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Protein

Acyl-coenzyme A synthetase ACSM2, mitochondrial

Gene

Acsm2

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

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).By similarity

Catalytic activityi

ATP + a carboxylate + CoA = AMP + diphosphate + an acyl-CoA.

Cofactori

Mg2+By similarity, Mn2+By similarity

Enzyme regulationi

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

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei139 – 1391Coenzyme ABy similarity
Binding sitei365 – 3651SubstrateBy similarity
Binding sitei447 – 4471ATPBy similarity
Binding sitei462 – 4621ATPBy similarity
Binding sitei473 – 4731SubstrateBy similarity
Binding sitei502 – 5021Coenzyme ABy similarity
Binding sitei533 – 5331Coenzyme ABy similarity
Binding sitei558 – 5581ATPBy similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi221 – 2299ATPBy similarity
Nucleotide bindingi360 – 3656ATPBy similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Ligase

Keywords - Biological processi

Fatty acid metabolism, Lipid metabolism

Keywords - Ligandi

ATP-binding, Magnesium, Metal-binding, Nucleotide-binding

Enzyme and pathway databases

ReactomeiR-MMU-177128. Conjugation of salicylate with glycine.
R-MMU-177135. Conjugation of benzoate with glycine.
R-MMU-177162. Conjugation of phenylacetate with glutamine.

Names & Taxonomyi

Protein namesi
Recommended 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 namesi
Name:Acsm2
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 7

Organism-specific databases

MGIiMGI:2385289. Acsm2.

Subcellular locationi

GO - Cellular componenti

  • mitochondrial matrix Source: UniProtKB-SubCell
  • mitochondrion Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Mitochondrion

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei1 – 4646MitochondrionSequence analysisAdd
BLAST
Chaini47 – 575529Acyl-coenzyme A synthetase ACSM2, mitochondrialPRO_0000306095Add
BLAST

Proteomic databases

MaxQBiQ8K0L3.
PaxDbiQ8K0L3.
PRIDEiQ8K0L3.

PTM databases

iPTMnetiQ8K0L3.
PhosphoSiteiQ8K0L3.

Expressioni

Gene expression databases

BgeeiQ8K0L3.
CleanExiMM_ACSM2.
ExpressionAtlasiQ8K0L3. baseline and differential.
GenevisibleiQ8K0L3. MM.

Interactioni

Subunit structurei

Monomer.By similarity

Protein-protein interaction databases

IntActiQ8K0L3. 2 interactions.
MINTiMINT-4116780.
STRINGi10090.ENSMUSP00000095690.

Structurei

3D structure databases

ProteinModelPortaliQ8K0L3.
SMRiQ8K0L3. Positions 34-570.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni470 – 4723Coenzyme A bindingBy similarity
Regioni541 – 5433Coenzyme A bindingBy similarity

Sequence similaritiesi

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiKOG1175. Eukaryota.
COG0365. LUCA.
GeneTreeiENSGT00760000119178.
HOGENOMiHOG000229982.
HOVERGENiHBG053031.
InParanoidiQ8K0L3.
KOiK01896.
OMAiWADMETA.
OrthoDBiEOG7D85VZ.
PhylomeDBiQ8K0L3.
TreeFamiTF354287.

Family and domain databases

InterProiIPR025110. AMP-bd_C.
IPR020845. AMP-binding_CS.
IPR000873. AMP-dep_Synth/Lig.
[Graphical view]
PfamiPF00501. AMP-binding. 1 hit.
PF13193. AMP-binding_C. 1 hit.
[Graphical view]
PROSITEiPS00455. AMP_BINDING. 1 hit.
[Graphical view]

Sequences (3)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 3 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q8K0L3-1) [UniParc]FASTAAdd to basket

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.

« Hide

        10         20         30         40         50
MHHLWKIPRL FTLWGNEISC RTFHMNIKKL IPIQWGHQEA PAKFNFASDV
60 70 80 90 100
IDHWASVEKA GKRSSGPALW WMNGSGKEIK WSFRELSEAS KQTANVLSGA
110 120 130 140 150
CGLHRGDRVA VVLPRIPEWW LMILGCMRTG LVFMPGTIQM RSSDILYRLQ
160 170 180 190 200
ASKARAIVAG DEVAQEVDAV APDCSFLKIK LLVSENSREG WLNFKALLKE
210 220 230 240 250
ASTIHQCVET ESRESAAIYF TSGTSGPPKM AEHSHCSLGI KAKMDAASWT
260 270 280 290 300
GLSTSDIIWT ISDTAWIMNI LGAFLEPWVL GACIFVHLLP KFDSQTVLKV
310 320 330 340 350
LSSYPINTLV GAPIIYRMLL QQDLSSYKFP HLHSCFSGGE TLLPETLENW
360 370 380 390 400
KAKTGLEIRE IYGQTETGLI CRVSRTMKVK PGYLGTAFAH YDVQVIDEQG
410 420 430 440 450
NVLPPGKEGD IAIRVKPIWP IGMFSGYVDN PKKTQDNIRG DFWLMGDRGI
460 470 480 490 500
KDPEGYFHFI GRSDDIINSS GYRIGPSEVE NALMEHPAVS ETAVISSPDP
510 520 530 540 550
SRGEVVKAFV VLAPEFLSHD RDQLTKVLQE HVKSVTAPYK YPRKVEFVLD
560 570
LPKTVTGKIE RAKLRAKEWK TSGRA
Length:575
Mass (Da):64,269
Last modified:October 1, 2002 - v1
Checksum:iA7E5956D54B119D8
GO
Isoform 2 (identifier: Q8K0L3-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-1: M → MTTGSLDLPFVGSHRWIKWTTASLTM

Note: No experimental confirmation available.
Show »
Length:600
Mass (Da):67,057
Checksum:iCD0F661EC08E1C4F
GO
Isoform 3 (identifier: Q8K0L3-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     471-471: G → GAYFCR

Note: No experimental confirmation available.
Show »
Length:580
Mass (Da):64,910
Checksum:i2D228B445D3D2DF3
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti515 – 5151E → G in BAB71542 (Ref. 2) Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 11M → MTTGSLDLPFVGSHRWIKWT TASLTM in isoform 2. 1 PublicationVSP_028393
Alternative sequencei471 – 4711G → GAYFCR in isoform 3. 1 PublicationVSP_028394

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS21782.1. [Q8K0L3-1]
CCDS52379.1. [Q8K0L3-2]
CCDS52380.1. [Q8K0L3-3]
RefSeqiNP_001171448.1. NM_001177977.1. [Q8K0L3-2]
NP_001171449.1. NM_001177978.1. [Q8K0L3-3]
NP_666309.1. NM_146197.4. [Q8K0L3-1]
UniGeneiMm.268448.

Genome annotation databases

EnsembliENSMUST00000084647; ENSMUSP00000081697; ENSMUSG00000030945. [Q8K0L3-3]
ENSMUST00000098084; ENSMUSP00000095690; ENSMUSG00000030945. [Q8K0L3-2]
ENSMUST00000167935; ENSMUSP00000126670; ENSMUSG00000030945. [Q8K0L3-1]
GeneIDi233799.
KEGGimmu:233799.
UCSCiuc009jlh.2. mouse. [Q8K0L3-1]
uc009jli.2. mouse. [Q8K0L3-3]
uc009jlj.2. mouse. [Q8K0L3-2]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS21782.1. [Q8K0L3-1]
CCDS52379.1. [Q8K0L3-2]
CCDS52380.1. [Q8K0L3-3]
RefSeqiNP_001171448.1. NM_001177977.1. [Q8K0L3-2]
NP_001171449.1. NM_001177978.1. [Q8K0L3-3]
NP_666309.1. NM_146197.4. [Q8K0L3-1]
UniGeneiMm.268448.

3D structure databases

ProteinModelPortaliQ8K0L3.
SMRiQ8K0L3. Positions 34-570.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiQ8K0L3. 2 interactions.
MINTiMINT-4116780.
STRINGi10090.ENSMUSP00000095690.

PTM databases

iPTMnetiQ8K0L3.
PhosphoSiteiQ8K0L3.

Proteomic databases

MaxQBiQ8K0L3.
PaxDbiQ8K0L3.
PRIDEiQ8K0L3.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000084647; ENSMUSP00000081697; ENSMUSG00000030945. [Q8K0L3-3]
ENSMUST00000098084; ENSMUSP00000095690; ENSMUSG00000030945. [Q8K0L3-2]
ENSMUST00000167935; ENSMUSP00000126670; ENSMUSG00000030945. [Q8K0L3-1]
GeneIDi233799.
KEGGimmu:233799.
UCSCiuc009jlh.2. mouse. [Q8K0L3-1]
uc009jli.2. mouse. [Q8K0L3-3]
uc009jlj.2. mouse. [Q8K0L3-2]

Organism-specific databases

CTDi233799.
MGIiMGI:2385289. Acsm2.

Phylogenomic databases

eggNOGiKOG1175. Eukaryota.
COG0365. LUCA.
GeneTreeiENSGT00760000119178.
HOGENOMiHOG000229982.
HOVERGENiHBG053031.
InParanoidiQ8K0L3.
KOiK01896.
OMAiWADMETA.
OrthoDBiEOG7D85VZ.
PhylomeDBiQ8K0L3.
TreeFamiTF354287.

Enzyme and pathway databases

ReactomeiR-MMU-177128. Conjugation of salicylate with glycine.
R-MMU-177135. Conjugation of benzoate with glycine.
R-MMU-177162. Conjugation of phenylacetate with glutamine.

Miscellaneous databases

NextBioi381829.
PROiQ8K0L3.
SOURCEiSearch...

Gene expression databases

BgeeiQ8K0L3.
CleanExiMM_ACSM2.
ExpressionAtlasiQ8K0L3. baseline and differential.
GenevisibleiQ8K0L3. MM.

Family and domain databases

InterProiIPR025110. AMP-bd_C.
IPR020845. AMP-binding_CS.
IPR000873. AMP-dep_Synth/Lig.
[Graphical view]
PfamiPF00501. AMP-binding. 1 hit.
PF13193. AMP-binding_C. 1 hit.
[Graphical view]
PROSITEiPS00455. AMP_BINDING. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  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.
    , 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] (ISOFORMS 1; 2 AND 3).
    Strain: C57BL/6J.
    Tissue: Embryonic head, Kidney and Spleen.
  2. 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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    Strain: FVB/N.
    Tissue: Kidney.
  4. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Kidney and Liver.

Entry informationi

Entry nameiACSM2_MOUSE
AccessioniPrimary (citable) accession number: Q8K0L3
Secondary accession number(s): Q3TNC6
, Q3US47, Q8R1L3, Q96LX4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 2, 2007
Last sequence update: October 1, 2002
Last modified: May 11, 2016
This is version 109 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.