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P47912 (LCF4_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 114. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | 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:
Long-chain-fatty-acid--CoA ligase 4

EC=6.2.1.3
Alternative name(s):
Fatty acid activator 4
Long-chain acyl-CoA synthetase 4
Gene names
Name:FAA4
Ordered Locus Names:YMR246W
ORF Names:YM9408.08
OrganismSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]
Taxonomic identifier559292 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces

Protein attributes

Sequence length694 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Esterification, concomitant with transport, of exogenous long-chain fatty acids into metabolically active CoA thioesters for subsequent degradation or incorporation into phospholipids. Contributes, with FAA1, to the activation of imported myristate.

Catalytic activity

ATP + a long-chain fatty acid + CoA = AMP + diphosphate + an acyl-CoA.

Cofactor

Magnesium By similarity.

Miscellaneous

Present with 31200 molecules/cell in log phase SD medium.

Sequence similarities

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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 694694Long-chain-fatty-acid--CoA ligase 4
PRO_0000193122

Experimental info

Sequence conflict5521N → G in CAA88635. Ref.1
Sequence conflict6311V → G in CAA88635. Ref.1

Sequences

Sequence LengthMass (Da)Tools
P47912 [UniParc].

Last modified February 1, 1996. Version 1.
Checksum: CF6524949C96D24D

FASTA69477,267
        10         20         30         40         50         60 
MTEQYSVAVG EAANEHETAP RRNIRVKDQP LIRPINSSAS TLYEFALECF TKGGKRDGMA 

        70         80         90        100        110        120 
WRDIIDIHET KKTIVKRVDG KDKPIEKTWL YYELTPYITM TYEEMICVMH DIGRGLIKIG 

       130        140        150        160        170        180 
VKPNGENKFH IFASTSHKWM KTFLGCMSQG IPVVTAYDTL GESGLIHSMV ETDSVAIFTD 

       190        200        210        220        230        240 
NQLLSKLAVP LKTAKNVKFV IHNEPIDPSD KRQNGKLYKA AKDAVDKIKE VRPDIKIYSF 

       250        260        270        280        290        300 
DEIIEIGKKA KDEVELHFPK PEDPACIMYT SGSTGTPKGV VLTHYNIVAG IGGVGHNVIG 

       310        320        330        340        350        360 
WIGPTDRIIA FLPLAHIFEL TFEFEAFYWN GILGYANVKT LTPTSTRNCQ GDLMEFKPTV 

       370        380        390        400        410        420 
MVGVAAVWET VRKGILAKIN ELPGWSQTLF WTVYALKERN IPCSGLLSGL IFKRIREATG 

       430        440        450        460        470        480 
GNLRFILNGG SAISIDAQKF LSNLLCPMLI GYGLTEGVAN ACVLEPEHFD YGIAGDLVGT 

       490        500        510        520        530        540 
ITAKLVDVED LGYFAKNNQG ELLFKGAPIC SEYYKNPEET AAAFTDDGWF RTGDIAEWTP 

       550        560        570        580        590        600 
KGQVKIIDRK KNLVKTLNGE YIALEKLESI YRSNPYVQNI CVYADENKVK PVGIVVPNLG 

       610        620        630        640        650        660 
HLSKLAIELG IMVPGEDVES YIHEKKLQDA VCKDMLSTAK SQGLNGIELL CGIVFFEEEW 

       670        680        690 
TPENGLVTSA QKLKRRDILA AVKPDVERVY KENT 

« Hide

References

« Hide 'large scale' references
[1]"Saccharomyces cerevisiae contains four fatty acid activation (FAA) genes: an assessment of their role in regulating protein N-myristoylation and cellular lipid metabolism."
Johnson D.R., Knoll L.J., Levin D.E., Gordon J.I.
J. Cell Biol. 127:751-762(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], CHARACTERIZATION.
[2]"The nucleotide sequence of Saccharomyces cerevisiae chromosome XIII."
Bowman S., Churcher C.M., Badcock K., Brown D., Chillingworth T., Connor R., Dedman K., Devlin K., Gentles S., Hamlin N., Hunt S., Jagels K., Lye G., Moule S., Odell C., Pearson D., Rajandream M.A., Rice P. expand/collapse author list , Skelton J., Walsh S.V., Whitehead S., Barrell B.G.
Nature 387:90-93(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 204508 / S288c.
[3]"The reference genome sequence of Saccharomyces cerevisiae: Then and now."
Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R., Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S., Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.
G3 (Bethesda) 4:389-398(2014) [PubMed] [Europe PMC] [Abstract]
Cited for: GENOME REANNOTATION.
Strain: ATCC 204508 / S288c.
[4]"Global analysis of protein expression in yeast."
Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N., O'Shea E.K., Weissman J.S.
Nature 425:737-741(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
[5]"N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB."
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
Z48744 Genomic DNA. Translation: CAA88635.1.
Z48756 Genomic DNA. Translation: CAA88656.1.
BK006946 Genomic DNA. Translation: DAA10147.1.
PIRS56060.
RefSeqNP_013974.1. NM_001182754.1.

3D structure databases

ProteinModelPortalP47912.
SMRP47912. Positions 101-683.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid35425. 63 interactions.
DIPDIP-4361N.
IntActP47912. 29 interactions.
MINTMINT-516514.
STRING4932.YMR246W.

Proteomic databases

MaxQBP47912.
PaxDbP47912.
PeptideAtlasP47912.
PRIDEP47912.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiYMR246W; YMR246W; YMR246W.
GeneID855288.
KEGGsce:YMR246W.

Organism-specific databases

CYGDYMR246w.
SGDS000004860. FAA4.

Phylogenomic databases

eggNOGCOG1022.
GeneTreeENSGT00690000102168.
HOGENOMHOG000159459.
KOK01897.
OMAGYVTSAQ.
OrthoDBEOG7CCC0K.

Enzyme and pathway databases

BioCycYEAST:YMR246W-MONOMER.

Gene expression databases

GenevestigatorP47912.

Family and domain databases

InterProIPR020845. AMP-binding_CS.
IPR000873. AMP-dep_Synth/Lig.
[Graphical view]
PfamPF00501. AMP-binding. 1 hit.
[Graphical view]
PROSITEPS00455. AMP_BINDING. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio978932.

Entry information

Entry nameLCF4_YEAST
AccessionPrimary (citable) accession number: P47912
Secondary accession number(s): D6W073, Q05743
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1996
Last sequence update: February 1, 1996
Last modified: May 14, 2014
This is version 114 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

Yeast chromosome XIII

Yeast (Saccharomyces cerevisiae) chromosome XIII: entries and gene names

Yeast

Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD

SIMILARITY comments

Index of protein domains and families