ECI2_HUMAN
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 03-AUG-2022, entry version 214.
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};
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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; 104.
DR IntAct; O75521; 76.
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 UCD-2DPAGE; O75521; -.
DR EPD; O75521; -.
DR jPOST; O75521; -.
DR MassIVE; O75521; -.
DR MaxQB; O75521; -.
DR PaxDb; O75521; -.
DR PeptideAtlas; O75521; -.
DR PRIDE; O75521; -.
DR ProteomicsDB; 50059; -. [O75521-1]
DR ProteomicsDB; 50060; -. [O75521-2]
DR Antibodypedia; 9554; 299 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 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; TQLGLCP; -.
DR OrthoDB; 1471901at2759; -.
DR PhylomeDB; O75521; -.
DR TreeFam; TF313375; -.
DR BioCyc; MetaCyc:HS03615-MON; -.
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; 8 hits in 1078 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 195 other tissues.
DR ExpressionAtlas; O75521; baseline and differential.
DR Genevisible; O75521; HS.
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; IBA:GO_Central.
DR GO; GO:0006635; P:fatty acid beta-oxidation; ISS:UniProtKB.
DR GO; GO:0009062; P:fatty acid catabolic process; IDA:UniProtKB.
DR GO; GO:0006631; P:fatty acid metabolic process; IBA:GO_Central.
DR Gene3D; 1.10.12.10; -; 1.
DR Gene3D; 1.20.80.10; -; 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 Pfam; PF00887; ACBP; 1.
DR Pfam; PF00378; ECH_1; 1.
DR PRINTS; PR00689; ACOABINDINGP.
DR SUPFAM; SSF47027; SSF47027; 1.
DR SUPFAM; SSF52096; SSF52096; 1.
DR PROSITE; PS00880; ACB_1; 1.
DR PROSITE; PS51228; ACB_2; 1.
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
