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P0C7M7 (ACSM4_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 48. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | 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 ACSM4, mitochondrial

EC=6.2.1.2
Alternative name(s):
Acyl-CoA synthetase medium-chain family member 4
Gene names
Name:ACSM4
OrganismHomo sapiens (Human) [Reference 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 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.

Subcellular location

Mitochondrion matrix By similarity.

Sequence similarities

Belongs to the ATP-dependent AMP-binding enzyme family.

Ontologies

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

Natural variations

Natural variant4811R → H.
Corresponds to variant rs61584783 [ dbSNP | Ensembl ].
VAR_061010

Sequences

Sequence LengthMass (Da)Tools
P0C7M7 [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] [Europe PMC] [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] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AC131205 Genomic DNA. No translation available.
DY654856 mRNA. No translation available.
RefSeqNP_001073923.1. NM_001080454.1.
UniGeneHs.450804.

3D structure databases

ProteinModelPortalP0C7M7.
SMRP0C7M7. Positions 45-578.
ModBaseSearch...
MobiDBSearch...

PTM databases

PhosphoSiteP0C7M7.

Polymorphism databases

DMDM190358135.

Proteomic databases

PaxDbP0C7M7.
PRIDEP0C7M7.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000399422; ENSP00000382349; ENSG00000215009.
GeneID341392.
KEGGhsa:341392.
UCSCuc001qsx.1. human.

Organism-specific databases

CTD341392.
GeneCardsGC12P007456.
HGNCHGNC:32016. ACSM4.
HPAHPA049895.
MIM614360. gene.
neXtProtNX_P0C7M7.
PharmGKBPA162375472.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0365.
HOGENOMHOG000229982.
HOVERGENHBG053031.
InParanoidP0C7M7.
KOK01896.
OMAQFASEEH.
OrthoDBEOG7D85VZ.
PhylomeDBP0C7M7.
TreeFamTF354287.

Enzyme and pathway databases

ReactomeREACT_111217. Metabolism.

Gene expression databases

BgeeP0C7M7.
CleanExHS_ACSM4.
GenevestigatorP0C7M7.

Family and domain databases

InterProIPR025110. AMP-bd_C.
IPR020845. AMP-binding_CS.
IPR000873. AMP-dep_Synth/Lig.
[Graphical view]
PfamPF00501. AMP-binding. 1 hit.
PF13193. AMP-binding_C. 1 hit.
[Graphical view]
PROSITEPS00455. AMP_BINDING. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

GenomeRNAi341392.
NextBio98133.
PROP0C7M7.
SOURCESearch...

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: April 16, 2014
This is version 48 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
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

SIMILARITY comments

Index of protein domains and families

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 12

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