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Q8K0L3 (ACSM2_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified November 16, 2011. Version 75. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Acyl-coenzyme A synthetase ACSM2, mitochondrial

EC=6.2.1.2
Alternative name(s):
Acyl-CoA synthetase medium-chain family member 2
Butyrate--CoA ligase 2
Butyryl-coenzyme A synthetase 2
Middle-chain acyl-CoA synthetase 2
Gene names
Name:Acsm2
OrganismMus musculus (Mouse)
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length575 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

Has medium-chain fatty acid:CoA ligase activity with broad substrate specificity (in vitro). Acts on acids from C4 to C(11) and on the corresponding 3-hydroxy- and 2,3- or 3,4-unsaturated acids (in vitro) By similarity.

Catalytic activity

ATP + an acid + CoA = AMP + diphosphate + an acyl-CoA.

Cofactor

Magnesium or manganese By similarity.

Enzyme regulation

Activated by monovalent cations, such as potassium, rubidium or ammonium By similarity.

Subunit structure

Monomer By similarity.

Subcellular location

Mitochondrion matrix By similarity.

Sequence similarities

Belongs to the ATP-dependent AMP-binding enzyme family.

Ontologies

Keywords
   Biological processFatty acid metabolism
Lipid metabolism
   Cellular componentMitochondrion
   Coding sequence diversityAlternative splicing
   DomainTransit peptide
   LigandATP-binding
Magnesium
Metal-binding
Nucleotide-binding
   Molecular functionLigase
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological processfatty acid metabolic process

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular componentmitochondrial matrix

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

butyrate-CoA ligase activity

Inferred from electronic annotation. Source: EC

metal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q8K0L3-1)

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.
Isoform 2 (identifier: Q8K0L3-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-1: M → MTTGSLDLPFVGSHRWIKWTTASLTM
Note: No experimental confirmation available.
Isoform 3 (identifier: Q8K0L3-3)

The sequence of this isoform differs from the canonical sequence as follows:
     471-471: G → GAYFCR
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Transit peptide1 – 4646Mitochondrion Potential
Chain47 – 575529Acyl-coenzyme A synthetase ACSM2, mitochondrial
PRO_0000306095

Regions

Nucleotide binding221 – 2299ATP By similarity
Nucleotide binding360 – 3656ATP By similarity
Region470 – 4723Coenzyme A binding By similarity
Region541 – 5433Coenzyme A binding By similarity

Sites

Binding site1391Coenzyme A By similarity
Binding site3651Substrate By similarity
Binding site4471ATP By similarity
Binding site4621ATP By similarity
Binding site4731Substrate By similarity
Binding site5021Coenzyme A By similarity
Binding site5331Coenzyme A By similarity
Binding site5581ATP By similarity

Natural variations

Alternative sequence11M → MTTGSLDLPFVGSHRWIKWT TASLTM in isoform 2.
VSP_028393
Alternative sequence4711G → GAYFCR in isoform 3.
VSP_028394

Experimental info

Sequence conflict5151E → G in BAB71542. Ref.2

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified October 1, 2002. Version 1.
Checksum: A7E5956D54B119D8

FASTA57564,269
        10         20         30         40         50         60 
MHHLWKIPRL FTLWGNEISC RTFHMNIKKL IPIQWGHQEA PAKFNFASDV IDHWASVEKA 

        70         80         90        100        110        120 
GKRSSGPALW WMNGSGKEIK WSFRELSEAS KQTANVLSGA CGLHRGDRVA VVLPRIPEWW 

       130        140        150        160        170        180 
LMILGCMRTG LVFMPGTIQM RSSDILYRLQ ASKARAIVAG DEVAQEVDAV APDCSFLKIK 

       190        200        210        220        230        240 
LLVSENSREG WLNFKALLKE ASTIHQCVET ESRESAAIYF TSGTSGPPKM AEHSHCSLGI 

       250        260        270        280        290        300 
KAKMDAASWT GLSTSDIIWT ISDTAWIMNI LGAFLEPWVL GACIFVHLLP KFDSQTVLKV 

       310        320        330        340        350        360 
LSSYPINTLV GAPIIYRMLL QQDLSSYKFP HLHSCFSGGE TLLPETLENW KAKTGLEIRE 

       370        380        390        400        410        420 
IYGQTETGLI CRVSRTMKVK PGYLGTAFAH YDVQVIDEQG NVLPPGKEGD IAIRVKPIWP 

       430        440        450        460        470        480 
IGMFSGYVDN PKKTQDNIRG DFWLMGDRGI KDPEGYFHFI GRSDDIINSS GYRIGPSEVE 

       490        500        510        520        530        540 
NALMEHPAVS ETAVISSPDP SRGEVVKAFV VLAPEFLSHD RDQLTKVLQE HVKSVTAPYK 

       550        560        570 
YPRKVEFVLD LPKTVTGKIE RAKLRAKEWK TSGRA 

« Hide

Isoform 2 [UniParc].

Checksum: CD0F661EC08E1C4F
Show »

FASTA60067,057
Isoform 3 [UniParc].

Checksum: 2D228B445D3D2DF3
Show »

FASTA58064,910

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] (ISOFORMS 1; 2 AND 3).
Strain: C57BL/6J.
Tissue: Embryonic head, Kidney and Spleen.
[2]"NEDO cDNA sequencing project."
Suzuki O., Sasaki N., Aotsuka S., Shoji T., Ichihara T., Shiohata N., Matsumoto K., Hirano M., Sano S., Nomura R., Yoshikawa Y., Matsumura Y., Moriya S., Chiba E., Momiyama H., Onogawa S., Kaeriyama S., Satoh N. expand/collapse author list , Matsunawa H., Takahashi E., Kataoka R., Kuga N., Kuroda A., Satoh I., Kamata K., Takami S., Terashima Y., Watanabe M., Sugiyama T., Irie R., Otsuki T., Sato H., Ota T., Wakamatsu A., Ishii S., Yamamoto J., Isono Y., Kawai-Hio Y., Saito K., Nishikawa T., Kimura K., Yamashita H., Matsuo K., Nakamura Y., Sekine M., Kikuchi H., Kanda K., Wagatsuma M., Murakawa K., Kanehori K., Takahashi-Fujii A., Oshima A., Sugiyama A., Kawakami B., Suzuki Y., Sugano S., Nagahari K., Masuho Y., Nagai K., Isogai T.
Submitted (OCT-2001) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
[3]"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] (ISOFORM 1).
Strain: FVB/N.
Tissue: Kidney.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AK140827 mRNA. Translation: BAE24490.1.
AK143757 mRNA. Translation: BAE25526.1.
AK165353 mRNA. Translation: BAE38146.1.
AK165401 mRNA. Translation: BAE38163.1.
AK057650 mRNA. Translation: BAB71542.1.
BC024424 mRNA. Translation: AAH24424.1.
BC031140 mRNA. Translation: AAH31140.1.
IPIIPI00169586.
IPI00761916.
IPI00867792.
RefSeqNP_001171448.1. NM_001177977.1.
NP_001171449.1. NM_001177978.1.
NP_666309.1. NM_146197.4.
UniGeneMm.268448.

3D structure databases

HSSPHSSP built from PDB template 1LCI based on UniProtKB P08659.
ProteinModelPortalQ8K0L3.
SMRQ8K0L3. Positions 34-570.
ModBaseSearch...

PTM databases

PhosphoSiteQ8K0L3.

Proteomic databases

PRIDEQ8K0L3.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000084647; ENSMUSP00000081697; ENSMUSG00000030945.
ENSMUST00000098084; ENSMUSP00000095690; ENSMUSG00000030945.
ENSMUST00000167935; ENSMUSP00000126670; ENSMUSG00000030945.
GeneID233799.
KEGGmmu:233799.
NMPDRfig|10090.3.peg.17514.
UCSCuc009jlh.2. mouse.
uc009jli.2. mouse.

Organism-specific databases

CTD233799.
MGIMGI:2385289. Acsm2.

Phylogenomic databases

HOGENOMHBG547964.
HOVERGENHBG053031.
InParanoidQ8K0L3.
OMAISDTAWI.
OrthoDBEOG40ZQXB.
PhylomeDBQ8K0L3.

Gene expression databases

ArrayExpressQ8K0L3.
BgeeQ8K0L3.
CleanExMM_ACSM2.
GenevestigatorQ8K0L3.

Family and domain databases

InterProIPR020845. AMP-binding_CS.
IPR000873. AMP-dep_Synth/Lig.
[Graphical view]
KOK01896.
PfamPF00501. AMP-binding. 1 hit.
[Graphical view]
PROSITEPS00455. AMP_BINDING. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio381829.
SOURCESearch...

Entry information

Entry nameACSM2_MOUSE
AccessionPrimary (citable) accession number: Q8K0L3
Secondary accession number(s): Q3TNC6 expand/collapse secondary AC list , Q3US47, Q8R1L3, Q96LX4
Entry history
Integrated into UniProtKB/Swiss-Prot: October 2, 2007
Last sequence update: October 1, 2002
Last modified: November 16, 2011
This is version 75 of the entry and version 1 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

SIMILARITY comments

Index of protein domains and families