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UniProtKB/Swiss-Prot entry Q8BMS1


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name ECHA_MOUSE
Primary accession number Q8BMS1
Secondary accession number Q5U5Y5
Integrated into Swiss-Prot on March 18, 2008
Sequence was last modified on March 1, 2003 (Sequence version 1)
Annotations were last modified on    December 16, 2008 (Entry version 61)
Name and origin of the protein
Protein name Trifunctional enzyme subunit alpha, mitochondrial [Precursor]
Synonym TP-alpha
Includes Long-chain enoyl-CoA hydratase
     (EC 4.2.1.17)
Long chain 3-hydroxyacyl-CoA dehydrogenase
     (EC 1.1.1.211)
Gene name
Name: Hadha
From
Mus musculus (Mouse) [TaxID: 10090] 
Taxonomy Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; Muroidea; Muridae; Murinae; Mus.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=C57BL/6J, and NOD;
TISSUE=Skin;
DOI=10.1126/science.1112014; PubMed=16141072 [NCBI, ExPASy, EBI, Israel, Japan]
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).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=FVB/N;
TISSUE=Eye, Liver, and Olfactory epithelium;
DOI=10.1101/gr.2596504; PubMed=15489334 [NCBI, ExPASy, EBI, Israel, Japan]
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).
[3]
ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-569 AND LYS-728, AND MASS SPECTROMETRY.
TISSUE=Liver;
DOI=10.1016/j.molcel.2006.06.026; PubMed=16916647 [NCBI, ExPASy, EBI, Israel, Japan]
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.;
"Substrate and functional diversity of lysine acetylation revealed by a proteomics survey.";
Mol. Cell 23:607-618(2006).
Comments
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
AK029017; BAC26245.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AK170683; BAE41956.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC037009; AAH37009.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC046978; AAH46978.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC058569; AAH58569.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
RefSeq NP_849209.1; -.
UniGene Mm.200497
3D structure databases
HSSP P14604; 2DUB. [HSSP ENTRY / PDB]
ModBase Q8BMS1.
PTM databases
PhosphoSite Q8BMS1; -.
Organism-specific databases
MGI MGI:2135593; Hadha.
Ontologies
GO
GO:0016507; Cellular component: fatty acid beta-oxidation multienzyme complex (inferred from electronic annotation from InterPro).
GO:0005743; Cellular component: mitochondrial inner membrane (inferred from direct assay from MGI).
GO:0003857; Molecular function: 3-hydroxyacyl-CoA dehydrogenase activity (inferred from electronic annotation from InterPro).
GO:0050662; Molecular function: coenzyme binding (inferred from electronic annotation from InterPro).
GO:0004300; Molecular function: enoyl-CoA hydratase activity (traceable author statement from MGI).
GO:0016509; Molecular function: long-chain-3-hydroxyacyl-CoA dehydrogenase activity (inferred from direct assay from MGI).
GO:0006635; Biological process: fatty acid beta-oxidation (inferred from mutant phenotype from MGI).
GO:0055114; Biological process: oxidation reduction (inferred from electronic annotation from UniProtKB-KW).
QuickGo view.
Family and domain databases
InterPro IPR006180; 3-OHacyl-CoA_DHase_CS.
IPR006176; 3-OHacyl-CoA_DHase_NAD-bd.
IPR006108; 3HC_DHase_C.
IPR001753; Crotonase_core.
IPR013328; DHase_multihelical.
IPR012803; Fa_ox_alpha_mit.
IPR016040; NAD(P)-bd.
Graphical view of domain structure.
Gene3D G3DSA:3.40.50.720; NAD(P)-bd; 1.
G3DSA:1.10.1040.10; Opine_DH; 1.
Pfam PF00725; 3HCDH; 1.
PF02737; 3HCDH_N; 1.
PF00378; ECH; 1.
Pfam graphical view of domain structure.
TIGRFAMs TIGR02441; fa_ox_alpha_mit; 1.
PROSITE PS00067; 3HCDH; 1.
PS00166; ENOYL_COA_HYDRATASE; 1.
Proteomics databases
PRIDE Q8BMS1; -.
Genome annotation databases
Ensembl ENSMUSG00000025745; Mus musculus. [Contig view]
GeneID 97212; -.
KEGG mmu:97212; -.
NMPDR fig|10090.3.peg.11342; -.
Phylogenomic databases
HOVERGEN Q8BMS1; -.
Other
NextBio 352627; -.
SOURCE Hadha; Mus musculus.
ProtoNet Q8BMS1.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Acetylation; Fatty acid metabolism; Lipid metabolism; Lyase; Mitochondrion; Multifunctional enzyme; NAD; Oxidoreductase; Transit peptide.
Features
SEVIEWER logo Feature table viewer
KeyFrom   To Length Description FTId
TRANSIT   1    36  36     Mitochondrion (Potential). 
CHAIN   37   763  727     Trifunctional enzyme subunit alpha, mitochondrial. PRO_0000322639
ACT_SITE   151   151        By similarity. 
ACT_SITE   173   173        Proton donor (By similarity). 
MOD_RES   569   569        N6-acetyllysine. 
MOD_RES   728   728        N6-acetyllysine. 
CONFLICT   459   459        L -> S (in Ref. 2; AAH37009). 
Sequence information
Length: 763 AA [This is the length of the unprocessed precursor] Molecular weight: 82670 Da [This is the MW of the unprocessed precursor] CRC64: 73D203795D5C1141 [This is a checksum on the sequence]
        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 

Q8BMS1 in FASTA format

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