Reviewed, UniProtKB/Swiss-Prot Q9BV79 (MECR_HUMAN)

Names and origin

Protein names

Recommended name:
    Trans-2-enoyl-CoA reductase, mitochondrial
      Short name=HsNrbf-1
    EC=1.3.1.38
Alternative name(s):
    NRBF-1

Gene names

Name:	MECR
Synonyms:	NBRF1
ORF Names:	CGI-63

Organism

Homo sapiens (Human) [Complete proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

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

Protein attributes

Sequence length	373 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	Catalyzes the reduction of trans-2-enoyl-CoA to acyl-CoA with chain length from C6 to C16 in an NADPH-dependent manner with preference to medium chain length substrate. May have a role in the mitochondrial synthesis of fatty acids.
Catalytic activity	Acyl-CoA + NADP+ = trans-2,3-dehydroacyl-CoA + NADPH. Ref.5
Subunit structure	Homodimer. Ref.5
Subcellular location	Mitochondrion. Ref.5
Tissue specificity	Highly expressed in skeletal and heart muscle. Expressed at lower level in placenta, liver, kidney and pancreas. Weakly or not expressed in lung. Ref.5
Sequence similarities	Belongs to the zinc-containing alcohol dehydrogenase family. Quinone oxidoreductase subfamily.
Biophysicochemical properties	Kinetic parameters: KM=37 µM for trans-2-hexenoyl-CoA KM=7.1 µM for trans-2-decenoyl-CoA
Sequence caution	The sequence AAD34058.1 differs from that shown. Reason: Frameshift at positions 14 and 19. The sequence CAI14329.1 differs from that shown. Reason: Erroneous gene model prediction.

Ontologies

Keywords
Biological process	Fatty acid biosynthesis Lipid synthesis
Cellular component	Mitochondrion
Coding sequence diversity	Polymorphism
Domain	Transit peptide
Ligand	NADP
Molecular function	Oxidoreductase
Technical term	3D-structure Complete proteome
Gene Ontology (GO)
Biological process	fatty acid biosynthetic process Inferred from electronic annotation. Source: UniProtKB-KW oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	mitochondrion Ref.5 Inferred from direct assay. Source: UniProtKB
Molecular function	trans-2-enoyl-CoA reductase (NADPH) activity Ref.5 Inferred from direct assay. Source: UniProtKB zinc ion binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Transit peptide

1 – 53

53

Mitochondrion Potential

Chain

54 – 373

320

Trans-2-enoyl-CoA reductase, mitochondrial

PRO_0000000888

Natural variations

Natural variant

96

1

L → F: dbSNP rs1128400. Ref.3

VAR_027935

Natural variant

227

1

R → K: dbSNP rs11544658.

VAR_055486

Natural variant

258

1

R → L: dbSNP rs34835902.

VAR_055487

Experimental info

Sequence conflict

45 – 46

2

AL → GV in AAD34058. Ref.1

Sequence conflict

373

1

M → I in CAG32984. Ref.2

Secondary structure

1

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373

Helix Strand Turn

Details...

Beta strand

43 – 52

10

Helix

54 – 57

4

Beta strand

58 – 63

6

Beta strand

72 – 81

10

Helix

84 – 91

8

Beta strand

100 – 103

4

Beta strand

109 – 115

7

Beta strand

127 – 133

7

Beta strand

138 – 145

8

Helix

146 – 148

3

Beta strand

149 – 152

4

Beta strand

154 – 156

3

Helix

158 – 163

6

Helix

167 – 177

11

Beta strand

186 – 191

6

Helix

195 – 207

13

Beta strand

210 – 215

6

Helix

221 – 230

10

Beta strand

234 – 238

5

Helix

239 – 243

5

Helix

245 – 249

5

Beta strand

252 – 254

3

Beta strand

258 – 264

7

Helix

266 – 273

8

Beta strand

281 – 284

4

Beta strand

293 – 295

3

Helix

297 – 302

6

Beta strand

306 – 309

4

Helix

312 – 318

7

Helix

321 – 336

16

Beta strand

345 – 349

5

Helix

350 – 352

3

Helix

353 – 360

8

Beta strand

362 – 364

3

Beta strand

366 – 372

7

Sequences

	Sequence		Length	Mass (Da)
	Q9BV79-1 [UniParc]. Last modified June 1, 2001. Version 1. Checksum: 591758FA0D57CBA3	FASTA	373	40,428
	10 20 30 40 50 60 MWVCSTLWRV RTPARQWRGL LPASGCHGPA ASSYSASAEP ARVRALVYGH HGDPAKVVEL 70 80 90 100 110 120 KNLELAAVRG SDVRVKMLAA PINPSDINMI QGNYGLLPEL PAVGGNEGVA QVVAVGSNVT 130 140 150 160 170 180 GLKPGDWVIP ANAGLGTWRT EAVFSEEALI QVPSDIPLQS AATLGVNPCT AYRMLMDFEQ 190 200 210 220 230 240 LQPGDSVIQN ASNSGVGQAV IQIAAALGLR TINVVRDRPD IQKLSDRLKS LGAEHVITEE 250 260 270 280 290 300 ELRRPEMKNF FKDMPQPRLA LNCVGGKSST ELLRQLARGG TMVTYGGMAK QPVVASVSLL 310 320 330 340 350 360 IFKDLKLRGF WLSQWKKDHS PDQFKELILT LCDLIRRGQL TAPACSQVPL QDYQSALEAS 370 MKPFISSKQI LTM

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Identification of novel human genes evolutionarily conserved in Caenorhabditis elegans by comparative proteomics." Lai C.-H., Chou C.-Y., Ch'ang L.-Y., Liu C.-S., Lin W.-C. Genome Res. 10:703-713(2000) [PubMed: 10810093] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[2]	"Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)." Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B. Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[3]	"The DNA sequence and biological annotation of human chromosome 1." Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K. , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R. Nature 441:315-321(2006) [PubMed: 16710414] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], VARIANT PHE-96.
[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]. Tissue: Placenta.
[5]	"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: 12654921] [Abstract] Cited for: ENZYME ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
[6]	Colinge J., Superti-Furga G., Bennett K.L. Submitted (OCT-2008) to UniProtKB Cited for: IDENTIFICATION [LARGE SCALE ANALYSIS], MASS SPECTROMETRY.
[7]	"The structure of human mitochondrial 2-enoyl thioester reductase (CGI-63)." Structural genomics consortium (SGC) Submitted (JUN-2005) to the PDB data bank Cited for: X-RAY CRYSTALLOGRAPHY (1.75 ANGSTROMS) OF 40-373.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBLGenBankDDBJ

AF151821 mRNA. Translation: AAD34058.1. Frameshift.
CR456703 mRNA. Translation: CAG32984.1.
AL590729 Genomic DNA. Translation: CAI14329.1. Sequence problems.
AL590729 Genomic DNA. Translation: CAI14330.1.
BC001419 mRNA. Translation: AAH01419.1.

IPI

IPI00306159.

UniGene

Hs.183646

3D structure databases

PDBPDBe

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1ZSY	X-ray	1.75	A	40-373	[»]
2VCY	X-ray	2.41	A/B	31-373	[»]

ModBase

Search...

Proteomic databases

PRIDE

Q9BV79.

Genome annotation databases

Ensembl

ENSG00000116353. Homo sapiens. [Contig view]

UCSC

uc001brq.1. human.

Organism-specific databases

GeneCards

GC01M029391.

H-InvDB

HIX0000345.

HGNC

HGNC:19691. MECR.

MIM

608205. gene.

PharmGKB

PA142671471.

GenAtlas

Search...

Phylogenomic databases

HOGENOM

Q9BV79.

HOVERGEN

Q9BV79.

Enzyme and pathway databases

BRENDA

1.3.1.38. 247.

Gene expression databases

ArrayExpress

Q9BV79.

Bgee

Q9BV79.

CleanEx

HS_MECR.

GermOnline

ENSG00000116353. Homo sapiens.

Family and domain databases

InterPro

IPR013154. ADH_GroES-like.
IPR002085. ADH_SF_Zn.
IPR013149. ADH_Zn-bd.
IPR016040. NAD(P)-bd_dom.
[Graphical view]

Gene3D

G3DSA:3.40.50.720. NAD(P)-bd. 1 hit.

PANTHER

PTHR11695. ADH_Sf_Zn. 1 hit.

Pfam

PF08240. ADH_N. 1 hit.
PF00107. ADH_zinc_N. 1 hit.
[Graphical view]

ProtoNet

Search...

Other Resources

SOURCE

Search...

Entry information

Entry name

MECR_HUMAN

Accession

Primary (citable) accession number: Q9BV79
Secondary accession number(s): Q5SYU0 , Q5SYU1, Q5SYU2, Q6IBU9, Q9Y373

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 26, 2005
Last sequence update:	June 1, 2001
Last modified:	July 7, 2009
This is version 73 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)