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Protein

Very-long-chain enoyl-CoA reductase

Gene

Tecr

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

Functioni

Catalyzes the last of the four reactions of the long-chain fatty acids elongation cycle. This endoplasmic reticulum-bound enzymatic process, allows the addition of 2 carbons to the chain of long- and very long-chain fatty acids/VLCFAs per cycle. This enzyme reduces the trans-2,3-enoyl-CoA fatty acid intermediate to an acyl-CoA that can be further elongated by entering a new cycle of elongation. Thereby, it participates to the production of VLCFAs of different chain lengths that are involved in multiple biological processes as precursors of membrane lipids and lipid mediators.By similarity

Catalytic activityi

A very-long-chain acyl-CoA + NADP+ = a very-long-chain trans-2,3-dehydroacyl-CoA + NADPH.By similarity

Pathwayi: fatty acid biosynthesis

This protein is involved in the pathway fatty acid biosynthesis, which is part of Lipid metabolism.By similarity
View all proteins of this organism that are known to be involved in the pathway fatty acid biosynthesis and in Lipid metabolism.

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Biological processi

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

Keywords - Ligandi

NADP

Enzyme and pathway databases

BRENDAi1.3.1.38. 3474.
ReactomeiR-MMU-75876. Synthesis of very long-chain fatty acyl-CoAs.
UniPathwayiUPA00094.

Chemistry

SwissLipidsiSLP:000000437.

Names & Taxonomyi

Protein namesi
Recommended name:
Very-long-chain enoyl-CoA reductaseCurated (EC:1.3.1.93By similarity)
Alternative name(s):
Synaptic glycoprotein SC2
Trans-2,3-enoyl-CoA reductase
Short name:
TER
Gene namesi
Name:Tecr
Synonyms:Gpsn2
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 8

Organism-specific databases

MGIiMGI:1915408. Tecr.

Subcellular locationi

  • Endoplasmic reticulum membrane By similarity; Multi-pass membrane protein By similarity

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transmembranei87 – 10721HelicalSequence analysisAdd
BLAST
Transmembranei194 – 21421HelicalSequence analysisAdd
BLAST
Transmembranei255 – 27521HelicalSequence analysisAdd
BLAST

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Endoplasmic reticulum, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 308308Very-long-chain enoyl-CoA reductasePRO_0000213684Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei22 – 221N6-acetyllysineBy similarity
Modified residuei58 – 581PhosphoserineCombined sources
Modified residuei60 – 601N6-acetyllysineCombined sources
Glycosylationi164 – 1641N-linked (GlcNAc...)Sequence analysis
Glycosylationi247 – 2471N-linked (GlcNAc...)Sequence analysis

Post-translational modificationi

Glycosylated.By similarity

Keywords - PTMi

Acetylation, Glycoprotein, Phosphoprotein

Proteomic databases

EPDiQ9CY27.
MaxQBiQ9CY27.
PaxDbiQ9CY27.
PeptideAtlasiQ9CY27.
PRIDEiQ9CY27.

PTM databases

iPTMnetiQ9CY27.
PhosphoSiteiQ9CY27.
SwissPalmiQ9CY27.

Expressioni

Gene expression databases

BgeeiQ9CY27.
CleanExiMM_GPSN2.
ExpressionAtlasiQ9CY27. baseline and differential.
GenevisibleiQ9CY27. MM.

Interactioni

Subunit structurei

Interacts with ELOVL1 and LASS2.By similarity

Protein-protein interaction databases

BioGridi223073. 1 interaction.
IntActiQ9CY27. 3 interactions.
MINTiMINT-1858664.
STRINGi10090.ENSMUSP00000019382.

Structurei

3D structure databases

ProteinModelPortaliQ9CY27.
SMRiQ9CY27. Positions 1-81.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the steroid 5-alpha reductase family.Curated

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiKOG1639. Eukaryota.
ENOG410XR2S. LUCA.
GeneTreeiENSGT00510000046645.
HOGENOMiHOG000190918.
InParanoidiQ9CY27.
KOiK10258.
OrthoDBiEOG7D2FF3.
PhylomeDBiQ9CY27.

Family and domain databases

InterProiIPR001104. 3-oxo-5_a-steroid_4-DH_C.
IPR029071. Ubiquitin-rel_dom.
[Graphical view]
PfamiPF02544. Steroid_dh. 1 hit.
[Graphical view]
SUPFAMiSSF54236. SSF54236. 1 hit.
PROSITEiPS50244. S5A_REDUCTASE. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q9CY27-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKHYEVEIRD AKTREKLCFL DKVEPQATIS EIKTLFTKTH PQWYPARQSL
60 70 80 90 100
RLDPKGKSLK DEDVLQKLPV GTTATLYFRD LGAQISWVTV FLTEYAGPLF
110 120 130 140 150
IYLLFYFRVP FIYGRKYDFT SSRHTVVHLA CMCHSFHYIK RLLETLFVHR
160 170 180 190 200
FSHGTMPLRN IFKNCTYYWG FAAWMAYYIN HPLYTPPTYG VQQVKLALAV
210 220 230 240 250
FVICQLGNFS IHMALRDLRP AGSKTRKIPY PTKNPFTWLF LLVSCPNYTY
260 270 280 290 300
EVGSWIGFAI LTQCVPVALF SLVGFTQMTI WAKGKHRSYL KEFRDYPPLR

MPIIPFLL
Length:308
Mass (Da):36,090
Last modified:June 1, 2001 - v1
Checksum:i0576C2813F2C5E4A
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK010984 mRNA. Translation: BAB27305.1.
BC019984 mRNA. Translation: AAH19984.1.
CCDSiCCDS40403.1.
RefSeqiNP_081455.1. NM_027179.1.
NP_598879.1. NM_134118.5.
UniGeneiMm.352239.

Genome annotation databases

EnsembliENSMUST00000019382; ENSMUSP00000019382; ENSMUSG00000031708.
GeneIDi106529.
KEGGimmu:106529.
UCSCiuc009mkl.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK010984 mRNA. Translation: BAB27305.1.
BC019984 mRNA. Translation: AAH19984.1.
CCDSiCCDS40403.1.
RefSeqiNP_081455.1. NM_027179.1.
NP_598879.1. NM_134118.5.
UniGeneiMm.352239.

3D structure databases

ProteinModelPortaliQ9CY27.
SMRiQ9CY27. Positions 1-81.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi223073. 1 interaction.
IntActiQ9CY27. 3 interactions.
MINTiMINT-1858664.
STRINGi10090.ENSMUSP00000019382.

Chemistry

SwissLipidsiSLP:000000437.

PTM databases

iPTMnetiQ9CY27.
PhosphoSiteiQ9CY27.
SwissPalmiQ9CY27.

Proteomic databases

EPDiQ9CY27.
MaxQBiQ9CY27.
PaxDbiQ9CY27.
PeptideAtlasiQ9CY27.
PRIDEiQ9CY27.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000019382; ENSMUSP00000019382; ENSMUSG00000031708.
GeneIDi106529.
KEGGimmu:106529.
UCSCiuc009mkl.2. mouse.

Organism-specific databases

CTDi9524.
MGIiMGI:1915408. Tecr.

Phylogenomic databases

eggNOGiKOG1639. Eukaryota.
ENOG410XR2S. LUCA.
GeneTreeiENSGT00510000046645.
HOGENOMiHOG000190918.
InParanoidiQ9CY27.
KOiK10258.
OrthoDBiEOG7D2FF3.
PhylomeDBiQ9CY27.

Enzyme and pathway databases

UniPathwayiUPA00094.
BRENDAi1.3.1.38. 3474.
ReactomeiR-MMU-75876. Synthesis of very long-chain fatty acyl-CoAs.

Miscellaneous databases

ChiTaRSiTecr. mouse.
PROiQ9CY27.
SOURCEiSearch...

Gene expression databases

BgeeiQ9CY27.
CleanExiMM_GPSN2.
ExpressionAtlasiQ9CY27. baseline and differential.
GenevisibleiQ9CY27. MM.

Family and domain databases

InterProiIPR001104. 3-oxo-5_a-steroid_4-DH_C.
IPR029071. Ubiquitin-rel_dom.
[Graphical view]
PfamiPF02544. Steroid_dh. 1 hit.
[Graphical view]
SUPFAMiSSF54236. SSF54236. 1 hit.
PROSITEiPS50244. S5A_REDUCTASE. 1 hit.
[Graphical view]
ProtoNetiSearch...

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: Embryonic liver.
  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].
    Tissue: Kidney.
  3. "Mitochondrial phosphoproteome revealed by an improved IMAC method and MS/MS/MS."
    Lee J., Xu Y., Chen Y., Sprung R., Kim S.C., Xie S., Zhao Y.
    Mol. Cell. Proteomics 6:669-676(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-58, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  4. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas, Spleen and Testis.
  5. "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-60, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Embryonic fibroblast.

Entry informationi

Entry nameiTECR_MOUSE
AccessioniPrimary (citable) accession number: Q9CY27
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 16, 2002
Last sequence update: June 1, 2001
Last modified: July 6, 2016
This is version 119 of the entry and version 1 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. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.