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Q9WUR2 (ECI2_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 87. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | 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:
Enoyl-CoA delta isomerase 2, mitochondrial

EC=5.3.3.8
Alternative name(s):
Delta(3),delta(2)-enoyl-CoA isomerase
Short name=D3,D2-enoyl-CoA isomerase
Dodecenoyl-CoA isomerase
Peroxisomal 3,2-trans-enoyl-CoA isomerase
Short name=pECI
Gene names
Name:Eci2
Synonyms:Peci
OrganismMus musculus (Mouse)
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length391 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Able to isomerize both 3-cis and 3-trans double bonds into the 2-trans form in a range of enoyl-CoA species. Has a preference for 3-trans substrates By similarity.

Catalytic activity

(3Z)-dodec-3-enoyl-CoA = (2E)-dodec-2-enoyl-CoA.

Subcellular location

Isoform 1: Mitochondrion By similarity.

Isoform 2: Peroxisome matrix By similarity.

Post-translational modification

Acetylation of Lys-60 is observed in liver mitochondria from fasted mice but not from fed mice.

Sequence similarities

In the C-terminal section; belongs to the enoyl-CoA hydratase/isomerase family.

Contains 1 ACB (acyl-CoA-binding) domain.

Sequence caution

The sequence AAH01983.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

Ontologies

Keywords
   Cellular componentMitochondrion
Peroxisome
   Coding sequence diversityAlternative splicing
   DomainTransit peptide
   Molecular functionIsomerase
   PTMAcetylation
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological processfatty acid catabolic process

Inferred from sequence or structural similarity Ref.1. Source: UniProtKB

   Cellular componentmitochondrion

Inferred from direct assay. Source: MGI

peroxisomal matrix

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functiondodecenoyl-CoA delta-isomerase activity

Inferred from electronic annotation. Source: EC

fatty-acyl-CoA binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q9WUR2-1)

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: Q9WUR2-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-33: Missing.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Transit peptide1 – 3636Mitochondrion Potential
Chain37 – 391355Enoyl-CoA delta isomerase 2, mitochondrial
PRO_0000214028

Regions

Domain37 – 12286ACB
Region149 – 319171ECH-like
Motif389 – 3913Microbody targeting signal Potential

Amino acid modifications

Modified residue491N6-acetyllysine By similarity
Modified residue601N6-acetyllysine Ref.4
Modified residue901N6-acetyllysine By similarity

Natural variations

Alternative sequence1 – 3333Missing in isoform 2.
VSP_037855

Experimental info

Sequence conflict351R → K in BAB26315. Ref.2
Sequence conflict1281R → C in AAH01983. Ref.3
Sequence conflict1351R → Q in AAH01983. Ref.3

Sequences

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

Last modified September 1, 2009. Version 2.
Checksum: 0B93D3908DF77AF8

FASTA39143,268
        10         20         30         40         50         60 
MAAVTWSRAR CWCPSVLQVF RLQVAKLHLG RPTMRASQQD FENALNQVKL LKKDPGNEVK 

        70         80         90        100        110        120 
LRLYALYKQA TEGPCNMPKP GMLDFVNKAK WDAWNALGSL PKETARQNYV DLVSSLSSSS 

       130        140        150        160        170        180 
EAPSQGKRGA DEKARESKDI LVTSEDGITK ITFNRPTKKN AISFQMYRDI ILALKNASTD 

       190        200        210        220        230        240 
NTVMAVFTGT GDYYCSGNDL TNFTSATGGI EEAASNGAVL LRDFVNSFID FPKPLVAVVN 

       250        260        270        280        290        300 
GPAVGISVTL LGLFDAVFAS DRATFHTPFS QLGQSPEACS SYTFPKMMGS AKAAEMLLFG 

       310        320        330        340        350        360 
KKLTAREAWA QGLVTEVFPE STFETEVWTR LKTYAKLPPN AMRISKELIR KNEKEKLYAV 

       370        380        390 
NAEECTTLQA RWLSEECMNA IMSFVSRKPK L 

« Hide

Isoform 2 [UniParc].

Checksum: 2E22207290123AE5
Show »

FASTA35839,503

References

« Hide 'large scale' references
[1]"Characterization of PECI, a novel monofunctional D3,D2-enoyl-CoA isomerase of mammalian peroxisomes."
Geisbrecht B.V., Zhang D., Schulz H., Gould S.J.
J. Biol. Chem. 274:21797-21803(1999) [PubMed: 10419495] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
[2]"The transcriptional landscape of the mammalian genome."
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. expand/collapse author list , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
Science 309:1559-1563(2005) [PubMed: 16141072] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Strain: C57BL/6J.
Tissue: Tongue.
[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: 15489334] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 8-391 (ISOFORM 1).
Strain: Czech II.
Tissue: Mammary tumor.
[4]"Substrate and functional diversity of lysine acetylation revealed by a proteomics survey."
Kim S.C., Sprung R., Chen Y., Xu Y., Ball H., Pei J., Cheng T., Kho Y., Xiao H., Xiao L., Grishin N.V., White M., Yang X.-J., Zhao Y.
Mol. Cell 23:607-618(2006) [PubMed: 16916647] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-60, MASS SPECTROMETRY.
Tissue: Liver.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF153613 mRNA. Translation: AAD34174.1.
AK009478 mRNA. Translation: BAB26315.2.
BC001983 mRNA. Translation: AAH01983.1. Different initiation.
IPIIPI00322931.
IPI00877214.
RefSeqNP_001103801.1. NM_001110331.1.
NP_001103802.1. NM_001110332.1.
NP_035998.2. NM_011868.2.
UniGeneMm.28883.

3D structure databases

ProteinModelPortalQ9WUR2.
SMRQ9WUR2. Positions 29-131, 140-387.
ModBaseSearch...

Protein-protein interaction databases

IntActQ9WUR2. 1 interaction.
STRINGQ9WUR2.

PTM databases

PhosphoSiteQ9WUR2.

Proteomic databases

PRIDEQ9WUR2.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000021854; ENSMUSP00000021854; ENSMUSG00000021417.
ENSMUST00000171229; ENSMUSP00000131735; ENSMUSG00000021417.
GeneID23986.
KEGGmmu:23986.
UCSCuc007qbx.2. mouse.
uc007qbz.2. mouse.

Organism-specific databases

CTD10455.
MGIMGI:1346064. Eci2.

Phylogenomic databases

GeneTreeENSGT00560000077142.
HOGENOMHBG748731.
HOVERGENHBG006723.
InParanoidQ9WUR2.
OMARWLSDEC.
OrthoDBEOG49P9ZK.
PhylomeDBQ9WUR2.

Gene expression databases

ArrayExpressQ9WUR2.
BgeeQ9WUR2.
GenevestigatorQ9WUR2.
GermOnlineENSMUSG00000021417. Mus musculus.

Family and domain databases

InterProIPR022408. Acyl-CoA-binding_prot_CS.
IPR000582. Acyl-CoA-binding_protein.
IPR001753. Crotonase_core.
IPR014352. FERM/acyl-CoA-bd_prot_3-hlx.
[Graphical view]
Gene3DG3DSA:1.20.80.10. ACBP. 1 hit.
KOK13239.
PfamPF00887. ACBP. 1 hit.
PF00378. ECH. 1 hit.
[Graphical view]
PRINTSPR00689. ACOABINDINGP.
SUPFAMSSF47027. ACBP. 1 hit.
PROSITEPS00880. ACB_1. 1 hit.
PS51228. ACB_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio303881.
SOURCESearch...

Entry information

Entry nameECI2_MOUSE
AccessionPrimary (citable) accession number: Q9WUR2
Secondary accession number(s): Q99M61, Q9D785
Entry history
Integrated into UniProtKB/Swiss-Prot: January 24, 2001
Last sequence update: September 1, 2009
Last modified: January 25, 2012
This is version 87 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot

SIMILARITY comments

Index of protein domains and families