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P54869 (HMCS2_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 3, 2013. Version 110. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Hydroxymethylglutaryl-CoA synthase, mitochondrial
Short name=HMG-CoA synthase
EC=2.3.3.10
Alternative name(s):
3-hydroxy-3-methylglutaryl coenzyme A synthase
Gene names
Name:Hmgcs2
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length508 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

This enzyme condenses acetyl-CoA with acetoacetyl-CoA to form HMG-CoA, which is the substrate for HMG-CoA reductase.

Catalytic activity

Acetyl-CoA + H2O + acetoacetyl-CoA = (S)-3-hydroxy-3-methylglutaryl-CoA + CoA.

Pathway

Metabolic intermediate biosynthesis; (R)-mevalonate biosynthesis; (R)-mevalonate from acetyl-CoA: step 2/3.

Subcellular location

Mitochondrion.

Tissue specificity

Liver and kidney.

Post-translational modification

Acetylation of Lys-427 is observed in liver mitochondria from fasted mice but not from fed mice.

Sequence similarities

Belongs to the HMG-CoA synthase family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Transit peptide1 – 3737Mitochondrion Probable
Chain38 – 508471Hydroxymethylglutaryl-CoA synthase, mitochondrial
PRO_0000013484

Sites

Active site1661 Potential

Amino acid modifications

Modified residue831N6-acetyllysine Ref.4
Modified residue3101N6-succinyllysine By similarity
Modified residue4271N6-acetyllysine Ref.4
Modified residue4331Phosphoserine Ref.5
Modified residue4371N6-acetyllysine Ref.4

Experimental info

Sequence conflict29 – 313LSA → EFR Ref.2
Sequence conflict3941L → I in BAB23657. Ref.1

Sequences

Sequence LengthMass (Da)Tools
P54869 [UniParc].

Last modified March 15, 2005. Version 2.
Checksum: 5A20ACE918FF4758

FASTA50856,823
        10         20         30         40         50         60 
MQRLLAPARR VLQVKRAMQE TSLTPAHLLS AAQQRFSTIP PAPLAKTDTW PKDVGILALE 

        70         80         90        100        110        120 
VYFPAQYVDQ TDLEKFNNVE AGKYTVGLGQ TRMGFCSVQE DINSLCLTVV QRLMERTKLP 

       130        140        150        160        170        180 
WDAVGRLEVG TETIIDKSKA VKTVLMELFQ DSGNTDIEGI DTTNACYGGT ASLFNAANWM 

       190        200        210        220        230        240 
ESSYWDGRYA LVVCGDIAVY PSGNARPTGG AGAVAMLIGP KAPLVLEQGL RGTHMENAYD 

       250        260        270        280        290        300 
FYKPNLASEY PLVDGKLSIQ CYLRALDRCY AAYRKKIQNQ WKQAGNNQPF TLDDVQYMIF 

       310        320        330        340        350        360 
HTPFCKMVQK SLARLMFNDF LSSSSDKQNN LYKGLEAFRG LKLEETYTNK DVDKALLKAS 

       370        380        390        400        410        420 
LDMFNQKTKA SLYLSTNNGN MYTSSLYGCL ASLLSHHSAQ ELAGSRIGAF SYGSGLAASF 

       430        440        450        460        470        480 
FSFRVSKDAS PGSPLEKLVS SVSDLPKRLD SRRRMSPEEF TEIMNQREQF YHKVNFSPPG 

       490        500 
DTSNLFPGTW YLERVDEMHR RKYARCPV

« Hide

References

« Hide 'large scale' 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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: C57BL/6J.
Tissue: 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].
Strain: FVB/N.
Tissue: Colon and Liver.
[3]"Human mitochondrial HMG CoA synthase: liver cDNA and partial genomic cloning, chromosome mapping to 1p12-p13, and possible role in vertebrate evolution."
Boukaftane Y., Duncan A., Wang S., Labuda D., Robert M.-F., Sarrazin J., Schappert K.T., Mitchell G.A.
Genomics 23:552-559(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 29-508.
Strain: CHS.
Tissue: Liver.
[4]"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] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-83; LYS-427 AND LYS-437, MASS SPECTROMETRY.
Tissue: Liver.
[5]"Mitochondrial phosphoproteome revealed by an improved IMAC method and MS/MS/MS."
Lee J., Xu Y., Chen Y., Sprung R., Kim S.C., Xie S., Zhao Y.
Mol. Cell. Proteomics 6:669-676(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-433, MASS SPECTROMETRY.
Tissue: Liver.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AK004865 mRNA. Translation: BAB23626.1.
AK004902 mRNA. Translation: BAB23657.1.
BC014714 mRNA. Translation: AAH14714.1.
BC024744 mRNA. Translation: AAH24744.1.
U12790 Genomic DNA. Translation: AAA92675.1.
U12791 Genomic DNA. Translation: AAA92676.1.
IPIIPI00420718.
PIRB55729.
RefSeqNP_032282.2. NM_008256.4.
UniGeneMm.289131.

3D structure databases

ProteinModelPortalP54869.
SMRP54869. Positions 51-508.
ModBaseSearch...

PTM databases

PhosphoSiteP54869.

2D gel databases

REPRODUCTION-2DPAGEP54869.
SWISS-2DPAGEP54869.

Proteomic databases

PaxDbP54869.
PRIDEP54869.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000090746; ENSMUSP00000088249; ENSMUSG00000027875.
ENSMUST00000120541; ENSMUSP00000113296; ENSMUSG00000027875.
GeneID15360.
KEGGmmu:15360.
UCSCuc008qpr.2. mouse.

Organism-specific databases

CTD3158.
MGIMGI:101939. Hmgcs2.

Phylogenomic databases

eggNOGCOG3425.
GeneTreeENSGT00390000006096.
HOGENOMHOG000012351.
HOVERGENHBG051912.
InParanoidP54869.
KOK01641.
OMALDDLQFM.
OrthoDBEOG4H72B9.

Enzyme and pathway databases

BRENDA2.3.3.10. 3474.
UniPathwayUPA00058; UER00102.

Gene expression databases

BgeeP54869.
CleanExMM_HMGCS2.
GenevestigatorP54869.
GermOnlineENSMUSG00000027875. Mus musculus.

Family and domain databases

Gene3D3.40.47.10. 1 hit.
InterProIPR000590. HMG_CoA_synt_AS.
IPR013746. HMG_CoA_synt_C.
IPR013528. HMG_CoA_synth_N.
IPR010122. HMG_CoA_synthase_euk.
IPR016039. Thiolase-like.
IPR016038. Thiolase-like_subgr.
[Graphical view]
PfamPF08540. HMG_CoA_synt_C. 1 hit.
PF01154. HMG_CoA_synt_N. 1 hit.
[Graphical view]
SUPFAMSSF53901. Thiolase-like. 2 hits.
TIGRFAMsTIGR01833. HMG-CoA-S_euk. 1 hit.
PROSITEPS01226. HMG_COA_SYNTHASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSHMGCS2. mouse.
NextBio287976.
SOURCESearch...

Entry information

Entry nameHMCS2_MOUSE
AccessionPrimary (citable) accession number: P54869
Secondary accession number(s): Q64740, Q9DBK1, Q9DBM4
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: March 15, 2005
Last modified: April 3, 2013
This is version 110 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

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

to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents