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Q08AH3 (ACS2A_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 64. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | 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 ACSM2A, mitochondrial

EC=6.2.1.2
Alternative name(s):
Acyl-CoA synthetase medium-chain family member 2A
Butyrate--CoA ligase 2A
Butyryl-coenzyme A synthetase 2A
Middle-chain acyl-CoA synthetase 2A
Gene names
Name:ACSM2A
Synonyms:ACSM2, MACS2
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length577 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein 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.

Subunit structure

Monomer By similarity.

Subcellular location

Mitochondrion matrix By similarity.

Sequence similarities

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

Sequence caution

The sequence AAC23497.1 differs from that shown. Reason: Erroneous gene model prediction.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Transit peptide1 – 4646Mitochondrion Potential
Chain47 – 577531Acyl-coenzyme A synthetase ACSM2A, mitochondrial
PRO_0000306093

Regions

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

Sites

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

Natural variations

Natural variant3351V → L.
Corresponds to variant rs4643305 [ dbSNP | Ensembl ].
VAR_058692
Natural variant3361T → A.
Corresponds to variant rs5002299 [ dbSNP | Ensembl ].
VAR_058693
Natural variant3371V → G.
Corresponds to variant rs4586421 [ dbSNP | Ensembl ].
VAR_058694
Natural variant5131S → L. Ref.4 Ref.7 Ref.8
Corresponds to variant rs1133607 [ dbSNP | Ensembl ].
VAR_035247
Natural variant5611A → T.
Corresponds to variant rs1054977 [ dbSNP | Ensembl ].
VAR_035248

Experimental info

Sequence conflict4631N → D in BAG53201. Ref.1
Sequence conflict4631N → D in AAI25177. Ref.3
Sequence conflict4631N → D in AAC23497. Ref.4

Secondary structure

.................................................................................................. 577
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q08AH3 [UniParc].

Last modified September 1, 2009. Version 2.
Checksum: 16167FC69562436F

FASTA57764,223
        10         20         30         40         50         60 
MHWLRKVQGL CTLWGTQMSS RTLYINSRQL VSLQWGHQEV PAKFNFASDV LDHWADMEKA 

        70         80         90        100        110        120 
GKRLPSPALW WVNGKGKELM WNFRELSENS QQAANVLSGA CGLQRGDRVA VVLPRVPEWW 

       130        140        150        160        170        180 
LVILGCIRAG LIFMPGTIQM KSTDILYRLQ MSKAKAIVAG DEVIQEVDTV ASECPSLRIK 

       190        200        210        220        230        240 
LLVSEKSCDG WLNFKKLLNE ASTTHHCVET GSQEASAIYF TSGTSGLPKM AEHSYSSLGL 

       250        260        270        280        290        300 
KAKMDAGWTG LQASDIMWTI SDTGWILNIL CSLMEPWALG ACTFVHLLPK FDPLVILKTL 

       310        320        330        340        350        360 
SSYPIKSMMG APIVYRMLLQ QDLSSYKFPH LQNCVTVGES LLPETLENWR AQTGLDIRES 

       370        380        390        400        410        420 
YGQTETGLTC MVSKTMKIKP GYMGTAASCY DVQIIDDKGN VLPPGTEGDI GIRVKPIRPI 

       430        440        450        460        470        480 
GIFSGYVDNP DKTAANIRGD FWLLGDRGIK DEDGYFQFMG RANDIINSSG YRIGPSEVEN 

       490        500        510        520        530        540 
ALMEHPAVVE TAVISSPDPV RGEVVKAFVV LASQFLSHDP EQLTKELQQH VKSVTAPYKY 

       550        560        570 
PRKIEFVLNL PKTVTGKIQR AKLRDKEWKM SGKARAQ 

« Hide

References

« Hide 'large scale' references
[1]"Complete sequencing and characterization of 21,243 full-length human cDNAs."
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. expand/collapse author list , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Kidney.
[2]"The sequence and analysis of duplication-rich human chromosome 16."
Martin J., Han C., Gordon L.A., Terry A., Prabhakar S., She X., Xie G., Hellsten U., Chan Y.M., Altherr M., Couronne O., Aerts A., Bajorek E., Black S., Blumer H., Branscomb E., Brown N.C., Bruno W.J. expand/collapse author list , Buckingham J.M., Callen D.F., Campbell C.S., Campbell M.L., Campbell E.W., Caoile C., Challacombe J.F., Chasteen L.A., Chertkov O., Chi H.C., Christensen M., Clark L.M., Cohn J.D., Denys M., Detter J.C., Dickson M., Dimitrijevic-Bussod M., Escobar J., Fawcett J.J., Flowers D., Fotopulos D., Glavina T., Gomez M., Gonzales E., Goodstein D., Goodwin L.A., Grady D.L., Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Hildebrand C.E., Huang W., Israni S., Jett J., Jewett P.B., Kadner K., Kimball H., Kobayashi A., Krawczyk M.-C., Leyba T., Longmire J.L., Lopez F., Lou Y., Lowry S., Ludeman T., Manohar C.F., Mark G.A., McMurray K.L., Meincke L.J., Morgan J., Moyzis R.K., Mundt M.O., Munk A.C., Nandkeshwar R.D., Pitluck S., Pollard M., Predki P., Parson-Quintana B., Ramirez L., Rash S., Retterer J., Ricke D.O., Robinson D.L., Rodriguez A., Salamov A., Saunders E.H., Scott D., Shough T., Stallings R.L., Stalvey M., Sutherland R.D., Tapia R., Tesmer J.G., Thayer N., Thompson L.S., Tice H., Torney D.C., Tran-Gyamfi M., Tsai M., Ulanovsky L.E., Ustaszewska A., Vo N., White P.S., Williams A.L., Wills P.L., Wu J.-R., Wu K., Yang J., DeJong P., Bruce D., Doggett N.A., Deaven L., Schmutz J., Grimwood J., Richardson P., Rokhsar D.S., Eichler E.E., Gilna P., Lucas S.M., Myers R.M., Rubin E.M., Pennacchio L.A.
Nature 432:988-994(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[3]"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].
[4]"Genome duplications and other features in 12 Mb of DNA sequence from human chromosome 16p and 16q."
Loftus B.J., Kim U.-J., Sneddon V.P., Kalush F., Brandon R., Fuhrmann J., Mason T., Crosby M.L., Barnstead M., Cronin L., Mays A.D., Cao Y., Xu R.X., Kang H.-L., Mitchell S., Eichler E.E., Harris P.C., Venter J.C., Adams M.D.
Genomics 60:295-308(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] OF 299-577, VARIANT LEU-513.
[5]"Crystal structure of L64P mutant of human acyl-CoA synthetase medium-chain family member 2A."
Structural genomics consortium (SGC)
Submitted (FEB-2008) to the PDB data bank
Cited for: X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS) IN COMPLEX WITH AMP AND MAGNESIUM.
[6]"Structural snapshots for the conformation-dependent catalysis by human medium-chain acyl-coenzyme A synthetase ACSM2A."
Kochan G., Pilka E.S., von Delft F., Oppermann U., Yue W.W.
J. Mol. Biol. 388:997-1008(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS) OF 32-577 IN COMPLEXES WITH ATP; COENZYME A; IBUPROFEN AND MAGNESIUM.
[7]"An acyl-CoA synthetase gene family in chromosome 16p12 may contribute to multiple risk factors."
Iwai N., Mannami T., Tomoike H., Ono K., Iwanaga Y.
Hypertension 41:1041-1046(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT LEU-513.
[8]"The L513S polymorphism in medium-chain acyl-CoA synthetase 2 (MACS2) is associated with risk factors of the metabolic syndrome in a Caucasian study population."
Lindner I., Rubin D., Helwig U., Nitz I., Hampe J., Schreiber S., Schrezenmeir J., Doering F.
Mol. Nutr. Food Res. 50:270-274(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT LEU-513.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AK096039 mRNA. Translation: BAG53201.1.
AC137056 Genomic DNA. No translation available.
BC125176 mRNA. Translation: AAI25177.1.
AC003034 Genomic DNA. Translation: AAC23497.1. Sequence problems.
RefSeqNP_001010845.1. NM_001010845.2.
XP_005255150.1. XM_005255093.1.
UniGeneHs.298252.
Hs.656497.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2VZEX-ray2.45A/B/C32-577[»]
2WD9X-ray2.60A/B/C32-576[»]
3B7WX-ray2.00A32-577[»]
3C5EX-ray1.60A32-577[»]
3DAYX-ray1.95A32-577[»]
3EQ6X-ray2.40A/B32-577[»]
3GPCX-ray1.90A/B32-577[»]
ProteinModelPortalQ08AH3.
SMRQ08AH3. Positions 34-569.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING9606.ENSP00000219054.

PTM databases

PhosphoSiteQ08AH3.

Polymorphism databases

DMDM257050995.

Proteomic databases

PaxDbQ08AH3.
PRIDEQ08AH3.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000219054; ENSP00000219054; ENSG00000183747.
ENST00000396104; ENSP00000379411; ENSG00000183747.
ENST00000573854; ENSP00000459451; ENSG00000183747.
ENST00000575690; ENSP00000460349; ENSG00000183747.
GeneID123876.
KEGGhsa:123876.
UCSCuc002dhf.4. human.

Organism-specific databases

CTD123876.
GeneCardsGC16P020463.
H-InvDBHIX0012859.
HGNCHGNC:32017. ACSM2A.
HPAHPA057699.
MIM614358. gene.
neXtProtNX_Q08AH3.
PharmGKBPA162375402.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0365.
HOGENOMHOG000229982.
HOVERGENHBG053031.
InParanoidQ08AH3.
KOK01896.
OMAKNDRRRT.
OrthoDBEOG7D85VZ.
PhylomeDBQ08AH3.
TreeFamTF354264.

Enzyme and pathway databases

ReactomeREACT_111217. Metabolism.

Gene expression databases

BgeeQ08AH3.
GenevestigatorQ08AH3.

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

EvolutionaryTraceQ08AH3.
GenomeRNAi123876.
NextBio81177.
PROQ08AH3.
SOURCESearch...

Entry information

Entry nameACS2A_HUMAN
AccessionPrimary (citable) accession number: Q08AH3
Secondary accession number(s): B3KTT9, O75202
Entry history
Integrated into UniProtKB/Swiss-Prot: October 2, 2007
Last sequence update: September 1, 2009
Last modified: April 16, 2014
This is version 64 of the entry and version 2 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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

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 16

Human chromosome 16: entries, gene names and cross-references to MIM