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Reviewed, UniProtKB/Swiss-Prot Q99JY0 (ECHB_MOUSE)

Last modified February 9, 2010. Version 69. 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 beta, mitochondrial
Alternative name(s):
    TP-beta
Including the following 1 domains:
    1- Recommended name:
            3-ketoacyl-CoA thiolase
              EC=2.3.1.16
        Alternative name(s):
            Acetyl-CoA acyltransferase
            Beta-ketothiolase
Gene names
Name: Hadhb
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 length475 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)

Catalytic activity

Acyl-CoA + acetyl-CoA = CoA + 3-oxoacyl-CoA.

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-202 is observed in liver mitochondria from fasted mice but not from fed mice.

Sequence similarities

Belongs to the thiolase family.

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Ontologies

Keywords
   Biological processFatty acid metabolism
Lipid metabolism
   Cellular componentMitochondrion
   DomainTransit peptide
   Molecular functionAcyltransferase
Transferase
   PTMAcetylation
Gene Ontology (GO)
   Biological processfatty acid beta-oxidation

Traceable author statement. Source: MGI

   Cellular componentmitochondrial inner membrane

Inferred from direct assay. Source: MGI

   Molecular functionacetyl-CoA C-acyltransferase activity

Inferred from direct assay. Source: MGI

Complete GO annotation...

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Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Transit peptide1 – 3434Mitochondrion By similarity
Chain35 – 475441Trifunctional enzyme subunit beta, mitochondrial
PRO_0000034082

Sites

Active site1391Acyl-thioester intermediate By similarity
Active site4291Proton acceptor By similarity
Active site4591Proton acceptor By similarity

Amino acid modifications

Modified residue731N6-acetyllysine By similarity
Modified residue1891N6-acetyllysine By similarity
Modified residue2021N6-acetyllysine Ref.3
Modified residue3491N6-acetyllysine Ref.3

Experimental info

Sequence conflict24 – 252IR → HK in BAC36493. Ref.1
Sequence conflict4251L → M in BAC38790. Ref.1
Sequence conflict4501G → R in BAC38790. Ref.1
Sequence conflict4501G → V in BAC39015. Ref.1

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Sequences

Sequence LengthMass (Da)Tools
Q99JY0-1 [UniParc].

Last modified June 1, 2001. Version 1.
Checksum: F131B497C4F5FAF4

FASTA47551,386
        10         20         30         40         50         60 
MTTILTSTFR NLSTTSKWAL RSSIRPLSCS SQLHSAPAVQ TKSKKTLAKP NMKNIVVVEG 

        70         80         90        100        110        120 
VRIPFLLSGT SYKDLMPHDL ARAALSGLLH RTNIPKDVVD YIIFGTVIQE VKTSNVAREA 

       130        140        150        160        170        180 
ALGAGFSDKT PAHTVTMACI SSNQAMTTAV GLIASGQCDV VVAGGVELMS DVPIRHSRNM 

       190        200        210        220        230        240 
RKMMLDLNKA KTLGQRLSLL SKFRLNFLSP ELPAVAEFST NETMGHSADR LAAAFAVSRM 

       250        260        270        280        290        300 
EQDEYALRSH SLAKKAQDEG HLSDIVPFKV PGKDTVTKDN GIRPSSLEQM AKLKPAFIKP 

       310        320        330        340        350        360 
YGTVTAANSS FLTDGASAML IMSEDRALAM GYKPKAYLRD FIYVSQDPKD QLLLGPTYAT 

       370        380        390        400        410        420 
PKVLEKAGLT MNDIDAFEFH EAFSGQILAN FKAMDSDWFA QNYMGRKTKV GSPPLEKFNI 

       430        440        450        460        470 
WGGSLSLGHP FGATGCRLVM AAANRLRKDG GQYALVAACA AGGQGHAMIV EAYPK

« Hide

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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.
Tissue: Bone marrow, Colon, Hippocampus, Spinal ganglion, Testis and Thymus.
[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: Mammary tumor.
[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-202 AND LYS-349, MASS SPECTROMETRY.
Tissue: Liver.
+Additional computationally mapped references.

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Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AK033462 mRNA. Translation: BAC28300.1.
AK076814 mRNA. Translation: BAC36493.1.
AK083164 mRNA. Translation: BAC38790.1.
AK083767 mRNA. Translation: BAC39015.1.
AK150889 mRNA. Translation: BAE29936.1.
AK169637 mRNA. Translation: BAE41269.1.
BC005585 mRNA. Translation: AAH05585.1.
IPIIPI00115607.
RefSeqNP_663533.1.
UniGeneMm.291463
Mm.389348

3D structure databases

SMRQ99JY0. Positions 55-472.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ99JY0.

PTM databases

PhosphoSiteQ99JY0.

Proteomic databases

PRIDEQ99JY0.

Genome annotation databases

EnsemblENSMUST00000026841; ENSMUSP00000026841; ENSMUSG00000059447; Mus musculus. [Genome view]
ENSMUST00000114783; ENSMUSP00000110431; ENSMUSG00000059447; Mus musculus. [Genome view]
ENSMUST00000114786; ENSMUSP00000110434; ENSMUSG00000059447; Mus musculus. [Genome view]
GeneID231086.
KEGGmmu:231086.
NMPDRfig|10090.3.peg.11343.
UCSCuc008wve.1. mouse.

Organism-specific databases

CTD231086.
MGIMGI:2136381. Hadhb.

Phylogenomic databases

eggNOGroNOG05435.
HOGENOMHBG370930.
HOVERGENQ99JY0.
InParanoidQ99JY0.
OMAKAGLTMN.
OrthoDBEOG9BGCFC.
PhylomeDBQ99JY0.

Enzyme and pathway databases

BRENDA2.3.1.16. 244.

Gene expression databases

BgeeQ99JY0.
GenevestigatorQ99JY0.
GermOnlineENSMUSG00000063684. Mus musculus.

Family and domain databases

InterProIPR002155. Thiolase.
IPR016039. Thiolase-like.
IPR020615. Thiolase_acyl_enz_int_AS.
IPR020610. Thiolase_AS.
IPR020617. Thiolase_C.
IPR020613. Thiolase_CS.
IPR020616. Thiolase_N.
[Graphical view]
PANTHERPTHR18919. Thiolase. 1 hit.
PfamPF02803. Thiolase_C. 1 hit.
PF00108. Thiolase_N. 1 hit.
[Graphical view]
TIGRFAMsTIGR01930. AcCoA-C-Actrans. 1 hit.
PROSITEPS00098. THIOLASE_1. 1 hit.
PS00737. THIOLASE_2. 1 hit.
PS00099. THIOLASE_3. 1 hit.
[Graphical view]
ProtoNetSearch...

Other Resources

NextBio380391.
SOURCESearch...

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Entry information

Entry nameECHB_MOUSE
AccessionPrimary (citable) accession number: Q99JY0
Secondary accession number(s): Q3TEH9 expand/collapse secondary AC list , Q8BJI5, Q8BJM0, Q8BK52
Entry history
Integrated into UniProtKB/Swiss-Prot: August 16, 2004
Last sequence update: June 1, 2001
Last modified: February 9, 2010
This is version 69 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