NUCLEOTIDE SEQUENCE [MRNA].
DOI=10.1016/S0378-1119(98)00461-2; PubMed=9795230 [NCBI, ExPASy, EBI, Israel, Japan]
Masuda N., Yasumo H., Furusawa T., Tsukamoto T., Sadano H., Osumi T.;
"Nuclear receptor binding factor-1 (NRBF-1), a protein interacting with a wide spectrum of nuclear hormone receptors.";
Gene 221:225-233(1998).

[2]

SUBCELLULAR LOCATION.
DOI=10.1074/jbc.M302851200; PubMed=12654921 [NCBI, ExPASy, EBI, Israel, Japan]
Miinalainen I.J., Chen Z.-J., Torkko J.M., Pirilae P.L., Sormunen R.T., Bergmann U., Qin Y.-M., Hiltunen J.K.;
"Characterization of 2-enoyl thioester reductase from mammals: an ortholog of Ybr026p/Mrf1'p of the yeast mitochondrial fatty acid synthesis type II.";
J. Biol. Chem. 278:20154-20161(2003).

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 (By similarity).
CATALYTIC ACTIVITY: Acyl-CoA + NADP⁺ = trans-2,3-dehydroacyl-CoA + NADPH.
SUBUNIT: Homodimer (By similarity).
SUBCELLULAR LOCATION: Mitochondrion.
SIMILARITY: Belongs to the zinc-containing alcohol dehydrogenase family. Quinone oxidoreductase subfamily.
CAUTION: Was originally (PubMed:9795230) thought to be a nuclear protein that interact with nuclear receptor. However, it was shown later to be mitochondrial (PubMed:12654921), a function related to nuclear receptors being unsure.

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

AB015724; BAA34804.1; -; mRNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

RefSeq

NP_058905.1; -.

UniGene

Rn.15375

3D structure databases

HSSP

Q8WZM3; 1GU7. [HSSP ENTRY / PDB]

SMR

Q9Z311; 38-373.

ModBase

Q9Z311.

Organism-specific databases

RGD

3208; Mecr.

Gene expression databases

ArrayExpress

Q9Z311; -.

GermOnline

ENSRNOG00000028047; Rattus norvegicus.

Ontologies

GO:0005739;	Cellular component: mitochondrion (inferred from direct assay from UniProtKB).
GO:0019166;	Molecular function: trans-2-enoyl-CoA reductase (NADPH) activity (inferred from sequence or structural similarity from UniProtKB).
GO:0006631;	Biological process: fatty acid metabolic process (inferred from sequence or structural similarity from UniProtKB).
QuickGo view.

Family and domain databases

InterPro

IPR013154; AlcDHase_GroES-like.
IPR002085; AlcDHase_SF_Zn.
IPR013149; AlcDHase_Zn-bd.
IPR016040; NAD(P)-bd.
Graphical view of domain structure.

Gene3D

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

PANTHER

PTHR11695; ADH_Sf_Zn; 1.

Pfam

PF08240; ADH_N; 1.
PF00107; ADH_zinc_N; 1.
Pfam graphical view of domain structure.

BLOCKS

Q9Z311.

Genome annotation databases

Ensembl

ENSRNOG00000028047; Rattus norvegicus. [Contig view]

GeneID

29470; -.

KEGG

rno:29470; -.

Phylogenomic databases

HOVERGEN

Q9Z311; -.

Other

ProtoNet

Q9Z311.

UniRef

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

Fatty acid biosynthesis; Lipid synthesis; Mitochondrion; NADP; Oxidoreductase; Transit peptide.

Features

Feature table viewer

`Key`	`From To`	`Length`	`Description`	`FTId`
`TRANSIT`	`1 53`	`53`	`Mitochondrion (Potential).`
`CHAIN`	`54 373`	`320`	`Trans-2-enoyl-CoA reductase, mitochondrial.`	`PRO_0000000890`

Sequence information

Length: 373 AA [This is the length of the unprocessed precursor]

Molecular weight: 40327 Da [This is the MW of the unprocessed precursor]

CRC64: 94D5A057D666320D [This is a checksum on the sequence]

        10         20         30         40         50         60 
MLVSRRLTGA RARAPLLASL LEAWCRQGRT TSSYSAFSEP SHVRALVYGN HGDPAKVIQL 

        70         80         90        100        110        120 
KNLELTAVEG SDVHVKMLAA PINPSDINMI QGNYGLLPKL PAVGGNEGVG QVIAVGSSVS 

       130        140        150        160        170        180 
GLKPGDWVIP ANAGLGTWRT EAVFSEEALI GVPKDIPLQS AATLGVNPCT AYRMLVDFEQ 

       190        200        210        220        230        240 
LQPGDSVIQN ASNSGVGQAV IQIASALGLK TINVIRDRPD IKKLTDRLKD LGADYVLTEE 

       250        260        270        280        290        300 
ELRMPETKNI FKDLPLPRLA LNCVGGKSST ELLRHLAPGG TMVTYGGMAK QPVTASVSML 

       310        320        330        340        350        360 
IFKDLKLRGF WLSQWKKNHS PDEFKELILI LCNLIRQGQL TAPAWSGIPL QDYQQALEAS 

       370 
MKPFVSLKQI LTM

Q9Z311 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools