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O70490 (ACSM2_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified April 3, 2013. Version 69. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
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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
Kidney-specific protein KS
Middle-chain acyl-CoA synthetase 2
Gene names
Name:Acsm2
Synonyms:Ks
OrganismRattus norvegicus (Rat) [Reference proteome]
Taxonomic identifier10116 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Rattus

Protein attributes

Sequence length572 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 C11 and on the corresponding 3-hydroxy- and 2,3- or 3,4-unsaturated acids (in vitro) By similarity.

Catalytic activity

ATP + a carboxylate + 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.

Tissue specificity

Detected in kidney, in proximal tubules. Ref.1

Developmental stage

First detected in kidney from 1 week old rats. Not detectable in fetal kidney and in kidney from newborn rats. Ref.1

Induction

Down-regulated in kidneys from a strain of spontaneously hypertensive rats (SHR). Down-regulated after unilateral ureteral obstruction or unilateral nephrectomy. Ref.1

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
   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 – 4646Mitochondrion Potential
Chain47 – 572526Acyl-coenzyme A synthetase ACSM2, mitochondrial
PRO_0000306096

Regions

Nucleotide binding221 – 2299ATP By similarity
Nucleotide binding359 – 3646ATP By similarity
Region469 – 4713Coenzyme A binding By similarity
Region540 – 5423Coenzyme A binding By similarity

Sites

Binding site1391Coenzyme A By similarity
Binding site3641Substrate By similarity
Binding site4461ATP By similarity
Binding site4611ATP By similarity
Binding site4721Substrate By similarity
Binding site5011Coenzyme A By similarity
Binding site5321Coenzyme A By similarity
Binding site5571ATP By similarity

Experimental info

Sequence conflict221T → S in AAD05209. Ref.1
Sequence conflict991G → R in AAH78721. Ref.2

Sequences

Sequence LengthMass (Da)Tools
O70490 [UniParc].

Last modified October 2, 2007. Version 2.
Checksum: 34BB5FB87A43958C

FASTA57264,145
        10         20         30         40         50         60 
MHWLWKIPRL CTFWGTEMFH RTFHMNIKKL MPIQWGHQEV PAKFNFASDV IDHWASLEKA 

        70         80         90        100        110        120 
GKRSPGPALW WMNGSGEELK WNFRELSEIS KQTANVLTGA CGLQRGDRVA VVLPRVPEWW 

       130        140        150        160        170        180 
LVTLGCMRSG LVFMPGTTQM KSTDILYRLQ SSKARAIVAG DEVVQEVDAV APDCSFLKIK 

       190        200        210        220        230        240 
LLVSEKNREG WLNFKALLKD ASPIHQCVET VSQESAAIYF TSGTSGPPKM AEHSHCSLGL 

       250        260        270        280        290        300 
KAKMDAGWTG LGPSDTMWTI SDTGWILNIL GSFLEPWVLG TCIFVHLLPK FDPQTVLKVL 

       310        320        330        340        350        360 
SSYPINTLLG APLIYRMLLQ QDLSSYKFPH LHSCFSGGET LLPETLESWK AKTGLEIREI 

       370        380        390        400        410        420 
YGQTETGITC RVSRTMKVKP GYLGTAIVPY DVQVIDEQGN VLPPGKEGDM ALRVKPIRPI 

       430        440        450        460        470        480 
GMFSGYVDNP KKTQANIRGD FWLLGDRGIK DTEGYFHFMG RTDDIINSSG YRIGPSEVEN 

       490        500        510        520        530        540 
ALMEHPAVVE TAVISSPDPI RREVVKAFVV LAPEFLSHDQ DQLTKVLQEH VKSVTAPYKY 

       550        560        570 
PRKVEFVLDL PKTITGKIER AKLRAKEWKT SG

« Hide

References

« Hide 'large scale' references
[1]"Molecular cloning of KS, a novel rat gene expressed exclusively in the kidney."
Hilgers K.F., Nagaraj S.K., Karginova E.A., Kazakova I.G., Chevalier R.L., Carey R.M., Pentz E.S., Gomez R.A.
Kidney Int. 54:1444-1454(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], DEVELOPMENTAL STAGE, INDUCTION, TISSUE SPECIFICITY.
Strain: Sprague-Dawley.
Tissue: Kidney.
[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].
Tissue: Kidney.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AF062389 mRNA. Translation: AAD05209.1.
BC078721 mRNA. Translation: AAH78721.1.
IPIIPI00198641.
RefSeqNP_653349.1. NM_144748.1.
UniGeneRn.14875.

3D structure databases

HSSPHSSP built from PDB template 1LCI based on UniProtKB P08659.
ProteinModelPortalO70490.
SMRO70490. Positions 34-569.
ModBaseSearch...

Protein-protein interaction databases

STRING10116.ENSRNOP00000020587.

PTM databases

PhosphoSiteO70490.

Proteomic databases

PaxDbO70490.
PRIDEO70490.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSRNOT00000020587; ENSRNOP00000020587; ENSRNOG00000014976.
GeneID246263.
KEGGrno:246263.
UCSCRGD:708383. rat.

Organism-specific databases

CTD123876.
RGD708383. Acsm2.

Phylogenomic databases

eggNOGCOG0365.
GeneTreeENSGT00700000104176.
HOGENOMHOG000229982.
HOVERGENHBG053031.
InParanoidO70490.
KOK01896.
OrthoDBEOG40ZQXB.

Gene expression databases

GenevestigatorO70490.

Family and domain databases

InterProIPR020845. AMP-binding_CS.
IPR000873. AMP-dep_Synth/Lig.
IPR025110. DUF4009.
[Graphical view]
PfamPF00501. AMP-binding. 1 hit.
PF13193. DUF4009. 1 hit.
[Graphical view]
PROSITEPS00455. AMP_BINDING. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio623619.

Entry information

Entry nameACSM2_RAT
AccessionPrimary (citable) accession number: O70490
Secondary accession number(s): Q6AZ63
Entry history
Integrated into UniProtKB/Swiss-Prot: October 2, 2007
Last sequence update: October 2, 2007
Last modified: April 3, 2013
This is version 69 of the entry and version 2 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

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