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Enoyl-CoA delta isomerase 2, mitochondrial (EC 5.3.3.8) (DRS-1) (Delta(3),delta(2)-enoyl-CoA isomerase) (D3,D2-enoyl-CoA isomerase) (Diazepam-binding inhibitor-related protein 1) (DBI-related protein 1) (Dodecenoyl-CoA isomerase) (Hepatocellular carcinoma-associated antigen 88) (Peroxisomal 3,2-trans-enoyl-CoA isomerase) (pECI) (Renal carcinoma antigen NY-REN-1)

 ECI2_HUMAN              Reviewed;         394 AA.
O75521; Q5JYK5; Q5JYK7; Q7L124; Q8N0X0; Q9BUE9; Q9H0T9; Q9NQH1;
Q9NYH7; Q9UN55;
15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
01-SEP-2009, sequence version 4.
20-JUN-2018, entry version 188.
RecName: Full=Enoyl-CoA delta isomerase 2, mitochondrial;
EC=5.3.3.8;
AltName: Full=DRS-1;
AltName: Full=Delta(3),delta(2)-enoyl-CoA isomerase;
Short=D3,D2-enoyl-CoA isomerase;
AltName: Full=Diazepam-binding inhibitor-related protein 1;
Short=DBI-related protein 1;
AltName: Full=Dodecenoyl-CoA isomerase;
AltName: Full=Hepatocellular carcinoma-associated antigen 88;
AltName: Full=Peroxisomal 3,2-trans-enoyl-CoA isomerase;
Short=pECI;
AltName: Full=Renal carcinoma antigen NY-REN-1;
Flags: Precursor;
Name=ECI2; Synonyms=DRS1, HCA88, PECI;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), AND VARIANT VAL-344.
TISSUE=Pancreatic islet;
PubMed=10354522; DOI=10.1016/S0925-4439(99)00033-2;
Suk K., Kim Y.-H., Hwang D.-Y., Ihm S.-H., Yoo H.J., Lee M.-S.;
"Molecular cloning and expression of a novel human cDNA related to the
diazepam binding inhibitor.";
Biochim. Biophys. Acta 1454:126-131(1999).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Brain;
PubMed=11230166; DOI=10.1101/gr.GR1547R;
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., Tampe J., Heubner D.,
Wambutt R., Korn B., Klein M., Poustka A.;
"Towards a catalog of human genes and proteins: sequencing and
analysis of 500 novel complete protein coding human cDNAs.";
Genome Res. 11:422-435(2001).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
TISSUE=Placenta;
PubMed=14702039; DOI=10.1038/ng1285;
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.,
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.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=14574404; DOI=10.1038/nature02055;
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., 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.;
"The DNA sequence and analysis of human chromosome 6.";
Nature 425:805-811(2003).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
TISSUE=Bone marrow, Skin, and Uterus;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[6]
NUCLEOTIDE SEQUENCE [MRNA] OF 4-394 (ISOFORM 1), AND SUBCELLULAR
LOCATION.
PubMed=10419495; DOI=10.1074/jbc.274.31.21797;
Geisbrecht B.V., Zhang D., Schulz H., Gould S.J.;
"Characterization of PECI, a novel monofunctional D3,D2-enoyl-CoA
isomerase of mammalian peroxisomes.";
J. Biol. Chem. 274:21797-21803(1999).
[7]
NUCLEOTIDE SEQUENCE [MRNA] OF 4-394 (ISOFORM 1), AND VARIANT VAL-344.
TISSUE=Hepatoma;
PubMed=12097419; DOI=10.4049/jimmunol.169.2.1102;
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.;
"Large scale identification of human hepatocellular carcinoma-
associated antigens by autoantibodies.";
J. Immunol. 169:1102-1109(2002).
[8]
IDENTIFICATION AS A RENAL CANCER ANTIGEN.
TISSUE=Renal cell carcinoma;
PubMed=10508479;
DOI=10.1002/(SICI)1097-0215(19991112)83:4<456::AID-IJC4>3.0.CO;2-5;
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.;
"Antigens recognized by autologous antibody in patients with renal-
cell carcinoma.";
Int. J. Cancer 83:456-464(1999).
[9]
SUBCELLULAR LOCATION.
PubMed=11256614; DOI=10.1093/embo-reports/kvd058;
Simpson J.C., Wellenreuther R., Poustka A., Pepperkok R., Wiemann S.;
"Systematic subcellular localization of novel proteins identified by
large-scale cDNA sequencing.";
EMBO Rep. 1:287-292(2000).
[10]
TISSUE SPECIFICITY.
PubMed=15217832; DOI=10.1182/blood-2004-05-1839;
Feng X., Chuhjo T., Sugimori C., Kotani T., Lu X., Takami A.,
Takamatsu H., Yamazaki H., Nakao S.;
"Diazepam-binding inhibitor-related protein 1: a candidate autoantigen
in acquired aplastic anemia patients harboring a minor population of
paroxysmal nocturnal hemoglobinuria-type cells.";
Blood 104:2425-2431(2004).
[11]
ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-51 AND LYS-92, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19608861; DOI=10.1126/science.1175371;
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M.,
Walther T.C., Olsen J.V., Mann M.;
"Lysine acetylation targets protein complexes and co-regulates major
cellular functions.";
Science 325:834-840(2009).
[12]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[13]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-119, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[14]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-101, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[15]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=25944712; DOI=10.1002/pmic.201400617;
Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M.,
Ayoub D., Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
"N-terminome analysis of the human mitochondrial proteome.";
Proteomics 15:2519-2524(2015).
[16]
STRUCTURE BY NMR OF 36-133.
RIKEN structural genomics initiative (RSGI);
"Solution structure of RSGI RUH-045, a human acyl-CoA binding
protein.";
Submitted (NOV-2005) to the PDB data bank.
[17]
X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS) OF 138-394.
Structural genomics consortium (SGC);
"The crystal structure of human peroxisomal delta3, delta2 enoyl-CoA
isomerase (pECI).";
Submitted (FEB-2009) to the PDB data bank.
-!- 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). {ECO:0000250}.
-!- CATALYTIC ACTIVITY: A (3Z)-alk-3-enoyl-CoA = a (2E)-alk-2-enoyl-
CoA.
-!- CATALYTIC ACTIVITY: A (3E)-alk-3-enoyl-CoA = a (2E)-alk-2-enoyl-
CoA.
-!- SUBCELLULAR LOCATION: Isoform 1: Mitochondrion {ECO:0000250}.
-!- SUBCELLULAR LOCATION: Isoform 2: Peroxisome matrix.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=O75521-1; Sequence=Displayed;
Name=2;
IsoId=O75521-2; Sequence=VSP_037854;
-!- TISSUE SPECIFICITY: Abundant in heart, skeletal muscle and liver.
Expressed in CD34(+) T-cells and CD34(+) bone marrow cells.
{ECO:0000269|PubMed:15217832}.
-!- SIMILARITY: In the C-terminal section; belongs to the enoyl-CoA
hydratase/isomerase family. {ECO:0000305}.
-!- CAUTION: It is uncertain whether Met-1 or Met-3 is the initiator.
{ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=AAC19317.1; Type=Erroneous initiation; Note=Translation N-terminally shortened.; Evidence={ECO:0000305};
Sequence=AAD34173.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
Sequence=AAF66247.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
Sequence=AAH02668.3; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
Sequence=AAH16781.1; Type=Erroneous initiation; Note=Translation N-terminally shortened.; Evidence={ECO:0000305};
Sequence=AAH17474.1; Type=Erroneous initiation; Note=Translation N-terminally shortened.; Evidence={ECO:0000305};
Sequence=AAH33841.3; Type=Erroneous initiation; Note=Translation N-terminally shortened.; Evidence={ECO:0000305};
Sequence=AAH34702.1; Type=Erroneous initiation; Note=Translation N-terminally shortened.; Evidence={ECO:0000305};
Sequence=BAG52068.1; Type=Erroneous initiation; Note=Translation N-terminally shortened.; Evidence={ECO:0000305};
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EMBL; AF069301; AAC19317.1; ALT_INIT; mRNA.
EMBL; AL136642; CAB66577.1; -; mRNA.
EMBL; AK075108; BAG52068.1; ALT_INIT; mRNA.
EMBL; AL033383; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BC002668; AAH02668.3; ALT_INIT; mRNA.
EMBL; BC016781; AAH16781.1; ALT_INIT; mRNA.
EMBL; BC017474; AAH17474.1; ALT_INIT; mRNA.
EMBL; BC033841; AAH33841.3; ALT_INIT; mRNA.
EMBL; BC034702; AAH34702.1; ALT_INIT; mRNA.
EMBL; AF153612; AAD34173.1; ALT_INIT; mRNA.
EMBL; AF244138; AAF66247.1; ALT_INIT; mRNA.
CCDS; CCDS43420.2; -. [O75521-1]
RefSeq; NP_001159482.1; NM_001166010.1.
RefSeq; NP_006108.2; NM_006117.2.
RefSeq; NP_996667.2; NM_206836.2. [O75521-1]
UniGene; Hs.15250; -.
PDB; 2CQU; NMR; -; A=31-133.
PDB; 2F6Q; X-ray; 1.95 A; A/B/C=138-394.
PDB; 4U18; X-ray; 2.64 A; A/B/C=138-390.
PDB; 4U19; X-ray; 1.88 A; A/B/C=138-390.
PDB; 4U1A; X-ray; 2.85 A; A/B/C=138-384.
PDBsum; 2CQU; -.
PDBsum; 2F6Q; -.
PDBsum; 4U18; -.
PDBsum; 4U19; -.
PDBsum; 4U1A; -.
ProteinModelPortal; O75521; -.
SMR; O75521; -.
BioGrid; 115718; 37.
IntAct; O75521; 53.
MINT; O75521; -.
STRING; 9606.ENSP00000369461; -.
DrugBank; DB08231; MYRISTIC ACID.
SwissLipids; SLP:000001195; -. [O75521-2]
iPTMnet; O75521; -.
PhosphoSitePlus; O75521; -.
SwissPalm; O75521; -.
BioMuta; ECI2; -.
REPRODUCTION-2DPAGE; IPI00419263; -.
UCD-2DPAGE; O75521; -.
EPD; O75521; -.
MaxQB; O75521; -.
PaxDb; O75521; -.
PeptideAtlas; O75521; -.
PRIDE; O75521; -.
ProteomicsDB; 50059; -.
ProteomicsDB; 50060; -. [O75521-2]
DNASU; 10455; -.
Ensembl; ENST00000380118; ENSP00000369461; ENSG00000198721. [O75521-1]
GeneID; 10455; -.
KEGG; hsa:10455; -.
UCSC; uc003mwd.4; human. [O75521-1]
CTD; 10455; -.
DisGeNET; 10455; -.
EuPathDB; HostDB:ENSG00000198721.12; -.
GeneCards; ECI2; -.
H-InvDB; HIX0025043; -.
HGNC; HGNC:14601; ECI2.
HPA; HPA022130; -.
HPA; HPA031626; -.
MIM; 608024; gene.
neXtProt; NX_O75521; -.
OpenTargets; ENSG00000198721; -.
PharmGKB; PA33168; -.
eggNOG; KOG0016; Eukaryota.
eggNOG; KOG0817; Eukaryota.
eggNOG; COG1024; LUCA.
eggNOG; COG4281; LUCA.
GeneTree; ENSGT00890000139344; -.
HOVERGEN; HBG006723; -.
InParanoid; O75521; -.
KO; K13239; -.
OMA; GCFIDFP; -.
OrthoDB; EOG091G0T5I; -.
PhylomeDB; O75521; -.
TreeFam; TF313375; -.
BioCyc; MetaCyc:HS03615-MONOMER; -.
Reactome; R-HSA-390247; Beta-oxidation of very long chain fatty acids.
Reactome; R-HSA-9033241; Peroxisomal protein import.
ChiTaRS; ECI2; human.
EvolutionaryTrace; O75521; -.
GeneWiki; PECI_(gene); -.
GenomeRNAi; 10455; -.
PRO; PR:O75521; -.
Proteomes; UP000005640; Chromosome 6.
Bgee; ENSG00000198721; -.
ExpressionAtlas; O75521; baseline and differential.
Genevisible; O75521; HS.
GO; GO:0005829; C:cytosol; TAS:Reactome.
GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:HPA.
GO; GO:0016020; C:membrane; HDA:UniProtKB.
GO; GO:0005739; C:mitochondrion; IDA:LIFEdb.
GO; GO:0005654; C:nucleoplasm; IDA:HPA.
GO; GO:0005782; C:peroxisomal matrix; IDA:UniProtKB.
GO; GO:0005777; C:peroxisome; IDA:HPA.
GO; GO:0004165; F:dodecenoyl-CoA delta-isomerase activity; IDA:UniProtKB.
GO; GO:0000062; F:fatty-acyl-CoA binding; IEA:InterPro.
GO; GO:0005102; F:signaling receptor binding; IPI:UniProtKB.
GO; GO:0033540; P:fatty acid beta-oxidation using acyl-CoA oxidase; TAS:Reactome.
GO; GO:0009062; P:fatty acid catabolic process; IDA:UniProtKB.
GO; GO:0006625; P:protein targeting to peroxisome; TAS:Reactome.
Gene3D; 1.10.12.10; -; 1.
Gene3D; 1.20.80.10; -; 1.
InterPro; IPR022408; Acyl-CoA-binding_prot_CS.
InterPro; IPR000582; Acyl-CoA-binding_protein.
InterPro; IPR035984; Acyl-CoA-binding_sf.
InterPro; IPR029045; ClpP/crotonase-like_dom_sf.
InterPro; IPR001753; Enoyl-CoA_hydra/iso.
InterPro; IPR014748; Enoyl-CoA_hydra_C.
InterPro; IPR014352; FERM/acyl-CoA-bd_prot_sf.
Pfam; PF00887; ACBP; 1.
Pfam; PF00378; ECH_1; 1.
PRINTS; PR00689; ACOABINDINGP.
SUPFAM; SSF47027; SSF47027; 1.
SUPFAM; SSF52096; SSF52096; 1.
PROSITE; PS00880; ACB_1; 1.
PROSITE; PS51228; ACB_2; 1.
1: Evidence at protein level;
3D-structure; Acetylation; Alternative splicing; Complete proteome;
Isomerase; Mitochondrion; Peroxisome; Phosphoprotein; Polymorphism;
Reference proteome; Transit peptide.
TRANSIT 1 38 Mitochondrion. {ECO:0000255}.
CHAIN 39 394 Enoyl-CoA delta isomerase 2,
mitochondrial.
/FTId=PRO_0000214027.
DOMAIN 39 124 ACB. {ECO:0000255|PROSITE-
ProRule:PRU00573}.
REGION 66 70 Acyl-CoA binding. {ECO:0000250}.
REGION 151 322 ECH-like.
REGION 198 202 Substrate binding.
{ECO:0000250|UniProtKB:Q05871}.
MOTIF 392 394 Microbody targeting signal.
{ECO:0000255}.
BINDING 92 92 Acyl-CoA. {ECO:0000250}.
BINDING 111 111 Acyl-CoA. {ECO:0000250}.
SITE 280 280 Important for catalytic activity.
{ECO:0000250|UniProtKB:Q05871}.
MOD_RES 51 51 N6-acetyllysine; alternate.
{ECO:0000244|PubMed:19608861}.
MOD_RES 51 51 N6-succinyllysine; alternate.
{ECO:0000250|UniProtKB:Q9WUR2}.
MOD_RES 55 55 N6-succinyllysine.
{ECO:0000250|UniProtKB:Q9WUR2}.
MOD_RES 62 62 N6-acetyllysine; alternate.
{ECO:0000250|UniProtKB:Q9WUR2}.
MOD_RES 62 62 N6-succinyllysine; alternate.
{ECO:0000250|UniProtKB:Q9WUR2}.
MOD_RES 70 70 N6-succinyllysine.
{ECO:0000250|UniProtKB:Q9WUR2}.
MOD_RES 81 81 N6-succinyllysine.
{ECO:0000250|UniProtKB:Q9WUR2}.
MOD_RES 90 90 N6-succinyllysine.
{ECO:0000250|UniProtKB:Q9WUR2}.
MOD_RES 92 92 N6-acetyllysine; alternate.
{ECO:0000244|PubMed:19608861}.
MOD_RES 92 92 N6-succinyllysine; alternate.
{ECO:0000250|UniProtKB:Q9WUR2}.
MOD_RES 101 101 Phosphoserine.
{ECO:0000244|PubMed:24275569}.
MOD_RES 119 119 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 161 161 N6-succinyllysine.
{ECO:0000250|UniProtKB:Q9WUR2}.
MOD_RES 289 289 N6-succinyllysine.
{ECO:0000250|UniProtKB:Q9WUR2}.
VAR_SEQ 1 35 Missing (in isoform 2).
{ECO:0000303|PubMed:10354522,
ECO:0000303|PubMed:14702039,
ECO:0000303|PubMed:15489334}.
/FTId=VSP_037854.
VARIANT 47 47 M -> I (in dbSNP:rs3177253).
/FTId=VAR_058493.
VARIANT 344 344 A -> V (in dbSNP:rs7166).
{ECO:0000269|PubMed:10354522,
ECO:0000269|PubMed:12097419}.
/FTId=VAR_058494.
CONFLICT 119 119 S -> C (in Ref. 2; CAB66577).
{ECO:0000305}.
CONFLICT 195 195 Y -> C (in Ref. 1; AAC19317).
{ECO:0000305}.
HELIX 40 52 {ECO:0000244|PDB:2CQU}.
HELIX 59 69 {ECO:0000244|PDB:2CQU}.
TURN 70 74 {ECO:0000244|PDB:2CQU}.
HELIX 87 99 {ECO:0000244|PDB:2CQU}.
HELIX 104 118 {ECO:0000244|PDB:2CQU}.
STRAND 140 147 {ECO:0000244|PDB:4U19}.
STRAND 150 155 {ECO:0000244|PDB:4U19}.
HELIX 158 160 {ECO:0000244|PDB:4U19}.
HELIX 166 181 {ECO:0000244|PDB:4U19}.
STRAND 185 192 {ECO:0000244|PDB:4U19}.
HELIX 203 205 {ECO:0000244|PDB:2F6Q}.
HELIX 212 232 {ECO:0000244|PDB:4U19}.
STRAND 238 242 {ECO:0000244|PDB:4U19}.
HELIX 249 252 {ECO:0000244|PDB:4U19}.
HELIX 253 256 {ECO:0000244|PDB:4U19}.
STRAND 258 263 {ECO:0000244|PDB:4U19}.
STRAND 267 269 {ECO:0000244|PDB:4U19}.
HELIX 273 275 {ECO:0000244|PDB:4U19}.
HELIX 283 291 {ECO:0000244|PDB:4U19}.
HELIX 293 300 {ECO:0000244|PDB:4U19}.
STRAND 305 307 {ECO:0000244|PDB:4U18}.
HELIX 308 313 {ECO:0000244|PDB:4U19}.
STRAND 318 321 {ECO:0000244|PDB:4U19}.
TURN 323 325 {ECO:0000244|PDB:4U19}.
HELIX 326 337 {ECO:0000244|PDB:4U19}.
HELIX 342 353 {ECO:0000244|PDB:4U19}.
HELIX 354 356 {ECO:0000244|PDB:4U19}.
HELIX 357 375 {ECO:0000244|PDB:4U19}.
HELIX 378 383 {ECO:0000244|PDB:4U19}.
HELIX 385 388 {ECO:0000244|PDB:4U19}.
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


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