P42126 (ECI1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Enoyl-CoA delta isomerase 1, mitochondrial
EC=5.3.3.8

Alternative name(s):
3,2-trans-enoyl-CoA isomerase
Delta(3),Delta(2)-enoyl-CoA isomerase
Short name=D3,D2-enoyl-CoA isomerase
Dodecenoyl-CoA isomerase

Gene names

Name:	ECI1
Synonyms:	DCI

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	302 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Able to isomerize both 3-cis and 3-trans double bonds into the 2-trans form in a range of enoyl-CoA species.
Catalytic activity	(3Z)-dodec-3-enoyl-CoA = (2E)-dodec-2-enoyl-CoA. Ref.6
Pathway	Lipid metabolism; fatty acid beta-oxidation.
Subunit structure	Homotrimer. Ref.9
Subcellular location	Mitochondrion matrix.
Sequence similarities	Belongs to the enoyl-CoA hydratase/isomerase family.

Ontologies

Keywords
Biological process	Fatty acid metabolism Lipid metabolism
Cellular component	Mitochondrion
Coding sequence diversity	Alternative splicing
Domain	Transit peptide
Molecular function	Isomerase
PTM	Acetylation
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological process	fatty acid beta-oxidation Non-traceable author statement Ref.1. Source: UniProtKB
Cellular component	mitochondrial matrix Non-traceable author statement Ref.1. Source: UniProtKB
Molecular function	dodecenoyl-CoA delta-isomerase activity Non-traceable author statement Ref.6Ref.1. Source: UniProtKB
Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: P42126-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

Isoform 2 (identifier: P42126-2)

The sequence of this isoform differs from the canonical sequence as follows:
     172-188: Missing.

Note: No experimental confirmation available.

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Transit peptide

1 – 41

41

Mitochondrion By similarity

Chain

42 – 302

261

Enoyl-CoA delta isomerase 1, mitochondrial

PRO_0000007420

Regions

Region

106 – 110

5

Substrate binding

Sites

Binding site

153

1

Substrate; via amide nitrogen

Binding site

177

1

Substrate

Site

178

1

Important for catalytic activity

Amino acid modifications

Modified residue

89

1

N6-acetyllysine Ref.7

Modified residue

283

1

N6-acetyllysine Ref.7

Natural variations

Alternative sequence

172 – 188

17

Missing in isoform 2.

VSP_001358

Experimental info

Mutagenesis

178

1

E → A: Loss of activity. Ref.9

Sequence conflict

14

1

L → P in AAH00762. Ref.4

Sequence conflict

14

1

L → P in AAH19316. Ref.4

Sequence conflict

41

1

R → P in CAA81065. Ref.1

Sequence conflict

44

1

S → C AA sequence Ref.6

Sequence conflict

54

1

G → A in CAA81065. Ref.1

Sequence conflict

78

1

L → F AA sequence Ref.6

Sequence conflict

93

1

G → V in AAA35485. Ref.5

Sequence conflict

114

1

Missing AA sequence Ref.6

Sequence conflict

192 – 193

2

TL → PY AA sequence Ref.6

Sequence conflict

204 – 207

4

RALQ → SAPE in AAA35485. Ref.5

Sequence conflict

210

1

L → S AA sequence Ref.6

Sequence conflict

213 – 215

3

PPA → RRP in AAA35485. Ref.5

Sequence conflict

242

1

Q → K AA sequence Ref.6

Sequence conflict

245

1

A → T AA sequence Ref.6

Sequence conflict

248

1

D → E AA sequence Ref.6

Sequence conflict

291

1

Q → E AA sequence Ref.6

Secondary structure

1

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302

Helix Strand Turn

Details...

Beta strand

46 – 52

7

Turn

53 – 56

4

Beta strand

57 – 62

6

Turn

65 – 67

3

Helix

72 – 87

16

Beta strand

93 – 100

8

Beta strand

102 – 104

3

Helix

110 – 113

4

Helix

118 – 136

19

Beta strand

139 – 146

8

Beta strand

148 – 150

3

Helix

152 – 158

7

Beta strand

161 – 167

7

Helix

178 – 181

4

Helix

187 – 197

11

Helix

199 – 208

10

Helix

214 – 219

6

Beta strand

222 – 227

6

Helix

229 – 231

3

Helix

232 – 244

13

Helix

248 – 267

20

Helix

270 – 281

12

Helix

284 – 290

7

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified November 1, 1995. Version 1. Checksum: 6E63827DE9BE886B	FASTA	302	32,816
	10 20 30 40 50 60 MALVASVRVP ARVLLRAGAR LPGAALGRTE RAAGGGDGAR RFGSQRVLVE PDAGAGVAVM 70 80 90 100 110 120 KFKNPPVNSL SLEFLTELVI SLEKLENDKS FRGVILTSDR PGVFSAGLDL TEMCGRSPAH 130 140 150 160 170 180 YAGYWKAVQE LWLRLYQSNL VLVSAINGAC PAGGCLVALT CDYRILADNP RYCIGLNETQ 190 200 210 220 230 240 LGIIAPFWLK DTLENTIGHR AAERALQLGL LFPPAEALQV GIVDQVVPEE QVQSTALSAI 250 260 270 280 290 300 AQWMAIPDHA RQLTKAMMRK ATASRLVTQR DADVQNFVSF ISKDSIQKSL QMYLERLKEE KG
	Isoform 2 [UniParc]. Checksum: F3689BA4B6F7FC72	FASTA	285	30,896
	10 20 30 40 50 60 MALVASVRVP ARVLLRAGAR LPGAALGRTE RAAGGGDGAR RFGSQRVLVE PDAGAGVAVM 70 80 90 100 110 120 KFKNPPVNSL SLEFLTELVI SLEKLENDKS FRGVILTSDR PGVFSAGLDL TEMCGRSPAH 130 140 150 160 170 180 YAGYWKAVQE LWLRLYQSNL VLVSAINGAC PAGGCLVALT CDYRILADNP RLKDTLENTI 190 200 210 220 230 240 GHRAAERALQ LGLLFPPAEA LQVGIVDQVV PEEQVQSTAL SAIAQWMAIP DHARQLTKAM 250 260 270 280 MRKATASRLV TQRDADVQNF VSFISKDSIQ KSLQMYLERL KEEKG

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Human mitochondrial 3,2-trans-enoyl-CoA isomerase (DCI): gene structure and localization to chromosome 16p13.3." Janssen U., Fink T., Lichter P., Stoffel W. Genomics 23:223-228(1994) [PubMed: 7829074] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORM 1). Tissue: Liver and Placenta.
[2]	"Complete sequencing and characterization of 21,243 full-length human cDNAs." 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. Nat. Genet. 36:40-45(2004) [PubMed: 14702039] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
[3]	Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C. Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2). Tissue: Lung and Placenta.
[5]	"cDNA cloning and amino acid sequence of human mitochondrial delta 3 delta 2-enoyl-CoA isomerase: comparison of the human enzyme with its rat counterpart, mitochondrial short-chain isomerase." Kilponen J.M., Haeyrinen H.M., Rehn M.V., Hiltunen K.J. Biochem. J. 300:1-5(1994) [PubMed: 8198519] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 37-302 (ISOFORM 1).
[6]	"Delta 3, delta 2-enoyl-CoA isomerase is the protein that copurifies with human glutathione S-transferases from S-hexylglutathione affinity matrices." Takahashi Y., Hirata Y., Burstein Y., Listowsky I. Biochem. J. 304:849-852(1994) [PubMed: 7818490] [Abstract] Cited for: PROTEIN SEQUENCE OF 42-84; 89-116; 190-220; 242-255 AND 288-298, CATALYTIC ACTIVITY. Tissue: Liver.
[7]	"Lysine acetylation targets protein complexes and co-regulates major cellular functions." Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T., Olsen J.V., Mann M. Science 325:834-840(2009) [PubMed: 19608861] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-89 AND LYS-283, MASS SPECTROMETRY.
[8]	"Initial characterization of the human central proteome." Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J. BMC Syst. Biol. 5:17-17(2011) [PubMed: 21269460] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[9]	"The 1.3 A crystal structure of human mitochondrial Delta3-Delta2-enoyl-CoA isomerase shows a novel mode of binding for the fatty acyl group." Partanen S.T., Novikov D.K., Popov A.N., Mursula A.M., Hiltunen J.K., Wierenga R.K. J. Mol. Biol. 342:1197-1208(2004) [PubMed: 15351645] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.3 ANGSTROMS) OF 43-302 IN COMPLEX WITH OCTANOYL-COENZYME A, SUBUNIT, MUTAGENESIS OF GLU-178.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

Z25820 mRNA. Translation: CAA81065.1.
Z25821 , Z25822, Z25823, Z25824 Genomic DNA. Translation: CAA81066.1.
AK291127 mRNA. Translation: BAF83816.1.
CH471112 Genomic DNA. Translation: EAW85524.1.
BC000762 mRNA. Translation: AAH00762.1.
BC002746 mRNA. Translation: AAH02746.1.
BC020228 mRNA. Translation: AAH20228.1.
BC019316 mRNA. Translation: AAH19316.1.
L24774 mRNA. Translation: AAA35485.1.

IPI

IPI00300567.
IPI00398758.

PIR

A55723.

RefSeq

NP_001171500.1. NM_001178029.1.
NP_001910.2. NM_001919.3.

UniGene

Hs.403436.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1SG4	X-ray	1.30	A/B/C	43-302	[»]

ProteinModelPortal

P42126.

SMR

P42126. Positions 45-302.

ModBase

Search...

Protein-protein interaction databases

IntAct

P42126. 2 interactions.

STRING

P42126.

PTM databases

PhosphoSite

P42126.

Polymorphism databases

DMDM

1169204.

2D gel databases

OGP

P42126.

Proteomic databases

PeptideAtlas

P42126.

PRIDE

P42126.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000301729; ENSP00000301729; ENSG00000167969.

GeneID

1632.

KEGG

hsa:1632.

UCSC

uc002cpr.1. human.
uc002cps.1. human.

Organism-specific databases

CTD

1632.

GeneCards

GC16M002292.

H-InvDB

HIX0012721.

HGNC

HGNC:2703. ECI1.

HPA

HPA041746.
HPA043227.

MIM

600305. gene.

neXtProt

NX_P42126.

PharmGKB

PA27173.

GenAtlas

Search...

Phylogenomic databases

eggNOG

prNOG09473.

HOGENOM

HBG621614.

HOVERGEN

HBG001112.

InParanoid

P42126.

OMA

AGGCLMA.

OrthoDB

EOG4R23VQ.

PhylomeDB

P42126.

Enzyme and pathway databases

Reactome

REACT_22258. Metabolism of lipids and lipoproteins.

Gene expression databases

ArrayExpress

P42126.

Bgee

P42126.

CleanEx

HS_DCI.

Genevestigator

P42126.

GermOnline

ENSG00000167969. Homo sapiens.

Family and domain databases

InterPro

IPR001753. Crotonase_core.
IPR018376. Enoyl-CoA_hyd/isom_CS.
[Graphical view]

KO

K13238.

Pfam

PF00378. ECH. 1 hit.
[Graphical view]

PROSITE

PS00166. ENOYL_COA_HYDRATASE. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

NextBio

6694.

SOURCE

Search...

Entry information

Entry name

ECI1_HUMAN

Accession

Primary (citable) accession number: P42126
Secondary accession number(s): A8K512 , Q13290, Q7Z2L6, Q7Z2L7, Q9BUB8, Q9BW05, Q9UDG6

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1995
Last sequence update:	November 1, 1995
Last modified:	January 25, 2012
This is version 121 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.