EC 1.1.1.35) (17-beta-hydroxysteroid dehydrogenase 10) (17-beta-HSD 10) (EC 1.1.1.51) (2-methyl-3-hydroxybutyryl-CoA dehydrogenase) (MHBD) (3-hydroxy-2-methylbutyryl-CoA dehydrogenase) (EC 1.1.1.178) (3-hydroxyacyl-CoA dehydrogenase type II) (Endoplasmic reticulum-associated amyloid beta-peptide-binding protein) (Mitochondrial ribonuclease P protein 2) (Mitochondrial RNase P protein 2) (Short chain dehydrogenase/reductase family 5C member 1) (Short-chain type dehydrogenase/reductase XH98G2) (Type II HADH)

 HCD2_HUMAN              Reviewed;         261 AA.
Q99714; Q5H927; Q6IBS9; Q8TCV9; Q96HD5;
01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
23-JAN-2007, sequence version 3.
23-MAY-2018, entry version 198.
RecName: Full=3-hydroxyacyl-CoA dehydrogenase type-2;
EC=1.1.1.35 {ECO:0000269|PubMed:12917011, ECO:0000269|PubMed:18996107, ECO:0000269|PubMed:25925575, ECO:0000269|PubMed:28888424, ECO:0000269|PubMed:9553139};
AltName: Full=17-beta-hydroxysteroid dehydrogenase 10;
Short=17-beta-HSD 10;
EC=1.1.1.51 {ECO:0000269|PubMed:12917011, ECO:0000269|PubMed:28888424};
AltName: Full=2-methyl-3-hydroxybutyryl-CoA dehydrogenase {ECO:0000303|PubMed:16148061};
Short=MHBD {ECO:0000303|PubMed:16148061};
AltName: Full=3-hydroxy-2-methylbutyryl-CoA dehydrogenase;
EC=1.1.1.178 {ECO:0000269|PubMed:12917011};
AltName: Full=3-hydroxyacyl-CoA dehydrogenase type II;
AltName: Full=Endoplasmic reticulum-associated amyloid beta-peptide-binding protein;
AltName: Full=Mitochondrial ribonuclease P protein 2;
Short=Mitochondrial RNase P protein 2;
AltName: Full=Short chain dehydrogenase/reductase family 5C member 1;
AltName: Full=Short-chain type dehydrogenase/reductase XH98G2;
AltName: Full=Type II HADH;
Name=HSD17B10; Synonyms=ERAB, HADH2, MRPP2, SCHAD, SDR5C1, XH98G2;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, AND TISSUE
SPECIFICITY.
TISSUE=Brain;
PubMed=9338779; DOI=10.1038/39522;
Yan S.D., Fu J., Soto C., Chen X., Zhu H., Al-Mohanna F.,
Collinson K., Zhu A., Stern E., Saido T., Tohyama M., Ogawa S.,
Roher A., Stern D.;
"An intracellular protein that binds amyloid-beta peptide and mediates
neurotoxicity in Alzheimer's disease.";
Nature 389:689-695(1997).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
Zhuchenko O.P., Wehnert M., Bailey J., Sun Z.S., Lee C.C.;
Submitted (JAN-1997) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
PubMed=9671743; DOI=10.1073/pnas.95.15.8709;
Miller A.P., Willard H.F.;
"Chromosomal basis of X chromosome inactivation: identification of a
multigene domain in Xp11.21-p11.22 that escapes X inactivation.";
Proc. Natl. Acad. Sci. U.S.A. 95:8709-8714(1998).
[4]
NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORM 1), FUNCTION, AND
CATALYTIC ACTIVITY.
TISSUE=Brain;
PubMed=9553139; DOI=10.1074/jbc.273.17.10741;
He X.Y., Schulz H., Yang S.Y.;
"A human brain L-3-hydroxyacyl-coenzyme A dehydrogenase is identical
to an amyloid beta-peptide-binding protein involved in Alzheimer's
disease.";
J. Biol. Chem. 273:10741-10746(1998).
[5]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
"Cloning of human full open reading frames in Gateway(TM) system entry
vector (pDONR201).";
Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15772651; DOI=10.1038/nature03440;
Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D.,
Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A.,
Lovell F.L., Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G.,
Jones M.C., Hurles M.E., Andrews T.D., Scott C.E., Searle S.,
Ramser J., Whittaker A., Deadman R., Carter N.P., Hunt S.E., Chen R.,
Cree A., Gunaratne P., Havlak P., Hodgson A., Metzker M.L.,
Richards S., Scott G., Steffen D., Sodergren E., Wheeler D.A.,
Worley K.C., Ainscough R., Ambrose K.D., Ansari-Lari M.A., Aradhya S.,
Ashwell R.I., Babbage A.K., Bagguley C.L., Ballabio A., Banerjee R.,
Barker G.E., Barlow K.F., Barrett I.P., Bates K.N., Beare D.M.,
Beasley H., Beasley O., Beck A., Bethel G., Blechschmidt K., Brady N.,
Bray-Allen S., Bridgeman A.M., Brown A.J., Brown M.J., Bonnin D.,
Bruford E.A., Buhay C., Burch P., Burford D., Burgess J., Burrill W.,
Burton J., Bye J.M., Carder C., Carrel L., Chako J., Chapman J.C.,
Chavez D., Chen E., Chen G., Chen Y., Chen Z., Chinault C.,
Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S.,
Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S.,
Corby N., Connor R.E., David R., Davies J., Davis C., Davis J.,
Delgado O., Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S.,
Draper H., Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I.,
Eades T., Ellwood M., Emery-Cohen A., Errington H., Evans K.L.,
Faulkner L., Francis F., Frankland J., Fraser A.E., Galgoczy P.,
Gilbert J., Gill R., Gloeckner G., Gregory S.G., Gribble S.,
Griffiths C., Grocock R., Gu Y., Gwilliam R., Hamilton C., Hart E.A.,
Hawes A., Heath P.D., Heitmann K., Hennig S., Hernandez J.,
Hinzmann B., Ho S., Hoffs M., Howden P.J., Huckle E.J., Hume J.,
Hunt P.J., Hunt A.R., Isherwood J., Jacob L., Johnson D., Jones S.,
de Jong P.J., Joseph S.S., Keenan S., Kelly S., Kershaw J.K., Khan Z.,
Kioschis P., Klages S., Knights A.J., Kosiura A., Kovar-Smith C.,
Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L., Liu W.,
Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D.,
Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H.,
McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T.,
Milne S., Miner G., Mistry S.L., Morgan M., Morris S., Mueller I.,
Mullikin J.C., Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N.,
Okwuonu G., Palmer S., Pandian R., Parker D., Parrish J.,
Pasternak S., Patel D., Pearce A.V., Pearson D.M., Pelan S.E.,
Perez L., Porter K.M., Ramsey Y., Reichwald K., Rhodes S.,
Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K.,
Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D.,
Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R.,
Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T.,
Teague B., Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S.,
Tromans A.C., d'Urso M., Verduzco D., Villasana D., Waldron L.,
Wall M., Wang Q., Warren J., Warry G.L., Wei X., West A.,
Whitehead S.L., Whiteley M.N., Wilkinson J.E., Willey D.L.,
Williams G., Williams L., Williamson A., Williamson H., Wilming L.,
Woodmansey R.L., Wray P.W., Yen J., Zhang J., Zhou J., Zoghbi H.,
Zorilla S., Buck D., Reinhardt R., Poustka A., Rosenthal A.,
Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F.,
Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A.,
Nelson D.L., Weinstock G., Sulston J.E., Durbin R.M., Hubbard T.,
Gibbs R.A., Beck S., Rogers J., Bentley D.R.;
"The DNA sequence of the human X chromosome.";
Nature 434:325-337(2005).
[7]
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.
[8]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
TISSUE=Brain, and Lung;
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).
[9]
NUCLEOTIDE SEQUENCE [MRNA] OF 51-246.
Deininger M.H., Meyermann R., Schluesener H.J.;
"Expression, release and induction of endoplasmic reticulum-associated
amyloid beta-binding protein in brain disease.";
Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
[10]
FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND
SUBCELLULAR LOCATION.
PubMed=12917011; DOI=10.1042/BJ20030877;
Shafqat N., Marschall H.U., Filling C., Nordling E., Wu X.Q.,
Bjork L., Thyberg J., Martensson E., Salim S., Jornvall H.,
Oppermann U.;
"Expanded substrate screenings of human and Drosophila type 10 17beta-
hydroxysteroid dehydrogenases (HSDs) reveal multiple specificities in
bile acid and steroid hormone metabolism: characterization of
multifunctional 3alpha/7alpha/7beta/17beta/20beta/21-HSD.";
Biochem. J. 376:49-60(2003).
[11]
INVOLVEMENT IN HSD10MD.
PubMed=17236142; DOI=10.1086/511527;
Lenski C., Kooy R.F., Reyniers E., Loessner D., Wanders R.J.A.,
Winnepenninckx B., Hellebrand H., Engert S., Schwartz C.E., Meindl A.,
Ramser J.;
"The reduced expression of the HADH2 protein causes X-linked mental
retardation, choreoathetosis, and abnormal behavior.";
Am. J. Hum. Genet. 80:372-377(2007).
[12]
INVOLVEMENT IN MRX17.
PubMed=18252223; DOI=10.1016/j.ajhg.2007.11.002;
Froyen G., Corbett M., Vandewalle J., Jarvela I., Lawrence O.,
Meldrum C., Bauters M., Govaerts K., Vandeleur L., Van Esch H.,
Chelly J., Sanlaville D., van Bokhoven H., Ropers H.-H.,
Laumonnier F., Ranieri E., Schwartz C.E., Abidi F., Tarpey P.S.,
Futreal P.A., Whibley A., Raymond F.L., Stratton M.R., Fryns J.-P.,
Scott R., Peippo M., Sipponen M., Partington M., Mowat D., Field M.,
Hackett A., Marynen P., Turner G., Gecz J.;
"Submicroscopic duplications of the hydroxysteroid dehydrogenase
HSD17B10 and the E3 ubiquitin ligase HUWE1 are associated with mental
retardation.";
Am. J. Hum. Genet. 82:432-443(2008).
[13]
IDENTIFICATION BY MASS SPECTROMETRY, FUNCTION, INTERACTION WITH
KIAA0391 AND TRMT10C, AND SUBCELLULAR LOCATION.
PubMed=18984158; DOI=10.1016/j.cell.2008.09.013;
Holzmann J., Frank P., Loeffler E., Bennett K.L., Gerner C.,
Rossmanith W.;
"RNase P without RNA: identification and functional reconstitution of
the human mitochondrial tRNA processing enzyme.";
Cell 135:462-474(2008).
[14]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[15]
FUNCTION, INTERACTION WITH TRMT10C, AND MUTAGENESIS OF SER-20 AND
LYS-172.
PubMed=23042678; DOI=10.1093/nar/gks910;
Vilardo E., Nachbagauer C., Buzet A., Taschner A., Holzmann J.,
Rossmanith W.;
"A subcomplex of human mitochondrial RNase P is a bifunctional
methyltransferase--extensive moonlighting in mitochondrial tRNA
biogenesis.";
Nucleic Acids Res. 40:11583-11593(2012).
[16]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[17]
INVOLVEMENT IN HSD10MD.
PubMed=25575635; DOI=10.1016/j.mito.2014.12.005;
Chatfield K.C., Coughlin C.R. II, Friederich M.W., Gallagher R.C.,
Hesselberth J.R., Lovell M.A., Ofman R., Swanson M.A., Thomas J.A.,
Wanders R.J., Wartchow E.P., Van Hove J.L.;
"Mitochondrial energy failure in HSD10 disease is due to defective
mtDNA transcript processing.";
Mitochondrion 21:1-10(2015).
[18]
ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=25944712; DOI=10.1002/pmic.201400617;
Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M.,
Ayoub D., Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
"N-terminome analysis of the human mitochondrial proteome.";
Proteomics 15:2519-2524(2015).
[19]
FUNCTION, AND INTERACTION WITH TRMT10C.
PubMed=29040705; DOI=10.1093/nar/gkx902;
Reinhard L., Sridhara S., Haellberg B.M.;
"The MRPP1/MRPP2 complex is a tRNA-maturation platform in human
mitochondria.";
Nucleic Acids Res. 45:12469-12480(2017).
[20]
X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) IN COMPLEX WITH NAD.
PubMed=15342248; DOI=10.1016/j.jmb.2004.07.071;
Kissinger C.R., Rejto P.A., Pelletier L.A., Thomson J.A.,
Showalter R.E., Abreo M.A., Agree C.S., Margosiak S., Meng J.J.,
Aust R.M., Vanderpool D., Li B., Tempczyk-Russell A.,
Villafranca J.E.;
"Crystal structure of human ABAD/HSD10 with a bound inhibitor:
implications for design of Alzheimer's disease therapeutics.";
J. Mol. Biol. 342:943-952(2004).
[21]
X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS).
PubMed=15087549; DOI=10.1126/science.1091230;
Lustbader J.W., Cirilli M., Lin C., Xu H.W., Takuma K., Wang N.,
Caspersen C., Chen X., Pollak S., Chaney M., Trinchese F., Liu S.,
Gunn-Moore F., Lue L.-F., Walker D.G., Kuppusamy P., Zewier Z.L.,
Arancio O., Stern D., Yan S.-S., Wu H.;
"ABAD directly links Abeta to mitochondrial toxicity in Alzheimer's
disease.";
Science 304:448-452(2004).
[22]
X-RAY CRYSTALLOGRAPHY (1.20 ANGSTROMS), FUNCTION, SUBUNIT, VARIANTS
HSD10MD GLY-86; CYS-130 AND HIS-165, AND CHARACTERIZATION OF VARIANTS
HSD10MD GLY-86; CYS-130 AND HIS-165.
PubMed=20077426; DOI=10.1002/emmm.200900055;
Rauschenberger K., Schoeler K., Sass J.O., Sauer S., Djuric Z.,
Rumig C., Wolf N.I., Okun J.G., Koelker S., Schwarz H., Fischer C.,
Grziwa B., Runz H., Nuemann A., Shafqat N., Kavanagh K.L.,
Haemmerling G., Wanders R.J., Shield J.P., Wendel U., Stern D.,
Nawroth P., Hoffmann G.F., Bartram C.R., Arnold B., Bierhaus A.,
Oppermann U., Steinbeisser H., Zschocke J.;
"A non-enzymatic function of 17beta-hydroxysteroid dehydrogenase type
10 is required for mitochondrial integrity and cell survival.";
EMBO Mol. Med. 2:51-62(2010).
[23]
VARIANTS HSD10MD VAL-122 AND CYS-130.
PubMed=12696021; DOI=10.1086/375116;
Ofman R., Ruiter J.P.N., Feenstra M., Duran M., Poll-The B.T.,
Zschocke J., Ensenauer R., Lehnert W., Sass J.O., Sperl W.,
Wanders R.J.A.;
"2-methyl-3-hydroxybutyryl-CoA dehydrogenase deficiency is caused by
mutations in the HADH2 gene.";
Am. J. Hum. Genet. 72:1300-1307(2003).
[24]
VARIANTS HSD10MD CYS-130 AND SER-247, AND CHARACTERIZATION OF VARIANT
HSD10MD SER-247.
PubMed=16148061; DOI=10.1203/01.pdr.0000176916.94328.cd;
Perez-Cerda C., Garcia-Villoria J., Ofman R., Sala P.R., Merinero B.,
Ramos J., Garcia-Silva M.T., Beseler B., Dalmau J., Wanders R.J.A.,
Ugarte M., Ribes A.;
"2-methyl-3-hydroxybutyryl-CoA dehydrogenase (MHBD) deficiency: an X-
linked inborn error of isoleucine metabolism that may mimic a
mitochondrial disease.";
Pediatr. Res. 58:488-491(2005).
[25]
ERRATUM.
Perez-Cerda C., Garcia-Villoria J., Ofman R., Sala P.R., Merinero B.,
Ramos J., Garcia-Silva M.T., Beseler B., Dalmau J., Wanders R.J.,
Ugarte M., Ribes A.;
Pediatr. Res. 59:162-162(2006).
[26]
VARIANTS HSD10MD CYS-130; SER-210; GLN-226 AND SER-247, FUNCTION, AND
CATALYTIC ACTIVITY.
PubMed=18996107; DOI=10.1016/j.clinbiochem.2008.10.006;
Garcia-Villoria J., Navarro-Sastre A., Fons C., Perez-Cerda C.,
Baldellou A., Fuentes-Castello M.A., Gonzalez I.,
Hernandez-Gonzalez A., Fernandez C., Campistol J., Delpiccolo C.,
Cortes N., Messeguer A., Briones P., Ribes A.;
"Study of patients and carriers with 2-methyl-3-hydroxybutyryl-CoA
dehydrogenase (MHBD) deficiency: difficulties in the diagnosis.";
Clin. Biochem. 42:27-33(2009).
[27]
VARIANTS HSD10MD CYS-130 AND GLN-249, AND CHARACTERIZATION OF VARIANTS
HSD10MD CYS-130 AND GLN-249.
PubMed=19706438; DOI=10.1073/pnas.0902377106;
Yang S.Y., He X.Y., Olpin S.E., Sutton V.R., McMenamin J., Philipp M.,
Denman R.B., Malik M.;
"Mental retardation linked to mutations in the HSD17B10 gene
interfering with neurosteroid and isoleucine metabolism.";
Proc. Natl. Acad. Sci. U.S.A. 106:14820-14824(2009).
[28]
VARIANT HSD10MD ALA-65.
PubMed=22132097; DOI=10.1371/journal.pone.0027348;
Seaver L.H., He X.Y., Abe K., Cowan T., Enns G.M., Sweetman L.,
Philipp M., Lee S., Malik M., Yang S.Y.;
"A novel mutation in the HSD17B10 gene of a 10-year-old boy with
refractory epilepsy, choreoathetosis and learning disability.";
PLoS ONE 6:E27348-E27348(2011).
[29]
VARIANTS HSD10MD CYS-130 AND HIS-165, CHARACTERIZATION OF VARIANT
HSD10MD CYS-130, AND FUNCTION.
PubMed=24549042; DOI=10.1093/hmg/ddu072;
Deutschmann A.J., Amberger A., Zavadil C., Steinbeisser H., Mayr J.A.,
Feichtinger R.G., Oerum S., Yue W.W., Zschocke J.;
"Mutation or knock-down of 17beta-hydroxysteroid dehydrogenase type 10
cause loss of MRPP1 and impaired processing of mitochondrial heavy
strand transcripts.";
Hum. Mol. Genet. 23:3618-3628(2014).
[30]
VARIANTS HSD10MD CYS-130; SER-210; GLN-226 AND SER-247, FUNCTION,
CATALYTIC ACTIVITY, SUBUNIT, MUTAGENESIS OF LYS-172, AND
CHARACTERIZATION OF VARIANTS HSD10MD CYS-130; SER-210; GLN-226 AND
SER-247.
PubMed=25925575; DOI=10.1093/nar/gkv408;
Vilardo E., Rossmanith W.;
"Molecular insights into HSD10 disease: impact of SDR5C1 mutations on
the human mitochondrial RNase P complex.";
Nucleic Acids Res. 43:5112-5119(2015).
[31]
VARIANT HSD10MD GLU-212, FUNCTION, INTERACTION WITH TRMT10C, AND
CHARACTERIZATION OF VARIANT HSD10MD GLU-212.
PubMed=26950678; DOI=10.1080/15476286.2016.1159381;
Falk M.J., Gai X., Shigematsu M., Vilardo E., Takase R., McCormick E.,
Christian T., Place E., Pierce E.A., Consugar M., Gamper H.B.,
Rossmanith W., Hou Y.M.;
"A novel HSD17B10 mutation impairing the activities of the
mitochondrial RNase P complex causes X-linked intractable epilepsy and
neurodevelopmental regression.";
RNA Biol. 13:477-485(2016).
[32]
VARIANTS HSD10MD LEU-12 AND MET-176, FUNCTION, CATALYTIC ACTIVITY,
BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, AND CHARACTERIZATION OF
VARIANTS HSD10MD LEU-12 AND MET-176.
PubMed=28888424; DOI=10.1016/j.bbadis.2017.09.002;
Oerum S., Roovers M., Leichsenring M., Acquaviva-Bourdain C.,
Beermann F., Gemperle-Britschgi C., Fouilhoux A., Korwitz-Reichelt A.,
Bailey H.J., Droogmans L., Oppermann U., Sass J.O., Yue W.W.;
"Novel patient missense mutations in the HSD17B10 gene affect
dehydrogenase and mitochondrial tRNA modification functions of the
encoded protein.";
Biochim. Biophys. Acta 1863:3294-3302(2017).
-!- FUNCTION: Mitochondrial dehydrogenase that catalyzes the beta-
oxidation at position 17 of androgens and estrogens and has 3-
alpha-hydroxysteroid dehydrogenase activity with androsterone
(PubMed:9553139, PubMed:23042678, PubMed:12917011,
PubMed:18996107, PubMed:25925575, PubMed:28888424). Catalyzes the
third step in the beta-oxidation of fatty acids (PubMed:9553139,
PubMed:12917011, PubMed:18996107, PubMed:25925575,
PubMed:28888424). Carries out oxidative conversions of 7-alpha-OH
and 7-beta-OH bile acids (PubMed:12917011). Also exhibits 20-beta-
OH and 21-OH dehydrogenase activities with C21 steroids
(PubMed:12917011). By interacting with intracellular amyloid-beta,
it may contribute to the neuronal dysfunction associated with
Alzheimer disease (AD) (PubMed:9338779). Essential for structural
and functional integrity of mitochondria (PubMed:20077426).
{ECO:0000269|PubMed:12917011, ECO:0000269|PubMed:18996107,
ECO:0000269|PubMed:20077426, ECO:0000269|PubMed:23042678,
ECO:0000269|PubMed:25925575, ECO:0000269|PubMed:26950678,
ECO:0000269|PubMed:28888424, ECO:0000269|PubMed:9338779,
ECO:0000269|PubMed:9553139}.
-!- FUNCTION: In addition to mitochondrial dehydrogenase activity,
moonlights as a component of mitochondrial ribonuclease P, a
complex that cleaves tRNA molecules in their 5'-ends
(PubMed:18984158, PubMed:24549042, PubMed:25925575,
PubMed:26950678, PubMed:28888424). Together with HSD17B10/MRPP2,
forms a subcomplex of the mitochondrial ribonuclease P, named
MRPP1-MRPP2 subcomplex, which displays functions that are
independent of the ribonuclease P activity (PubMed:23042678,
PubMed:29040705). The MRPP1-MRPP2 subcomplex catalyzes the
formation of N(1)-methylguanine and N(1)-methyladenine at position
9 (m1G9 and m1A9, respectively) in tRNAs; HSD17B10/MRPP2 acting as
a non-catalytic subunit (PubMed:23042678, PubMed:25925575,
PubMed:28888424). The MRPP1-MRPP2 subcomplex also acts as a tRNA
maturation platform: following 5'-end cleavage by the
mitochondrial ribonuclease P complex, the MRPP1-MRPP2 subcomplex
enhances the efficiency of 3'-processing catalyzed by ELAC2,
retains the tRNA product after ELAC2 processing and presents the
nascent tRNA to the mitochondrial CCA tRNA nucleotidyltransferase
TRNT1 enzyme (PubMed:29040705). {ECO:0000269|PubMed:18984158,
ECO:0000269|PubMed:23042678, ECO:0000269|PubMed:24549042,
ECO:0000269|PubMed:25925575, ECO:0000269|PubMed:26950678,
ECO:0000269|PubMed:28888424, ECO:0000269|PubMed:29040705}.
-!- CATALYTIC ACTIVITY: (2S,3S)-3-hydroxy-2-methylbutanoyl-CoA +
NAD(+) = 2-methylacetoacetyl-CoA + NADH.
{ECO:0000269|PubMed:12917011}.
-!- CATALYTIC ACTIVITY: Testosterone + NAD(P)(+) = androst-4-ene-3,17-
dione + NAD(P)H. {ECO:0000269|PubMed:12917011,
ECO:0000269|PubMed:28888424}.
-!- CATALYTIC ACTIVITY: (S)-3-hydroxyacyl-CoA + NAD(+) = 3-oxoacyl-CoA
+ NADH. {ECO:0000269|PubMed:12917011, ECO:0000269|PubMed:18996107,
ECO:0000269|PubMed:25925575, ECO:0000269|PubMed:28888424,
ECO:0000269|PubMed:9553139}.
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Kinetic parameters:
KM=25.7 uM for acetoacetyl-CoA (in the presence of 0.2 mM NADH,
at pH 7.0 and 25 degrees Celsius) {ECO:0000269|PubMed:12917011};
KM=85.2 uM for beta-hydroxybutyryl-CoA (in the presence of 1 mM
NAD, at pH 9.3 and 25 degrees Celsius)
{ECO:0000269|PubMed:12917011};
KM=41 uM for androsterone (in the presence of 1 mM NAD, at pH
9.3 and 25 degrees Celsius) {ECO:0000269|PubMed:12917011};
KM=5 uM for 5-alpha-pregnan-20-beta-ol-3-one (in the presence of
1 mM NAD, at pH 9.3 and 25 degrees Celsius)
{ECO:0000269|PubMed:12917011};
KM=219 uM for isoursodeoxycholic acid (in the presence of 1 mM
NAD, at pH 9.3 and 25 degrees Celsius)
{ECO:0000269|PubMed:12917011};
KM=36.4 uM for chenodeoxycholic acid (in the presence of 1 mM
NAD, at pH 9.3 and 25 degrees Celsius)
{ECO:0000269|PubMed:12917011};
KM=1.7 uM for dehydrocorticosterone (in the presence of 1 mM
NAD, at pH 9.3 and 25 degrees Celsius)
{ECO:0000269|PubMed:12917011};
KM=30.6 uM for NADH (in the presence of acetoacetyl-CoA, at pH
7.0 and 25 degrees Celsius) {ECO:0000269|PubMed:12917011};
KM=42.3 uM for NAD (in the presence of beta-hydroxybutyryl-CoA,
at pH 9.3 and 25 degrees Celsius) {ECO:0000269|PubMed:12917011};
KM=69 uM for for DL-3-hydroxybutyryl-CoA
{ECO:0000269|PubMed:28888424};
KM=7.7 uM for for allopregnanolone
{ECO:0000269|PubMed:28888424};
Note=Kcat is 458 min(-1) for DL-3-hydroxybutyryl-CoA
(PubMed:28888424). Kcat is 706 min(-1) for allopregnanolone
(PubMed:28888424). {ECO:0000269|PubMed:28888424};
pH dependence:
Optimum pH is 9.3 for the dehydrogenase reaction at 25 degrees
Celsius, and 7.0 for the reductase reaction at 25 degrees
Celsius. {ECO:0000269|PubMed:12917011};
-!- SUBUNIT: Homotetramer (PubMed:15342248, PubMed:20077426,
PubMed:25925575). Component of mitochondrial ribonuclease P, a
complex composed of TRMT10C/MRPP1, HSD17B10/MRPP2 and MRPP31
(PubMed:18984158, PubMed:25925575, PubMed:26950678,
PubMed:28888424). Interacts with TRMT10C/MRPP1; forming the MRPP1-
MRPP2 subcomplex of the mitochondrial ribonuclease P complex
(PubMed:23042678, PubMed:29040705). {ECO:0000269|PubMed:15342248,
ECO:0000269|PubMed:18984158, ECO:0000269|PubMed:20077426,
ECO:0000269|PubMed:23042678, ECO:0000269|PubMed:25925575,
ECO:0000269|PubMed:26950678, ECO:0000269|PubMed:28888424,
ECO:0000269|PubMed:29040705}.
-!- INTERACTION:
P05067:APP; NbExp=4; IntAct=EBI-79964, EBI-77613;
Q7L0Y3:TRMT10C; NbExp=4; IntAct=EBI-79964, EBI-2107046;
-!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:12917011,
ECO:0000269|PubMed:18984158}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=Q99714-1; Sequence=Displayed;
Name=2;
IsoId=Q99714-2; Sequence=VSP_007830;
Note=No experimental confirmation available.;
-!- TISSUE SPECIFICITY: Ubiquitously expressed in normal tissues but
is overexpressed in neurons affected in AD.
{ECO:0000269|PubMed:9338779}.
-!- DISEASE: HDS10 mitochondrial disease (HSD10MD) [MIM:300438]: An X-
linked multisystemic disorder with highly variable severity. Age
at onset ranges from the neonatal period to early childhood.
Features include progressive neurodegeneration, psychomotor
retardation, loss of mental and motor skills, seizures,
cardiomyopathy, and visual and hearing impairment. Some patients
manifest lactic acidosis and metabolic acidosis.
{ECO:0000269|PubMed:12696021, ECO:0000269|PubMed:16148061,
ECO:0000269|PubMed:17236142, ECO:0000269|PubMed:18996107,
ECO:0000269|PubMed:19706438, ECO:0000269|PubMed:20077426,
ECO:0000269|PubMed:22132097, ECO:0000269|PubMed:24549042,
ECO:0000269|PubMed:25575635, ECO:0000269|PubMed:25925575,
ECO:0000269|PubMed:26950678, ECO:0000269|PubMed:28888424}.
Note=The disease is caused by mutations affecting the gene
represented in this entry.
-!- DISEASE: Mental retardation, X-linked 17 (MRX17) [MIM:300705]: A
disorder characterized by significantly below average general
intellectual functioning associated with impairments in adaptive
behavior and manifested during the developmental period.
Intellectual deficiency is the only primary symptom of non-
syndromic X-linked mental retardation, while syndromic mental
retardation presents with associated physical, neurological and/or
psychiatric manifestations. {ECO:0000269|PubMed:18252223}.
Note=The gene represented in this entry is involved in disease
pathogenesis. A chromosomal microduplication involving HSD17B10
and HUWE1 has been found in patients with mental retardation.
-!- SIMILARITY: Belongs to the short-chain dehydrogenases/reductases
(SDR) family. {ECO:0000305}.
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; U96132; AAC51812.1; -; mRNA.
EMBL; U73514; AAB68958.1; -; mRNA.
EMBL; AF069134; AAC39900.1; -; mRNA.
EMBL; AF035555; AAC15902.1; -; mRNA.
EMBL; AF037438; AAC16419.1; -; Genomic_DNA.
EMBL; CR456723; CAG33004.1; -; mRNA.
EMBL; Z97054; CAI42652.1; -; Genomic_DNA.
EMBL; Z97054; CAI42653.1; -; Genomic_DNA.
EMBL; CH471154; EAW93157.1; -; Genomic_DNA.
EMBL; CH471154; EAW93158.1; -; Genomic_DNA.
EMBL; BC000372; AAH00372.1; -; mRNA.
EMBL; BC008708; AAH08708.1; -; mRNA.
EMBL; AY092415; AAM18189.1; -; mRNA.
CCDS; CCDS14354.1; -. [Q99714-1]
CCDS; CCDS35300.1; -. [Q99714-2]
RefSeq; NP_001032900.1; NM_001037811.2. [Q99714-2]
RefSeq; NP_004484.1; NM_004493.2. [Q99714-1]
UniGene; Hs.171280; -.
PDB; 1F67; Model; -; A=1-261.
PDB; 1SO8; X-ray; 2.30 A; A=1-261.
PDB; 1U7T; X-ray; 2.00 A; A/B/C/D=1-261.
PDB; 2O23; X-ray; 1.20 A; A/B=1-261.
PDBsum; 1F67; -.
PDBsum; 1SO8; -.
PDBsum; 1U7T; -.
PDBsum; 2O23; -.
ProteinModelPortal; Q99714; -.
SMR; Q99714; -.
BioGrid; 109278; 381.
IntAct; Q99714; 33.
MINT; Q99714; -.
STRING; 9606.ENSP00000168216; -.
BindingDB; Q99714; -.
ChEMBL; CHEMBL4159; -.
DrugBank; DB00157; NADH.
SwissLipids; SLP:000000787; -.
iPTMnet; Q99714; -.
PhosphoSitePlus; Q99714; -.
SwissPalm; Q99714; -.
BioMuta; HSD17B10; -.
DMDM; 2492759; -.
REPRODUCTION-2DPAGE; IPI00017726; -.
REPRODUCTION-2DPAGE; Q99714; -.
UCD-2DPAGE; Q99714; -.
EPD; Q99714; -.
MaxQB; Q99714; -.
PaxDb; Q99714; -.
PeptideAtlas; Q99714; -.
PRIDE; Q99714; -.
TopDownProteomics; Q99714-1; -. [Q99714-1]
TopDownProteomics; Q99714-2; -. [Q99714-2]
DNASU; 3028; -.
Ensembl; ENST00000168216; ENSP00000168216; ENSG00000072506. [Q99714-1]
Ensembl; ENST00000375304; ENSP00000364453; ENSG00000072506. [Q99714-2]
GeneID; 3028; -.
KEGG; hsa:3028; -.
UCSC; uc004dsl.2; human. [Q99714-1]
CTD; 3028; -.
DisGeNET; 3028; -.
EuPathDB; HostDB:ENSG00000072506.12; -.
GeneCards; HSD17B10; -.
HGNC; HGNC:4800; HSD17B10.
HPA; HPA001432; -.
MalaCards; HSD17B10; -.
MIM; 300256; gene.
MIM; 300438; phenotype.
MIM; 300705; phenotype.
neXtProt; NX_Q99714; -.
OpenTargets; ENSG00000072506; -.
Orphanet; 85295; HSD10 disease, atypical type.
Orphanet; 391428; HSD10 disease, infantile type.
Orphanet; 391457; HSD10 disease, neonatal type.
PharmGKB; PA162391638; -.
eggNOG; KOG1199; Eukaryota.
eggNOG; ENOG410XNNW; LUCA.
GeneTree; ENSGT00910000144076; -.
HOVERGEN; HBG002145; -.
InParanoid; Q99714; -.
KO; K08683; -.
OMA; LMGLVNC; -.
OrthoDB; EOG091G0G9O; -.
PhylomeDB; Q99714; -.
TreeFam; TF354307; -.
BioCyc; MetaCyc:HS01071-MONOMER; -.
BRENDA; 1.1.1.178; 2681.
BRENDA; 1.1.1.35; 2681.
Reactome; R-HSA-6785470; tRNA processing in the mitochondrion.
Reactome; R-HSA-6787450; tRNA modification in the mitochondrion.
Reactome; R-HSA-70895; Branched-chain amino acid catabolism.
Reactome; R-HSA-8868766; rRNA processing in the mitochondrion.
SABIO-RK; Q99714; -.
ChiTaRS; HSD17B10; human.
EvolutionaryTrace; Q99714; -.
GeneWiki; HSD17B10; -.
GenomeRNAi; 3028; -.
PRO; PR:Q99714; -.
Proteomes; UP000005640; Chromosome X.
Bgee; ENSG00000072506; -.
CleanEx; HS_HSD17B10; -.
ExpressionAtlas; Q99714; baseline and differential.
Genevisible; Q99714; HS.
GO; GO:0005737; C:cytoplasm; TAS:ProtInc.
GO; GO:0005759; C:mitochondrial matrix; TAS:Reactome.
GO; GO:0030678; C:mitochondrial ribonuclease P complex; IDA:UniProtKB.
GO; GO:0005739; C:mitochondrion; IDA:CAFA.
GO; GO:0005886; C:plasma membrane; TAS:ProtInc.
GO; GO:0047015; F:3-hydroxy-2-methylbutyryl-CoA dehydrogenase activity; IEA:UniProtKB-EC.
GO; GO:0003857; F:3-hydroxyacyl-CoA dehydrogenase activity; IDA:UniProtKB.
GO; GO:0008709; F:cholate 7-alpha-dehydrogenase activity; TAS:ProtInc.
GO; GO:0003723; F:RNA binding; HDA:UniProtKB.
GO; GO:0030283; F:testosterone dehydrogenase [NAD(P)] activity; IDA:UniProtKB.
GO; GO:0000049; F:tRNA binding; IDA:UniProtKB.
GO; GO:0009083; P:branched-chain amino acid catabolic process; TAS:Reactome.
GO; GO:0006629; P:lipid metabolic process; TAS:ProtInc.
GO; GO:1990180; P:mitochondrial tRNA 3'-end processing; IDA:UniProtKB.
GO; GO:0097745; P:mitochondrial tRNA 5'-end processing; IDA:UniProtKB.
GO; GO:0070901; P:mitochondrial tRNA methylation; IDA:UniProtKB.
GO; GO:0090646; P:mitochondrial tRNA processing; TAS:Reactome.
GO; GO:0007005; P:mitochondrion organization; IMP:UniProtKB.
GO; GO:0051289; P:protein homotetramerization; IDA:UniProtKB.
InterPro; IPR036291; NAD(P)-bd_dom_sf.
InterPro; IPR020904; Sc_DH/Rdtase_CS.
InterPro; IPR002347; SDR_fam.
Pfam; PF00106; adh_short; 1.
PRINTS; PR00081; GDHRDH.
PRINTS; PR00080; SDRFAMILY.
SUPFAM; SSF51735; SSF51735; 1.
PROSITE; PS00061; ADH_SHORT; 1.
1: Evidence at protein level;
3D-structure; Acetylation; Alternative splicing;
Chromosomal rearrangement; Complete proteome; Disease mutation;
Mental retardation; Mitochondrion; NAD; Neurodegeneration;
Oxidoreductase; Reference proteome; tRNA processing.
INIT_MET 1 1 Removed. {ECO:0000244|PubMed:25944712}.
CHAIN 2 261 3-hydroxyacyl-CoA dehydrogenase type-2.
/FTId=PRO_0000054810.
NP_BIND 12 41 NAD. {ECO:0000269|PubMed:15342248}.
ACT_SITE 168 168 Proton acceptor.
{ECO:0000269|PubMed:15087549}.
BINDING 155 155 Substrate. {ECO:0000269|PubMed:15087549}.
BINDING 172 172 NAD. {ECO:0000269|PubMed:15342248}.
MOD_RES 2 2 N-acetylalanine.
{ECO:0000244|PubMed:25944712}.
MOD_RES 53 53 N6-acetyllysine; alternate.
{ECO:0000250|UniProtKB:O08756}.
MOD_RES 53 53 N6-succinyllysine; alternate.
{ECO:0000250|UniProtKB:O08756}.
MOD_RES 69 69 N6-acetyllysine.
{ECO:0000250|UniProtKB:O08756}.
MOD_RES 99 99 N6-acetyllysine.
{ECO:0000250|UniProtKB:O08756}.
MOD_RES 105 105 N6-acetyllysine.
{ECO:0000250|UniProtKB:O08756}.
MOD_RES 212 212 N6-acetyllysine; alternate.
{ECO:0000250|UniProtKB:O08756}.
MOD_RES 212 212 N6-succinyllysine; alternate.
{ECO:0000250|UniProtKB:O08756}.
VAR_SEQ 191 199 Missing (in isoform 2).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_007830.
VARIANT 12 12 V -> L (in HSD10MD; decreased
dehydrogenase activity; decreased tRNA
methylation; decreased mitochondrial tRNA
5'-end processing).
{ECO:0000269|PubMed:28888424}.
/FTId=VAR_080049.
VARIANT 65 65 V -> A (in HSD10MD; unknown pathological
significance; dbSNP:rs104886492).
{ECO:0000269|PubMed:22132097}.
/FTId=VAR_078863.
VARIANT 86 86 D -> G (in HSD10MD; decreased 3-hydroxy-
2-methylbutyryl-CoA dehydrogenase
activity; no effect on NAD+ binding;
dbSNP:rs587777651).
{ECO:0000269|PubMed:20077426}.
/FTId=VAR_078864.
VARIANT 122 122 L -> V (in HSD10MD; dbSNP:rs28935476).
{ECO:0000269|PubMed:12696021}.
/FTId=VAR_015987.
VARIANT 130 130 R -> C (in HSD10MD; decreased stability;
decreased 3-hydroxy-2-methylbutyryl-CoA
dehydrogenase activity; decreased
mitochondrial tRNA 5'-end processing;
decreased tRNA methylation; does not
affect homotetramerization;
dbSNP:rs28935475).
{ECO:0000269|PubMed:12696021,
ECO:0000269|PubMed:16148061,
ECO:0000269|PubMed:18996107,
ECO:0000269|PubMed:19706438,
ECO:0000269|PubMed:20077426,
ECO:0000269|PubMed:24549042,
ECO:0000269|PubMed:25925575}.
/FTId=VAR_015988.
VARIANT 165 165 Q -> H (in HSD10MD; loss of 3-hydroxy-2-
methylbutyryl-CoA dehydrogenase activity;
does not bind NAD+).
{ECO:0000269|PubMed:20077426,
ECO:0000269|PubMed:24549042}.
/FTId=VAR_078865.
VARIANT 176 176 V -> M (in HSD10MD; decreased
dehydrogenase activity; strongly
decreased tRNA methylation; strongly
decreased mitochondrial tRNA 5'-end
processing).
{ECO:0000269|PubMed:28888424}.
/FTId=VAR_080050.
VARIANT 210 210 P -> S (in HSD10MD; decreased 3-
hydroxyacyl-CoA dehydrogenase activity;
decreased mitochondrial tRNA 5'-end
processing; decreased tRNA methylation;
does not affect homotetramerization).
{ECO:0000269|PubMed:18996107,
ECO:0000269|PubMed:25925575}.
/FTId=VAR_080051.
VARIANT 212 212 K -> E (in HSD10MD; 4-fold decrease of 3-
hydroxyacyl-CoA dehydrogenase; decreased
interaction with TRMT10C; decreased
function in mitochondrial tRNA
methylation; decreased function in
mitochondrial tRNA processing;
dbSNP:rs886041974).
{ECO:0000269|PubMed:26950678}.
/FTId=VAR_078866.
VARIANT 226 226 R -> Q (in HSD10MD; strongly decreased 3-
hydroxyacyl-CoA dehydrogenase activity;
abolished mitochondrial tRNA 5'-end
processing; abolished tRNA methylation;
impaired homotetramerization).
{ECO:0000269|PubMed:18996107,
ECO:0000269|PubMed:25925575}.
/FTId=VAR_080052.
VARIANT 247 247 N -> S (in HSD10MD; strongly decreased 3-
hydroxyacyl-CoA dehydrogenase activity;
abolished mitochondrial tRNA 5'-end
processing; abolished tRNA methylation;
impaired homotetramerization;
dbSNP:rs122461163).
{ECO:0000269|PubMed:16148061,
ECO:0000269|PubMed:18996107,
ECO:0000269|PubMed:25925575}.
/FTId=VAR_032093.
VARIANT 249 249 E -> Q (in HSD10MD; decreased 3-hydroxy-
2-methylbutyryl-CoA dehydrogenase
activity; dbSNP:rs62626305).
{ECO:0000269|PubMed:19706438}.
/FTId=VAR_078867.
MUTAGEN 20 20 S->F: Decreased dehydrogenase activity.
Does not affect mitochondrial tRNA 5'-end
processing. Does not affect tRNA
methylation.
{ECO:0000269|PubMed:23042678,
ECO:0000269|PubMed:25925575}.
MUTAGEN 172 172 K->A: Abolishes dehydrogenase activity.
Does not affect mitochondrial tRNA 5'-end
processing. Does not affect tRNA
methylation. Does not affect
homotetramerization.
{ECO:0000269|PubMed:23042678,
ECO:0000269|PubMed:25925575}.
STRAND 12 16 {ECO:0000244|PDB:2O23}.
TURN 17 19 {ECO:0000244|PDB:2O23}.
HELIX 21 32 {ECO:0000244|PDB:2O23}.
STRAND 36 41 {ECO:0000244|PDB:2O23}.
HELIX 47 54 {ECO:0000244|PDB:2O23}.
STRAND 58 62 {ECO:0000244|PDB:2O23}.
HELIX 68 82 {ECO:0000244|PDB:2O23}.
STRAND 87 90 {ECO:0000244|PDB:2O23}.
STRAND 100 102 {ECO:0000244|PDB:2O23}.
TURN 103 106 {ECO:0000244|PDB:2O23}.
HELIX 111 121 {ECO:0000244|PDB:2O23}.
HELIX 123 136 {ECO:0000244|PDB:2O23}.
STRAND 148 153 {ECO:0000244|PDB:2O23}.
HELIX 157 160 {ECO:0000244|PDB:2O23}.
HELIX 166 186 {ECO:0000244|PDB:2O23}.
HELIX 187 189 {ECO:0000244|PDB:2O23}.
STRAND 191 198 {ECO:0000244|PDB:2O23}.
HELIX 204 208 {ECO:0000244|PDB:1U7T}.
HELIX 216 219 {ECO:0000244|PDB:2O23}.
STRAND 222 224 {ECO:0000244|PDB:2O23}.
HELIX 230 242 {ECO:0000244|PDB:2O23}.
STRAND 250 254 {ECO:0000244|PDB:2O23}.
SEQUENCE 261 AA; 26923 MW; 9E74F242E3E6FEF1 CRC64;
MAAACRSVKG LVAVITGGAS GLGLATAERL VGQGASAVLL DLPNSGGEAQ AKKLGNNCVF
APADVTSEKD VQTALALAKG KFGRVDVAVN CAGIAVASKT YNLKKGQTHT LEDFQRVLDV
NLMGTFNVIR LVAGEMGQNE PDQGGQRGVI INTASVAAFE GQVGQAAYSA SKGGIVGMTL
PIARDLAPIG IRVMTIAPGL FGTPLLTSLP EKVCNFLASQ VPFPSRLGDP AEYAHLVQAI
IENPFLNGEV IRLDGAIRMQ P


Related products :

Catalog number Product name Quantity
15-288-22261 Short chain 3-hydroxyacyl-CoA dehydrogenase. mitochondrial - EC 1.1.1.35; HCDH; Medium and short chain L-3-hydroxyacyl-coenzyme A dehydrogenase Polyclonal 0.05 mg
15-288-22261 Short chain 3-hydroxyacyl-CoA dehydrogenase. mitochondrial - EC 1.1.1.35; HCDH; Medium and short chain L-3-hydroxyacyl-coenzyme A dehydrogenase Polyclonal 0.1 mg
20-272-190169 ERAB - Mitochondrial Marker - Mouse monoclonal [10D12] to ERAB - Mitochondrial Marker; EC 1.1.1.35; 3-hydroxyacyl-CoA dehydrogenase type II; Type II HADH; 3-hydroxy-2-methylbutyryl-CoA dehydrogenase; 0.1 ml
10-288-22261F Short chain 3-hydroxyacyl-CoA dehydrogenase. mitochondrial - EC 1.1.1.35; HCDH; Medium and short chain L-3-hydroxyacyl-coenzyme A dehydrogenase 0.05 mg
10-288-22261F Short chain 3-hydroxyacyl-CoA dehydrogenase. mitochondrial - EC 1.1.1.35; HCDH; Medium and short chain L-3-hydroxyacyl-coenzyme A dehydrogenase 0.1 mg
EIAAB34168 EPHD-2,Epidermal retinol dehydrogenase 2,Mouse,Mus musculus,Rdhe2,RDH-E2,Retinal short-chain dehydrogenase reductase 2,retSDR2,Scdr9,Sdr16c5,Short-chain dehydrogenase reductase 9,Short-chain dehydroge
EIAAB11146 11-beta-HSD3,11-beta-hydroxysteroid dehydrogenase type 3,11-DH3,Homo sapiens,HSD11B1L,HSD3,Human,Hydroxysteroid 11-beta-dehydrogenase 1-like protein,SCDR10,Short-chain dehydrogenase_reductase 10
20-272-190170 ERAB - Mitochondrial Marker - Mouse monoclonal [5F3] to ERAB - Mitochondrial Marker; EC 1.1.1.35; 3-hydroxyacyl-CoA dehydrogenase type II; Type II HADH; 3-hydroxy-2-methylbutyryl-CoA dehydrogenase; EC 0.1 ml
EIAAB11117 17-beta-HSD 8,17-beta-hydroxysteroid dehydrogenase 8,3-oxoacyl-[acyl-carrier-protein] reductase,Estradiol 17-beta-dehydrogenase 8,Hsd17b8,Rat,Rattus norvegicus,Testosterone 17-beta-dehydrogenase 8
EIAAB11102 17-beta-HSD 14,17-beta-hydroxysteroid dehydrogenase 14,17-beta-hydroxysteroid dehydrogenase DHRS10,Dehydrogenase_reductase SDR family member 10,DHRS10,Homo sapiens,HSD17B14,Human,Retinal short-chain d
EIAAB11101 17-beta-HSD 14,17-beta-hydroxysteroid dehydrogenase 14,17-beta-hydroxysteroid dehydrogenase DHRS10,Bos taurus,Bovine,Dehydrogenase_reductase SDR family member 10,DHRS10,HSD17B14,Retinal short-chain de
EIAAB34167 EPHD-2,Epidermal retinol dehydrogenase 2,Homo sapiens,Human,RDHE2,RDH-E2,Retinal short-chain dehydrogenase reductase 2,retSDR2,SDR16C5,Short-chain dehydrogenase_reductase family 16C member 5
AKR1C4 AKR1C2 Gene aldo-keto reductase family 1, member C2 (dihydrodiol dehydrogenase 2; bile acid binding protein; 3-alpha hydroxysteroid dehydrogenase, type III)
EIAAB11152 11-beta-HSD2,11-beta-hydroxysteroid dehydrogenase type 2,11-DH2,Corticosteroid 11-beta-dehydrogenase isozyme 2,Homo sapiens,HSD11B2,HSD11K,Human,NAD-dependent 11-beta-hydroxysteroid dehydrogenase
EIAAB11148 11-beta-HSD2,11-beta-hydroxysteroid dehydrogenase type 2,11-DH2,Corticosteroid 11-beta-dehydrogenase isozyme 2,Hsd11b2,Hsd11k,NAD-dependent 11-beta-hydroxysteroid dehydrogenase,Rat,Rattus norvegicus
EIAAB11151 11-beta-HSD2,11-beta-hydroxysteroid dehydrogenase type 2,11-DH2,Corticosteroid 11-beta-dehydrogenase isozyme 2,Hsd11b2,Hsd11k,Mouse,Mus musculus,NAD-dependent 11-beta-hydroxysteroid dehydrogenase
EIAAB11149 11-beta-HSD2,11-beta-hydroxysteroid dehydrogenase type 2,11-DH2,Corticosteroid 11-beta-dehydrogenase isozyme 2,HSD11B2,NAD-dependent 11-beta-hydroxysteroid dehydrogenase,Oryctolagus cuniculus,Rabbit
EIAAB11106 17-beta-HSD 3,17-beta-hydroxysteroid dehydrogenase type 3,EDH17B3,Homo sapiens,HSD17B3,Human,Testicular 17-beta-hydroxysteroid dehydrogenase,Testosterone 17-beta-dehydrogenase 3
EIAAB11150 11-beta-HSD2,11-beta-hydroxysteroid dehydrogenase type 2,11-DH2,Bos taurus,Bovine,Corticosteroid 11-beta-dehydrogenase isozyme 2,HSD11B2,NAD-dependent 11-beta-hydroxysteroid dehydrogenase
CSB-EL001543HU Human aldo-keto reductase family 1, member C2 (dihydrodiol dehydrogenase 2; bile acid binding protein; 3-alpha hydroxysteroid dehydrogenase, type III) (AKR1C2) ELISA kit, Species Human, Sample Type se 96T
EIAAB11104 17-beta-HSD 2,17-beta-hydroxysteroid dehydrogenase type 2,Edh17b2,Estradiol 17-beta-dehydrogenase 2,Hsd17b2,Mouse,Mus musculus,Testosterone 17-beta-dehydrogenase
EIAAB11103 17-beta-HSD 2,17-beta-hydroxysteroid dehydrogenase type 2,Edh17b2,Estradiol 17-beta-dehydrogenase 2,Hsd17b2,Rat,Rattus norvegicus,Testosterone 17-beta-dehydrogenase
EIAAB34164 Cis-retinol_3alpha-hydroxysterol short-chain dehydrogenase isozyme 2,Cis-retinol_androgen dehydrogenase type 2,Crad2,CRAD-2,Mouse,Mus musculus,Rdh7,Retinol dehydrogenase 7
EIAAB11108 17-beta-HSD 3,17-beta-hydroxysteroid dehydrogenase type 3,Edh17b3,Hsd17b3,Rat,Rattus norvegicus,Testicular 17-beta-hydroxysteroid dehydrogenase,Testosterone 17-beta-dehydrogenase 3
EIAAB11107 17-beta-HSD 3,17-beta-hydroxysteroid dehydrogenase type 3,Edh17b3,Hsd17b3,Mouse,Mus musculus,Testicular 17-beta-hydroxysteroid dehydrogenase,Testosterone 17-beta-dehydrogenase 3


 

GENTAUR Belgium BVBA BE0473327336
Voortstraat 49, 1910 Kampenhout BELGIUM
Tel 0032 16 58 90 45

Fax 0032 16 50 90 45
info@gentaur.com | Gentaur





GENTAUR Ltd.
Howard Frank Turnberry House
1404-1410 High Road
Whetstone London N20 9BH
Tel 020 3393 8531 Fax 020 8445 9411
uk@gentaur.com | Gentaur

 

 




GENTAUR France SARL
9, rue Lagrange, 75005 Paris
Tel 01 43 25 01 50

Fax 01 43 25 01 60
RCS Paris B 484 237 888

SIRET 48423788800017

BNP PARIBAS PARIS PL MAUBERT BIC BNPAFRPPPRG

france@gentaur.com | Gentaur

GENTAUR GmbH
Marienbongard 20
52062 Aachen Deutschland
Support Karolina Elandt
Tel: 0035929830070
Fax: (+49) 241 56 00 47 88

Logistic :0241 40 08 90 86
Bankleitzahl 39050000
IBAN lautet DE8839050000107569353
Handelsregister Aachen HR B 16058
Umsatzsteuer-Identifikationsnummer *** DE 815175831
Steuernummer 201/5961/3925
de@gentaur.com | Gentaur

GENTAUR U.S.A
Genprice Inc, Logistics
547, Yurok Circle
San Jose, CA 95123
CA 95123
Tel (408) 780-0908,
Fax (408) 780-0908,
sales@genprice.com

Genprice Inc, Invoices and accounting
6017 Snell Ave, Ste 357
San Jose, CA 95123




GENTAUR Nederland BV
NL850396268B01 KVK nummer 52327027
Kuiper 1
5521 DG Eersel Nederland
Tel:  0208-080893  Fax: 0497-517897
nl@gentaur.com | Gentaur
IBAN: NL04 RABO 0156 9854 62   SWIFT RABONL2U






GENTAUR Spain
tel:0911876558
spain@gentaur.com | Gentaur






ГЕНТАУЪР БЪЛГАРИЯ
ID # 201 358 931 /BULSTAT
София 1000, ул. "Граф Игнатиев" 53 вх. В, ет. 2
Tel 0035924682280 Fax 0035924808322
e-mail: Sofia@gentaur.com | Gentaur
IBAN: BG11FINV91501014771636
BIC: FINVBGSF

GENTAUR Poland Sp. z o.o.


ul. Grunwaldzka 88/A m.2
81-771 Sopot, Poland
TEL Gdansk 058 710 33 44 FAX  058 710 33 48              

poland@gentaur.com | Gentaur

Other countries

Österreich +43720880899

Canada Montreal +15149077481

Ceská republika Praha +420246019719

Danmark +4569918806

Finland Helsset +358942419041

Magyarország Budapest +3619980547

Ireland Dublin+35316526556

Luxembourg+35220880274

Norge Oslo+4721031366

Sverige Stockholm+46852503438

Schweiz Züri+41435006251

US New York+17185132983

GENTAUR Italy
SRL IVA IT03841300167
Piazza Giacomo Matteotti, 6
24122 Bergamo Tel 02 36 00 65 93
Fax 02 36 00 65 94
italia@gentaur.com | Gentaur