Q9BV79 (MECR_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Trans-2-enoyl-CoA reductase, mitochondrial
EC=1.3.1.38

Alternative name(s):
Nuclear receptor-binding factor 1
Short name=HsNrbf-1
Short name=NRBF-1

Gene names

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

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › 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.7
Subunit structure	Homodimer. Ref.7
Subcellular location	Mitochondrion Ref.7.
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.7
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 Ref.7 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.

Ontologies

Keywords
Biological process	Fatty acid biosynthesis Fatty acid metabolism Lipid biosynthesis Lipid metabolism
Cellular component	Mitochondrion
Coding sequence diversity	Alternative splicing Polymorphism
Domain	Transit peptide
Ligand	NADP
Molecular function	Oxidoreductase
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	fatty acid biosynthetic process Inferred from electronic annotation. Source: UniProtKB-KW fatty acid metabolic process Inferred from direct assay Ref.7. Source: UniProtKB
Cellular_component	mitochondrion Inferred from direct assay Ref.7. Source: UniProtKB
Molecular_function	trans-2-enoyl-CoA reductase (NADPH) activity Inferred from direct assay Ref.7. Source: UniProtKB zinc ion binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Alternative products

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

Isoform 1 (identifier: Q9BV79-1)

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: Q9BV79-2)

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

Note: No experimental confirmation available.

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

Alternative sequence

1 – 76

76

Missing in isoform 2.

VSP_041131

Natural variant

96

1

F → L. Ref.1 Ref.2 Ref.3 Ref.5 Ref.6
Corresponds to variant rs1128400 [ dbSNP | Ensembl ].

VAR_027935

Natural variant

227

1

R → K.
Corresponds to variant rs11544658 [ dbSNP | Ensembl ].

VAR_055486

Natural variant

258

1

R → L.
Corresponds to variant rs34835902 [ dbSNP | Ensembl ].

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

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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)
	Isoform 1 [UniParc]. Last modified May 31, 2011. Version 2. Checksum: DB13F6B0ED54A823	FASTA	373	40,462
	10 20 30 40 50 60 MWVCSTLWRV RTPARQWRGL LPASGCHGPA ASSYSASAEP ARVRALVYGH HGDPAKVVEL 70 80 90 100 110 120 KNLELAAVRG SDVRVKMLAA PINPSDINMI QGNYGFLPEL 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
	Isoform 2 [UniParc]. Checksum: 1A27621E27728B76	FASTA	297	32,228
	10 20 30 40 50 60 MLAAPINPSD INMIQGNYGF LPELPAVGGN EGVAQVVAVG SNVTGLKPGD WVIPANAGLG 70 80 90 100 110 120 TWRTEAVFSE EALIQVPSDI PLQSAATLGV NPCTAYRMLM DFEQLQPGDS VIQNASNSGV 130 140 150 160 170 180 GQAVIQIAAA LGLRTINVVR DRPDIQKLSD RLKSLGAEHV ITEEELRRPE MKNFFKDMPQ 190 200 210 220 230 240 PRLALNCVGG KSSTELLRQL ARGGTMVTYG GMAKQPVVAS VSLLIFKDLK LRGFWLSQWK 250 260 270 280 290 KDHSPDQFKE LILTLCDLIR RGQLTAPACS QVPLQDYQSA LEASMKPFIS SKQILTM

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] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), VARIANT LEU-96.
[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] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), VARIANT LEU-96. Tissue: Hippocampus.
[3]	"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] (ISOFORM 1), VARIANT LEU-96.
[4]	"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] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]	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], VARIANT LEU-96.
[6]	"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] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), VARIANT LEU-96. Tissue: Placenta.
[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.
[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] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[9]	"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

EMBL
GenBank
DDBJ

AF151821 mRNA. Translation: AAD34058.1. Frameshift.
AK095099 mRNA. Translation: BAG52984.1.
CR456703 mRNA. Translation: CAG32984.1.
AL590729 Genomic DNA. Translation: CAI14329.1.
AL590729 Genomic DNA. Translation: CAI14330.1.
CH471059 Genomic DNA. Translation: EAX07655.1.
BC001419 mRNA. Translation: AAH01419.1.

IPI

IPI00306159.
IPI00607794.

RefSeq

NP_001019903.1. NM_001024732.1.
NP_057095.2. NM_016011.2.

UniGene

Hs.183646.

3D structure databases

PDBe
RCSB PDB
PDBj

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

ProteinModelPortal

Q9BV79.

SMR

Q9BV79. Positions 40-373.

ModBase

Search...

Protein-protein interaction databases

STRING

9606.ENSP00000263702.

PTM databases

PhosphoSite

Q9BV79.

Polymorphism databases

DMDM

62900596.

Proteomic databases

PaxDb

Q9BV79.

PRIDE

Q9BV79.

Protocols and materials databases

DNASU

51102.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000263702; ENSP00000263702; ENSG00000116353.
ENST00000373791; ENSP00000362896; ENSG00000116353.

GeneID

51102.

KEGG

hsa:51102.

UCSC

uc001brp.1. human.

Organism-specific databases

CTD

51102.

GeneCards

GC01M029519.

HGNC

HGNC:19691. MECR.

HPA

HPA022018.
HPA022030.
HPA028740.

MIM

608205. gene.

neXtProt

NX_Q9BV79.

PharmGKB

PA142671471.

GenAtlas

Search...

Phylogenomic databases

eggNOG

COG0604.

HOVERGEN

HBG052446.

InParanoid

Q9BV79.

KO

K07512.

OMA

CSTLWRV.

OrthoDB

EOG43N7DB.

PhylomeDB

Q9BV79.

Enzyme and pathway databases

SABIO-RK

Q9BV79.

Gene expression databases

ArrayExpress

Q9BV79.

Bgee

Q9BV79.

CleanEx

HS_MECR.

Genevestigator

Q9BV79.

GermOnline

ENSG00000116353. Homo sapiens.

Family and domain databases

Gene3D

3.40.50.720. 1 hit.
3.90.180.10. 1 hit.

InterPro

IPR013149. ADH_C.
IPR013154. ADH_GroES-like.
IPR002085. ADH_SF_Zn-type.
IPR011032. GroES-like.
IPR016040. NAD(P)-bd_dom.
[Graphical view]

PANTHER

PTHR11695. PTHR11695. 1 hit.

Pfam

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

SUPFAM

SSF50129. GroES_like. 1 hit.

ProtoNet

Search...

Other

EvolutionaryTrace

Q9BV79.

GenomeRNAi

51102.

NextBio

53817.

SOURCE

Search...

Entry information

Entry name

MECR_HUMAN

Accession

Primary (citable) accession number: Q9BV79
Secondary accession number(s): B3KT72 , Q5SYU0, Q5SYU1, Q5SYU2, Q6IBU9, Q9Y373

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 26, 2005
Last sequence update:	May 31, 2011
Last modified:	May 29, 2013
This is version 108 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.