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Q08558 (DCI1_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 84. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | 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:
Delta(3,5)-Delta(2,4)-dienoyl-CoA isomerase

EC=5.3.3.-
Gene names
Name:DCI1
Synonyms:ECI2, EHD2
Ordered Locus Names:YOR180C
OrganismSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]
Taxonomic identifier559292 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces

Protein attributes

Sequence length271 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Converts 3,5-dienoyl-CoAs to the corresponding 2,4-dienoyl-CoAs. Involved in fatty acid metabolism. Required for ECI1 to be peroxisomal located. Ref.5 Ref.6 Ref.8

Pathway

Lipid metabolism; fatty acid beta-oxidation.

Subunit structure

Interacts with ECI1. Ref.5

Subcellular location

Peroxisome Ref.5 Ref.6 Ref.7.

Induction

By oleate, through the binding of the OAF1-PIP2 transcriptional activator complex to its promoter ORE element. Expression is also induced during ammonia pulses in yeast colonies, at the beginning of detectable ammonia production. Ref.4 Ref.6 Ref.7 Ref.9

Sequence similarities

Belongs to the enoyl-CoA hydratase/isomerase family.

Ontologies

Keywords
   Biological processFatty acid metabolism
Lipid metabolism
   Cellular componentPeroxisome
   Molecular functionIsomerase
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processfatty acid beta-oxidation

Inferred from mutant phenotype Ref.5. Source: SGD

   Cellular_componentperoxisomal matrix

Inferred from direct assay Ref.5. Source: SGD

   Molecular_functiondodecenoyl-CoA delta-isomerase activity

Inferred from direct assay Ref.6. Source: SGD

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 271271Delta(3,5)-Delta(2,4)-dienoyl-CoA isomerase
PRO_0000232996

Regions

Region62 – 665Substrate binding By similarity
Motif269 – 2713Microbody targeting signal Potential

Sites

Binding site1201Substrate; via amide nitrogen By similarity
Site1521Important for catalytic activity By similarity

Sequences

Sequence LengthMass (Da)Tools
Q08558 [UniParc].

Last modified November 1, 1996. Version 1.
Checksum: 0AA0BF3A981F733F

FASTA27130,058
        10         20         30         40         50         60 
MSSRVCYHIN GPFFIIKLID PKHLNSLTFE DFVYIALLLH KANDIDSVLF TVLQSSGKYF 

        70         80         90        100        110        120 
SSGGKFSAVN KLNDGDVTSE VEKVSKLVSA ISSPNIFVAN AFAIHKKVLV CCLNGPAIGL 

       130        140        150        160        170        180 
SASLVALCDI VYSQNDSVFL LFPFSNLGFV AEVGTSVTLT QKLGINSANE HMIFSTPVLF 

       190        200        210        220        230        240 
KELIGTIITK NYQLTNTETF NEKVLQDIKQ NLEGLYPKSV LGMKELLHSE MKQKLIKAQA 

       250        260        270 
METNGTLPFW ASGEPFKRFK QLQEGNRRHK L 

« Hide

References

« Hide 'large scale' references
[1]"The nucleotide sequence of Saccharomyces cerevisiae chromosome XV."
Dujon B., Albermann K., Aldea M., Alexandraki D., Ansorge W., Arino J., Benes V., Bohn C., Bolotin-Fukuhara M., Bordonne R., Boyer J., Camasses A., Casamayor A., Casas C., Cheret G., Cziepluch C., Daignan-Fornier B., Dang V.-D. expand/collapse author list , de Haan M., Delius H., Durand P., Fairhead C., Feldmann H., Gaillon L., Galisson F., Gamo F.-J., Gancedo C., Goffeau A., Goulding S.E., Grivell L.A., Habbig B., Hand N.J., Hani J., Hattenhorst U., Hebling U., Hernando Y., Herrero E., Heumann K., Hiesel R., Hilger F., Hofmann B., Hollenberg C.P., Hughes B., Jauniaux J.-C., Kalogeropoulos A., Katsoulou C., Kordes E., Lafuente M.J., Landt O., Louis E.J., Maarse A.C., Madania A., Mannhaupt G., Marck C., Martin R.P., Mewes H.-W., Michaux G., Paces V., Parle-McDermott A.G., Pearson B.M., Perrin A., Pettersson B., Poch O., Pohl T.M., Poirey R., Portetelle D., Pujol A., Purnelle B., Ramezani Rad M., Rechmann S., Schwager C., Schweizer M., Sor F., Sterky F., Tarassov I.A., Teodoru C., Tettelin H., Thierry A., Tobiasch E., Tzermia M., Uhlen M., Unseld M., Valens M., Vandenbol M., Vetter I., Vlcek C., Voet M., Volckaert G., Voss H., Wambutt R., Wedler H., Wiemann S., Winsor B., Wolfe K.H., Zollner A., Zumstein E., Kleine K.
Nature 387:98-102(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 204508 / S288c.
[2]"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.
[3]"Approaching a complete repository of sequence-verified protein-encoding clones for Saccharomyces cerevisiae."
Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F., Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J., Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J. expand/collapse author list , Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D., LaBaer J.
Genome Res. 17:536-543(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: ATCC 204508 / S288c.
[4]"Global regulatory functions of Oaf1p and Pip2p (Oaf2p), transcription factors that regulate genes encoding peroxisomal proteins in Saccharomyces cerevisiae."
Karpichev I.V., Small G.M.
Mol. Cell. Biol. 18:6560-6570(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: INDUCTION.
[5]"Preliminary characterization of Yor180Cp: identification of a novel peroxisomal protein of Saccharomyces cerevisiae involved in fatty acid metabolism."
Geisbrecht B.V., Schulz K., Nau K., Geraghty M.T., Schulz H., Erdmann R., Gould S.J.
Biochem. Biophys. Res. Commun. 260:28-34(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION, FUNCTION, INTERACTION WITH ECI1.
[6]"Alternatives to the isomerase-dependent pathway for the beta-oxidation of oleic acid are dispensable in Saccharomyces cerevisiae. Identification of YOR180c/DCI1 encoding peroxisomal delta(3,5)-delta(2,4)-dienoyl-CoA isomerase."
Gurvitz A., Mursula A.M., Yagi A.I., Hartig A., Ruis H., Rottensteiner H., Hiltunen J.K.
J. Biol. Chem. 274:24514-24521(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: INDUCTION, SUBCELLULAR LOCATION, FUNCTION.
[7]"Evidence for a novel pathway for the targeting of a Saccharomyces cerevisiae peroxisomal protein belonging to the isomerase/hydratase family."
Karpichev I.V., Small G.M.
J. Cell Sci. 113:533-544(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: INDUCTION, SUBCELLULAR LOCATION.
[8]"Eci1p uses a PTS1 to enter peroxisomes: either its own or that of a partner, Dci1p."
Yang X., Purdue P.E., Lazarow P.B.
Eur. J. Cell Biol. 80:126-138(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[9]"Ammonia pulses and metabolic oscillations guide yeast colony development."
Palkova Z., Devaux F., Icicova M., Minarikova L., Le Crom S., Jacq C.
Mol. Biol. Cell 13:3901-3914(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: INDUCTION.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
Z75088 Genomic DNA. Translation: CAA99389.1.
AY558432 Genomic DNA. Translation: AAS56758.1.
BK006948 Genomic DNA. Translation: DAA10952.1.
PIRS67072.
RefSeqNP_014823.3. NM_001183599.3.

3D structure databases

ProteinModelPortalQ08558.
SMRQ08558. Positions 2-262.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid34575. 21 interactions.
DIPDIP-4132N.
IntActQ08558. 2 interactions.
MINTMINT-386432.
STRING4932.YOR180C.

Proteomic databases

PaxDbQ08558.
PeptideAtlasQ08558.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiYOR180C; YOR180C; YOR180C.
GeneID854352.
KEGGsce:YOR180C.

Organism-specific databases

CYGDYOR180c.
SGDS000005706. DCI1.

Phylogenomic databases

eggNOGCOG1024.
GeneTreeENSGT00670000097595.
HOGENOMHOG000027948.
OMAGQKKHKL.
OrthoDBEOG70PC7K.

Enzyme and pathway databases

BioCycMetaCyc:YOR180C-MONOMER.
YEAST:YOR180C-MONOMER.
UniPathwayUPA00659.

Gene expression databases

GenevestigatorQ08558.

Family and domain databases

Gene3D3.90.226.10. 1 hit.
InterProIPR029045. ClpP/crotonase-like_dom.
IPR001753. Crotonase_core_superfam.
[Graphical view]
PfamPF00378. ECH. 1 hit.
[Graphical view]
SUPFAMSSF52096. SSF52096. 1 hit.
ProtoNetSearch...

Other

NextBio976443.

Entry information

Entry nameDCI1_YEAST
AccessionPrimary (citable) accession number: Q08558
Secondary accession number(s): D6W2N6
Entry history
Integrated into UniProtKB/Swiss-Prot: April 18, 2006
Last sequence update: November 1, 1996
Last modified: June 11, 2014
This is version 84 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 XV

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

Yeast

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

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways