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Q6NUN0 (ACSM5_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 85. 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·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Acyl-coenzyme A synthetase ACSM5, mitochondrial

EC=6.2.1.2
Alternative name(s):
Acyl-CoA synthetase medium-chain family member 5
Gene names
Name:ACSM5
Synonyms:MACS3
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length579 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.

Tissue specificity

Detected in kidney and liver. Ref.4

Sequence similarities

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

Sequence caution

The sequence BAA91273.1 differs from that shown. Reason: Frameshift at position 560.

Ontologies

Keywords
   Biological processFatty acid metabolism
Lipid metabolism
   Cellular componentMitochondrion
   Coding sequence diversityAlternative splicing
Polymorphism
   DomainTransit peptide
   LigandATP-binding
GTP-binding
Magnesium
Metal-binding
Nucleotide-binding
   Molecular functionLigase
   PTMAcetylation
   Technical termComplete proteome
Reference 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

GTP binding

Inferred from electronic annotation. Source: UniProtKB-KW

butyrate-CoA ligase activity

Inferred from electronic annotation. Source: UniProtKB-EC

metal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q6NUN0-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform 2 (identifier: Q6NUN0-2)

The sequence of this isoform differs from the canonical sequence as follows:
     209-579: Missing.
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Transit peptide1 – 2626Mitochondrion Potential
Chain27 – 579553Acyl-coenzyme A synthetase ACSM5, mitochondrial
PRO_0000306101

Regions

Nucleotide binding230 – 2389ATP By similarity
Nucleotide binding368 – 3736ATP By similarity

Sites

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

Amino acid modifications

Modified residue971N6-acetyllysine; alternate By similarity
Modified residue971N6-succinyllysine; alternate By similarity
Modified residue1521N6-acetyllysine By similarity
Modified residue3031N6-acetyllysine; alternate By similarity
Modified residue3031N6-succinyllysine; alternate By similarity

Natural variations

Alternative sequence209 – 579371Missing in isoform 2.
VSP_028398
Natural variant651R → Q.
Corresponds to variant rs9928053 [ dbSNP | Ensembl ].
VAR_055495
Natural variant1591Q → H. Ref.4
VAR_035252
Natural variant1821E → K.
Corresponds to variant rs7192210 [ dbSNP | Ensembl ].
VAR_055496
Natural variant2171M → V.
Corresponds to variant rs59025904 [ dbSNP | Ensembl ].
VAR_061011
Natural variant3521P → R. Ref.4
Corresponds to variant rs8062344 [ dbSNP | Ensembl ].
VAR_035253
Natural variant3601H → R. Ref.4
Corresponds to variant rs12931877 [ dbSNP | Ensembl ].
VAR_035254
Natural variant5331T → M. Ref.4
Corresponds to variant rs56308819 [ dbSNP | Ensembl ].
VAR_035255

Experimental info

Sequence conflict1421M → V in AAH16703. Ref.3
Sequence conflict231 – 2344SGTT → KREPP in BAA91273. Ref.1
Sequence conflict5021V → A in AAH68516. Ref.3

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified November 24, 2009. Version 2.
Checksum: 9493CB853CE29CB1

FASTA57964,760
        10         20         30         40         50         60 
MRPWLRHLVL QALRNSRAFC GSHGKPAPLP VPQKIVATWE AISLGRQLVP EYFNFAHDVL 

        70         80         90        100        110        120 
DVWSRLEEAG HRPPNPAFWW VNGTGAEIKW SFEELGKQSR KAANVLGGAC GLQPGDRMML 

       130        140        150        160        170        180 
VLPRLPEWWL VSVACMRTGT VMIPGVTQLT EKDLKYRLQA SRAKSIITSD SLAPRVDAIS 

       190        200        210        220        230        240 
AECPSLQTKL LVSDSSRPGW LNFRELLREA STEHNCMRTK SRDPLAIYFT SGTTGAPKMV 

       250        260        270        280        290        300 
EHSQSSYGLG FVASGRRWVA LTESDIFWNT TDTGWVKAAW TLFSAWPNGS CIFVHELPRV 

       310        320        330        340        350        360 
DAKVILNTLS KFPITTLCCV PTIFRLLVQE DLTRYQFQSL RHCLTGGEAL NPDVREKWKH 

       370        380        390        400        410        420 
QTGVELYEGY GQSETVVICA NPKGMKIKSG SMGKASPPYD VQIVDDEGNV LPPGEEGNVA 

       430        440        450        460        470        480 
VRIRPTRPFC FFNCYLDNPE KTAASEQGDF YITGDRARMD KDGYFWFMGR NDDVINSSSY 

       490        500        510        520        530        540 
RIGPVEVESA LAEHPAVLES AVVSSPDPIR GEVVKAFIVL TPAYSSHDPE ALTRELQEHV 

       550        560        570 
KRVTAPYKYP RKVAFVSELP KTVSGKIQRS KLRSQEWGK 

« Hide

Isoform 2 [UniParc].

Checksum: 5C29746BE07D3E30
Show »

FASTA20823,320

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] (ISOFORM 1).
[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] (ISOFORMS 1 AND 2).
Tissue: Brain and Kidney.
[4]"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: VARIANTS HIS-159; ARG-352; ARG-360 AND MET-533, TISSUE SPECIFICITY.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AK000588 mRNA. Translation: BAA91273.1. Frameshift.
AC137056 Genomic DNA. No translation available.
BC013753 mRNA. Translation: AAH13753.1.
BC016703 mRNA. Translation: AAH16703.1.
BC068516 mRNA. Translation: AAH68516.1.
RefSeqNP_060358.2. NM_017888.2.
UniGeneHs.659606.

3D structure databases

ProteinModelPortalQ6NUN0.
SMRQ6NUN0. Positions 11-577.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid120323. 1 interaction.
IntActQ6NUN0. 1 interaction.
STRING9606.ENSP00000327916.

PTM databases

PhosphoSiteQ6NUN0.

Polymorphism databases

DMDM269849538.

Proteomic databases

PaxDbQ6NUN0.
PRIDEQ6NUN0.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000331849; ENSP00000327916; ENSG00000183549. [Q6NUN0-1]
ENST00000575584; ENSP00000460112; ENSG00000183549. [Q6NUN0-2]
GeneID54988.
KEGGhsa:54988.
UCSCuc002dhd.1. human. [Q6NUN0-2]
uc002dhe.3. human. [Q6NUN0-1]

Organism-specific databases

CTD54988.
GeneCardsGC16P020420.
H-InvDBHIX0023110.
HGNCHGNC:26060. ACSM5.
HPAHPA041435.
MIM614361. gene.
neXtProtNX_Q6NUN0.
PharmGKBPA162375501.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0365.
HOGENOMHOG000229982.
HOVERGENHBG053031.
InParanoidQ6NUN0.
KOK01896.
OMAQTGVELY.
OrthoDBEOG7D85VZ.
PhylomeDBQ6NUN0.
TreeFamTF354287.

Enzyme and pathway databases

ReactomeREACT_111217. Metabolism.

Gene expression databases

ArrayExpressQ6NUN0.
BgeeQ6NUN0.
CleanExHS_ACSM5.
GenevestigatorQ6NUN0.

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

GenomeRNAi54988.
NextBio58283.
PROQ6NUN0.
SOURCESearch...

Entry information

Entry nameACSM5_HUMAN
AccessionPrimary (citable) accession number: Q6NUN0
Secondary accession number(s): Q96AV1, Q96CX8, Q9NWV3
Entry history
Integrated into UniProtKB/Swiss-Prot: October 2, 2007
Last sequence update: November 24, 2009
Last modified: April 16, 2014
This is version 85 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

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