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Protein

Acyl-coenzyme A synthetase ACSM1, mitochondrial

Gene

Acsm1

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

Functioni

Functions as GTP-dependent lipoate-activating enzyme that generates the substrate for lipoyltransferase (By similarity). 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 similarity1 Publication

Catalytic activityi

ATP + a carboxylate + CoA = AMP + diphosphate + an acyl-CoA.
GTP + lipoate = diphosphate + lipoyl-GMP.

Cofactori

Mg2+By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei448 – 4481ATPBy similarity
Binding sitei463 – 4631ATPBy similarity
Binding sitei559 – 5591ATPBy similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi222 – 2309ATPBy similarity

GO - Molecular functioni

  • acyl-CoA ligase activity Source: UniProtKB
  • ATP binding Source: UniProtKB-KW
  • butyrate-CoA ligase activity Source: UniProtKB
  • fatty acid ligase activity Source: MGI
  • GTP binding Source: UniProtKB-KW
  • metal ion binding Source: UniProtKB-KW

GO - Biological processi

  • fatty acid biosynthetic process Source: MGI
Complete GO annotation...

Keywords - Molecular functioni

Ligase

Keywords - Biological processi

Fatty acid metabolism, Lipid metabolism

Keywords - Ligandi

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

Enzyme and pathway databases

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

Chemistry

SwissLipidsiSLP:000001205.

Names & Taxonomyi

Protein namesi
Recommended name:
Acyl-coenzyme A synthetase ACSM1, mitochondrial (EC:6.2.1.2)
Alternative name(s):
Acyl-CoA synthetase medium-chain family member 1
Butyrate--CoA ligase 1
Butyryl-coenzyme A synthetase 1
Lipoate-activating enzyme
Middle-chain acyl-CoA synthetase 1
Gene namesi
Name:Acsm1
Synonyms:Bucs1, Lae, Macs1
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 7

Organism-specific databases

MGIiMGI:2152200. Acsm1.

Subcellular locationi

GO - Cellular componenti

  • blood microparticle Source: MGI
  • extracellular exosome Source: MGI
  • mitochondrial matrix Source: UniProtKB
  • mitochondrion Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Mitochondrion

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei1 – 3535MitochondrionSequence analysisAdd
BLAST
Chaini36 – 573538Acyl-coenzyme A synthetase ACSM1, mitochondrialPRO_0000306092Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei81 – 811N6-succinyllysineCombined sources
Modified residuei142 – 1421N6-acetyllysine; alternateCombined sources
Modified residuei142 – 1421N6-succinyllysine; alternateCombined sources
Modified residuei179 – 1791N6-succinyllysineCombined sources
Modified residuei200 – 2001N6-acetyllysine; alternateCombined sources
Modified residuei200 – 2001N6-succinyllysine; alternateCombined sources
Modified residuei210 – 2101N6-acetyllysineCombined sources
Modified residuei233 – 2331N6-succinyllysineCombined sources
Modified residuei324 – 3241N6-succinyllysineCombined sources
Modified residuei352 – 3521N6-acetyllysine; alternateCombined sources
Modified residuei352 – 3521N6-succinyllysine; alternateCombined sources
Modified residuei387 – 3871N6-acetyllysine; alternateCombined sources
Modified residuei387 – 3871N6-succinyllysine; alternateCombined sources
Modified residuei501 – 5011N6-succinyllysineCombined sources
Modified residuei527 – 5271N6-acetyllysineCombined sources
Modified residuei534 – 5341N6-acetyllysine; alternateCombined sources
Modified residuei534 – 5341N6-succinyllysine; alternateCombined sources
Modified residuei545 – 5451N6-acetyllysineCombined sources

Keywords - PTMi

Acetylation

Proteomic databases

EPDiQ91VA0.
MaxQBiQ91VA0.
PaxDbiQ91VA0.
PRIDEiQ91VA0.

PTM databases

iPTMnetiQ91VA0.
PhosphoSiteiQ91VA0.
SwissPalmiQ91VA0.

Expressioni

Tissue specificityi

Highly expressed in liver and kidney.1 Publication

Gene expression databases

BgeeiQ91VA0.
CleanExiMM_ACSM1.
ExpressionAtlasiQ91VA0. baseline and differential.
GenevisibleiQ91VA0. MM.

Interactioni

Subunit structurei

Monomer.By similarity

Protein-protein interaction databases

IntActiQ91VA0. 3 interactions.
MINTiMINT-1860696.
STRINGi10090.ENSMUSP00000036140.

Structurei

3D structure databases

ProteinModelPortaliQ91VA0.
SMRiQ91VA0. Positions 39-570.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiKOG1175. Eukaryota.
COG0365. LUCA.
GeneTreeiENSGT00760000119178.
HOGENOMiHOG000229982.
HOVERGENiHBG053031.
InParanoidiQ91VA0.
KOiK01896.
OMAiFMGYEDN.
OrthoDBiEOG7D85VZ.
PhylomeDBiQ91VA0.
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 (2)i

Sequence statusi: Complete.

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

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q91VA0-1) [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
MQWLKSFQIC KVLQGFSLSP TQLHRRLFSR VGAPRWNDHD SPEEFNFASD
60 70 80 90 100
VLDYWAQMEE EGKRGPSPAF WWVNGQGDEI KWSFRKLRDL TCRTANVFEQ
110 120 130 140 150
ICGLQQGDHL ALILPRVPEW WLVTVGCMRT GIIFMPGTTQ LKAKDILYRI
160 170 180 190 200
QISRAKAIVT TASLVPEVES VASECPDLKT KLVVSDHSHE GWLDFCSLIK
210 220 230 240 250
SASPDHTCIK SKMKDPMAIF FTSGTTGYPK MAKHNQGLAF RSYIPSCRKL
260 270 280 290 300
LKLKTSDILW CMSDPGWILA TVGCLIEPWT SGCTVFIHHL PQFDPKVIVE
310 320 330 340 350
VLFKYPITQC LAAPGVYRMV LQQKTSNLRF PTLEHCTTGG ESLLPEEYEQ
360 370 380 390 400
WKQRTGLSIH EVYGQSETGI SSATLREMKI KRGSIGKAIL PFDLQIIDEK
410 420 430 440 450
GNILPPNTEG YIGIRIKPTR PLGLFMEYEN SPESTSEVEC GDFYNSGDRA
460 470 480 490 500
TIDEEGYIWF LGRGDDVINA SGYRIGPVEV ENALAEHPAV AESAVVSSPD
510 520 530 540 550
KDRGEVVKAF IVLNPEFLSH DQEQLIKELQ HHVKSVTAPY KYPRKVEFVS
560 570
ELPKTVTGKI KRKELRNKEF GQL
Length:573
Mass (Da):64,760
Last modified:December 1, 2001 - v1
Checksum:i557F25D467CA305B
GO
Isoform 2 (identifier: Q91VA0-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     369-395: Missing.

Note: No experimental confirmation available.
Show »
Length:546
Mass (Da):61,848
Checksum:iDAAF1F2C5EADB8F4
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti465 – 4651D → V in BAE28977 (PubMed:16141072).Curated
Sequence conflicti525 – 5251L → F in BAE28977 (PubMed:16141072).Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei369 – 39527Missing in isoform 2. 1 PublicationVSP_028392Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB059428 mRNA. Translation: BAB64534.1.
AK149550 mRNA. Translation: BAE28952.1.
AK149586 mRNA. Translation: BAE28977.1.
BC016414 mRNA. Translation: AAH16414.1.
BC022149 mRNA. Translation: AAH22149.1.
CCDSiCCDS21783.1. [Q91VA0-1]
RefSeqiNP_473435.1. NM_054094.5. [Q91VA0-1]
UniGeneiMm.427560.

Genome annotation databases

EnsembliENSMUST00000047929; ENSMUSP00000036140; ENSMUSG00000033533. [Q91VA0-1]
GeneIDi117147.
KEGGimmu:117147.
UCSCiuc009jlm.1. mouse. [Q91VA0-1]
uc012fsv.1. mouse. [Q91VA0-2]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB059428 mRNA. Translation: BAB64534.1.
AK149550 mRNA. Translation: BAE28952.1.
AK149586 mRNA. Translation: BAE28977.1.
BC016414 mRNA. Translation: AAH16414.1.
BC022149 mRNA. Translation: AAH22149.1.
CCDSiCCDS21783.1. [Q91VA0-1]
RefSeqiNP_473435.1. NM_054094.5. [Q91VA0-1]
UniGeneiMm.427560.

3D structure databases

ProteinModelPortaliQ91VA0.
SMRiQ91VA0. Positions 39-570.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiQ91VA0. 3 interactions.
MINTiMINT-1860696.
STRINGi10090.ENSMUSP00000036140.

Chemistry

SwissLipidsiSLP:000001205.

PTM databases

iPTMnetiQ91VA0.
PhosphoSiteiQ91VA0.
SwissPalmiQ91VA0.

Proteomic databases

EPDiQ91VA0.
MaxQBiQ91VA0.
PaxDbiQ91VA0.
PRIDEiQ91VA0.

Protocols and materials databases

DNASUi117147.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000047929; ENSMUSP00000036140; ENSMUSG00000033533. [Q91VA0-1]
GeneIDi117147.
KEGGimmu:117147.
UCSCiuc009jlm.1. mouse. [Q91VA0-1]
uc012fsv.1. mouse. [Q91VA0-2]

Organism-specific databases

CTDi116285.
MGIiMGI:2152200. Acsm1.

Phylogenomic databases

eggNOGiKOG1175. Eukaryota.
COG0365. LUCA.
GeneTreeiENSGT00760000119178.
HOGENOMiHOG000229982.
HOVERGENiHBG053031.
InParanoidiQ91VA0.
KOiK01896.
OMAiFMGYEDN.
OrthoDBiEOG7D85VZ.
PhylomeDBiQ91VA0.
TreeFamiTF354287.

Enzyme and pathway databases

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

Miscellaneous databases

NextBioi369520.
PROiQ91VA0.
SOURCEiSearch...

Gene expression databases

BgeeiQ91VA0.
CleanExiMM_ACSM1.
ExpressionAtlasiQ91VA0. baseline and differential.
GenevisibleiQ91VA0. 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

« Hide 'large scale' publications
  1. "Molecular identification and characterization of two medium-chain acyl-CoA synthetases, MACS1 and the Sa gene product."
    Fujino T., Takei Y.A., Sone H., Ioka R.X., Kamataki A., Magoori K., Takahashi S., Sakai J., Yamamoto T.T.
    J. Biol. Chem. 276:35961-35966(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
    Tissue: Kidney.
  2. "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 AND 2).
    Strain: C57BL/6J.
    Tissue: Liver.
  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 and Liver.
  4. Lubec G., Sunyer B., Chen W.-Q.
    Submitted (JAN-2009) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 249-254, IDENTIFICATION BY MASS SPECTROMETRY.
    Strain: OF1.
    Tissue: Hippocampus.
  5. "Purification, characterization, and mass spectrometric sequencing of a medium chain acyl-CoA synthetase from mouse liver mitochondria and comparisons with the homologues of rat and bovine."
    Kasuya F., Tatsuki T., Ohta M., Kawai Y., Igarashi K.
    Protein Expr. Purif. 47:405-414(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY.
  6. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Kidney, Liver and Lung.
  7. "SIRT5-mediated lysine desuccinylation impacts diverse metabolic pathways."
    Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.
    Mol. Cell 50:919-930(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUCCINYLATION [LARGE SCALE ANALYSIS] AT LYS-81; LYS-142; LYS-179; LYS-200; LYS-233; LYS-324; LYS-352; LYS-387; LYS-501 AND LYS-534, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  8. "Label-free quantitative proteomics of the lysine acetylome in mitochondria identifies substrates of SIRT3 in metabolic pathways."
    Rardin M.J., Newman J.C., Held J.M., Cusack M.P., Sorensen D.J., Li B., Schilling B., Mooney S.D., Kahn C.R., Verdin E., Gibson B.W.
    Proc. Natl. Acad. Sci. U.S.A. 110:6601-6606(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-142; LYS-200; LYS-210; LYS-352; LYS-387; LYS-527; LYS-534 AND LYS-545, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.

Entry informationi

Entry nameiACSM1_MOUSE
AccessioniPrimary (citable) accession number: Q91VA0
Secondary accession number(s): Q3UED4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 2, 2007
Last sequence update: December 1, 2001
Last modified: May 11, 2016
This is version 120 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, Direct protein sequencing, 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.