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Q80W40 (ACSM4_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified November 16, 2011. Version 73. 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·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
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 ACSM4, mitochondrial
EC=6.2.1.2
Alternative name(s):
Olfactory specific medium-chain acyl CoA synthetase
Short name=O-MACS
Gene names
Name:Acsm4
Synonyms:Omacs
OrganismMus musculus (Mouse)
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

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 – 2222Mitochondrion Potential
Chain23 – 580558Acyl-coenzyme A synthetase ACSM4, mitochondrial
PRO_0000306104

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 residue5471Phosphotyrosine By similarity

Sequences

Sequence LengthMass (Da)Tools
Q80W40 [UniParc].

Last modified June 1, 2003. Version 1.
Checksum: 56A74EC03217D1C2

FASTA58065,427
        10         20         30         40         50         60 
MKVLLHCQRL RFIWLAKPAG RHFHRDSQLW APLTLDDFEA INRCEKPLPK NFNFAADVLD 

        70         80         90        100        110        120 
QWSLKEKSGE RPANPALWWV NGKGDEVKWS FQELGSLSRK AANVLTKPCG LQRGDRVAVI 

       130        140        150        160        170        180 
LPRIPEWWLI NVACMRTGLV FMPGTIQLTR KDILYRLQAS KAKCIVASEE VAPAVDSIVS 

       190        200        210        220        230        240 
ECPSLKTKLL VSPHHWDGWL NFQELLQSAS EEHNCVETGS QEPMAIYFTS GTTGSPKMAQ 

       250        260        270        280        290        300 
HSQGSLGIGY TLCGRYWLDL TSSDIMWNMS DTGWIKAAIG SVFSTWLRGA CVFVHRMAQF 

       310        320        330        340        350        360 
DTDIFLDTLT TYPITTLCSA PTVYRMLVQK DLKRYQFKRL RHCLTGGEPL NPEVLEQWKM 

       370        380        390        400        410        420 
QTGLELYEGY GQTEVGIICA NRKGEAIKPG SMGKGVVPYD VQIIDENGNI LPSGKEGEIA 

       430        440        450        460        470        480 
LRLKSDRPFC FFSEYVDNPE KTDATIRRNF YVTGDRGVMD DDGYFWFVGR ADDVIISSGY 

       490        500        510        520        530        540 
RIGPFEVESA LIEHPAVVES AVVSSPDPIR GEVVKAFIVL AAPYKCSNRE KLTAELQDHV 

       550        560        570        580 
KNSTAPYKYP RKVEFVQELP KTITGKIKRN VLRDQEWGRA

« Hide

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].
Strain: C57BL/6J.
Tissue: Head.
[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].
Strain: C57BL/6.
Tissue: Olfactory epithelium.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AK132127 mRNA. Translation: BAE20992.1.
BC048390 mRNA. Translation: AAH48390.1.
IPIIPI00265698.
RefSeqNP_848501.1. NM_178414.3.
UniGeneMm.240412.

3D structure databases

HSSPHSSP built from PDB template 1LCI based on UniProtKB P08659.
ProteinModelPortalQ80W40.
SMRQ80W40. Positions 46-577.
ModBaseSearch...

PTM databases

PhosphoSiteQ80W40.

Proteomic databases

PRIDEQ80W40.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000047045; ENSMUSP00000045160; ENSMUSG00000047026.
GeneID233801.
KEGGmmu:233801.
NMPDRfig|10090.3.peg.17516.
UCSCuc009jln.2. mouse.

Organism-specific databases

CTD341392.
MGIMGI:2681844. Acsm4.

Phylogenomic databases

eggNOGmaNOG11572.
GeneTreeENSGT00550000074278.
HOGENOMHBG547964.
HOVERGENHBG053031.
InParanoidQ80W40.
OMAKAKCIVA.
OrthoDBEOG4ZPDTX.
PhylomeDBQ80W40.

Gene expression databases

ArrayExpressQ80W40.
BgeeQ80W40.
CleanExMM_ACSM4.
GenevestigatorQ80W40.

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

NextBio381833.
SOURCESearch...

Entry information

Entry nameACSM4_MOUSE
AccessionPrimary (citable) accession number: Q80W40
Entry history
Integrated into UniProtKB/Swiss-Prot: October 2, 2007
Last sequence update: June 1, 2003
Last modified: November 16, 2011
This is version 73 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

to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents