P0C7M7 (ACSM4_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended 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

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	580 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence 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

Keywords
Biological process	Fatty acid metabolism Lipid metabolism
Cellular component	Mitochondrion
Coding sequence diversity	Polymorphism
Domain	Transit peptide
Ligand	ATP-binding Magnesium Metal-binding Nucleotide-binding
Molecular function	Ligase
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	acyl-CoA metabolic process Inferred from electronic annotation. Source: Compara fatty acid metabolic process Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	mitochondrial matrix Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW butyrate-CoA ligase activity Inferred from electronic annotation. Source: EC fatty-acyl-CoA synthase activity Inferred from electronic annotation. Source: Compara metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Transit peptide	1 – 22	22	Mitochondrion Potential
	Chain	23 – 580	558	Acyl-coenzyme A synthetase ACSM4, mitochondrial		PRO_0000339384
Regions
	Nucleotide binding	229 – 237	9	ATP By similarity
	Nucleotide binding	368 – 373	6	ATP By similarity
Sites
	Binding site	455	1	ATP By similarity
	Binding site	470	1	ATP By similarity
	Binding site	566	1	ATP By similarity
Natural variations
	Natural variant	481	1	R → H. Corresponds to variant rs61584783 [ dbSNP | Ensembl ].		VAR_061010

Sequences

	Sequence		Length	Mass (Da)
	P0C7M7 [UniParc]. Last modified June 10, 2008. Version 1. Checksum: 217EF355B93BACC0	FASTA	580	65,703
	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

References

	« Hide 'large scale' referencesShow '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. , 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.
IPI	IPI00243302.
RefSeq	NP_001073923.1. NM_001080454.1.
UniGene	Hs.450804.
3D structure databases
ProteinModelPortal	P0C7M7.
ModBase	Search...
PTM databases
PhosphoSite	P0C7M7.
Polymorphism databases
DMDM	190358135.
Proteomic databases
PaxDb	P0C7M7.
PRIDE	P0C7M7.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000399422; ENSP00000382349; ENSG00000215009.
GeneID	341392.
KEGG	hsa:341392.
UCSC	uc001qsx.1. human.
Organism-specific databases
CTD	341392.
GeneCards	GC12P007456.
HGNC	HGNC:32016. ACSM4.
HPA	HPA049895.
MIM	614360. gene.
neXtProt	NX_P0C7M7.
PharmGKB	PA162375472.
GenAtlas	Search...
Phylogenomic databases
eggNOG	COG0365.
HOGENOM	HOG000229982.
HOVERGEN	HBG053031.
InParanoid	P0C7M7.
KO	K01896.
OMA	QTFRFIW.
OrthoDB	EOG4ZPDTX.
Gene expression databases
Bgee	P0C7M7.
CleanEx	HS_ACSM4.
Genevestigator	P0C7M7.
Family and domain databases
InterPro	IPR020845. AMP-binding_CS. IPR000873. AMP-dep_Synth/Lig. IPR025110. DUF4009. [Graphical view]
Pfam	PF00501. AMP-binding. 1 hit. PF13193. DUF4009. 1 hit. [Graphical view]
PROSITE	PS00455. AMP_BINDING. 1 hit. [Graphical view]
ProtoNet	Search...
Other
GenomeRNAi	341392.
NextBio	98133.
SOURCE	Search...

Entry information

Entry name

ACSM4_HUMAN

Accession

Primary (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:	May 1, 2013
This is version 41 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.