ECI3_MOUSE
ID ECI3_MOUSE Reviewed; 317 AA.
AC Q78JN3; D3U0D8;
DT 20-JAN-2016, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 147.
DE RecName: Full=Enoyl-CoA delta isomerase 3, peroxisomal {ECO:0000305};
DE EC=5.3.3.8 {ECO:0000269|PubMed:24344334};
DE AltName: Full=Delta(3),delta(2)-enoyl-CoA isomerase {ECO:0000305};
DE Short=D3,D2-enoyl-CoA isomerase {ECO:0000305};
DE AltName: Full=Dodecenoyl-CoA isomerase {ECO:0000305};
GN Name=Eci3 {ECO:0000312|MGI:MGI:1916373};
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090 {ECO:0000312|EMBL:AAH14724.1};
RN [1] {ECO:0000312|EMBL:ACV81748.1}
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=BALB/cJ {ECO:0000312|EMBL:ACV81748.1};
RC TISSUE=Kidney {ECO:0000312|EMBL:ACV81748.1};
RA Zheng L., Zeng F., Tong Q.;
RL Submitted (FEB-2009) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000312|EMBL:BAE20705.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J {ECO:0000312|EMBL:BAE20705.1};
RC TISSUE=Kidney {ECO:0000312|EMBL:BAE20705.1};
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3] {ECO:0000312|Proteomes:UP000000589}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J {ECO:0000312|Proteomes:UP000000589};
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [4] {ECO:0000312|EMBL:EDL40898.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [5] {ECO:0000312|EMBL:AAH14724.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N {ECO:0000312|EMBL:AAH14724.1};
RC TISSUE=Colon {ECO:0000312|EMBL:AAH14724.1};
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 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Kidney;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [7] {ECO:0000305}
RP FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=24344334; DOI=10.1096/fj.13-240416;
RA van Weeghel M., Ofman R., Argmann C.A., Ruiter J.P., Claessen N.,
RA Oussoren S.V., Wanders R.J., Aten J., Houten S.M.;
RT "Identification and characterization of Eci3, a murine kidney-specific
RT Delta3,Delta2-enoyl-CoA isomerase.";
RL FASEB J. 28:1365-1374(2014).
CC -!- FUNCTION: Catalyzes the isomerization of trans-3-nonenoyl-CoA into
CC trans-2-nonenoyl-CoA (PubMed:24344334). May also have activity towards
CC other enoyl-CoA species (Probable). {ECO:0000269|PubMed:24344334,
CC ECO:0000305}.
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:0000269|PubMed:24344334};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:45901;
CC Evidence={ECO:0000305|PubMed:24344334};
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:0000269|PubMed:24344334};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:45229;
CC Evidence={ECO:0000305|PubMed:24344334};
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:0000269|PubMed:24344334};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:46069;
CC Evidence={ECO:0000305|PubMed:24344334};
CC -!- SUBCELLULAR LOCATION: Peroxisome {ECO:0000269|PubMed:24344334}.
CC -!- TISSUE SPECIFICITY: Expressed at high levels in the kidney. Also
CC detected at very low levels in the duodenum, jejunum, ileum, heart,
CC liver, lung, and brown adipose tissue (at protein level). In the
CC kidney, expression seems to be localized mainly to the proximal tubule.
CC {ECO:0000269|PubMed:24344334}.
CC -!- DOMAIN: The ACB (acyl-CoA-binding) domain is truncated and may be non-
CC functional. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the enoyl-CoA hydratase/isomerase family.
CC {ECO:0000305}.
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DR EMBL; FJ687155; ACV81748.1; -; mRNA.
DR EMBL; AK131590; BAE20705.1; -; mRNA.
DR EMBL; AC124537; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH466546; EDL40898.1; -; Genomic_DNA.
DR EMBL; CH466546; EDL40899.1; -; Genomic_DNA.
DR EMBL; BC014724; AAH14724.1; -; mRNA.
DR CCDS; CCDS26449.1; -.
DR RefSeq; NP_081223.1; NM_026947.4.
DR RefSeq; XP_006516828.1; XM_006516765.3.
DR AlphaFoldDB; Q78JN3; -.
DR SMR; Q78JN3; -.
DR STRING; 10090.ENSMUSP00000021853; -.
DR SwissLipids; SLP:000001193; -.
DR iPTMnet; Q78JN3; -.
DR PhosphoSitePlus; Q78JN3; -.
DR SwissPalm; Q78JN3; -.
DR jPOST; Q78JN3; -.
DR MaxQB; Q78JN3; -.
DR PaxDb; Q78JN3; -.
DR PRIDE; Q78JN3; -.
DR ProteomicsDB; 275436; -.
DR DNASU; 69123; -.
DR Ensembl; ENSMUST00000021853; ENSMUSP00000021853; ENSMUSG00000021416.
DR GeneID; 69123; -.
DR KEGG; mmu:69123; -.
DR UCSC; uc007qbv.1; mouse.
DR CTD; 69123; -.
DR MGI; MGI:1916373; Eci3.
DR VEuPathDB; HostDB:ENSMUSG00000021416; -.
DR eggNOG; KOG0016; Eukaryota.
DR eggNOG; KOG0817; Eukaryota.
DR GeneTree; ENSGT00940000155105; -.
DR InParanoid; Q78JN3; -.
DR OMA; LGTHLNQ; -.
DR OrthoDB; 1471901at2759; -.
DR PhylomeDB; Q78JN3; -.
DR TreeFam; TF313375; -.
DR BRENDA; 5.3.3.8; 3474.
DR BioGRID-ORCS; 69123; 0 hits in 73 CRISPR screens.
DR PRO; PR:Q78JN3; -.
DR Proteomes; UP000000589; Chromosome 13.
DR RNAct; Q78JN3; protein.
DR Bgee; ENSMUSG00000021416; Expressed in right kidney and 68 other tissues.
DR ExpressionAtlas; Q78JN3; baseline and differential.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; ISO:MGI.
DR GO; GO:0005739; C:mitochondrion; ISO:MGI.
DR GO; GO:0005782; C:peroxisomal matrix; ISO:MGI.
DR GO; GO:0005777; C:peroxisome; IDA:MGI.
DR GO; GO:0004165; F:delta(3)-delta(2)-enoyl-CoA isomerase activity; IDA:MGI.
DR GO; GO:0000062; F:fatty-acyl-CoA binding; IBA:GO_Central.
DR GO; GO:0016863; F:intramolecular oxidoreductase activity, transposing C=C bonds; ISO:MGI.
DR GO; GO:0006635; P:fatty acid beta-oxidation; ISO:MGI.
DR GO; GO:0009062; P:fatty acid catabolic process; ISO:MGI.
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; 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; PF00378; ECH_1; 1.
DR SUPFAM; SSF47027; SSF47027; 1.
DR SUPFAM; SSF52096; SSF52096; 1.
DR PROSITE; PS51228; ACB_2; 1.
PE 1: Evidence at protein level;
KW Isomerase; Peroxisome; Reference proteome.
FT CHAIN 1..317
FT /note="Enoyl-CoA delta isomerase 3, peroxisomal"
FT /id="PRO_0000435335"
FT DOMAIN 1..46
FT /note="ACB"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00573"
FT REGION 40..60
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 315..317
FT /note="Microbody targeting signal"
FT /evidence="ECO:0000255"
FT BINDING 120..124
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q05871"
FT SITE 201
FT /note="Important for catalytic activity"
FT /evidence="ECO:0000250|UniProtKB:Q05871"
FT CONFLICT 108
FT /note="I -> V (in Ref. 1; ACV81748)"
FT /evidence="ECO:0000305"
FT CONFLICT 257
FT /note="T -> P (in Ref. 1; ACV81748)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 317 AA; 35231 MW; 52BF28A3CD8D8E50 CRC64;
MPKPGVFNFV NKATWDARNA LGSLPKETAR KNYVDLVSSL SSSSEAPSQG KRGADEKARE
SKDILVTSED GITKITFNRP TKKNAISFQM YLDIMHALKN ASTDNSVITV FTGTGDYYSS
GNDLKNLIND AGEIQDVVAT STKILREFVN CFIDFPKPLV AVVNGPAVGI AVTILALFDA
VFASDRATFH TPFSQLSQIP EACSTYMFPK IMGPTKAAEM LLFGKKLTAR EAWAQGLVTE
VFPESTFETE VWTRLKTYSK LSPNVMRISK ELIRKHEKQK LYTVNAEECA AALERMPREE
YAKALRNFLF RKAKAKL
