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O75521 (ECI2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 149. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | 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):
DRS-1
Delta(3),delta(2)-enoyl-CoA isomerase
Short name=D3,D2-enoyl-CoA isomerase
Diazepam-binding inhibitor-related protein 1
Short name=DBI-related protein 1
Dodecenoyl-CoA isomerase
Hepatocellular carcinoma-associated antigen 88
Peroxisomal 3,2-trans-enoyl-CoA isomerase
Short name=pECI
Renal carcinoma antigen NY-REN-1
Gene names
Name:ECI2
Synonyms:DRS1, HCA88, PECI
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length394 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 Ref.6 Ref.9.

Isoform 2: Peroxisome matrix Ref.6 Ref.9.

Tissue specificity

Abundant in heart, skeletal muscle and liver. Expressed in CD34+ T-cells and CD34+ bone marrow cells. Ref.10

Sequence similarities

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

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

Caution

It is uncertain whether Met-1 or Met-3 is the initiator.

Sequence caution

The sequence AAC19317.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

The sequence AAD34173.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

The sequence AAF66247.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

The sequence AAH02668.3 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

The sequence AAH16781.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

The sequence AAH17474.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

The sequence AAH33841.3 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

The sequence AAH34702.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

The sequence BAG52068.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: O75521-1)

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: O75521-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-35: Missing.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Transit peptide1 – 3838Mitochondrion Potential
Chain39 – 394356Enoyl-CoA delta isomerase 2, mitochondrial
PRO_0000214027

Regions

Domain39 – 12486ACB
Region66 – 705Acyl-CoA binding By similarity
Region151 – 322172ECH-like
Motif392 – 3943Microbody targeting signal Potential

Sites

Binding site921Acyl-CoA By similarity
Binding site1111Acyl-CoA By similarity

Amino acid modifications

Modified residue511N6-acetyllysine; alternate Ref.11
Modified residue511N6-succinyllysine; alternate By similarity
Modified residue551N6-succinyllysine By similarity
Modified residue621N6-acetyllysine; alternate By similarity
Modified residue621N6-succinyllysine; alternate By similarity
Modified residue701N6-succinyllysine By similarity
Modified residue811N6-succinyllysine By similarity
Modified residue901N6-succinyllysine By similarity
Modified residue921N6-acetyllysine; alternate Ref.11
Modified residue921N6-succinyllysine; alternate By similarity
Modified residue1611N6-succinyllysine By similarity
Modified residue2891N6-succinyllysine By similarity

Natural variations

Alternative sequence1 – 3535Missing in isoform 2.
VSP_037854
Natural variant471M → I.
Corresponds to variant rs3177253 [ dbSNP | Ensembl ].
VAR_058493
Natural variant3441A → V. Ref.1 Ref.7
Corresponds to variant rs7166 [ dbSNP | Ensembl ].
VAR_058494

Experimental info

Sequence conflict1191S → C in CAB66577. Ref.2
Sequence conflict1951Y → C in AAC19317. Ref.1

Secondary structure

.................................................. 394
Helix Strand Turn

Details...

Sequences

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

Last modified September 1, 2009. Version 4.
Checksum: 8AC633D43A320102

FASTA39443,585
        10         20         30         40         50         60 
MAMAYLAWRL ARRSCPSSLQ VTSFPVVQLH MNRTAMRASQ KDFENSMNQV KLLKKDPGNE 

        70         80         90        100        110        120 
VKLKLYALYK QATEGPCNMP KPGVFDLINK AKWDAWNALG SLPKEAARQN YVDLVSSLSP 

       130        140        150        160        170        180 
SLESSSQVEP GTDRKSTGFE TLVVTSEDGI TKIMFNRPKK KNAINTEMYH EIMRALKAAS 

       190        200        210        220        230        240 
KDDSIITVLT GNGDYYSSGN DLTNFTDIPP GGVEEKAKNN AVLLREFVGC FIDFPKPLIA 

       250        260        270        280        290        300 
VVNGPAVGIS VTLLGLFDAV YASDRATFHT PFSHLGQSPE GCSSYTFPKI MSPAKATEML 

       310        320        330        340        350        360 
IFGKKLTAGE ACAQGLVTEV FPDSTFQKEV WTRLKAFAKL PPNALRISKE VIRKREREKL 

       370        380        390 
HAVNAEECNV LQGRWLSDEC TNAVVNFLSR KSKL 

« Hide

Isoform 2 [UniParc].

Checksum: B9EC60A0D445C9F0
Show »

FASTA35939,609

References

« Hide 'large scale' references
[1]"Molecular cloning and expression of a novel human cDNA related to the diazepam binding inhibitor."
Suk K., Kim Y.-H., Hwang D.-Y., Ihm S.-H., Yoo H.J., Lee M.-S.
Biochim. Biophys. Acta 1454:126-131(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), VARIANT VAL-344.
Tissue: Pancreatic islet.
[2]"Towards a catalog of human genes and proteins: sequencing and analysis of 500 novel complete protein coding human cDNAs."
Wiemann S., Weil B., Wellenreuther R., Gassenhuber J., Glassl S., Ansorge W., Boecher M., Bloecker H., Bauersachs S., Blum H., Lauber J., Duesterhoeft A., Beyer A., Koehrer K., Strack N., Mewes H.-W., Ottenwaelder B., Obermaier B. expand/collapse author list , Tampe J., Heubner D., Wambutt R., Korn B., Klein M., Poustka A.
Genome Res. 11:422-435(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Tissue: Brain.
[3]"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 2).
Tissue: Placenta.
[4]"The DNA sequence and analysis of human chromosome 6."
Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L., Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D., Andrews T.D. expand/collapse author list , Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V., Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J., Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J., French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.
Nature 425:805-811(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]"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: Bone marrow, Skin and Uterus.
[6]"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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 4-394 (ISOFORM 1), SUBCELLULAR LOCATION.
[7]"Large scale identification of human hepatocellular carcinoma-associated antigens by autoantibodies."
Wang Y., Han K.-J., Pang X.-W., Vaughan H.A., Qu W., Dong X.-Y., Peng J.-R., Zhao H.-T., Rui J.-A., Leng X.-S., Cebon J., Burgess A.W., Chen W.-F.
J. Immunol. 169:1102-1109(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 4-394 (ISOFORM 1), VARIANT VAL-344.
Tissue: Hepatoma.
[8]"Antigens recognized by autologous antibody in patients with renal-cell carcinoma."
Scanlan M.J., Gordan J.D., Williamson B., Stockert E., Bander N.H., Jongeneel C.V., Gure A.O., Jaeger D., Jaeger E., Knuth A., Chen Y.-T., Old L.J.
Int. J. Cancer 83:456-464(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION AS A RENAL CANCER ANTIGEN.
Tissue: Renal cell carcinoma.
[9]"Systematic subcellular localization of novel proteins identified by large-scale cDNA sequencing."
Simpson J.C., Wellenreuther R., Poustka A., Pepperkok R., Wiemann S.
EMBO Rep. 1:287-292(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION.
[10]"Diazepam-binding inhibitor-related protein 1: a candidate autoantigen in acquired aplastic anemia patients harboring a minor population of paroxysmal nocturnal hemoglobinuria-type cells."
Feng X., Chuhjo T., Sugimori C., Kotani T., Lu X., Takami A., Takamatsu H., Yamazaki H., Nakao S.
Blood 104:2425-2431(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: TISSUE SPECIFICITY.
[11]"Lysine acetylation targets protein complexes and co-regulates major cellular functions."
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-51 AND LYS-92, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[12]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[13]"Solution structure of RSGI RUH-045, a human acyl-CoA binding protein."
RIKEN structural genomics initiative (RSGI)
Submitted (NOV-2005) to the PDB data bank
Cited for: STRUCTURE BY NMR OF 36-133.
[14]"The crystal structure of human peroxisomal delta3, delta2 enoyl-CoA isomerase (pECI)."
Structural genomics consortium (SGC)
Submitted (FEB-2009) to the PDB data bank
Cited for: X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS) OF 138-394.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF069301 mRNA. Translation: AAC19317.1. Different initiation.
AL136642 mRNA. Translation: CAB66577.1.
AK075108 mRNA. Translation: BAG52068.1. Different initiation.
AL033383 Genomic DNA. Translation: CAI42125.1.
AL033383 Genomic DNA. Translation: CAI42127.1.
BC002668 mRNA. Translation: AAH02668.3. Different initiation.
BC016781 mRNA. Translation: AAH16781.1. Different initiation.
BC017474 mRNA. Translation: AAH17474.1. Different initiation.
BC033841 mRNA. Translation: AAH33841.3. Different initiation.
BC034702 mRNA. Translation: AAH34702.1. Different initiation.
AF153612 mRNA. Translation: AAD34173.1. Different initiation.
AF244138 mRNA. Translation: AAF66247.1. Different initiation.
CCDSCCDS43420.2. [O75521-1]
RefSeqNP_001159482.1. NM_001166010.1.
NP_006108.2. NM_006117.2.
NP_996667.2. NM_206836.2. [O75521-1]
UniGeneHs.15250.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2CQUNMR-A31-133[»]
2F6QX-ray1.95A/B/C138-394[»]
ProteinModelPortalO75521.
SMRO75521. Positions 31-133, 139-390.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid115718. 12 interactions.
IntActO75521. 7 interactions.
MINTMINT-3001383.

PTM databases

PhosphoSiteO75521.

2D gel databases

REPRODUCTION-2DPAGEIPI00419263.
UCD-2DPAGEO75521.

Proteomic databases

MaxQBO75521.
PaxDbO75521.
PRIDEO75521.

Protocols and materials databases

DNASU10455.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000361538; ENSP00000354737; ENSG00000198721.
ENST00000380118; ENSP00000369461; ENSG00000198721. [O75521-1]
ENST00000380125; ENSP00000369468; ENSG00000198721.
ENST00000465828; ENSP00000420309; ENSG00000198721.
GeneID10455.
KEGGhsa:10455.
UCSCuc003mwc.3. human. [O75521-1]

Organism-specific databases

CTD10455.
GeneCardsGC06M004115.
H-InvDBHIX0025043.
HGNCHGNC:14601. ECI2.
HPAHPA022130.
HPA031626.
MIM608024. gene.
neXtProtNX_O75521.
PharmGKBPA33168.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG4281.
HOVERGENHBG006723.
InParanoidO75521.
KOK13239.
OMARWLSDEC.
OrthoDBEOG72RN06.
PhylomeDBO75521.
TreeFamTF313375.

Gene expression databases

ArrayExpressO75521.
BgeeO75521.
GenevestigatorO75521.

Family and domain databases

Gene3D1.20.80.10. 1 hit.
3.90.226.10. 1 hit.
InterProIPR022408. Acyl-CoA-binding_prot_CS.
IPR000582. Acyl-CoA-binding_protein.
IPR029045. ClpP/crotonase-like_dom.
IPR001753. Crotonase_core_superfam.
IPR014352. FERM/acyl-CoA-bd_prot_3-hlx.
[Graphical view]
PfamPF00887. ACBP. 1 hit.
PF00378. ECH. 1 hit.
[Graphical view]
PRINTSPR00689. ACOABINDINGP.
SUPFAMSSF47027. SSF47027. 1 hit.
SSF52096. SSF52096. 1 hit.
PROSITEPS00880. ACB_1. 1 hit.
PS51228. ACB_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceO75521.
GeneWikiPECI_(gene).
GenomeRNAi10455.
NextBio39633.
PROO75521.
SOURCESearch...

Entry information

Entry nameECI2_HUMAN
AccessionPrimary (citable) accession number: O75521
Secondary accession number(s): Q5JYK5 expand/collapse secondary AC list , Q5JYK7, Q7L124, Q8N0X0, Q9BUE9, Q9H0T9, Q9NQH1, Q9NYH7, Q9UN55
Entry history
Integrated into UniProtKB/Swiss-Prot: July 15, 1999
Last sequence update: September 1, 2009
Last modified: July 9, 2014
This is version 149 of the entry and version 4 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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

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 6

Human chromosome 6: entries, gene names and cross-references to MIM