ECI2_RAT
ID ECI2_RAT Reviewed; 391 AA.
AC Q5XIC0;
DT 01-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT 23-NOV-2004, sequence version 1.
DT 03-AUG-2022, entry version 121.
DE RecName: Full=Enoyl-CoA delta isomerase 2 {ECO:0000303|PubMed:11781327, ECO:0000305};
DE EC=5.3.3.8;
DE AltName: Full=Delta(3),delta(2)-enoyl-CoA isomerase;
DE Short=D3,D2-enoyl-CoA isomerase;
DE AltName: Full=Dodecenoyl-CoA isomerase;
DE AltName: Full=Peroxisomal 3,2-trans-enoyl-CoA isomerase {ECO:0000303|PubMed:11781327};
DE Short=pECI {ECO:0000303|PubMed:11781327};
DE Flags: Precursor;
GN Name=Eci2 {ECO:0000312|RGD:1359427}; Synonyms=Peci;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Heart;
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 [2]
RP FUNCTION, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=11781327; DOI=10.1074/jbc.m112228200;
RA Zhang D., Yu W., Geisbrecht B.V., Gould S.J., Sprecher H., Schulz H.;
RT "Functional characterization of delta3,delta2-enoyl-CoA isomerases from rat
RT liver.";
RL J. Biol. Chem. 277:9127-9132(2002).
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:11781327}.
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:11781327};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:45901;
CC Evidence={ECO:0000305|PubMed:11781327};
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:0000305|PubMed:11781327};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:45229;
CC Evidence={ECO:0000305|PubMed:11781327};
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:0000269|PubMed:11781327};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:29849;
CC Evidence={ECO:0000269|PubMed:11781327};
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:0000269|PubMed:11781327};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:47477;
CC Evidence={ECO:0000269|PubMed:11781327};
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:0000269|PubMed:11781327};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:49853;
CC Evidence={ECO:0000269|PubMed:11781327};
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:0000250|UniProtKB:O75521};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:46045;
CC Evidence={ECO:0000250|UniProtKB:O75521};
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 -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=1600 uM for (3Z)-hexenoyl-CoA {ECO:0000269|PubMed:11781327};
CC KM=120 uM for (3Z)-octenoyl-CoA {ECO:0000269|PubMed:11781327};
CC KM=29 uM for (3Z)-tetradecenoyl-CoA {ECO:0000269|PubMed:11781327};
CC KM=1200 uM for (3E)-hexenoyl-CoA {ECO:0000269|PubMed:11781327};
CC KM=100 uM for (3E)-octenoyl-CoA {ECO:0000269|PubMed:11781327};
CC KM=21 uM for (3E)-tetradecenoyl-CoA {ECO:0000269|PubMed:11781327};
CC Note=kcat are 100 sec(-1), 210 sec(-1), 540 sec(-1), 58 sec(-1), 47
CC sec(-1) and 210 sec(-1) for (3Z)-hexenoyl-CoA, (3Z)-octenoyl-CoA,
CC (3Z)-tetradecenoyl-CoA, (3E)-hexenoyl-CoA, (3E)-octenoyl-CoA and
CC (3E)-tetradecenoyl-CoA, respectively. {ECO:0000269|PubMed:11781327};
CC -!- PATHWAY: Lipid metabolism; fatty acid beta-oxidation.
CC {ECO:0000269|PubMed:11781327}.
CC -!- SUBCELLULAR LOCATION: Peroxisome matrix {ECO:0000269|PubMed:11781327}.
CC Mitochondrion {ECO:0000269|PubMed:11781327}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=1;
CC Comment=Additional isoforms may exist.;
CC Name=1;
CC IsoId=Q5XIC0-1; Sequence=Displayed;
CC -!- TISSUE SPECIFICITY: Liver (at protein level).
CC {ECO:0000269|PubMed:11781327}.
CC -!- SIMILARITY: In the C-terminal section; belongs to the enoyl-CoA
CC hydratase/isomerase family. {ECO:0000305}.
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DR EMBL; BC083764; AAH83764.1; -; mRNA.
DR RefSeq; NP_001006967.1; NM_001006966.1. [Q5XIC0-1]
DR AlphaFoldDB; Q5XIC0; -.
DR SMR; Q5XIC0; -.
DR IntAct; Q5XIC0; 1.
DR STRING; 10116.ENSRNOP00000022022; -.
DR SwissLipids; SLP:000001588; -.
DR iPTMnet; Q5XIC0; -.
DR PhosphoSitePlus; Q5XIC0; -.
DR jPOST; Q5XIC0; -.
DR PaxDb; Q5XIC0; -.
DR PRIDE; Q5XIC0; -.
DR GeneID; 291075; -.
DR KEGG; rno:291075; -.
DR UCSC; RGD:1359427; rat. [Q5XIC0-1]
DR CTD; 10455; -.
DR RGD; 1359427; Eci2.
DR VEuPathDB; HostDB:ENSRNOG00000066714; -.
DR eggNOG; KOG0016; Eukaryota.
DR eggNOG; KOG0817; Eukaryota.
DR HOGENOM; CLU_009834_7_2_1; -.
DR InParanoid; Q5XIC0; -.
DR OrthoDB; 1471901at2759; -.
DR PhylomeDB; Q5XIC0; -.
DR TreeFam; TF313375; -.
DR Reactome; R-RNO-390247; Beta-oxidation of very long chain fatty acids.
DR Reactome; R-RNO-9033241; Peroxisomal protein import.
DR SABIO-RK; Q5XIC0; -.
DR UniPathway; UPA00659; -.
DR PRO; PR:Q5XIC0; -.
DR Proteomes; UP000002494; Chromosome 17.
DR Bgee; ENSRNOG00000029549; Expressed in adult mammalian kidney and 19 other tissues.
DR ExpressionAtlas; Q5XIC0; baseline and differential.
DR Genevisible; Q5XIC0; RN.
DR GO; GO:0005739; C:mitochondrion; IDA:RGD.
DR GO; GO:0005782; C:peroxisomal matrix; IEA:UniProtKB-SubCell.
DR GO; GO:0005777; C:peroxisome; IDA:RGD.
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:0016863; F:intramolecular oxidoreductase activity, transposing C=C bonds; IDA:RGD.
DR GO; GO:0006635; P:fatty acid beta-oxidation; IDA:RGD.
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 Acetylation; Alternative splicing; Isomerase; Mitochondrion; Peroxisome;
KW Phosphoprotein; Reference proteome; Transit peptide.
FT TRANSIT 1..36
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 37..391
FT /note="Enoyl-CoA delta isomerase 2"
FT /id="PRO_0000381943"
FT DOMAIN 37..122
FT /note="ACB"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00573"
FT REGION 149..319
FT /note="ECH-like"
FT MOTIF 389..391
FT /note="Microbody targeting signal"
FT /evidence="ECO:0000255"
FT BINDING 64..68
FT /ligand="an acyl-CoA"
FT /ligand_id="ChEBI:CHEBI:58342"
FT /evidence="ECO:0000250"
FT BINDING 90
FT /ligand="an acyl-CoA"
FT /ligand_id="ChEBI:CHEBI:58342"
FT /evidence="ECO:0000250"
FT BINDING 109
FT /ligand="an acyl-CoA"
FT /ligand_id="ChEBI:CHEBI:58342"
FT /evidence="ECO:0000250"
FT BINDING 196..200
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q05871"
FT SITE 277
FT /note="Important for catalytic activity"
FT /evidence="ECO:0000250|UniProtKB:Q05871"
FT MOD_RES 49
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:O75521"
FT MOD_RES 49
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q9WUR2"
FT MOD_RES 53
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q9WUR2"
FT MOD_RES 60
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q9WUR2"
FT MOD_RES 60
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q9WUR2"
FT MOD_RES 68
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q9WUR2"
FT MOD_RES 79
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q9WUR2"
FT MOD_RES 88
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q9WUR2"
FT MOD_RES 90
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:O75521"
FT MOD_RES 90
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q9WUR2"
FT MOD_RES 99
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O75521"
FT MOD_RES 117
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O75521"
FT MOD_RES 127
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q9WUR2"
FT MOD_RES 159
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q9WUR2"
FT MOD_RES 286
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q9WUR2"
SQ SEQUENCE 391 AA; 43021 MW; A8BFC0E900967C32 CRC64;
MAAVTWSRAR CWCPSLLQVL RLPVTKLHLG RPAMRATQQD FENAMNQVKL LKKDPGNEVK
LRLYALYKQA TEGPCTMPKP GVFDFVNKAK WDAWNALGSL PKETARQNYV DLVSSLSSSS
EASSQGKGGA DGKAQESKGI LVTSEGGITK ITFNRPSKKN AITFQMYQDI ILALKNASTD
DTVITVFTGA GDYYSSGNDL TNFTSASGGM EEAANKGAIV LREFVNTFID FPKPLVAVVN
GPAVGISVTL LGLFDAVYAS DRATFHTPFS HLGQSPEACS SYTFPKMMGS AKAAEMLLFG
KKLTAREAWA QGLVTEVFPE STFETEVWTR LKTYAKLPPN SMRISKELIR KNEKEKLHAV
NEEECTTLRA RWLSEECINA IMSFVTRKPK L
