UniProt ID | TECR_RAT | |
---|---|---|
UniProt AC | Q64232 | |
Protein Name | Very-long-chain enoyl-CoA reductase {ECO:0000305} | |
Gene Name | Tecr | |
Organism | Rattus norvegicus (Rat). | |
Sequence Length | 308 | |
Subcellular Localization |
Endoplasmic reticulum membrane Multi-pass membrane protein . |
|
Protein Description | 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 in the production of VLCFAs of different chain lengths that are involved in multiple biological processes as precursors of membrane lipids and lipid mediators.. | |
Protein Sequence | MKHYEVEIRDAKTREKLCFLDKVEPQATISEIKTLFTKTHPQWYPARQSLRLDPKGKSLKDEDVLQKLPVGTTATLYFRDLGAQISWVTVFLTEYAGPLFIYLLFYFRVPFIYGRKYDFTSSRHTVVHLACMCHSFHYIKRLLETLFVHRFSHGTMPLRNIFKNCTYYWGFAAWMAYYINHPLYTPPTYGVQQVKLALAIFVICQLGNFSIHMALRDLRPAGSKTRKIPYPTKNPFTWLFLLVSCPNYTYEVGSWIGFAIMTQCVPVALFSLVGFTQMTIWAKGKHRSYLKEFRDYPPLRMPIIPFLL | |
Overview of Protein Modification Sites with Functional and Structural Information | ||
|
* ASA = Accessible Surface Area
Locations | Modification | Substrate Peptides & Secondary Structure |
ASA (%) | Reference | Orthologous Protein Cluster |
---|---|---|---|---|---|
2 | Acetylation | ------MKHYEVEIR ------CCCEEEEEE | 55.69 | 22902405 | |
22 | Acetylation | EKLCFLDKVEPQATI HHEECCCCCCCCCCH | 51.12 | 22902405 | |
38 | Acetylation | EIKTLFTKTHPQWYP HHHHHHHCCCCCCCC | 37.19 | 22902405 | |
58 | Phosphorylation | RLDPKGKSLKDEDVL CCCCCCCCCCCHHHH | 49.69 | 29779826 | |
60 | Acetylation | DPKGKSLKDEDVLQK CCCCCCCCCHHHHHH | 67.19 | 22902405 | |
60 | Succinylation | DPKGKSLKDEDVLQK CCCCCCCCCHHHHHH | 67.19 | 26843850 | |
164 | N-linked_Glycosylation | PLRNIFKNCTYYWGF CHHHHHCCCCHHHHH | 16.77 | - | |
247 | N-linked_Glycosylation | FLLVSCPNYTYEVGS EEEECCCCCCCCCCH | 46.21 | - | |
291 | Acetylation | GKHRSYLKEFRDYPP CCCHHHHHHHCCCCC | 46.72 | 22902405 | |
291 | Ubiquitination | GKHRSYLKEFRDYPP CCCHHHHHHHCCCCC | 46.72 | - |
Modified Location | Modified Residue | Modification | Type of Upstream Proteins | Gene Name of Upstream Proteins | UniProt AC of Upstream Proteins | Sources |
---|---|---|---|---|---|---|
Oops, there are no upstream regulatory protein records of TECR_RAT !! |
Modified Location | Modified Residue | Modification | Function | Reference | ||
---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of TECR_RAT !! |
* Distance = the distance between SAP position and PTM sites.
Modified Location | Modification | Variant Position (Distance <= 10) |
Residue Change | SAP | Related Disease | Reference |
---|---|---|---|---|---|---|
Oops, there are no SNP-PTM records of TECR_RAT !! |
Interacting Protein | Gene Name | Interaction Type | PPI Reference | Domain-Domain Interactions |
---|---|---|---|---|
Oops, there are no PPI records of TECR_RAT !! |
Kegg Drug | ||||||
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DrugBank | ||||||
There are no disease associations of PTM sites. |
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