O75521 (ECI2_HUMAN) Reviewed, UniProtKB/Swiss-Prot
Last modified
May 1, 2013.
Version 137.
History...
Names·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
Names·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize orderNames and origin
| Protein names | Recommended 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 |
| ||||
| Organism | Homo sapiens (Human) [Reference proteome] | ||||
| Taxonomic identifier | 9606 [NCBI] | ||||
| Taxonomic lineage | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo![]() |
Protein attributes
| Sequence length | 394 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is further processed into a mature form. |
| Protein existence | Evidence 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. |
Ontologies
| Keywords | |
|---|---|
| Cellular component | Mitochondrion Peroxisome |
| Coding sequence diversity | Alternative splicing Polymorphism |
| Domain | Transit peptide |
| Molecular function | Isomerase |
| PTM | Acetylation |
| Technical term | 3D-structure Complete proteome Reference proteome |
| Gene Ontology (GO) | |
| Biological_process | fatty acid catabolic process Inferred from direct assay Ref.6. Source: UniProtKB |
| Cellular_component | mitochondrion Inferred from direct assay. Source: LIFEdb peroxisomal matrixInferred from direct assay Ref.6. Source: UniProtKB |
| Molecular_function | dodecenoyl-CoA delta-isomerase activity Inferred from direct assay Ref.6. Source: UniProtKB fatty-acyl-CoA bindingInferred from electronic annotation. Source: InterPro |
| Complete GO annotation... | |
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 key | Position(s) | Length | Description | Graphical view | Feature identifier | |||||||||||||||||||||||||||||||||||||||||||||||||||||
Molecule processing | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
| Transit peptide | 1 – 38 | 38 | Mitochondrion Potential | |||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Chain | 39 – 394 | 356 | Enoyl-CoA delta isomerase 2, mitochondrial | PRO_0000214027 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||
Regions | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Domain | 39 – 124 | 86 | ACB | |||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Region | 66 – 70 | 5 | Acyl-CoA binding By similarity | |||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Region | 151 – 322 | 172 | ECH-like | |||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Motif | 392 – 394 | 3 | Microbody targeting signal Potential | |||||||||||||||||||||||||||||||||||||||||||||||||||||||
Sites | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Binding site | 92 | 1 | Acyl-CoA By similarity | |||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Binding site | 111 | 1 | Acyl-CoA By similarity | |||||||||||||||||||||||||||||||||||||||||||||||||||||||
Amino acid modifications | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Modified residue | 51 | 1 | N6-acetyllysine Ref.11 | |||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Modified residue | 62 | 1 | N6-acetyllysine By similarity | |||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Modified residue | 92 | 1 | N6-acetyllysine Ref.11 | |||||||||||||||||||||||||||||||||||||||||||||||||||||||
Natural variations | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Alternative sequence | 1 – 35 | 35 | Missing in isoform 2. | VSP_037854 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Natural variant | 47 | 1 | M → I. Corresponds to variant rs3177253 [ dbSNP | Ensembl ]. | VAR_058493 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Natural variant | 344 | 1 | A → V. Ref.1 Ref.7 Corresponds to variant rs7166 [ dbSNP | Ensembl ]. | VAR_058494 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||
Experimental info | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Sequence conflict | 119 | 1 | S → C in CAB66577. Ref.2 | |||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Sequence conflict | 195 | 1 | Y → C in AAC19317. Ref.1 | |||||||||||||||||||||||||||||||||||||||||||||||||||||||
Secondary structure | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Helix Strand Turn | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Helix | 40 – 52 | 13 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Helix | 59 – 69 | 11 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Turn | 70 – 74 | 5 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Helix | 87 – 99 | 13 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Helix | 104 – 118 | 15 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Beta strand | 140 – 147 | 8 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Beta strand | 150 – 155 | 6 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Helix | 158 – 160 | 3 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Helix | 166 – 181 | 16 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Beta strand | 185 – 192 | 8 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Helix | 212 – 232 | 21 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Beta strand | 238 – 242 | 5 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Helix | 249 – 252 | 4 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Helix | 253 – 256 | 4 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Beta strand | 258 – 263 | 6 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Beta strand | 267 – 269 | 3 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Helix | 273 – 275 | 3 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Helix | 283 – 291 | 9 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Helix | 293 – 300 | 8 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Helix | 308 – 313 | 6 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Beta strand | 318 – 321 | 4 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Turn | 323 – 325 | 3 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Helix | 326 – 337 | 12 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Helix | 342 – 353 | 12 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Helix | 354 – 356 | 3 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Helix | 357 – 375 | 19 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Helix | 378 – 381 | 4 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Sequences
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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. 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. 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. 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, MASS SPECTROMETRY. |
| [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. | ||||||||||||||||||
| IPI | IPI00419263. IPI00639841. | ||||||||||||||||||
| RefSeq | NP_001159482.1. NM_001166010.1. NP_006108.2. NM_006117.2. NP_996667.2. NM_206836.2. | ||||||||||||||||||
| UniGene | Hs.15250. | ||||||||||||||||||
3D structure databases | |||||||||||||||||||
| PDBe RCSB PDB PDBj |
| ||||||||||||||||||
| ProteinModelPortal | O75521. | ||||||||||||||||||
| ModBase | Search... | ||||||||||||||||||
Protein-protein interaction databases | |||||||||||||||||||
| IntAct | O75521. 5 interactions. | ||||||||||||||||||
PTM databases | |||||||||||||||||||
| PhosphoSite | O75521. | ||||||||||||||||||
2D gel databases | |||||||||||||||||||
| REPRODUCTION-2DPAGE | IPI00419263. | ||||||||||||||||||
| UCD-2DPAGE | O75521. | ||||||||||||||||||
Proteomic databases | |||||||||||||||||||
| PaxDb | O75521. | ||||||||||||||||||
| PRIDE | O75521. | ||||||||||||||||||
Protocols and materials databases | |||||||||||||||||||
| DNASU | 10455. | ||||||||||||||||||
| StructuralBiologyKnowledgebase | Search... | ||||||||||||||||||
Genome annotation databases | |||||||||||||||||||
| Ensembl | ENST00000361538; ENSP00000354737; ENSG00000198721. ENST00000380118; ENSP00000369461; ENSG00000198721. ENST00000380125; ENSP00000369468; ENSG00000198721. ENST00000465828; ENSP00000420309; ENSG00000198721. | ||||||||||||||||||
| GeneID | 10455. | ||||||||||||||||||
| KEGG | hsa:10455. | ||||||||||||||||||
| UCSC | uc003mwc.3. human. | ||||||||||||||||||
Organism-specific databases | |||||||||||||||||||
| CTD | 10455. | ||||||||||||||||||
| GeneCards | GC06M004115. | ||||||||||||||||||
| H-InvDB | HIX0025043. | ||||||||||||||||||
| HGNC | HGNC:14601. ECI2. | ||||||||||||||||||
| HPA | HPA022130. | ||||||||||||||||||
| MIM | 608024. gene. | ||||||||||||||||||
| neXtProt | NX_O75521. | ||||||||||||||||||
| PharmGKB | PA33168. | ||||||||||||||||||
| GenAtlas | Search... | ||||||||||||||||||
Phylogenomic databases | |||||||||||||||||||
| eggNOG | COG4281. | ||||||||||||||||||
| HOVERGEN | HBG006723. | ||||||||||||||||||
| InParanoid | O75521. | ||||||||||||||||||
| KO | K13239. | ||||||||||||||||||
| OMA | RWLSDEC. | ||||||||||||||||||
| OrthoDB | EOG49P9ZK. | ||||||||||||||||||
Gene expression databases | |||||||||||||||||||
| ArrayExpress | O75521. | ||||||||||||||||||
| Bgee | O75521. | ||||||||||||||||||
| Genevestigator | O75521. | ||||||||||||||||||
| GermOnline | ENSG00000198721. Homo sapiens. | ||||||||||||||||||
Family and domain databases | |||||||||||||||||||
| Gene3D | 1.20.80.10. 1 hit. | ||||||||||||||||||
| InterPro | IPR022408. Acyl-CoA-binding_prot_CS. IPR000582. Acyl-CoA-binding_protein. IPR001753. Crotonase_core_superfam. IPR014352. FERM/acyl-CoA-bd_prot_3-hlx. [Graphical view] | ||||||||||||||||||
| Pfam | PF00887. ACBP. 1 hit. PF00378. ECH. 1 hit. [Graphical view] | ||||||||||||||||||
| PRINTS | PR00689. ACOABINDINGP. | ||||||||||||||||||
| SUPFAM | SSF47027. ACBP. 1 hit. | ||||||||||||||||||
| PROSITE | PS00880. ACB_1. 1 hit. PS51228. ACB_2. 1 hit. [Graphical view] | ||||||||||||||||||
| ProtoNet | Search... | ||||||||||||||||||
Other | |||||||||||||||||||
| EvolutionaryTrace | O75521. | ||||||||||||||||||
| GenomeRNAi | 10455. | ||||||||||||||||||
| NextBio | 39633. | ||||||||||||||||||
| SOURCE | Search... | ||||||||||||||||||
Entry information
| Entry name | ECI2_HUMAN | ||||||||
| Accession | Primary (citable) accession number: O75521 Secondary accession number(s): Q5JYK5 Q9UN55 | ||||||||
| Entry history |
| ||||||||
| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | Chordata Protein Annotation Program | ||||||||
| Disclaimer | Any 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
| Human chromosome 6 Human chromosome 6: entries, gene names and cross-references to MIM |
| Human entries with polymorphisms or disease mutations List of human entries with polymorphisms or disease mutations |
| Human polymorphisms and disease mutations Index of human polymorphisms and disease mutations |
| MIM cross-references Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot |
| PDB cross-references Index of Protein Data Bank (PDB) cross-references |
| SIMILARITY comments Index of protein domains and families |

Clusters with
