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Reviewed, UniProtKB/Swiss-Prot Q8BMS1 (ECHA_MOUSE)

Last modified February 9, 2010. Version 75. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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Names and origin

Protein namesRecommended name:
    Trifunctional enzyme subunit alpha, mitochondrial
Alternative name(s):
    TP-alpha
Including the following 2 domains:
    1- Recommended name:
            Long-chain enoyl-CoA hydratase
              EC=4.2.1.17
    2- Recommended name:
            Long chain 3-hydroxyacyl-CoA dehydrogenase
              EC=1.1.1.211
Gene names
Name: Hadha
OrganismMus musculus (Mouse)
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus

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Protein attributes

Sequence length763 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level.

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General annotation (Comments)

Function

Bifunctional subunit.

Catalytic activity

(3S)-3-hydroxyacyl-CoA = trans-2(or 3)-enoyl-CoA + H2O.

(S)-3-hydroxyacyl-CoA + NAD+ = 3-oxoacyl-CoA + NADH.

Pathway

Lipid metabolism; fatty acid beta-oxidation.

Subunit structure

Octamer of 4 alpha (HADHA) and 4 beta (HADHB) subunits By similarity.

Subcellular location

Mitochondrion matrix By similarity.

Post-translational modification

Acetylation of Lys-569 and Lys-728 is observed in liver mitochondria from fasted mice but not from fed mice.

Sequence similarities

In the N-terminal section; belongs to the enoyl-CoA hydratase/isomerase family.

In the central section; belongs to the 3-hydroxyacyl-CoA dehydrogenase family.

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Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Transit peptide1 – 3636Mitochondrion Potential
Chain37 – 763727Trifunctional enzyme subunit alpha, mitochondrial
PRO_0000322639

Sites

Site1511Important for catalytic activity By similarity
Site1731Important for catalytic activity By similarity

Amino acid modifications

Modified residue1291N6-acetyllysine Ref.3
Modified residue2951N6-acetyllysine By similarity
Modified residue3031N6-acetyllysine By similarity
Modified residue3261N6-acetyllysine Ref.3
Modified residue3501N6-acetyllysine Ref.3
Modified residue3531N6-acetyllysine By similarity
Modified residue3591N6-acetyllysine By similarity
Modified residue4061N6-acetyllysine By similarity
Modified residue5051N6-acetyllysine By similarity
Modified residue5401N6-acetyllysine By similarity
Modified residue5691N6-acetyllysine Ref.3
Modified residue6441N6-acetyllysine By similarity
Modified residue7281N6-acetyllysine Ref.3

Experimental info

Sequence conflict1961A → D in BAE41822. Ref.1
Sequence conflict4591L → S in AAH37009. Ref.2

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Sequences

Sequence LengthMass (Da)Tools
Q8BMS1-1 [UniParc].

Last modified March 1, 2003. Version 1.
Checksum: 73D203795D5C1141

FASTA76382,670
        10         20         30         40         50         60 
MVASRAIGSL SRFSAFRILR SRGCICRSFT TSSALLTRTH INYGVKGDVA VIRINSPNSK 

        70         80         90        100        110        120 
VNTLNKEVQS EFIEVMNEIW ANDQIRSAVL ISSKPGCFVA GADINMLSSC TTPQEATRIS 

       130        140        150        160        170        180 
QEGQRMFEKL EKSPKPVVAA ISGSCLGGGL ELAIACQYRI ATKDRKTVLG VPEVLLGILP 

       190        200        210        220        230        240 
GAGGTQRLPK MVGVPAAFDM MLTGRNIRAD RAKKMGLVDQ LVEPLGPGIK SPEERTIEYL 

       250        260        270        280        290        300 
EEVAVNFAKG LADRKVSAKQ SKGLVEKLTT YAMTVPFVRQ QVYKTVEEKV KKQTKGLYPA 

       310        320        330        340        350        360 
PLKIIDAVKA GLEQGSDAGY LAESQKFGEL ALTKESKALM GLYNGQVLCK KNKFGAPQKN 

       370        380        390        400        410        420 
VQQLAILGAG LMGAGIAQVS VDKGLKTLLK DTTVTGLGRG QQQVFKGLND KVKKKALTSF 

       430        440        450        460        470        480 
ERDSIFSNLI GQLDYKGFEK ADMVIEAVFE DLGVKHKVLK EVESVTPEHC IFASNTSALP 

       490        500        510        520        530        540 
INQIAAVSKR PEKVIGMHYF SPVDKMQLLE IITTDKTSKD TTASAVAVGL RQGKVIIVVK 

       550        560        570        580        590        600 
DGPGFYTTRC LAPMMSEVMR ILQEGVDPKK LDALTTGFGF PVGAATLADE VGVDVAQHVA 

       610        620        630        640        650        660 
EDLGKAFGER FGGGSVELLK QMVSKGFLGR KSGKGFYIYQ EGSKNKSLNS EMDNILANLR 

       670        680        690        700        710        720 
LPAKPEVSSD EDVQYRVITR FVNEAVLCLQ EGILATPAEG DIGAVFGLGF PPCLGGPFRF 

       730        740        750        760 
VDLYGAQKVV DRLRKYESAY GTQFTPCQLL LDHANNSSKK FYQ

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References

[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. expand/collapse author list , 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: 16141072] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: C57BL/6J and NOD.
Tissue: Skin.
[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: 15489334] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: FVB/N.
Tissue: Eye, Liver and Olfactory epithelium.
[3]"Substrate and functional diversity of lysine acetylation revealed by a proteomics survey."
Kim S.C., Sprung R., Chen Y., Xu Y., Ball H., Pei J., Cheng T., Kho Y., Xiao H., Xiao L., Grishin N.V., White M., Yang X.-J., Zhao Y.
Mol. Cell 23:607-618(2006) [PubMed: 16916647] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-129; LYS-326; LYS-350; LYS-569 AND LYS-728, MASS SPECTROMETRY.
Tissue: Liver.
+Additional computationally mapped references.

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Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AK029017 mRNA. Translation: BAC26245.1.
AK170478 mRNA. Translation: BAE41822.1.
AK170683 mRNA. Translation: BAE41956.1.
BC027156 mRNA. Translation: AAH27156.1.
BC037009 mRNA. Translation: AAH37009.1.
BC046978 mRNA. Translation: AAH46978.1.
BC058569 mRNA. Translation: AAH58569.1.
IPIIPI00223092.
RefSeqNP_849209.1.
UniGeneMm.200497

3D structure databases

HSSPHSSP built from PDB template 2DUB based on UniProtKB P14604.
SMRQ8BMS1. Positions 45-762.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ8BMS1.

PTM databases

PhosphoSiteQ8BMS1.

Proteomic databases

PRIDEQ8BMS1.

Genome annotation databases

EnsemblENSMUST00000026843; ENSMUSP00000026843; ENSMUSG00000025745; Mus musculus. [Genome view]
GeneID97212.
KEGGmmu:97212.
NMPDRfig|10090.3.peg.11342.
UCSCuc008wvc.1. mouse.

Organism-specific databases

CTD97212.
MGIMGI:2135593. Hadha.

Phylogenomic databases

HOGENOMHBG691737.
HOVERGENQ8BMS1.
InParanoidQ8BMS1.
OMAHATTSDE.
OrthoDBEOG90CM27.
PhylomeDBQ8BMS1.

Enzyme and pathway databases

BRENDA1.1.1.211. 244.
4.2.1.17. 244.

Gene expression databases

ArrayExpressQ8BMS1.
BgeeQ8BMS1.
GenevestigatorQ8BMS1.

Family and domain databases

InterProIPR006180. 3-OHacyl-CoA_DH_CS.
IPR006176. 3-OHacyl-CoA_DH_NAD-bd.
IPR006108. 3HC_DH_C.
IPR008927. 6-PGluconate_DH_C-like.
IPR001753. Crotonase_core.
IPR013328. DH_multihelical.
IPR018376. Enoyl-CoA_hyd/isom_CS.
IPR012803. Fa_ox_alpha_mit.
IPR016040. NAD(P)-bd_dom.
[Graphical view]
Gene3DG3DSA:3.40.50.720. NAD(P)-bd. 1 hit.
G3DSA:1.10.1040.10. Opine_DH. 1 hit.
PfamPF00725. 3HCDH. 2 hits.
PF02737. 3HCDH_N. 1 hit.
PF00378. ECH. 1 hit.
[Graphical view]
TIGRFAMsTIGR02441. fa_ox_alpha_mit. 1 hit.
PROSITEPS00067. 3HCDH. 1 hit.
PS00166. ENOYL_COA_HYDRATASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Other Resources

NextBio352627.
SOURCESearch...

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Entry information

Entry nameECHA_MOUSE
AccessionPrimary (citable) accession number: Q8BMS1
Secondary accession number(s): Q3TCY3, Q5U5Y5, Q8QZU4
Entry history
Integrated into UniProtKB/Swiss-Prot: March 18, 2008
Last sequence update: March 1, 2003
Last modified: February 9, 2010
This is version 75 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)

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Relevant documents

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents