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Protein

Hydroxyacid-oxoacid transhydrogenase, mitochondrial

Gene

Adhfe1

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Catalyzes the cofactor-independent reversible oxidation of gamma-hydroxybutyrate (GHB) to succinic semialdehyde (SSA) coupled to reduction of 2-ketoglutarate (2-KG) to D-2-hydroxyglutarate (D-2-HG). L-3-hydroxybutyrate (L-3-OHB) is also a substrate for HOT when using 2-KG as hydrogen acceptor, resulting in the formation of D-2-HG (By similarity).By similarity

Catalytic activityi

(S)-3-hydroxybutanoate + 2-oxoglutarate = acetoacetate + (R)-2-hydroxyglutarate.
4-hydroxybutanoate + 2-oxoglutarate = succinic semialdehyde + (R)-2-hydroxyglutarate.

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Enzyme and pathway databases

ReactomeiR-MMU-880009. Interconversion of 2-oxoglutarate and 2-hydroxyglutarate.
SABIO-RKQ8R0N6.

Names & Taxonomyi

Protein namesi
Recommended name:
Hydroxyacid-oxoacid transhydrogenase, mitochondrial (EC:1.1.99.24)
Short name:
HOT
Alternative name(s):
Alcohol dehydrogenase iron-containing protein 1
Short name:
ADHFe1
Gene namesi
Name:Adhfe1
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 1

Organism-specific databases

MGIiMGI:1923437. Adhfe1.

Subcellular locationi

GO - Cellular componenti

  • mitochondrion Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Mitochondrion

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini? – 465Hydroxyacid-oxoacid transhydrogenase, mitochondrialPRO_0000322997
Transit peptidei1 – ?MitochondrionSequence analysis

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei443 – 4431N6-acetyllysineCombined sources
Modified residuei450 – 4501PhosphoserineCombined sources

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

EPDiQ8R0N6.
MaxQBiQ8R0N6.
PaxDbiQ8R0N6.
PeptideAtlasiQ8R0N6.
PRIDEiQ8R0N6.

PTM databases

iPTMnetiQ8R0N6.
PhosphoSiteiQ8R0N6.
SwissPalmiQ8R0N6.

Expressioni

Tissue specificityi

Expressed in white and brown adipose tissues, liver, and kidney. Expression is differentiation-dependent during in vitro brown and white adipogenesis.1 Publication

Inductioni

Down-regulated of 40% in white adipose tissue of ob/ob obese mice.1 Publication

Gene expression databases

BgeeiQ8R0N6.
CleanExiMM_ADHFE1.
ExpressionAtlasiQ8R0N6. baseline and differential.
GenevisibleiQ8R0N6. MM.

Interactioni

Protein-protein interaction databases

IntActiQ8R0N6. 2 interactions.
MINTiMINT-4118408.
STRINGi10090.ENSMUSP00000116627.

Structurei

3D structure databases

ProteinModelPortaliQ8R0N6.
SMRiQ8R0N6. Positions 55-458.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiKOG3857. Eukaryota.
COG1454. LUCA.
GeneTreeiENSGT00390000003849.
HOGENOMiHOG000243335.
HOVERGENiHBG057032.
InParanoidiQ8R0N6.
KOiK11173.
OMAiRAACQCP.
OrthoDBiEOG77WWC7.
PhylomeDBiQ8R0N6.
TreeFamiTF105710.

Family and domain databases

InterProiIPR001670. ADH_Fe.
[Graphical view]
PfamiPF00465. Fe-ADH. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q8R0N6-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MAAAARARVT HLLRHLQSTA CQCPTHSHTY SQAPGPSGKT ADYAFEMAVS
60 70 80 90 100
NIRYGAGVTK EVGMDLQNMG AKNVCLMTDK NLSQLPPVQI VMDSLSKNGI
110 120 130 140 150
SFQVYDDVRV EPTDGSFMDA IEFAKKGAFD AYVAVGGGST MDTCKAANLY
160 170 180 190 200
ASSPHSEFLD YVNAPIGKGK PVTVPLKPLI AVPTTSGTGS ETTGVAIFDY
210 220 230 240 250
EHLKVKTGIA SRAIKPTLGL VDPLHTLHMP CQVVANSGFD VLCHALESYT
260 270 280 290 300
AIPYSMRSPC PSNPIQRPAY QGSNPISDIW AVHALQIVAK YLKRAVRNPD
310 320 330 340 350
DLEARSKMHL ASAFAGIGFG NAGVHLCHGM SYPISGLVKT YKAKEYNVDH
360 370 380 390 400
PLVPHGLSVV LTSPAVFTFT AQMFPERHLE TAGILGANIR TARIQDAGLV
410 420 430 440 450
LADALRKFLF DLNVDDGLAA LGYSKDDIPS LVKGTLPQER VTKLAPRAQS
460
EEDLSALFEA SMKLY
Length:465
Mass (Da):49,937
Last modified:July 5, 2004 - v2
Checksum:iCD1463685F788C2A
GO
Isoform 2 (identifier: Q8R0N6-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-46: Missing.

Show »
Length:419
Mass (Da):45,015
Checksum:i510F18E8678AB656
GO

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 4646Missing in isoform 2. 1 PublicationVSP_031987Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK038853 mRNA. Translation: BAC30151.1.
AK050178 mRNA. Translation: BAC34108.1.
BC026584 mRNA. Translation: AAH26584.2.
CCDSiCCDS14812.1. [Q8R0N6-1]
RefSeqiNP_780445.1. NM_175236.4. [Q8R0N6-1]
XP_006495649.1. XM_006495586.2. [Q8R0N6-2]
UniGeneiMm.28514.

Genome annotation databases

EnsembliENSMUST00000144177; ENSMUSP00000116627; ENSMUSG00000025911. [Q8R0N6-1]
GeneIDi76187.
KEGGimmu:76187.
UCSCiuc007agl.2. mouse. [Q8R0N6-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK038853 mRNA. Translation: BAC30151.1.
AK050178 mRNA. Translation: BAC34108.1.
BC026584 mRNA. Translation: AAH26584.2.
CCDSiCCDS14812.1. [Q8R0N6-1]
RefSeqiNP_780445.1. NM_175236.4. [Q8R0N6-1]
XP_006495649.1. XM_006495586.2. [Q8R0N6-2]
UniGeneiMm.28514.

3D structure databases

ProteinModelPortaliQ8R0N6.
SMRiQ8R0N6. Positions 55-458.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiQ8R0N6. 2 interactions.
MINTiMINT-4118408.
STRINGi10090.ENSMUSP00000116627.

PTM databases

iPTMnetiQ8R0N6.
PhosphoSiteiQ8R0N6.
SwissPalmiQ8R0N6.

Proteomic databases

EPDiQ8R0N6.
MaxQBiQ8R0N6.
PaxDbiQ8R0N6.
PeptideAtlasiQ8R0N6.
PRIDEiQ8R0N6.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000144177; ENSMUSP00000116627; ENSMUSG00000025911. [Q8R0N6-1]
GeneIDi76187.
KEGGimmu:76187.
UCSCiuc007agl.2. mouse. [Q8R0N6-1]

Organism-specific databases

CTDi137872.
MGIiMGI:1923437. Adhfe1.

Phylogenomic databases

eggNOGiKOG3857. Eukaryota.
COG1454. LUCA.
GeneTreeiENSGT00390000003849.
HOGENOMiHOG000243335.
HOVERGENiHBG057032.
InParanoidiQ8R0N6.
KOiK11173.
OMAiRAACQCP.
OrthoDBiEOG77WWC7.
PhylomeDBiQ8R0N6.
TreeFamiTF105710.

Enzyme and pathway databases

ReactomeiR-MMU-880009. Interconversion of 2-oxoglutarate and 2-hydroxyglutarate.
SABIO-RKQ8R0N6.

Miscellaneous databases

ChiTaRSiAdhfe1. mouse.
PROiQ8R0N6.
SOURCEiSearch...

Gene expression databases

BgeeiQ8R0N6.
CleanExiMM_ADHFE1.
ExpressionAtlasiQ8R0N6. baseline and differential.
GenevisibleiQ8R0N6. MM.

Family and domain databases

InterProiIPR001670. ADH_Fe.
[Graphical view]
PfamiPF00465. Fe-ADH. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "The transcriptional landscape of the mammalian genome."
    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.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
    Strain: C57BL/6J.
    Tissue: Hypothalamus and Liver.
  2. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    Strain: FVB/N.
    Tissue: Kidney.
  3. "Differentiation-dependent expression of Adhfe1 in adipogenesis."
    Kim J.Y., Tillison K.S., Zhou S., Lee J.H., Smas C.M.
    Arch. Biochem. Biophys. 464:100-111(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION, TISSUE SPECIFICITY, INDUCTION.
  4. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-450, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brown adipose tissue, Heart, Kidney, Liver and Pancreas.
  5. "Label-free quantitative proteomics of the lysine acetylome in mitochondria identifies substrates of SIRT3 in metabolic pathways."
    Rardin M.J., Newman J.C., Held J.M., Cusack M.P., Sorensen D.J., Li B., Schilling B., Mooney S.D., Kahn C.R., Verdin E., Gibson B.W.
    Proc. Natl. Acad. Sci. U.S.A. 110:6601-6606(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-443, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.

Entry informationi

Entry nameiHOT_MOUSE
AccessioniPrimary (citable) accession number: Q8R0N6
Secondary accession number(s): Q78SV3, Q8BYP0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 18, 2008
Last sequence update: July 5, 2004
Last modified: July 6, 2016
This is version 99 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.