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Reviewed, UniProtKB/Swiss-Prot Q4G176 (ACSF3_HUMAN)

Last modified November 3, 2009. Version 38. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Alternative products · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Acyl-CoA synthetase family member 3, mitochondrial
    EC=6.2.1.-
Gene names
Name: ACSF3
ORF Names: PSEC0197
OrganismHomo sapiens (Human) [Complete proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length576 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level.

General annotation (Comments)

Function

Acyl-CoA synthases catalyze the initial reaction in fatty acid metabolism, by forming a thioester with CoA. May have some preference toward very-long-chain substrates. Ref.5

Subcellular location

Mitochondrion Potential.

Sequence similarities

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

Ontologies

Keywords
   Biological processFatty acid metabolism
Lipid metabolism
   Cellular componentMitochondrion
   Coding sequence diversityAlternative splicing
Polymorphism
   DomainTransit peptide
   LigandATP-binding
Nucleotide-binding
   Molecular functionLigase
   PTMAcetylation
   Technical termComplete proteome
Gene Ontology (GO)
   Biological processfatty acid metabolic process Ref.5

Inferred from direct assay. Source: UniProtKB

   Cellular componentmitochondrion

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

acid-thiol ligase activity Ref.5

Inferred from direct assay. Source: UniProtKB

Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q4G176-1)

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: Q4G176-2)

The sequence of this isoform differs from the canonical sequence as follows:
     466-576: YWIRGRTSVD...KALIRHFHPS → LTRAPFPQGT...WPTPASQMWL
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Transit peptide1 – 8383Mitochondrion Potential
Chain84 – 576493Acyl-CoA synthetase family member 3, mitochondrial
PRO_0000315800

Regions

Nucleotide binding202 – 2109ATP By similarity

Sites

Binding site4571ATP By similarity
Binding site4711ATP By similarity
Binding site5631ATP By similarity

Amino acid modifications

Modified residue4391N6-acetyllysine Ref.7

Natural variations

Alternative sequence466 – 576111YWIRG…HFHPS → LTRAPFPQGTPWCLRMASTG SEAGPQWTSSRLEATRSAPW RWSGTCWPTPASQMWL in isoform 2.
VSP_030704
Natural variant21P → L: dbSNP rs7188200. Ref.1 Ref.2 Ref.3
VAR_038306
Natural variant171A → P: dbSNP rs11547019. Ref.4
VAR_038307
Natural variant3721V → M: dbSNP rs3743979. Ref.4
VAR_038308

Experimental info

Sequence conflict1481A → V in AAH28399. Ref.4
Sequence conflict2781K → E in BAC11654. Ref.2

Sequences

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

Last modified January 15, 2008. Version 2.
Checksum: 707F3A628057EAF5

FASTA57664,114
        10         20         30         40         50         60 
MPPHVVLTFR RLGCALASCR LAPARHRGSG LLHTAPVARS DRSAPVFTRA LAFGDRIALV 

        70         80         90        100        110        120 
DQHGRHTYRE LYSRSLRLSQ EICRLCGCVG GDLREERVSF LCANDASYVV AQWASWMSGG 

       130        140        150        160        170        180 
VAVPLYRKHP AAQLEYVICD SQSSVVLASQ EYLELLSPVV RKLGVPLLPL TPAIYTGAVE 

       190        200        210        220        230        240 
EPAEVPVPEQ GWRNKGAMII YTSGTTGRPK GVLSTHQNIR AVVTGLVHKW AWTKDDVILH 

       250        260        270        280        290        300 
VLPLHHVHGV VNALLCPLWV GATCVMMPEF SPQQVWEKFL SSETPRINVF MAVPTIYTKL 

       310        320        330        340        350        360 
MEYYDRHFTQ PHAQDFLRAV CEEKIRLMVS GSAALPLPVL EKWKNITGHT LLERYGMTEI 

       370        380        390        400        410        420 
GMALSGPLTT AVRLPGSVGT PLPGVQVRIV SENPQREACS YTIHAEGDER GTKVTPGFEE 

       430        440        450        460        470        480 
KEGELLVRGP SVFREYWNKP EETKSAFTLD GWFKTGDTVV FKDGQYWIRG RTSVDIIKTG 

       490        500        510        520        530        540 
GYKVSALEVE WHLLAHPSIT DVAVIGVPDM TWGQRVTAVV TLREGHSLSH RELKEWARNV 

       550        560        570 
LAPYAVPSEL VLVEEIPRNQ MGKIDKKALI RHFHPS 

« Hide

Isoform 2.

Checksum: 077DDEDF3607028D
Show »

FASTA52157,820

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] (ISOFORM 1), VARIANT LEU-2.
[2]"Signal sequence and keyword trap in silico for selection of full-length human cDNAs encoding secretion or membrane proteins from oligo-capped cDNA libraries."
Otsuki T., Ota T., Nishikawa T., Hayashi K., Suzuki Y., Yamamoto J., Wakamatsu A., Kimura K., Sakamoto K., Hatano N., Kawai Y., Ishii S., Saito K., Kojima S., Sugiyama T., Ono T., Okano K., Yoshikawa Y. expand/collapse author list , Aotsuka S., Sasaki N., Hattori A., Okumura K., Nagai K., Sugano S., Isogai T.
DNA Res. 12:117-126(2005) [PubMed: 16303743] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), VARIANT LEU-2.
Tissue: Embryo.
[3]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], VARIANT LEU-2.
[4]"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] (ISOFORMS 1 AND 2), VARIANTS PRO-17 AND MET-372.
Tissue: Brain.
[5]"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: 17762044] [Abstract]
Cited for: FUNCTION, ENZYME ACTIVITY.
[6]Colinge J., Superti-Furga G., Bennett K.L.
Submitted (OCT-2008) to UniProtKB
Cited for: IDENTIFICATION [LARGE SCALE ANALYSIS], MASS SPECTROMETRY.
[7]"Lysine acetylation targets protein complexes and co-regulates major cellular functions."
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T., Olsen J.V., Mann M.
Science 325:834-840(2009) [PubMed: 19608861] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-439, MASS SPECTROMETRY.

Cross-references

Sequence databases

AK075499 mRNA. Translation: BAC11654.1.
AK290963 mRNA. Translation: BAF83652.1.
CH471184 Genomic DNA. Translation: EAW66744.1.
BC028399 mRNA. Translation: AAH28399.1.
BC072391 mRNA. Translation: AAH72391.1.
IPIIPI00166395.
IPI00450347.
RefSeqNP_001120686.1.
NP_777577.2.
UniGeneHs.461727

3D structure databases

ModBaseSearch...

Protein-protein interaction databases

STRINGQ4G176.

Proteomic databases

PRIDEQ4G176.

Genome annotation databases

EnsemblENST00000317447; ENSP00000320646; ENSG00000176715; Homo sapiens. [Genome view]
ENST00000378345; ENSP00000367596; ENSG00000176715; Homo sapiens. [Genome view]
ENST00000393145; ENSP00000376853; ENSG00000176715; Homo sapiens. [Genome view]
ENST00000406948; ENSP00000384627; ENSG00000176715; Homo sapiens. [Genome view]
GeneID197322.

Organism-specific databases

CTD197322.
GeneCardsGC16P087688.
HGNCHGNC:27288. ACSF3.
HPAHPA008322.
HPA008323.
GenAtlasSearch...

Phylogenomic databases

HOGENOMQ4G176.
HOVERGENQ4G176.

Gene expression databases

ArrayExpressQ4G176.
BgeeQ4G176.
CleanExHS_ACSF3.
GenevestigatorQ4G176.

Family and domain databases

InterProIPR000873. AMP-dep_Synth/Lig.
[Graphical view]
PfamPF00501. AMP-binding. 2 hits.
[Graphical view]
PROSITEPS00455. AMP_BINDING. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameACSF3_HUMAN
AccessionPrimary (citable) accession number: Q4G176
Secondary accession number(s): A8K4J8, Q6INA0, Q8N2F7
Entry history
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: January 15, 2008
Last modified: November 3, 2009
This is version 38 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)
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.

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Index of human polymorphisms and disease mutations

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Alternative products · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents