ID ECI2_HUMAN Reviewed; 394 AA. AC O75521; Q5JYK5; Q5JYK7; Q7L124; Q8N0X0; Q9BUE9; Q9H0T9; Q9NQH1; Q9NYH7; AC Q9UN55; DT 15-JUL-1999, integrated into UniProtKB/Swiss-Prot. DT 01-SEP-2009, sequence version 4. DT 27-MAR-2024, entry version 223. DE RecName: Full=Enoyl-CoA delta isomerase 2 {ECO:0000305}; DE EC=5.3.3.8 {ECO:0000269|PubMed:10419495}; DE AltName: Full=DRS-1; DE AltName: Full=Delta(3),delta(2)-enoyl-CoA isomerase; DE Short=D3,D2-enoyl-CoA isomerase; DE AltName: Full=Diazepam-binding inhibitor-related protein 1; DE Short=DBI-related protein 1; DE AltName: Full=Dodecenoyl-CoA isomerase; DE AltName: Full=Hepatocellular carcinoma-associated antigen 88; DE AltName: Full=Peroxisomal 3,2-trans-enoyl-CoA isomerase; DE Short=pECI {ECO:0000303|PubMed:10419495}; DE AltName: Full=Renal carcinoma antigen NY-REN-1; DE Flags: Precursor; GN Name=ECI2; Synonyms=DRS1, HCA88, PECI {ECO:0000303|PubMed:10419495}; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; OC Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), AND VARIANT VAL-344. RC TISSUE=Pancreatic islet; RX PubMed=10354522; DOI=10.1016/s0925-4439(99)00033-2; RA Suk K., Kim Y.-H., Hwang D.-Y., Ihm S.-H., Yoo H.J., Lee M.-S.; RT "Molecular cloning and expression of a novel human cDNA related to the RT diazepam binding inhibitor."; RL Biochim. Biophys. Acta 1454:126-131(1999). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC TISSUE=Brain; RX PubMed=11230166; DOI=10.1101/gr.gr1547r; RA Wiemann S., Weil B., Wellenreuther R., Gassenhuber J., Glassl S., RA Ansorge W., Boecher M., Bloecker H., Bauersachs S., Blum H., Lauber J., RA Duesterhoeft A., Beyer A., Koehrer K., Strack N., Mewes H.-W., RA Ottenwaelder B., Obermaier B., Tampe J., Heubner D., Wambutt R., Korn B., RA Klein M., Poustka A.; RT "Towards a catalog of human genes and proteins: sequencing and analysis of RT 500 novel complete protein coding human cDNAs."; RL Genome Res. 11:422-435(2001). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2). RC TISSUE=Placenta; RX PubMed=14702039; DOI=10.1038/ng1285; RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S., RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., RA Isogai T., Sugano S.; RT "Complete sequencing and characterization of 21,243 full-length human RT cDNAs."; RL Nat. Genet. 36:40-45(2004). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=14574404; DOI=10.1038/nature02055; RA Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L., RA Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R., RA Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D., RA Andrews T.D., Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., RA Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H., RA Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J., RA Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P., RA Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V., RA Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J., RA Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E., RA Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J., RA French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J., RA Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C., RA Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A., RA Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R., RA Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., RA Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., RA Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., RA Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., RA Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A., RA Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L., RA Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I., RA Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y., RA Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E., RA Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A., RA Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W., RA Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., RA West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J., RA Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M., RA Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I., RA Rogers J., Beck S.; RT "The DNA sequence and analysis of human chromosome 6."; RL Nature 425:805-811(2003). RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2). RC TISSUE=Bone marrow, Skin, and Uterus; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA project: RT the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [6] RP NUCLEOTIDE SEQUENCE [MRNA] OF 4-394 (ISOFORM 1), SUBCELLULAR LOCATION, RP CATALYTIC ACTIVITY, AND TISSUE SPECIFICITY. RX PubMed=10419495; DOI=10.1074/jbc.274.31.21797; RA Geisbrecht B.V., Zhang D., Schulz H., Gould S.J.; RT "Characterization of PECI, a novel monofunctional D3,D2-enoyl-CoA isomerase RT of mammalian peroxisomes."; RL J. Biol. Chem. 274:21797-21803(1999). RN [7] RP NUCLEOTIDE SEQUENCE [MRNA] OF 4-394 (ISOFORM 1), AND VARIANT VAL-344. RC TISSUE=Hepatoma; RX PubMed=12097419; DOI=10.4049/jimmunol.169.2.1102; RA Wang Y., Han K.-J., Pang X.-W., Vaughan H.A., Qu W., Dong X.-Y., RA Peng J.-R., Zhao H.-T., Rui J.-A., Leng X.-S., Cebon J., Burgess A.W., RA Chen W.-F.; RT "Large scale identification of human hepatocellular carcinoma-associated RT antigens by autoantibodies."; RL J. Immunol. 169:1102-1109(2002). RN [8] RP IDENTIFICATION AS A RENAL CANCER ANTIGEN. RC TISSUE=Renal cell carcinoma; RX PubMed=10508479; RX DOI=10.1002/(sici)1097-0215(19991112)83:4<456::aid-ijc4>3.0.co;2-5; RA Scanlan M.J., Gordan J.D., Williamson B., Stockert E., Bander N.H., RA Jongeneel C.V., Gure A.O., Jaeger D., Jaeger E., Knuth A., Chen Y.-T., RA Old L.J.; RT "Antigens recognized by autologous antibody in patients with renal-cell RT carcinoma."; RL Int. J. Cancer 83:456-464(1999). RN [9] RP SUBCELLULAR LOCATION. RX PubMed=11256614; DOI=10.1093/embo-reports/kvd058; RA Simpson J.C., Wellenreuther R., Poustka A., Pepperkok R., Wiemann S.; RT "Systematic subcellular localization of novel proteins identified by large- RT scale cDNA sequencing."; RL EMBO Rep. 1:287-292(2000). RN [10] RP TISSUE SPECIFICITY. RX PubMed=15217832; DOI=10.1182/blood-2004-05-1839; RA Feng X., Chuhjo T., Sugimori C., Kotani T., Lu X., Takami A., Takamatsu H., RA Yamazaki H., Nakao S.; RT "Diazepam-binding inhibitor-related protein 1: a candidate autoantigen in RT acquired aplastic anemia patients harboring a minor population of RT paroxysmal nocturnal hemoglobinuria-type cells."; RL Blood 104:2425-2431(2004). RN [11] RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-51 AND LYS-92, AND IDENTIFICATION RP BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=19608861; DOI=10.1126/science.1175371; RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., RA Olsen J.V., Mann M.; RT "Lysine acetylation targets protein complexes and co-regulates major RT cellular functions."; RL Science 325:834-840(2009). RN [12] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21269460; DOI=10.1186/1752-0509-5-17; RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., RA Bennett K.L., Superti-Furga G., Colinge J.; RT "Initial characterization of the human central proteome."; RL BMC Syst. Biol. 5:17-17(2011). RN [13] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-119, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Erythroleukemia; RX PubMed=23186163; DOI=10.1021/pr300630k; RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J., RA Mohammed S.; RT "Toward a comprehensive characterization of a human cancer cell RT phosphoproteome."; RL J. Proteome Res. 12:260-271(2013). RN [14] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-101, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Liver; RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014; RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., RA Ye M., Zou H.; RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver RT phosphoproteome."; RL J. Proteomics 96:253-262(2014). RN [15] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=25944712; DOI=10.1002/pmic.201400617; RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D., RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.; RT "N-terminome analysis of the human mitochondrial proteome."; RL Proteomics 15:2519-2524(2015). RN [16] RP STRUCTURE BY NMR OF 36-133. RG RIKEN structural genomics initiative (RSGI); RT "Solution structure of RSGI RUH-045, a human acyl-CoA binding protein."; RL Submitted (NOV-2005) to the PDB data bank. RN [17] RP X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS) OF 138-394. RG Structural genomics consortium (SGC); RT "The crystal structure of human peroxisomal delta3, delta2 enoyl-CoA RT isomerase (pECI)."; RL Submitted (FEB-2009) to the PDB data bank. CC -!- FUNCTION: Able to isomerize both 3-cis and 3-trans double bonds into CC the 2-trans form in a range of enoyl-CoA species. Has a preference for CC 3-trans substrates. {ECO:0000269|PubMed:10419495}. CC -!- CATALYTIC ACTIVITY: CC Reaction=a (3Z)-enoyl-CoA = a 4-saturated (2E)-enoyl-CoA; CC Xref=Rhea:RHEA:45900, ChEBI:CHEBI:85097, ChEBI:CHEBI:85489; CC EC=5.3.3.8; Evidence={ECO:0000305|PubMed:10419495}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:45901; CC Evidence={ECO:0000305|PubMed:10419495}; CC -!- CATALYTIC ACTIVITY: CC Reaction=(3Z)-octenoyl-CoA = (2E)-octenoyl-CoA; Xref=Rhea:RHEA:46044, CC ChEBI:CHEBI:62242, ChEBI:CHEBI:85640; CC Evidence={ECO:0000269|PubMed:10419495}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:46045; CC Evidence={ECO:0000269|PubMed:10419495}; CC -!- CATALYTIC ACTIVITY: CC Reaction=a (3E)-enoyl-CoA = a 4-saturated (2E)-enoyl-CoA; CC Xref=Rhea:RHEA:45228, ChEBI:CHEBI:58521, ChEBI:CHEBI:85097; CC EC=5.3.3.8; Evidence={ECO:0000250|UniProtKB:Q5XIC0}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:45229; CC Evidence={ECO:0000250|UniProtKB:Q5XIC0}; CC -!- CATALYTIC ACTIVITY: CC Reaction=(2E)-tetradecenoyl-CoA = (3Z)-tetradecenoyl-CoA; CC Xref=Rhea:RHEA:29847, ChEBI:CHEBI:61405, ChEBI:CHEBI:61968; CC Evidence={ECO:0000250|UniProtKB:Q5XIC0}; CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:29849; CC Evidence={ECO:0000250|UniProtKB:Q5XIC0}; CC -!- CATALYTIC ACTIVITY: CC Reaction=(3E)-tetradecenoyl-CoA = (2E)-tetradecenoyl-CoA; CC Xref=Rhea:RHEA:47476, ChEBI:CHEBI:61405, ChEBI:CHEBI:87710; CC Evidence={ECO:0000250|UniProtKB:Q5XIC0}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:47477; CC Evidence={ECO:0000250|UniProtKB:Q5XIC0}; CC -!- CATALYTIC ACTIVITY: CC Reaction=(3E)-octenoyl-CoA = (2E)-octenoyl-CoA; Xref=Rhea:RHEA:49852, CC ChEBI:CHEBI:62242, ChEBI:CHEBI:131962; CC Evidence={ECO:0000250|UniProtKB:Q5XIC0}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:49853; CC Evidence={ECO:0000250|UniProtKB:Q5XIC0}; CC -!- CATALYTIC ACTIVITY: CC Reaction=(3E)-nonenoyl-CoA = (2E)-nonenoyl-CoA; Xref=Rhea:RHEA:46068, CC ChEBI:CHEBI:76292, ChEBI:CHEBI:85655; CC Evidence={ECO:0000250|UniProtKB:Q9WUR2}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:46069; CC Evidence={ECO:0000250|UniProtKB:Q9WUR2}; CC -!- PATHWAY: Lipid metabolism; fatty acid beta-oxidation. CC {ECO:0000269|PubMed:10419495}. CC -!- INTERACTION: CC O75521; Q13011: ECH1; NbExp=4; IntAct=EBI-2512024, EBI-711968; CC O75521; Q9Y5L0: TNPO3; NbExp=3; IntAct=EBI-2512024, EBI-1042571; CC -!- SUBCELLULAR LOCATION: [Isoform 1]: Mitochondrion CC {ECO:0000250|UniProtKB:Q5XIC0}. CC -!- SUBCELLULAR LOCATION: [Isoform 2]: Peroxisome matrix CC {ECO:0000269|PubMed:10419495}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1; CC IsoId=O75521-1; Sequence=Displayed; CC Name=2; Synonyms=PECI {ECO:0000269|PubMed:15217832, CC ECO:0000303|PubMed:10419495}; CC IsoId=O75521-2; Sequence=VSP_037854; CC -!- TISSUE SPECIFICITY: Abundant in heart, skeletal muscle and liver. CC Expressed in CD34(+) T-cells and CD34(+) bone marrow cells. CC {ECO:0000269|PubMed:10419495, ECO:0000269|PubMed:15217832}. CC -!- SIMILARITY: In the C-terminal section; belongs to the enoyl-CoA CC hydratase/isomerase family. {ECO:0000305}. CC -!- CAUTION: It is uncertain whether Met-1 or Met-3 is the initiator. CC {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=AAC19317.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305}; CC Sequence=AAD34173.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305}; CC Sequence=AAF66247.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305}; CC Sequence=AAH02668.3; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305}; CC Sequence=AAH16781.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305}; CC Sequence=AAH17474.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305}; CC Sequence=AAH33841.3; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305}; CC Sequence=AAH34702.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305}; CC Sequence=BAG52068.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305}; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AF069301; AAC19317.1; ALT_INIT; mRNA. DR EMBL; AL136642; CAB66577.1; -; mRNA. DR EMBL; AK075108; BAG52068.1; ALT_INIT; mRNA. DR EMBL; AL033383; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; BC002668; AAH02668.3; ALT_INIT; mRNA. DR EMBL; BC016781; AAH16781.1; ALT_INIT; mRNA. DR EMBL; BC017474; AAH17474.1; ALT_INIT; mRNA. DR EMBL; BC033841; AAH33841.3; ALT_INIT; mRNA. DR EMBL; BC034702; AAH34702.1; ALT_INIT; mRNA. DR EMBL; AF153612; AAD34173.1; ALT_INIT; mRNA. DR EMBL; AF244138; AAF66247.1; ALT_INIT; mRNA. DR CCDS; CCDS43420.2; -. [O75521-1] DR RefSeq; NP_001159482.1; NM_001166010.1. DR RefSeq; NP_006108.2; NM_006117.2. DR RefSeq; NP_996667.2; NM_206836.2. [O75521-1] DR PDB; 2CQU; NMR; -; A=31-133. DR PDB; 2F6Q; X-ray; 1.95 A; A/B/C=138-394. DR PDB; 4U18; X-ray; 2.64 A; A/B/C=138-390. DR PDB; 4U19; X-ray; 1.88 A; A/B/C=138-390. DR PDB; 4U1A; X-ray; 2.85 A; A/B/C=138-384. DR PDBsum; 2CQU; -. DR PDBsum; 2F6Q; -. DR PDBsum; 4U18; -. DR PDBsum; 4U19; -. DR PDBsum; 4U1A; -. DR AlphaFoldDB; O75521; -. DR SMR; O75521; -. DR BioGRID; 115718; 112. DR IntAct; O75521; 77. DR MINT; O75521; -. DR STRING; 9606.ENSP00000369461; -. DR DrugBank; DB08231; Myristic acid. DR SwissLipids; SLP:000001195; -. [O75521-2] DR GlyGen; O75521; 1 site, 1 O-linked glycan (1 site). DR iPTMnet; O75521; -. DR MetOSite; O75521; -. DR PhosphoSitePlus; O75521; -. DR SwissPalm; O75521; -. DR BioMuta; ECI2; -. DR REPRODUCTION-2DPAGE; IPI00419263; -. DR EPD; O75521; -. DR jPOST; O75521; -. DR MassIVE; O75521; -. DR MaxQB; O75521; -. DR PaxDb; 9606-ENSP00000369461; -. DR PeptideAtlas; O75521; -. DR ProteomicsDB; 50059; -. [O75521-1] DR ProteomicsDB; 50060; -. [O75521-2] DR Pumba; O75521; -. DR Antibodypedia; 9554; 325 antibodies from 32 providers. DR DNASU; 10455; -. DR Ensembl; ENST00000380118.8; ENSP00000369461.3; ENSG00000198721.13. [O75521-1] DR GeneID; 10455; -. DR KEGG; hsa:10455; -. DR MANE-Select; ENST00000380118.8; ENSP00000369461.3; NM_206836.3; NP_996667.2. DR UCSC; uc003mwd.4; human. [O75521-1] DR AGR; HGNC:14601; -. DR CTD; 10455; -. DR DisGeNET; 10455; -. DR GeneCards; ECI2; -. DR HGNC; HGNC:14601; ECI2. DR HPA; ENSG00000198721; Tissue enhanced (liver). DR MIM; 608024; gene. DR neXtProt; NX_O75521; -. DR OpenTargets; ENSG00000198721; -. DR PharmGKB; PA33168; -. DR VEuPathDB; HostDB:ENSG00000198721; -. DR eggNOG; KOG0016; Eukaryota. DR eggNOG; KOG0817; Eukaryota. DR GeneTree; ENSGT00940000155105; -. DR InParanoid; O75521; -. DR OMA; LHCDFVY; -. DR OrthoDB; 553487at2759; -. DR PhylomeDB; O75521; -. DR TreeFam; TF313375; -. DR BioCyc; MetaCyc:HS03615-MONOMER; -. DR BRENDA; 5.3.3.8; 2681. DR PathwayCommons; O75521; -. DR Reactome; R-HSA-390247; Beta-oxidation of very long chain fatty acids. [O75521-2] DR Reactome; R-HSA-9033241; Peroxisomal protein import. [O75521-2] DR SignaLink; O75521; -. DR UniPathway; UPA00659; -. DR BioGRID-ORCS; 10455; 10 hits in 1159 CRISPR screens. DR ChiTaRS; ECI2; human. DR EvolutionaryTrace; O75521; -. DR GeneWiki; PECI_(gene); -. DR GenomeRNAi; 10455; -. DR Pharos; O75521; Tbio. DR PRO; PR:O75521; -. DR Proteomes; UP000005640; Chromosome 6. DR RNAct; O75521; Protein. DR Bgee; ENSG00000198721; Expressed in adrenal tissue and 197 other cell types or tissues. DR ExpressionAtlas; O75521; baseline and differential. DR GO; GO:0005829; C:cytosol; TAS:Reactome. DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:HPA. DR GO; GO:0016020; C:membrane; HDA:UniProtKB. DR GO; GO:0005739; C:mitochondrion; IDA:LIFEdb. DR GO; GO:0005782; C:peroxisomal matrix; IDA:UniProtKB. DR GO; GO:0005777; C:peroxisome; IDA:HPA. DR GO; GO:0004165; F:delta(3)-delta(2)-enoyl-CoA isomerase activity; IDA:UniProtKB. DR GO; GO:0000062; F:fatty-acyl-CoA binding; IEA:InterPro. DR GO; GO:0006635; P:fatty acid beta-oxidation; ISS:UniProtKB. DR GO; GO:0009062; P:fatty acid catabolic process; IDA:UniProtKB. DR CDD; cd06558; crotonase-like; 1. DR Gene3D; 1.20.80.10; -; 1. DR Gene3D; 1.10.12.10; Lyase 2-enoyl-coa Hydratase, Chain A, domain 2; 1. DR InterPro; IPR022408; Acyl-CoA-binding_prot_CS. DR InterPro; IPR000582; Acyl-CoA-binding_protein. DR InterPro; IPR035984; Acyl-CoA-binding_sf. DR InterPro; IPR029045; ClpP/crotonase-like_dom_sf. DR InterPro; IPR001753; Enoyl-CoA_hydra/iso. DR InterPro; IPR014748; Enoyl-CoA_hydra_C. DR InterPro; IPR014352; FERM/acyl-CoA-bd_prot_sf. DR PANTHER; PTHR43684; -; 1. DR PANTHER; PTHR43684:SF1; ENOYL-COA DELTA ISOMERASE 2; 1. DR Pfam; PF00887; ACBP; 1. DR Pfam; PF00378; ECH_1; 1. DR PRINTS; PR00689; ACOABINDINGP. DR SUPFAM; SSF47027; Acyl-CoA binding protein; 1. DR SUPFAM; SSF52096; ClpP/crotonase; 1. DR PROSITE; PS00880; ACB_1; 1. DR PROSITE; PS51228; ACB_2; 1. DR UCD-2DPAGE; O75521; -. DR Genevisible; O75521; HS. PE 1: Evidence at protein level; KW 3D-structure; Acetylation; Alternative splicing; Isomerase; Mitochondrion; KW Peroxisome; Phosphoprotein; Reference proteome; Transit peptide. FT TRANSIT 1..38 FT /note="Mitochondrion" FT /evidence="ECO:0000255" FT CHAIN 39..394 FT /note="Enoyl-CoA delta isomerase 2" FT /id="PRO_0000214027" FT DOMAIN 39..124 FT /note="ACB" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00573" FT REGION 151..322 FT /note="ECH-like" FT MOTIF 392..394 FT /note="Microbody targeting signal" FT /evidence="ECO:0000255" FT BINDING 66..70 FT /ligand="an acyl-CoA" FT /ligand_id="ChEBI:CHEBI:58342" FT /evidence="ECO:0000250" FT BINDING 92 FT /ligand="an acyl-CoA" FT /ligand_id="ChEBI:CHEBI:58342" FT /evidence="ECO:0000250" FT BINDING 111 FT /ligand="an acyl-CoA" FT /ligand_id="ChEBI:CHEBI:58342" FT /evidence="ECO:0000250" FT BINDING 198..202 FT /ligand="substrate" FT /evidence="ECO:0000250|UniProtKB:Q05871" FT SITE 280 FT /note="Important for catalytic activity" FT /evidence="ECO:0000250|UniProtKB:Q05871" FT MOD_RES 51 FT /note="N6-acetyllysine; alternate" FT /evidence="ECO:0007744|PubMed:19608861" FT MOD_RES 51 FT /note="N6-succinyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:Q9WUR2" FT MOD_RES 55 FT /note="N6-succinyllysine" FT /evidence="ECO:0000250|UniProtKB:Q9WUR2" FT MOD_RES 62 FT /note="N6-acetyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:Q9WUR2" FT MOD_RES 62 FT /note="N6-succinyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:Q9WUR2" FT MOD_RES 70 FT /note="N6-succinyllysine" FT /evidence="ECO:0000250|UniProtKB:Q9WUR2" FT MOD_RES 81 FT /note="N6-succinyllysine" FT /evidence="ECO:0000250|UniProtKB:Q9WUR2" FT MOD_RES 90 FT /note="N6-succinyllysine" FT /evidence="ECO:0000250|UniProtKB:Q9WUR2" FT MOD_RES 92 FT /note="N6-acetyllysine; alternate" FT /evidence="ECO:0007744|PubMed:19608861" FT MOD_RES 92 FT /note="N6-succinyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:Q9WUR2" FT MOD_RES 101 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:24275569" FT MOD_RES 119 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 161 FT /note="N6-succinyllysine" FT /evidence="ECO:0000250|UniProtKB:Q9WUR2" FT MOD_RES 289 FT /note="N6-succinyllysine" FT /evidence="ECO:0000250|UniProtKB:Q9WUR2" FT VAR_SEQ 1..35 FT /note="Missing (in isoform 2)" FT /evidence="ECO:0000303|PubMed:10354522, FT ECO:0000303|PubMed:14702039, ECO:0000303|PubMed:15489334" FT /id="VSP_037854" FT VARIANT 47 FT /note="M -> I (in dbSNP:rs3177253)" FT /id="VAR_058493" FT VARIANT 344 FT /note="A -> V (in dbSNP:rs7166)" FT /evidence="ECO:0000269|PubMed:10354522, FT ECO:0000269|PubMed:12097419" FT /id="VAR_058494" FT CONFLICT 119 FT /note="S -> C (in Ref. 2; CAB66577)" FT /evidence="ECO:0000305" FT CONFLICT 195 FT /note="Y -> C (in Ref. 1; AAC19317)" FT /evidence="ECO:0000305" FT HELIX 40..52 FT /evidence="ECO:0007829|PDB:2CQU" FT HELIX 59..69 FT /evidence="ECO:0007829|PDB:2CQU" FT TURN 70..74 FT /evidence="ECO:0007829|PDB:2CQU" FT HELIX 87..99 FT /evidence="ECO:0007829|PDB:2CQU" FT HELIX 104..118 FT /evidence="ECO:0007829|PDB:2CQU" FT STRAND 140..147 FT /evidence="ECO:0007829|PDB:4U19" FT STRAND 150..155 FT /evidence="ECO:0007829|PDB:4U19" FT HELIX 158..160 FT /evidence="ECO:0007829|PDB:4U19" FT HELIX 166..181 FT /evidence="ECO:0007829|PDB:4U19" FT STRAND 185..192 FT /evidence="ECO:0007829|PDB:4U19" FT HELIX 203..205 FT /evidence="ECO:0007829|PDB:2F6Q" FT HELIX 212..232 FT /evidence="ECO:0007829|PDB:4U19" FT STRAND 238..242 FT /evidence="ECO:0007829|PDB:4U19" FT HELIX 249..252 FT /evidence="ECO:0007829|PDB:4U19" FT HELIX 253..256 FT /evidence="ECO:0007829|PDB:4U19" FT STRAND 258..263 FT /evidence="ECO:0007829|PDB:4U19" FT STRAND 267..269 FT /evidence="ECO:0007829|PDB:4U19" FT HELIX 273..275 FT /evidence="ECO:0007829|PDB:4U19" FT HELIX 283..291 FT /evidence="ECO:0007829|PDB:4U19" FT HELIX 293..300 FT /evidence="ECO:0007829|PDB:4U19" FT STRAND 305..307 FT /evidence="ECO:0007829|PDB:4U18" FT HELIX 308..313 FT /evidence="ECO:0007829|PDB:4U19" FT STRAND 318..321 FT /evidence="ECO:0007829|PDB:4U19" FT TURN 323..325 FT /evidence="ECO:0007829|PDB:4U19" FT HELIX 326..337 FT /evidence="ECO:0007829|PDB:4U19" FT HELIX 342..353 FT /evidence="ECO:0007829|PDB:4U19" FT HELIX 354..356 FT /evidence="ECO:0007829|PDB:4U19" FT HELIX 357..375 FT /evidence="ECO:0007829|PDB:4U19" FT HELIX 378..383 FT /evidence="ECO:0007829|PDB:4U19" FT HELIX 385..388 FT /evidence="ECO:0007829|PDB:4U19" SQ SEQUENCE 394 AA; 43585 MW; 8AC633D43A320102 CRC64; MAMAYLAWRL ARRSCPSSLQ VTSFPVVQLH MNRTAMRASQ KDFENSMNQV KLLKKDPGNE VKLKLYALYK QATEGPCNMP KPGVFDLINK AKWDAWNALG SLPKEAARQN YVDLVSSLSP SLESSSQVEP GTDRKSTGFE TLVVTSEDGI TKIMFNRPKK KNAINTEMYH EIMRALKAAS KDDSIITVLT GNGDYYSSGN DLTNFTDIPP GGVEEKAKNN AVLLREFVGC FIDFPKPLIA VVNGPAVGIS VTLLGLFDAV YASDRATFHT PFSHLGQSPE GCSSYTFPKI MSPAKATEML IFGKKLTAGE ACAQGLVTEV FPDSTFQKEV WTRLKAFAKL PPNALRISKE VIRKREREKL HAVNAEECNV LQGRWLSDEC TNAVVNFLSR KSKL //