Primary Information | |
---|---|
BoMiProt ID | Bomi2719 |
Protein Name | Reticulon-3 |
Organism | Bos taurus |
Uniprot ID | Q08D83 |
Milk Fraction | MFGM, Exosome |
Ref Sequence ID | NP_872598.1 |
Aminoacid Length | 256 |
Molecular Weight | 27455 |
FASTA Sequence | Download |
Gene Name | RTN3 |
Gene ID | 359721 |
Protein Existence Status | Reveiwed:Experimental evidence at transcript level |
Secondary Information | |
Protein Function | Rtn3L is recruited to ER-endosome MCSs by endosomal protein Rab9a, which marks a transition stage between early and late endosomes.RTN3 functions as a novel suppressor of HCC by activating Chk2/p53 pathway and provide more clues to better understand the oncogenic effects of HBV. |
Biochemical Properties | The Reticulon (Rtn) proteins reside exclusively on tubular ER due to a conserved C-terminal reticulon homology domain (RHD). The RHD forms a characteristic hairpin transmembrane domain that restricts Rtn protein localization to regions of high membrane curvature like tubular ER membranes. |
PTMs | N-acetylation at Alanine,Phosphorylation at Ser |
Linking IDs | Bomi2719 |
Bibliography | 1.Song S, Shi Y, Wu W, Wu H, Chang L, Peng P, Zhang L, Fan J, Gu J, Ruan Y. Reticulon 3-mediated Chk2/p53 activation suppresses hepatocellular carcinogenesis and is blocked by hepatitis B virus. Gut. 2021 Nov;70(11):2159-2171. doi: 10.1136/gutjnl-2020-321386. Epub 2020 Dec 10. PMID: 33303565. 2.Wu H, Voeltz GK. Reticulon-3 Promotes Endosome Maturation at ER Membrane Contact Sites. Dev Cell. 2021 Jan 11;56(1):52-66.e7. doi: 10.1016/j.devcel.2020.12.014. PMID: 33434526; PMCID: PMC7837408. 3.Voeltz GK, Prinz WA, Shibata Y, Rist JM, and Rapoport TA (2006). A class of membrane proteins shaping the tubular endoplasmic reticulum. Cell 124, 573–586. |
Protein Function | Rtn3L is recruited to ER-endosome MCSs by endosomal protein Rab9a, which marks a transition stage between early and late endosomes.RTN3 functions as a novel suppressor of HCC by activating Chk2/p53 pathway and provide more clues to better understand the oncogenic effects of HBV. |
Biochemical Properties | The Reticulon (Rtn) proteins reside exclusively on tubular ER due to a conserved C-terminal reticulon homology domain (RHD). The RHD forms a characteristic hairpin transmembrane domain that restricts Rtn protein localization to regions of high membrane curvature like tubular ER membranes. |
PTMs | N-acetylation at Alanine,Phosphorylation at Ser |
Site(s) of PTM(s) N-glycosylation, O-glycosylation, Phosphorylation | |
Predicted Disorder Regions | (1-32) |
DisProt Annotation | |
TM Helix Prediction | 2TMHs; (88-110),(190-212) |
Linking IDs | |
Bibliography | 1.Song S, Shi Y, Wu W, Wu H, Chang L, Peng P, Zhang L, Fan J, Gu J, Ruan Y. Reticulon 3-mediated Chk2/p53 activation suppresses hepatocellular carcinogenesis and is blocked by hepatitis B virus. Gut. 2021 Nov;70(11):2159-2171. doi: 10.1136/gutjnl-2020-321386. Epub 2020 Dec 10. PMID: 33303565. 2.Wu H, Voeltz GK. Reticulon-3 Promotes Endosome Maturation at ER Membrane Contact Sites. Dev Cell. 2021 Jan 11;56(1):52-66.e7. doi: 10.1016/j.devcel.2020.12.014. PMID: 33434526; PMCID: PMC7837408. 3.Voeltz GK, Prinz WA, Shibata Y, Rist JM, and Rapoport TA (2006). A class of membrane proteins shaping the tubular endoplasmic reticulum. Cell 124, 573–586. |