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Q6SKG1 (ACSM3_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified November 16, 2011. Version 56. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | 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

Names and origin

Protein namesRecommended name:
Acyl-coenzyme A synthetase ACSM3, mitochondrial

EC=6.2.1.2
Alternative name(s):
Acyl-CoA synthetase medium-chain family member 3
Butyrate--CoA ligase 3
Butyryl-coenzyme A synthetase 3
Middle-chain acyl-CoA synthetase 3
SA rat hypertension-associated protein
Short name=Protein SA
Gene names
Name:Acsm3
Synonyms:Sah
OrganismRattus norvegicus (Rat)
Taxonomic identifier10116 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus

Protein attributes

Sequence length580 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.

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
   DomainTransit peptide
   LigandATP-binding
Magnesium
Metal-binding
Nucleotide-binding
   Molecular functionLigase
   PTMPhosphoprotein
   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...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Transit peptide1 – 2121Mitochondrion Potential
Chain22 – 580559Acyl-coenzyme A synthetase ACSM3, mitochondrial
PRO_0000306100

Regions

Nucleotide binding229 – 2379ATP By similarity
Nucleotide binding368 – 3736ATP By similarity

Sites

Binding site4551ATP By similarity
Binding site4701ATP By similarity
Binding site5661ATP By similarity

Amino acid modifications

Modified residue371Phosphotyrosine By similarity

Sequences

Sequence LengthMass (Da)Tools
Q6SKG1 [UniParc].

Last modified July 5, 2004. Version 1.
Checksum: E2F46C5C530D6278

FASTA58065,713
        10         20         30         40         50         60 
MAMLLRARCF HRLAIPDPRR ILYKDYRTAI PQNFSNYESM KHDFKIEIPE YFNFAKDVLD 

        70         80         90        100        110        120 
QWTNTEKTGK RLSNPAFWWV DGNGKEVRWS FEELGSLSRK FANILTEACS LQRGDRVMVI 

       130        140        150        160        170        180 
LPKIPEWWLA NVACLRTGTV LIPGTTQLTQ KDILYRLQSS KSKCIITDDT LAPAVDIVAA 

       190        200        210        220        230        240 
KCENLHSKLI VSQHSREGWG NLKEMMKYAS DSHTCVDTKH NELMAIYFTS GTTGPPKMIG 

       250        260        270        280        290        300 
HTHSSFGLGL SVNGRFWLDL IASDVMWNTS DTGWAKSAWS SVFSPWTQGA CVFAHYLPRF 

       310        320        330        340        350        360 
DSTSILQTLS KFPITVFCSA PTAYRMLIQN DITSYKFNSL KHCVSAGEPI NPEVMEQWKK 

       370        380        390        400        410        420 
KTGLDIYEGY GQTETVLICG NFKGMKIKPG SMGKPSPAFN VEILDENGTI LPPGQEGDIA 

       430        440        450        460        470        480 
VQVLPDRPFG LFTHYVDNPS KTASTLRGNF YITGDRGYMD EDGYFWFVAR SDDVILSSGY 

       490        500        510        520        530        540 
RIGPFEVESA LIEHPSIAES AVVSSPDPIR GEVVKAFIVL NPDYKLHDQE QLKKEIQEHV 

       550        560        570        580 
KKTTAPYKYP RKIEFIEELP KTVSGKVKRN ELRRKEWTTT 

« Hide

References

« Hide 'large scale' references
[1]"Exon repetition: a major pathway for processing mRNA of some genes is allele-specific."
Rigatti R., Jia J.-H., Samani N.J., Eperon I.C.
Nucleic Acids Res. 32:441-446(2004) [PubMed: 14739236] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: SHR and Wistar Kyoto.
[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: 15489334] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Kidney.
[3]"Possible alternative splicing of the rat SA gene."
Gu L., Dene H., Rapp J.P.
Mamm. Genome 6:683-684(1995) [PubMed: 8535086] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 374-479.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AY455861 Genomic DNA. Translation: AAR20710.1.
AY456695 Genomic DNA. Translation: AAR21570.1.
BC090325 mRNA. Translation: AAH90325.1.
U19832 Genomic DNA. Translation: AAA95995.1.
IPIIPI00421616.
RefSeqNP_150234.1. NM_033231.1.
UniGeneRn.88644.

3D structure databases

HSSPHSSP built from PDB template 1LCI based on UniProtKB P08659.
ProteinModelPortalQ6SKG1.
SMRQ6SKG1. Positions 46-578.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ6SKG1.

Proteomic databases

PRIDEQ6SKG1.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID24763.
KEGGrno:24763.

Organism-specific databases

CTD6296.
RGD62086. Acsm3.

Phylogenomic databases

eggNOGmaNOG11567.
GeneTreeENSGT00550000074278.
HOVERGENHBG053031.
InParanoidQ6SKG1.

Gene expression databases

ArrayExpressQ6SKG1.
GenevestigatorQ6SKG1.

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

NextBio604315.

Entry information

Entry nameACSM3_RAT
AccessionPrimary (citable) accession number: Q6SKG1
Secondary accession number(s): Q62742
Entry history
Integrated into UniProtKB/Swiss-Prot: October 2, 2007
Last sequence update: July 5, 2004
Last modified: November 16, 2011
This is version 56 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families