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Reviewed, UniProtKB/Swiss-Prot Q08AH3 (ACS2A_HUMAN)

Last modified July 7, 2009. Version 23. Feed History...

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

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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
    Middle-chain acyl-CoA synthetase 2A
    Butyryl coenzyme A synthetase 2A
    Butyrate--CoA ligase 2A
Gene names
Name: ACSM2A
Synonyms: ACSM2, MACS2
OrganismHomo sapiens (Human) [Complete proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

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Protein attributes

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

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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.

Subunit structure

Monomer By similarity.

Subcellular location

Mitochondrion matrix By similarity.

Sequence similarities

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

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Ontologies

Keywords
   Biological processFatty acid metabolism
Lipid metabolism
   Cellular componentMitochondrion
   Coding sequence diversityPolymorphism
   DomainTransit peptide
   LigandATP-binding
Magnesium
Metal-binding
Nucleotide-binding
   Molecular functionLigase
   Technical term3D-structure
Complete 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...

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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

Sites

Binding site4461ATP
Binding site4611ATP
Binding site5571ATP

Natural variations

Natural variant5131S → L: dbSNP rs1133607. Ref.3 Ref.5 Ref.6
VAR_035247
Natural variant5611A → T: dbSNP rs1054977.
VAR_035248

Secondary structure

1 ............................................................................................... 577
Helix Strand Turn

Details...

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Sequences

Sequence LengthMass (Da)Tools
Q08AH3-1 [UniParc].

Last modified October 31, 2006. Version 1.
Checksum: BC16787043B92ED9

FASTA57764,224
        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 RADDIINSSG YRIGPSEVEN 

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

       550        560        570 
PRKIEFVLNL PKTVTGKIQR AKLRDKEWKM SGKARAQ

« Hide

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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: 14702039] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Kidney.
[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].
[3]"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: 10493829] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] OF 371-577, VARIANT LEU-513.
[4]"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 ATP.
[5]"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: 12654705] [Abstract]
Cited for: VARIANT LEU-513.
[6]"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: 16521160] [Abstract]
Cited for: VARIANT LEU-513.
+Additional computationally mapped references.

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Cross-references

Sequence databases

AK096039 mRNA. Translation: BAG53201.1.
BC125176 mRNA. Translation: AAI25177.1.
AC003034 Genomic DNA. Translation: AAC23497.1.
IPIIPI00644771.
RefSeqNP_001010845.1.
UniGeneHs.298252

3D structure databases

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[»]
ModBaseSearch...

Proteomic databases

PRIDEQ08AH3.

Genome annotation databases

EnsemblENSG00000066813. Homo sapiens. [Contig view]
GeneID123876.
KEGGhsa:123876.
UCSCuc002dhf.2. human.

Organism-specific databases

GeneCardsGC16P020372.
HGNCHGNC:32017. ACSM2A.
GenAtlasSearch...

Phylogenomic databases

HOVERGENQ08AH3.

Enzyme and pathway databases

BRENDA6.2.1.2. 247.

Gene expression databases

ArrayExpressQ08AH3.
BgeeQ08AH3.

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

NextBio81177.

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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: October 31, 2006
Last modified: July 7, 2009
This is version 23 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)

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Relevant documents

Human chromosome 16

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

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

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