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Reviewed, UniProtKB/Swiss-Prot P0C7M7 (ACSM4_HUMAN)

Last modified October 13, 2009. Version 12. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Acyl-coenzyme A synthetase ACSM4, mitochondrial
    EC=6.2.1.2
Gene names
Name: ACSM4
OrganismHomo sapiens (Human) [Complete proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

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
   Technical termComplete 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

magnesium 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_0000339384

Regions

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

Sites

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

Sequences

Sequence LengthMass (Da)Tools
P0C7M7-1 [UniParc].

Last modified June 10, 2008. Version 1.
Checksum: 217EF355B93BACC0

FASTA58065,703
        10         20         30         40         50         60 
MKIFFRYQTF RFIWLTKPPG RRLHKDHQLW TPLTLADFEA INRCNRPLPK NFNFAADVLD 

        70         80         90        100        110        120 
QWSQKEKTGE RPANPALWWV NGKGDEVKWS FRELGSLSRK AANVLTKPCG LQRGDRLAVI 

       130        140        150        160        170        180 
LPRIPEWWLV NVACIRTGII FMPGTIQLTA KDILYRLRAS KAKCIVASEE VAPAVESIVL 

       190        200        210        220        230        240 
ECPDLKTKLL VSPQSWNGWL SFQELFQFAS EEHSCVETGS QEPMTIYFTS GTTGFPKMAQ 

       250        260        270        280        290        300 
HSQSSLGIGF TLCGRYWLDL KSSDIIWNMS DTGWVKAAIG SVFSSWLCGA CVFVHRMAQF 

       310        320        330        340        350        360 
DTDTFLDTLT TYPITTLCSP PTVYRMLVQK DLKRYKFKSL RHCLTGGEPL NPEVLEQWRV 

       370        380        390        400        410        420 
QTGLELYEGY GQTEVGMICA NQKGQEIKPG SMGKGMLPYD VQIIDENGNV LPPGKEGEIA 

       430        440        450        460        470        480 
LRLKPTRPFC FFSKYVDNPQ KTAATIRGDF YVTGDRGVMD SDGYFWFVGR ADDVIISSGY 

       490        500        510        520        530        540 
RIGPFEVESA LIEHPAVVES AVVSSPDQIR GEVVKAFVVL AAPFKSYNPE KLTLELQDHV 

       550        560        570        580 
KKSTAPYKYP RKVEFVQELP KTITGKIKRN VLRDQEWRGR 

« Hide

References

« Hide 'large scale' references
[1]"The finished DNA sequence of human chromosome 12."
Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R. expand/collapse author list , Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Montgomery K.T., Morgan M.B., Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z., Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H., Draper H., Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S., Kelly S.H., Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H., Santibanez J., Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q., Williams G.A., Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V., Bailey M., Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E., Burkett C.E., Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K., Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D., Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M., Dathorne S.R., David R., Davis C.M., Davy-Carroll L., Deshazo D.R., Donlin J.E., D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J., Escotto M., Flagg N., Forbes L.D., Gabisi A.M., Garza M., Hamilton C., Henderson N., Hernandez O., Hines S., Hogues M.E., Huang M., Idlebird D.G., Johnson R., Jolivet A., Jones S., Kagan R., King L.M., Leal B., Lebow H., Lee S., LeVan J.M., Lewis L.C., London P., Lorensuhewa L.M., Loulseged H., Lovett D.A., Lucier A., Lucier R.L., Ma J., Madu R.C., Mapua P., Martindale A.D., Martinez E., Massey E., Mawhiney S., Meador M.G., Mendez S., Mercado C., Mercado I.C., Merritt C.E., Miner Z.L., Minja E., Mitchell T., Mohabbat F., Mohabbat K., Montgomery B., Moore N., Morris S., Munidasa M., Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O., Nwokenkwo S., Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J., Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A., Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M., Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I., Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A., Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D., Trejos Z.Y., Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I., Vera V.A., Villasana D.M., Wang L., Ward-Moore S., Warren J.T., Wei X., White F., Williamson A.L., Wleczyk R., Wooden H.S., Wooden S.H., Yen J., Yoon L., Yoon V., Zorrilla S.E., Nelson D., Kucherlapati R., Weinstock G., Gibbs R.A.
Nature 440:346-351(2006) [PubMed: 16541075] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[2]"Exhaustive RT-PCR and sequencing of all novel TWINSCAN predictions in human."
Stevens M., Wei C., Gross S.S., McPherson J., Brent M.R.
Submitted (MAR-2006) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 330-474.
[3]"Evidence for 26 distinct acyl-coenzyme A synthetase genes in the human genome."
Watkins P.A., Maiguel D., Jia Z., Pevsner J.
J. Lipid Res. 48:2736-2750(2007) [PubMed: 17762044] [Abstract]
Cited for: IDENTIFICATION.

Cross-references

Sequence databases

AC131205 Genomic DNA. No translation available.
DY654856 mRNA. No translation available.
IPIIPI00243302.
RefSeqNP_001073923.1.
UniGeneHs.450804

3D structure databases

ModBaseSearch...

PTM databases

PhosphoSiteP0C7M7.

Proteomic databases

PRIDEP0C7M7.

Genome annotation databases

EnsemblENST00000399422; ENSP00000382349; ENSG00000215009; Homo sapiens. [Genome view]
GeneID341392.
KEGGhsa:341392.
UCSCuc001qsx.1. human.

Organism-specific databases

CTD341392.
GeneCardsGC12P007349.
HGNCHGNC:32016. ACSM4.
GenAtlasSearch...

Gene expression databases

CleanExHS_ACSM4.
GenevestigatorP0C7M7.

Family and domain databases

InterProIPR000873. AMP-dep_Synth/Lig.
[Graphical view]
PfamPF00501. AMP-binding. 1 hit.
[Graphical view]
PROSITEPS00455. AMP_BINDING. 1 hit.
[Graphical view]
ProtoNetSearch...

Other Resources

NextBio98133.

Entry information

Entry nameACSM4_HUMAN
AccessionPrimary (citable) accession number: P0C7M7
Secondary accession number(s): A8MTI6
Entry history
Integrated into UniProtKB/Swiss-Prot: June 10, 2008
Last sequence update: June 10, 2008
Last modified: October 13, 2009
This is version 12 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

Human chromosome 12

Human chromosome 12: entries, gene names and cross-references to MIM

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents