Q13011 (ECH1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Delta(3,5)-Delta(2,4)-dienoyl-CoA isomerase, mitochondrial
EC=5.3.3.-

Gene names

Name:

ECH1

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	328 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	Isomerization of 3-trans,5-cis-dienoyl-CoA to 2-trans,4-trans-dienoyl-CoA By similarity.
Pathway	Lipid metabolism; fatty acid beta-oxidation.
Subunit structure	Homohexamer By similarity.
Subcellular location	Mitochondrion By similarity. Peroxisome By similarity.
Sequence similarities	Belongs to the enoyl-CoA hydratase/isomerase family.

Ontologies

Keywords
Biological process	Fatty acid metabolism Lipid metabolism
Cellular component	Mitochondrion Peroxisome
Coding sequence diversity	Polymorphism
Domain	Transit peptide
Molecular function	Isomerase
PTM	Acetylation Phosphoprotein
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological process	fatty acid beta-oxidation Traceable author statement. Source: ProtInc generation of precursor metabolites and energy Traceable author statement. Source: ProtInc
Cellular component	mitochondrion Inferred from direct assay. Source: HPA peroxisome Traceable author statement. Source: ProtInc
Molecular function	enoyl-CoA hydratase activity Traceable author statement. Source: ProtInc isomerase activity Inferred from electronic annotation. Source: UniProtKB-KW protein binding Inferred from physical interaction. Source: IntAct
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
HTT	P42858	2	EBI-711968,EBI-466029
STAT3	P40763	2	EBI-711968,EBI-518675

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Transit peptide

1 – 33

33

Mitochondrion Potential

Chain

34 – 328

295

Delta(3,5)-Delta(2,4)-dienoyl-CoA isomerase, mitochondrial

PRO_0000007417

Regions

Motif

326 – 328

3

Microbody targeting signal Potential

Sites

Binding site

174

1

Substrate; via amide nitrogen By similarity

Site

197

1

Important for catalytic activity By similarity

Amino acid modifications

Modified residue

28

1

Phosphoserine Ref.8

Modified residue

30

1

Phosphoserine Ref.8

Modified residue

83

1

N6-acetyllysine Ref.9

Modified residue

95

1

N6-acetyllysine Ref.9

Modified residue

318

1

N6-acetyllysine Ref.9

Modified residue

327

1

N6-acetyllysine Ref.9

Natural variations

Natural variant

41

1

E → A. Ref.3 Ref.4 Ref.5
Corresponds to variant rs9419 [ dbSNP | Ensembl ].

VAR_014927

Natural variant

217

1

G → R.
Corresponds to variant rs2229259 [ dbSNP | Ensembl ].

VAR_033913

Experimental info

Sequence conflict

210

1

Q → E in AAC50222. Ref.1

Sequence conflict

210

1

Q → E in AAB86485. Ref.2

Sequence conflict

230

1

R → H in AAC50222. Ref.1

Sequence conflict

230

1

R → H in AAB86485. Ref.2

Sequence conflict

239

1

G → D in AAC50222. Ref.1

Sequence conflict

239

1

G → D in AAB86485. Ref.2

Sequence conflict

259

1

A → P in AAC50222. Ref.1

Sequence conflict

259

1

A → P in AAB86485. Ref.2

Sequence conflict

262

1

A → P in AAC50222. Ref.1

Sequence conflict

262

1

A → P in AAB86485. Ref.2

Sequence conflict

268 – 271

4

SPVA → TTVL in AAC50222. Ref.1

Sequence conflict

268 – 271

4

SPVA → TTVL in AAB86485. Ref.2

Sequence conflict

313

1

A → P in AAC50222. Ref.1

Sequence conflict

313

1

A → P in AAB86485. Ref.2

Secondary structure

1

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328

Helix Strand Turn

Details...

Beta strand

56 – 62

7

Beta strand

64 – 72

9

Helix

75 – 77

3

Helix

83 – 97

15

Beta strand

104 – 108

5

Helix

120 – 128

9

Helix

135 – 158

24

Beta strand

159 – 161

3

Beta strand

163 – 167

5

Helix

179 – 181

3

Beta strand

182 – 188

7

Beta strand

192 – 194

3

Helix

197 – 199

3

Turn

209 – 211

3

Helix

212 – 215

4

Helix

219 – 228

10

Beta strand

231 – 233

3

Helix

234 – 237

4

Beta strand

244 – 249

6

Helix

250 – 265

16

Helix

269 – 284

16

Helix

287 – 301

15

Helix

305 – 313

9

Sequences

	Sequence		Length	Mass (Da)
	Q13011 [UniParc]. Last modified November 22, 2005. Version 2. Checksum: 211E0FF40379E6DA	FASTA	328	35,816
	10 20 30 40 50 60 MAAGIVASRR LRDLLTRRLT GSNYPGLSIS LRLTGSSAQE EASGVALGEA PDHSYESLRV 70 80 90 100 110 120 TSAQKHVLHV QLNRPNKRNA MNKVFWREMV ECFNKISRDA DCRAVVISGA GKMFTAGIDL 130 140 150 160 170 180 MDMASDILQP KGDDVARISW YLRDIITRYQ ETFNVIERCP KPVIAAVHGG CIGGGVDLVT 190 200 210 220 230 240 ACDIRYCAQD AFFQVKEVDV GLAADVGTLQ RLPKVIGNQS LVNELAFTAR KMMADEALGS 250 260 270 280 290 300 GLVSRVFPDK EVMLDAALAL AAEISSKSPV AVQSTKVNLL YSRDHSVAES LNYVASWNMS 310 320 MLQTQDLVKS VQATTENKEL KTVTFSKL

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Isolation and characterization of rat and human cDNAs encoding a novel putative peroxisomal enoyl-CoA hydratase." Fitzpatrick D.R., Germain-Lee E., Valle D. Genomics 27:457-466(1995) [PubMed: 7558027] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Retina.
[2]	"Genomic structure of human ECH1." Fitzpatrick D.R., Valle D. Submitted (NOV-1997) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[3]	"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], VARIANT ALA-41. Tissue: Skeletal muscle.
[4]	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 (JUL-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], VARIANT ALA-41.
[5]	"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], VARIANT ALA-41. Tissue: Melanoma and Pancreatic carcinoma.
[6]	Bienvenut W.V., Claeys D. Submitted (NOV-2005) to UniProtKB Cited for: PROTEIN SEQUENCE OF 149-158 AND 215-230, MASS SPECTROMETRY. Tissue: Platelet.
[7]	Lubec G., Afjehi-Sadat L., Chen W.-Q., Sun Y. Submitted (DEC-2008) to UniProtKB Cited for: PROTEIN SEQUENCE OF 66-77; 113-131; 149-211; 215-230 AND 232-245, MASS SPECTROMETRY. Tissue: Brain, Cajal-Retzius cell and Fetal brain cortex.
[8]	"Global, in vivo, and site-specific phosphorylation dynamics in signaling networks." Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M. Cell 127:635-648(2006) [PubMed: 17081983] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-28 AND SER-30, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[9]	"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-83; LYS-95; LYS-318 AND LYS-327, MASS SPECTROMETRY.
[10]	"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].
[11]	"Crystal structure of human peroxisomal delta3,5,delta2,4-dienoyl CoA isomerase (ECH1)." Structural genomics consortium (SGC) Submitted (FEB-2009) to the PDB data bank Cited for: X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS) OF 50-322.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

U16660 mRNA. Translation: AAC50222.1.
AF030249 , AF030246, AF030247, AF030248 Genomic DNA. Translation: AAB86485.1.
AK291860 mRNA. Translation: BAF84549.1.
CH471126 Genomic DNA. Translation: EAW56824.1.
BC011792 mRNA. Translation: AAH11792.1.
BC017408 mRNA. Translation: AAH17408.1.

IPI

IPI00011416.

PIR

I38882.

RefSeq

NP_001389.2. NM_001398.2.

UniGene

Hs.196176.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2VRE	X-ray	1.95	A/B/C	50-322	[»]

ProteinModelPortal

Q13011.

SMR

Q13011. Positions 50-315.

ModBase

Search...

Protein-protein interaction databases

IntAct

Q13011. 14 interactions.

MINT

MINT-1393158.

STRING

Q13011.

PTM databases

PhosphoSite

Q13011.

Polymorphism databases

DMDM

82654933.

2D gel databases

REPRODUCTION-2DPAGE

IPI00011416.

UCD-2DPAGE

Q13011.

Proteomic databases

PeptideAtlas

Q13011.

PRIDE

Q13011.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000221418; ENSP00000221418; ENSG00000104823.

GeneID

1891.

KEGG

hsa:1891.

UCSC

uc002oji.1. human.

Organism-specific databases

CTD

1891.

GeneCards

GC19M039306.

H-InvDB

HIX0015101.

HGNC

HGNC:3149. ECH1.

HPA

HPA002907.
HPA005835.

MIM

600696. gene.

neXtProt

NX_Q13011.

PharmGKB

PA27596.

GenAtlas

Search...

Phylogenomic databases

eggNOG

prNOG07488.

GeneTree

ENSGT00580000081296.

HOGENOM

HBG748731.

HOVERGEN

HBG005556.

InParanoid

Q13011.

OMA

HTNQEGL.

OrthoDB

EOG4VQ9PW.

PhylomeDB

Q13011.

Gene expression databases

ArrayExpress

Q13011.

Bgee

Q13011.

CleanEx

HS_ECH1.

Genevestigator

Q13011.

GermOnline

ENSG00000104823. Homo sapiens.

Family and domain databases

InterPro

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

KO

K12663.

Pfam

PF00378. ECH. 1 hit.
[Graphical view]

PROSITE

PS00166. ENOYL_COA_HYDRATASE. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

NextBio

7711.

SOURCE

Search...

Entry information

Entry name

ECH1_HUMAN

Accession

Primary (citable) accession number: Q13011
Secondary accession number(s): A8K745, Q8WVX0, Q96EZ9

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1997
Last sequence update:	November 22, 2005
Last modified:	January 25, 2012
This is version 117 of the entry and version 2 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.