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Q9DCS3

- MECR_MOUSE

UniProt

Q9DCS3 - MECR_MOUSE

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Protein

Trans-2-enoyl-CoA reductase, mitochondrial

Gene

Mecr

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli

Functioni

Oxidoreductase with 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). May play a role in mitochondrial fatty acid synthesis (By similarity).By similarity

Catalytic activityi

Acyl-CoA + NADP+ = trans-2,3-dehydroacyl-CoA + NADPH.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei167 – 1671NADPBy similarity
Binding sitei368 – 3681NADPBy similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi193 – 1964NADPBy similarity
Nucleotide bindingi216 – 2183NADPBy similarity
Nucleotide bindingi285 – 2884NADPBy similarity
Nucleotide bindingi310 – 3123NADPBy similarity

GO - Molecular functioni

  1. ligand-dependent nuclear receptor binding Source: MGI
  2. trans-2-enoyl-CoA reductase (NADPH) activity Source: UniProtKB-EC
  3. zinc ion binding Source: InterPro

GO - Biological processi

  1. fatty acid biosynthetic process Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Biological processi

Fatty acid biosynthesis, Fatty acid metabolism, Lipid biosynthesis, Lipid metabolism

Keywords - Ligandi

NADP

Names & Taxonomyi

Protein namesi
Recommended name:
Trans-2-enoyl-CoA reductase, mitochondrial (EC:1.3.1.38)
Gene namesi
Name:Mecr
Synonyms:Nrbf1
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 4

Organism-specific databases

MGIiMGI:1349441. Mecr.

Subcellular locationi

Mitochondrion By similarity

GO - Cellular componenti

  1. cytosol Source: MGI
  2. mitochondrion Source: MGI
  3. nucleus Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Mitochondrion

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei1 – 5353MitochondrionSequence AnalysisAdd
BLAST
Chaini54 – 373320Trans-2-enoyl-CoA reductase, mitochondrialPRO_0000000889Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei61 – 611N6-acetyllysine; alternate1 Publication
Modified residuei61 – 611N6-succinyllysine; alternate1 Publication
Modified residuei252 – 2521N6-acetyllysine; alternate1 Publication
Modified residuei252 – 2521N6-succinyllysine; alternate1 Publication
Modified residuei267 – 2671N6-acetyllysine; alternate1 Publication
Modified residuei267 – 2671N6-succinyllysine; alternate1 Publication
Modified residuei316 – 3161N6-succinyllysine1 Publication

Keywords - PTMi

Acetylation

Proteomic databases

MaxQBiQ9DCS3.
PaxDbiQ9DCS3.
PRIDEiQ9DCS3.

PTM databases

PhosphoSiteiQ9DCS3.

Expressioni

Gene expression databases

BgeeiQ9DCS3.
CleanExiMM_MECR.
ExpressionAtlasiQ9DCS3. baseline and differential.
GenevestigatoriQ9DCS3.

Interactioni

Subunit structurei

Homodimer.By similarity

Protein-protein interaction databases

IntActiQ9DCS3. 2 interactions.
MINTiMINT-4128719.

Structurei

3D structure databases

ProteinModelPortaliQ9DCS3.
SMRiQ9DCS3. Positions 38-373.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiCOG0604.
GeneTreeiENSGT00740000115589.
HOGENOMiHOG000294683.
HOVERGENiHBG052446.
InParanoidiQ9DCS3.
KOiK07512.
OMAiCSTLWRV.
OrthoDBiEOG78M024.
PhylomeDBiQ9DCS3.
TreeFamiTF312886.

Family and domain databases

Gene3Di3.40.50.720. 1 hit.
3.90.180.10. 1 hit.
InterProiIPR013149. ADH_C.
IPR013154. ADH_GroES-like.
IPR002085. ADH_SF_Zn-type.
IPR011032. GroES-like.
IPR016040. NAD(P)-bd_dom.
[Graphical view]
PANTHERiPTHR11695. PTHR11695. 1 hit.
PfamiPF08240. ADH_N. 1 hit.
PF00107. ADH_zinc_N. 1 hit.
[Graphical view]
SUPFAMiSSF50129. SSF50129. 1 hit.

Sequencei

Sequence statusi: Complete.

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

Q9DCS3-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MLVSQRVTGA RARAPQLAGL LEAWYRHGRT TSSYSALSEP SRVRALVYGN
60 70 80 90 100
HGDPAKVVQL KNLELTAVEG SDVHVRMLAA PINPSDINMI QGNYGLLPKL
110 120 130 140 150
PAVGGNEGVG QVIAVGSSVS ALKPGDWVIP ANAGLGTWRT EAVFSEEALI
160 170 180 190 200
GIPKDIPLQS AATLGVNPCT AYRMLVDFEQ LQPGDSVIQN ASNSGVGQAV
210 220 230 240 250
IQIASALRLK TINVVRDRPD IKKLTDRLKD LGADYVLTEE ELRMPETKTI
260 270 280 290 300
FKDLPLPRLA LNCVGGKSST ELLRHLAPGG TMVTYGGMAK QPVTASVSLL
310 320 330 340 350
IFKDLKLRGF WLSQWKKNHS PDEFKELILT LCNLIRQGRL TAPSCSEVPL
360 370
QGYQQALEAS MKPFVSSKQI LTM
Length:373
Mass (Da):40,343
Last modified:April 26, 2005 - v2
Checksum:iEBA9A61A46386AEE
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti69 – 691E → K in BAB22169. (PubMed:16141072)Curated

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AK002533 mRNA. Translation: BAB22169.1.
BC003864 mRNA. Translation: AAH03864.1.
CCDSiCCDS18715.1.
RefSeqiNP_079573.2. NM_025297.2.
UniGeneiMm.192706.

Genome annotation databases

EnsembliENSMUST00000030742; ENSMUSP00000030742; ENSMUSG00000028910.
GeneIDi26922.
KEGGimmu:26922.
UCSCiuc008vae.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AK002533 mRNA. Translation: BAB22169.1 .
BC003864 mRNA. Translation: AAH03864.1 .
CCDSi CCDS18715.1.
RefSeqi NP_079573.2. NM_025297.2.
UniGenei Mm.192706.

3D structure databases

ProteinModelPortali Q9DCS3.
SMRi Q9DCS3. Positions 38-373.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

IntActi Q9DCS3. 2 interactions.
MINTi MINT-4128719.

PTM databases

PhosphoSitei Q9DCS3.

Proteomic databases

MaxQBi Q9DCS3.
PaxDbi Q9DCS3.
PRIDEi Q9DCS3.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000030742 ; ENSMUSP00000030742 ; ENSMUSG00000028910 .
GeneIDi 26922.
KEGGi mmu:26922.
UCSCi uc008vae.2. mouse.

Organism-specific databases

CTDi 51102.
MGIi MGI:1349441. Mecr.

Phylogenomic databases

eggNOGi COG0604.
GeneTreei ENSGT00740000115589.
HOGENOMi HOG000294683.
HOVERGENi HBG052446.
InParanoidi Q9DCS3.
KOi K07512.
OMAi CSTLWRV.
OrthoDBi EOG78M024.
PhylomeDBi Q9DCS3.
TreeFami TF312886.

Miscellaneous databases

NextBioi 304813.
PROi Q9DCS3.
SOURCEi Search...

Gene expression databases

Bgeei Q9DCS3.
CleanExi MM_MECR.
ExpressionAtlasi Q9DCS3. baseline and differential.
Genevestigatori Q9DCS3.

Family and domain databases

Gene3Di 3.40.50.720. 1 hit.
3.90.180.10. 1 hit.
InterProi IPR013149. ADH_C.
IPR013154. ADH_GroES-like.
IPR002085. ADH_SF_Zn-type.
IPR011032. GroES-like.
IPR016040. NAD(P)-bd_dom.
[Graphical view ]
PANTHERi PTHR11695. PTHR11695. 1 hit.
Pfami PF08240. ADH_N. 1 hit.
PF00107. ADH_zinc_N. 1 hit.
[Graphical view ]
SUPFAMi SSF50129. SSF50129. 1 hit.
ProtoNeti Search...

Publicationsi

  1. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6J.
    Tissue: Kidney.
  2. "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].
    Strain: FVB/N.
    Tissue: Mammary tumor.
  3. "SIRT5-mediated lysine desuccinylation impacts diverse metabolic pathways."
    Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.
    Mol. Cell 50:919-930(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-267, SUCCINYLATION [LARGE SCALE ANALYSIS] AT LYS-61; LYS-252; LYS-267 AND LYS-316, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Embryonic fibroblast and Liver.
  4. "Label-free quantitative proteomics of the lysine acetylome in mitochondria identifies substrates of SIRT3 in metabolic pathways."
    Rardin M.J., Newman J.C., Held J.M., Cusack M.P., Sorensen D.J., Li B., Schilling B., Mooney S.D., Kahn C.R., Verdin E., Gibson B.W.
    Proc. Natl. Acad. Sci. U.S.A. 110:6601-6606(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-61 AND LYS-252, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.

Entry informationi

Entry nameiMECR_MOUSE
AccessioniPrimary (citable) accession number: Q9DCS3
Secondary accession number(s): Q99L39
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 26, 2005
Last sequence update: April 26, 2005
Last modified: October 29, 2014
This is version 103 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3