MECR

Functionⁱ

Catalyzes the NADPH-dependent reduction of trans-2-enoyl thioesters in mitochondrial fatty acid synthesis (fatty acid synthesis type II). Fatty acid chain elongation in mitochondria uses acyl carrier protein (ACP) as an acyl group carrier, but the enzyme accepts both ACP and CoA thioesters as substrates in vitro. Has a preference for short and medium chain substrates, including trans-2-hexenoyl-CoA (C6), trans-2-decenoyl-CoA (C10), and trans-2-hexadecenoyl-CoA (C16).2 Publications

Catalytic activityⁱ

a 2,3-saturated acyl-[ACP]
Search proteins in UniProtKB for this molecule.
Search chemical reactions in Rhea for this molecule.
+
NADP⁺
Search proteins in UniProtKB for this molecule.
Search chemical reactions in Rhea for this molecule.
See the description of this molecule in ChEBI.
=
a (2E)-enoyl-[ACP]
Search proteins in UniProtKB for this molecule.
Search chemical reactions in Rhea for this molecule.
+
H⁺
Search proteins in UniProtKB for this molecule.
Search chemical reactions in Rhea for this molecule.
See the description of this molecule in ChEBI.
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NADPH
Search proteins in UniProtKB for this molecule.
Search chemical reactions in Rhea for this molecule.
See the description of this molecule in ChEBI.
2 Publications
Manual assertion inferred by curator fromⁱ
- Ref.7
  "Characterization of 2-enoyl thioester reductase from mammals: an ortholog of Ybr026p/Mrf1'p of the yeast mitochondrial fatty acid synthesis type II."
  Miinalainen I.J., Chen Z.-J., Torkko J.M., Pirilae P.L., Sormunen R.T., Bergmann U., Qin Y.-M., Hiltunen J.K.
  J. Biol. Chem. 278:20154-20161(2003) [PubMed] [Europe PMC] [Abstract]
  Cited for: ENZYME ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
- Ref.13
  "Structural enzymological studies of 2-enoyl thioester reductase of the human mitochondrial FAS II pathway: new insights into its substrate recognition properties."
  Chen Z.J., Pudas R., Sharma S., Smart O.S., Juffer A.H., Hiltunen J.K., Wierenga R.K., Haapalainen A.M.
  J. Mol. Biol. 379:830-844(2008) [PubMed] [Europe PMC] [Abstract]
  Cited for: X-RAY CRYSTALLOGRAPHY (2.41 ANGSTROMS) OF 31-373, FUNCTION, CATALYTIC ACTIVITY, SUBUNIT, BIOPHYSICOCHEMICAL PROPERTIES, MUTAGENESIS OF SER-85; TYR-94; ILE-129; GLY-165; THR-170; TRP-311 AND PHE-324.
EC:
1.3.1.104
- Search proteins in UniProtKB for this EC number.
- See the description of this EC number in ENZYME.
2 Publications
Manual assertion inferred by curator fromⁱ
- Ref.7
  "Characterization of 2-enoyl thioester reductase from mammals: an ortholog of Ybr026p/Mrf1'p of the yeast mitochondrial fatty acid synthesis type II."
  Miinalainen I.J., Chen Z.-J., Torkko J.M., Pirilae P.L., Sormunen R.T., Bergmann U., Qin Y.-M., Hiltunen J.K.
  J. Biol. Chem. 278:20154-20161(2003) [PubMed] [Europe PMC] [Abstract]
  Cited for: ENZYME ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
- Ref.13
  "Structural enzymological studies of 2-enoyl thioester reductase of the human mitochondrial FAS II pathway: new insights into its substrate recognition properties."
  Chen Z.J., Pudas R., Sharma S., Smart O.S., Juffer A.H., Hiltunen J.K., Wierenga R.K., Haapalainen A.M.
  J. Mol. Biol. 379:830-844(2008) [PubMed] [Europe PMC] [Abstract]
  Cited for: X-RAY CRYSTALLOGRAPHY (2.41 ANGSTROMS) OF 31-373, FUNCTION, CATALYTIC ACTIVITY, SUBUNIT, BIOPHYSICOCHEMICAL PROPERTIES, MUTAGENESIS OF SER-85; TYR-94; ILE-129; GLY-165; THR-170; TRP-311 AND PHE-324.
Source:
Rhea
Search for this reaction in UniProtKB.
See the description of this reaction in Rhea.
. Show »« Hide
a 2,3-saturated acyl-[ACP]
O-(S-(2,3-saturated)-acylpantetheine-4ʼ-phosphoryl)-L-serine residue
zoom
+
NADP⁺
zoom
=
a (2E)-enoyl-[ACP]
O-(S-(2E)-enoylpantetheine-4ʼ-phosphoryl)-L-serine residue
zoom
+
H⁺
+
NADPH

Kineticsⁱ

Sites

Feature key	Position(s)	DescriptionActions	Length
Active siteⁱ	94	Proton donorBy similarity	1
Binding siteⁱ	167	NADPBy similarity	1
Binding siteⁱ	368	NADPBy similarity	1

Regions

Feature key	Position(s)	DescriptionActions	Length
Nucleotide bindingⁱ	193 – 196	NADPBy similarity	4
Nucleotide bindingⁱ	216 – 218	NADPBy similarity	3
Nucleotide bindingⁱ	285 – 288	NADPBy similarity	4
Nucleotide bindingⁱ	310 – 312	NADPBy similarity	3

GO - Molecular functionⁱ

trans-2-enoyl-CoA reductase (NADPH) activity
Source: UniProtKB
Inferred from direct assayⁱ
- Ref.7
  "Characterization of 2-enoyl thioester reductase from mammals: an ortholog of Ybr026p/Mrf1'p of the yeast mitochondrial fatty acid synthesis type II."
  Miinalainen I.J., Chen Z.-J., Torkko J.M., Pirilae P.L., Sormunen R.T., Bergmann U., Qin Y.-M., Hiltunen J.K.
  J. Biol. Chem. 278:20154-20161(2003) [PubMed] [Europe PMC] [Abstract]
  Cited for: ENZYME ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.

Complete GO annotation on QuickGO ...

GO - Biological processⁱ

Complete GO annotation on QuickGO ...

Keywordsⁱ

Molecular function	Oxidoreductase
Biological process	Fatty acid biosynthesis, Fatty acid metabolism, Lipid biosynthesis, Lipid metabolism
Ligand	NADP

Enzyme and pathway databases

Reactomeⁱ	R-HSA-77346 Beta oxidation of decanoyl-CoA to octanoyl-CoA-CoA
SABIO-RKⁱ	Q9BV79

Chemistry databases

SwissLipidsⁱ	SLP:000001054

SwissLipidsⁱ

SLP:000001054

Names & Taxonomyⁱ

Protein namesⁱ	Recommended name: Enoyl-[acyl-carrier-protein] reductase, mitochondrialCurated (EC:1.3.1.1042 Publications) Alternative name(s): 2-enoyl thioester reductase Nuclear receptor-binding factor 1 Short name: HsNrbf-1 Short name: NRBF-1
Gene namesⁱ	Name:MECR Synonyms:NBRF1 ORF Names:CGI-63
Organismⁱ	Homo sapiens (Human)
Taxonomic identifierⁱ	9606 [NCBI]
Taxonomic lineageⁱ	cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Dipnotetrapodomorpha › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Boreoeutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo
Proteomesⁱ	UP000005640 Componentⁱ: Chromosome 1

Organism-specific databases

Human Gene Nomenclature Database More...HGNCⁱ	HGNC:19691 MECR
MIMⁱ	608205 gene
neXtProtⁱ	NX_Q9BV79

Keywords - Cellular componentⁱ

Cytoplasm, Mitochondrion, Nucleus

Pathology & Biotechⁱ

Involvement in diseaseⁱ

Dystonia, childhood-onset, with optic atrophy and basal ganglia abnormalities (DYTOABG)1 Publication

The disease is caused by mutations affecting the gene represented in this entry.

Disease descriptionAn autosomal recessive neurologic disorder characterized by childhood-onset dystonia, basal ganglia degeneration and optic atrophy with decreased visual acuity. Dystonia is defined by the presence of sustained involuntary muscle contraction, often leading to abnormal postures. DYTOABG severity is variable, and some patients lose independent ambulation.

Related information in OMIM

Feature key	Position(s)	DescriptionActions	Length
Natural variantⁱVAR_077997	232	G → E in DYTOABG; probably decreased protein abundance. 1 PublicationCorresponds to variant dbSNP:rs762913101EnsemblClinVar.	1
Natural variantⁱVAR_077998	258	R → W in DYTOABG. 1 PublicationCorresponds to variant dbSNP:rs145192716EnsemblClinVar.	1
Natural variantⁱVAR_077999	285 – 373	Missing in DYTOABG; probably decreased protein abundance. 1 PublicationAdd BLAST	89
Natural variantⁱVAR_078000	285	Y → C in DYTOABG. 1 PublicationCorresponds to variant dbSNP:rs759218713EnsemblClinVar.	1

Mutagenesis

Feature key	Position(s)	DescriptionActions	Length
Mutagenesisⁱ	85	S → A: Reduces catalytic activity by 68%. 1 Publication	1
Mutagenesisⁱ	94	Y → F: Reduces catalytic activity by 95%. Strongly reduces affinity for trans-oct-2-enoyl-CoA. 1 Publication	1
Mutagenesisⁱ	129	I → M: Strongly increases activity with trans-oct-2-enoyl-CoA. No effect on activity with trans-tetradec-2-enoyl-CoA. Decreases activity with trans-hexadec-2-enoyl-CoA by 20%. 1 Publication	1
Mutagenesisⁱ	165	G → S: Strongly increases activity with trans-oct-2-enoyl-CoA. Decreases activity with trans-tetradec-2-enoyl-CoA by 73%. Decreases activity with trans-hexadec-2-enoyl-CoA by 80%. 1 Publication	1
Mutagenesisⁱ	170	T → A: Reduces catalytic activity by 69%. 1 Publication	1
Mutagenesisⁱ	311	W → A: Reduces catalytic activity by 98%. Strongly reduces affinity for trans-oct-2-enoyl-CoA. 1 Publication	1
Mutagenesisⁱ	311	W → L: Reduces catalytic activity by 87%. Strongly reduces affinity for trans-oct-2-enoyl-CoA. 1 Publication	1
Mutagenesisⁱ	324	F → Y: Strongly increases activity with trans-oct-2-enoyl-CoA. Decreases activity with trans-tetradec-2-enoyl-CoA by 25%. Decreases activity with trans-hexadec-2-enoyl-CoA by 68%. 1 Publication	1

Keywords - Diseaseⁱ

Disease mutation, Dystonia

Organism-specific databases

DisGeNET More...DisGeNETⁱ	51102
MalaCards human disease database More...MalaCardsⁱ	MECR
MIMⁱ	617282 phenotype
Open Targets More...OpenTargetsⁱ	ENSG00000116353
Orphanetⁱ	508093 MEPAN syndrome
PharmGKBⁱ	PA142671471

Polymorphism and mutation databases

BioMutaⁱ	MECR
DMDMⁱ	334302832

PTM / Processingⁱ

Molecule processing

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Transit peptideⁱ	1 – 53	MitochondrionSequence analysisAdd BLAST		53
ChainⁱPRO_0000000888	54 – 373	Enoyl-[acyl-carrier-protein] reductase, mitochondrialAdd BLAST		320

Amino acid modifications

Feature key	Position(s)	DescriptionActions	Length
Modified residueⁱ	61	N6-acetyllysine; alternateBy similarity	1
Modified residueⁱ	61	N6-succinyllysine; alternateBy similarity	1
Modified residueⁱ	252	N6-acetyllysine; alternateBy similarity	1
Modified residueⁱ	252	N6-succinyllysine; alternateBy similarity	1
Modified residueⁱ	267	N6-acetyllysine; alternateBy similarity	1
Modified residueⁱ	267	N6-succinyllysine; alternateBy similarity	1
Modified residueⁱ	316	N6-succinyllysineBy similarity	1

Keywords - PTMⁱ

Acetylation

Proteomic databases

EPDⁱ	Q9BV79
jPOSTⁱ	Q9BV79
MaxQB - The MaxQuant DataBase More...MaxQBⁱ	Q9BV79
PaxDbⁱ	Q9BV79
PeptideAtlas More...PeptideAtlasⁱ	Q9BV79
PRIDEⁱ	Q9BV79
ProteomicsDBⁱ	79177 79178 [Q9BV79-2]

PTM databases

iPTMnetⁱ	Q9BV79
PhosphoSitePlusⁱ	Q9BV79

Expressionⁱ

Tissue specificityⁱ

Highly expressed in skeletal and heart muscle. Expressed at lower level in placenta, liver, kidney and pancreas. Weakly or not expressed in lung.1 Publication

Gene expression databases

Bgeeⁱ	ENSG00000116353 Expressed in 198 organ(s), highest expression level in muscle of leg
ExpressionAtlasⁱ	Q9BV79 baseline and differential
Genevisibleⁱ	Q9BV79 HS

Organism-specific databases

Human Protein Atlas More...HPAⁱ	HPA022018 HPA022030 HPA028740

HPAⁱ

HPA022018
HPA022030
HPA028740

Interactionⁱ

Subunit structureⁱ

Homodimer (PubMed:12654921, PubMed:18479707). Isoform 2 interacts with PPARA in the nucleus and increases its activity (By similarity).

By similarity2 Publications

Protein-protein interaction databases

BioGridⁱ	119291, 17 interactors
IntActⁱ	Q9BV79, 2 interactors
STRINGⁱ	9606.ENSP00000263702

Structureⁱ

Secondary structure

Legend: HelixTurnBeta strandPDB Structure known for this area

Feature key	Position(s)	DescriptionActions	Length
Beta strandⁱ	43 – 52	Combined sources	10
Helixⁱ	54 – 57	Combined sources	4
Beta strandⁱ	58 – 63	Combined sources	6
Beta strandⁱ	72 – 81	Combined sources	10
Helixⁱ	84 – 91	Combined sources	8
Beta strandⁱ	100 – 103	Combined sources	4
Beta strandⁱ	109 – 115	Combined sources	7
Beta strandⁱ	127 – 133	Combined sources	7
Beta strandⁱ	138 – 145	Combined sources	8
Helixⁱ	146 – 148	Combined sources	3
Beta strandⁱ	149 – 152	Combined sources	4
Beta strandⁱ	154 – 156	Combined sources	3
Helixⁱ	158 – 163	Combined sources	6
Helixⁱ	167 – 177	Combined sources	11
Beta strandⁱ	186 – 191	Combined sources	6
Helixⁱ	195 – 207	Combined sources	13
Beta strandⁱ	210 – 215	Combined sources	6
Helixⁱ	221 – 230	Combined sources	10
Beta strandⁱ	234 – 238	Combined sources	5
Helixⁱ	239 – 243	Combined sources	5
Helixⁱ	245 – 249	Combined sources	5
Beta strandⁱ	252 – 254	Combined sources	3
Beta strandⁱ	258 – 264	Combined sources	7
Helixⁱ	266 – 273	Combined sources	8
Beta strandⁱ	281 – 284	Combined sources	4
Beta strandⁱ	293 – 295	Combined sources	3
Helixⁱ	297 – 302	Combined sources	6
Beta strandⁱ	306 – 309	Combined sources	4
Helixⁱ	312 – 318	Combined sources	7
Helixⁱ	321 – 336	Combined sources	16
Beta strandⁱ	345 – 349	Combined sources	5
Helixⁱ	350 – 352	Combined sources	3
Helixⁱ	353 – 360	Combined sources	8
Beta strandⁱ	362 – 364	Combined sources	3
Beta strandⁱ	366 – 372	Combined sources	7

Show more details

3D structure databases

SMRⁱ	Q9BV79
ModBaseⁱ	Search...

Miscellaneous databases

EvolutionaryTraceⁱ

Q9BV79

Family & Domainsⁱ

Sequence similaritiesⁱ

Belongs to the zinc-containing alcohol dehydrogenase family. Quinone oxidoreductase subfamily.Curated

Keywords - Domainⁱ

Transit peptide

Phylogenomic databases

eggNOGⁱ	KOG0025 Eukaryota COG0604 LUCA
Ensembl GeneTree More...GeneTreeⁱ	ENSGT00940000156592
InParanoidⁱ	Q9BV79
KEGG Orthology (KO) More...KOⁱ	K07512
OMAⁱ	AFRGFWM
Database of Orthologous Groups More...OrthoDBⁱ	1269870at2759
PhylomeDBⁱ	Q9BV79
TreeFamⁱ	TF312886

Family and domain databases

InterProⁱ	View protein in InterPro IPR013149 ADH_C IPR013154 ADH_N IPR011032 GroES-like_sf IPR036291 NAD(P)-bd_dom_sf IPR020843 PKS_ER
Pfam protein domain database More...Pfamⁱ	View protein in Pfam PF08240 ADH_N, 1 hit PF00107 ADH_zinc_N, 1 hit
SMARTⁱ	View protein in SMART SM00829 PKS_ER, 1 hit
SUPFAMⁱ	SSF50129 SSF50129, 1 hit SSF51735 SSF51735, 1 hit

Sequences (2+)ⁱ

Sequence statusⁱ: Complete.

Sequence processingⁱ: The displayed sequence is further processed into a mature form.

This entry describes 2 isoformsⁱ produced by alternative splicing. Align Add to basket

This entry has 2 described isoforms and 1 potential isoform that is computationally mapped.Show all Align All

Isoform 1 (identifier: Q9BV79-1) [UniParc]FASTA Add to basket

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

« Hide

        10         20         30         40         50
MWVCSTLWRV RTPARQWRGL LPASGCHGPA ASSYSASAEP ARVRALVYGH 
        60         70         80         90        100
HGDPAKVVEL KNLELAAVRG SDVRVKMLAA PINPSDINMI QGNYGFLPEL 
       110        120        130        140        150
PAVGGNEGVA QVVAVGSNVT GLKPGDWVIP ANAGLGTWRT EAVFSEEALI 
       160        170        180        190        200
QVPSDIPLQS AATLGVNPCT AYRMLMDFEQ LQPGDSVIQN ASNSGVGQAV 
       210        220        230        240        250
IQIAAALGLR TINVVRDRPD IQKLSDRLKS LGAEHVITEE ELRRPEMKNF 
       260        270        280        290        300
FKDMPQPRLA LNCVGGKSST ELLRQLARGG TMVTYGGMAK QPVVASVSLL 
       310        320        330        340        350
IFKDLKLRGF WLSQWKKDHS PDQFKELILT LCDLIRRGQL TAPACSQVPL 
       360        370 
QDYQSALEAS MKPFISSKQI LTM

Length:373

Mass (Da):40,462

Last modified:May 31, 2011 - v2

Checksum:ⁱDB13F6B0ED54A823

GO

Isoform 2 (identifier: Q9BV79-2) [UniParc]FASTA Add to basket

Also known as: cMECR

The sequence of this isoform differs from the canonical sequence as follows:
1-76: Missing.

« Hide

        10         20         30         40         50
MLAAPINPSD INMIQGNYGF LPELPAVGGN EGVAQVVAVG SNVTGLKPGD 
        60         70         80         90        100
WVIPANAGLG TWRTEAVFSE EALIQVPSDI PLQSAATLGV NPCTAYRMLM 
       110        120        130        140        150
DFEQLQPGDS VIQNASNSGV GQAVIQIAAA LGLRTINVVR DRPDIQKLSD 
       160        170        180        190        200
RLKSLGAEHV ITEEELRRPE MKNFFKDMPQ PRLALNCVGG KSSTELLRQL 
       210        220        230        240        250
ARGGTMVTYG GMAKQPVVAS VSLLIFKDLK LRGFWLSQWK KDHSPDQFKE 
       260        270        280        290 
LILTLCDLIR RGQLTAPACS QVPLQDYQSA LEASMKPFIS SKQILTM

Show »

Length:297

Mass (Da):32,228

Checksum:ⁱ1A27621E27728B76

GO

Computationally mapped potential isoform sequencesⁱ

There is 1 potential isoform mapped to this entry.BLAST Align Show all Add to basket

	Entry	Entry name		Protein names	Gene names	Length	Annotation

	H3BM30	H3BM30_HUMAN		Enoyl-[acyl-carrier-protein] reduct... Enoyl-[acyl-carrier-protein] reductase, mitochondrial	MECR	212	Annotation score:

Sequence cautionⁱ

The sequence AAD34058 differs from that shown. Reason: Frameshift at positions 14 and 19.Curated

Experimental Info

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Sequence conflictⁱ	45 – 46	AL → GV in AAD34058 (PubMed:10810093).Curated		2
Sequence conflictⁱ	373	M → I in CAG32984 (PubMed:14702039).Curated		1

Natural variant

Feature key	Position(s)	DescriptionActions	Length
Natural variantⁱVAR_027935	96	F → L5 PublicationsCorresponds to variant dbSNP:rs1128400Ensembl.	1
Natural variantⁱVAR_055486	227	R → K. Corresponds to variant dbSNP:rs11544658Ensembl.	1
Natural variantⁱVAR_077997	232	G → E in DYTOABG; probably decreased protein abundance. 1 PublicationCorresponds to variant dbSNP:rs762913101EnsemblClinVar.	1
Natural variantⁱVAR_055487	258	R → L. Corresponds to variant dbSNP:rs34835902Ensembl.	1
Natural variantⁱVAR_077998	258	R → W in DYTOABG. 1 PublicationCorresponds to variant dbSNP:rs145192716EnsemblClinVar.	1
Natural variantⁱVAR_077999	285 – 373	Missing in DYTOABG; probably decreased protein abundance. 1 PublicationAdd BLAST	89
Natural variantⁱVAR_078000	285	Y → C in DYTOABG. 1 PublicationCorresponds to variant dbSNP:rs759218713EnsemblClinVar.	1

Alternative sequence

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Alternative sequenceⁱVSP_041131	1 – 76	Missing in isoform 2. 1 PublicationAdd BLAST		76

Sequence databases

Select the link destinations: EMBLⁱ GenBankⁱ DDBJⁱ Links Updated	AF151821 mRNA Translation: AAD34058.1 Frameshift. AK095099 mRNA Translation: BAG52984.1 CR456703 mRNA Translation: CAG32984.1 AL590729 Genomic DNA No translation available. CH471059 Genomic DNA Translation: EAX07655.1 BC001419 mRNA Translation: AAH01419.1
The Consensus CDS (CCDS) project More...CCDSⁱ	CCDS30659.1 [Q9BV79-1] CCDS30660.1 [Q9BV79-2]
NCBI Reference Sequences More...RefSeqⁱ	NP_001019903.2, NM_001024732.2 [Q9BV79-2] NP_057095.3, NM_016011.3 [Q9BV79-1] XP_005245944.1, XM_005245887.2 XP_016856902.1, XM_017001413.1 [Q9BV79-2] XP_016856903.1, XM_017001414.1 XP_016856904.1, XM_017001415.1

Genome annotation databases

Ensemblⁱ	ENST00000263702; ENSP00000263702; ENSG00000116353 [Q9BV79-1] ENST00000373791; ENSP00000362896; ENSG00000116353 [Q9BV79-2]
GeneIDⁱ	51102
KEGGⁱ	hsa:51102
UCSC genome browser More...UCSCⁱ	uc001brp.3 human [Q9BV79-1]

Keywords - Coding sequence diversityⁱ

Alternative splicing, Polymorphism

Similar proteinsⁱ

90% Identity
50% Identity

Protein	Similar proteins		Species	Score	Length	Source
Q9BV79	Mitochondrial trans-2-enoyl-CoA reductase		OTOGA		376	UniRef90_Q9BV79
MECR isoform 3		PANTR		373
Trans-2-enoyl-CoA reductase, mitochondrial isoform a		CALJA		373
Uncharacterized protein		AOTNA		373
Uncharacterized protein		RHIBE		373
+37
Q9BV79-2	Uncharacterized protein		CERAT		297	UniRef90_Q9BV79-2
Uncharacterized protein		MANLE		297
Uncharacterized protein		NOMLE		297
MECR isoform 4		PANTR		297
MECR isoform 5		PONAB		297
+19

Protein	Similar proteins		Species	Score	Length	Source
Q9BV79	Enoyl-[acyl-carrier-protein] reductase, mitochondrial		BOVIN		373	UniRef50_Q9BV79
Enoyl-[acyl-carrier-protein] reductase, mitochondrial		XENTR		350
Enoyl-[acyl-carrier-protein] reductase, mitochondrial		DANRE		377
Enoyl-[acyl-carrier-protein] reductase, mitochondrial		RAT		373
Enoyl-[acyl-carrier-protein] reductase, mitochondrial		MOUSE		373
+471
Q9BV79-2	MECR isoform 5		PONAB		297	UniRef50_Q9BV79-2
Uncharacterized protein		NOMLE		297
MECR isoform 4		PANTR		297
Uncharacterized protein		CERAT		297
Uncharacterized protein		MANLE		297
+76

Cross-referencesⁱ

Sequence databases

Select the link destinations: EMBLⁱ GenBankⁱ DDBJⁱ Links Updated	AF151821 mRNA Translation: AAD34058.1 Frameshift. AK095099 mRNA Translation: BAG52984.1 CR456703 mRNA Translation: CAG32984.1 AL590729 Genomic DNA No translation available. CH471059 Genomic DNA Translation: EAX07655.1 BC001419 mRNA Translation: AAH01419.1
CCDSⁱ	CCDS30659.1 [Q9BV79-1] CCDS30660.1 [Q9BV79-2]
RefSeqⁱ	NP_001019903.2, NM_001024732.2 [Q9BV79-2] NP_057095.3, NM_016011.3 [Q9BV79-1] XP_005245944.1, XM_005245887.2 XP_016856902.1, XM_017001413.1 [Q9BV79-2] XP_016856903.1, XM_017001414.1 XP_016856904.1, XM_017001415.1

3D structure databases

Select the link destinations: Protein Data Bank Europe More...PDBeⁱ Protein Data Bank RCSB More...RCSB PDBⁱ Protein Data Bank Japan More...PDBjⁱ Links Updated	PDB entry	Method	Resolution (Å)	Chain	Positions	PDBsum
	1ZSY	X-ray	1.75	A	40-373	[»]
	2VCY	X-ray	2.41	A/B	31-373	[»]
SMRⁱ	Q9BV79
ModBaseⁱ	Search...

Protein-protein interaction databases

BioGridⁱ	119291, 17 interactors
IntActⁱ	Q9BV79, 2 interactors
STRINGⁱ	9606.ENSP00000263702

Chemistry databases

SwissLipidsⁱ	SLP:000001054

SwissLipidsⁱ

SLP:000001054

PTM databases

iPTMnetⁱ	Q9BV79
PhosphoSitePlusⁱ	Q9BV79

Polymorphism and mutation databases

BioMutaⁱ	MECR
DMDMⁱ	334302832

Proteomic databases

EPDⁱ	Q9BV79
jPOSTⁱ	Q9BV79
MaxQBⁱ	Q9BV79
PaxDbⁱ	Q9BV79
PeptideAtlasⁱ	Q9BV79
PRIDEⁱ	Q9BV79
ProteomicsDBⁱ	79177 79178 [Q9BV79-2]

Protocols and materials databases

The DNASU plasmid repository More...DNASUⁱ	51102
Structural Biology Knowledgebase	Search...

Genome annotation databases

Ensemblⁱ	ENST00000263702; ENSP00000263702; ENSG00000116353 [Q9BV79-1] ENST00000373791; ENSP00000362896; ENSG00000116353 [Q9BV79-2]
GeneIDⁱ	51102
KEGGⁱ	hsa:51102
UCSCⁱ	uc001brp.3 human [Q9BV79-1]

Organism-specific databases

CTDⁱ	51102
DisGeNETⁱ	51102
GeneCardsⁱ	MECR
HGNCⁱ	HGNC:19691 MECR
HPAⁱ	HPA022018 HPA022030 HPA028740
MalaCardsⁱ	MECR
MIMⁱ	608205 gene 617282 phenotype
neXtProtⁱ	NX_Q9BV79
OpenTargetsⁱ	ENSG00000116353
Orphanetⁱ	508093 MEPAN syndrome
PharmGKBⁱ	PA142671471
GenAtlas: human gene database More...GenAtlasⁱ	Search...

Phylogenomic databases

eggNOGⁱ	KOG0025 Eukaryota COG0604 LUCA
GeneTreeⁱ	ENSGT00940000156592
InParanoidⁱ	Q9BV79
KOⁱ	K07512
OMAⁱ	AFRGFWM
OrthoDBⁱ	1269870at2759
PhylomeDBⁱ	Q9BV79
TreeFamⁱ	TF312886

Enzyme and pathway databases

Reactomeⁱ	R-HSA-77346 Beta oxidation of decanoyl-CoA to octanoyl-CoA-CoA
SABIO-RKⁱ	Q9BV79

Miscellaneous databases

EvolutionaryTraceⁱ	Q9BV79
GeneWikiⁱ	MECR
GenomeRNAiⁱ	51102
Protein Ontology More...PROⁱ	PR:Q9BV79
SOURCEⁱ	Search...

Gene expression databases

Bgeeⁱ	ENSG00000116353 Expressed in 198 organ(s), highest expression level in muscle of leg
ExpressionAtlasⁱ	Q9BV79 baseline and differential
Genevisibleⁱ	Q9BV79 HS

Family and domain databases

InterProⁱ	View protein in InterPro IPR013149 ADH_C IPR013154 ADH_N IPR011032 GroES-like_sf IPR036291 NAD(P)-bd_dom_sf IPR020843 PKS_ER
Pfamⁱ	View protein in Pfam PF08240 ADH_N, 1 hit PF00107 ADH_zinc_N, 1 hit
SMARTⁱ	View protein in SMART SM00829 PKS_ER, 1 hit
SUPFAMⁱ	SSF50129 SSF50129, 1 hit SSF51735 SSF51735, 1 hit
ProtoNetⁱ	Search...
MobiDBⁱ	Search...

Entry informationⁱ

Entry nameⁱ	MECR_HUMAN
Accessionⁱ	Q9BV79Primary (citable) accession number: Q9BV79 Secondary accession number(s): B3KT72 , Q5SYU0, Q5SYU1, Q5SYU2, Q6IBU9, Q9Y373
Entry historyⁱ	Integrated into UniProtKB/Swiss-Prot:	April 26, 2005
	Last sequence update:	May 31, 2011
	Last modified:	May 8, 2019
	This is version 155 of the entry and version 2 of the sequence. See complete history.
Entry statusⁱ	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.

Miscellaneousⁱ

Keywords - Technical termⁱ

3D-structure, Complete proteome, Reference proteome

Documents

PDB cross-references
Index of Protein Data Bank (PDB) cross-references
SIMILARITY comments
Index of protein domains and families
Human polymorphisms and disease mutations
Index of human polymorphisms and disease mutations
MIM cross-references
Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
Human chromosome 1
Human chromosome 1: entries, gene names and cross-references to MIM
Human entries with polymorphisms or disease mutations
List of human entries with polymorphisms or disease mutations

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UniProtKB - Q9BV79 (MECR_HUMAN)

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Enoyl-[acyl-carrier-protein] reductase, mitochondrial

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<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

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<p>This subsection of the ‘Sequence’ section reports difference(s) between the protein sequence shown in the UniProtKB entry and other available protein sequences derived from the same gene.<p><a href='/help/sequence_caution' target='_top'>More...</a></p>Sequence cautioni

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Functionⁱ

Catalytic activityⁱ

Kineticsⁱ

GO - Molecular functionⁱ

GO - Biological processⁱ

Names & Taxonomyⁱ

Subcellular locationⁱ

Keywords - Cellular componentⁱ

Pathology & Biotechⁱ

Keywords - Diseaseⁱ

PTM / Processingⁱ

Keywords - PTMⁱ

Expressionⁱ

Interactionⁱ

Structureⁱ

Family & Domainsⁱ

Sequence similaritiesⁱ

Keywords - Domainⁱ

Sequence cautionⁱ

Keywords - Coding sequence diversityⁱ

Cross-referencesⁱ

Entry informationⁱ

Miscellaneousⁱ

Keywords - Technical termⁱ