Search by BoMiProt ID - Bomi8721


Primary Information

BoMiProt ID Bomi8721
Protein Name Reticulophagy regulator 1
Organism Bos taurus
Uniprot IdQ5E9K8
Milk FractionWhey
Ref Sequence Id NP_001015672.1
Aminoacid Length 493
Molecular Weight 53680
Fasta Sequence https://www.uniprot.org/uniprot/Q5E9K8.fasta
Gene Name RETREG1
Gene Id 540068
Protein Existence Status reviewed

Secondary Information

Protein Function It is an autophagy receptor anchoroed to ER.RETREG1 participates in the formation of the mitophagophore by interacting with OPA1 and is responsible for delivering ER into lysosomes through sequestration into autophagosomes.
Biochemical Properties LC3 binding motif of RETREG1 is essential for autophagic degradation of AMFR.The reticulon homology domain provides capacity to bend the membrane and promotes ER scission.Structure analysis showed that the N-terminal half of FAM134B has 2 unusually long hydrophobic segments of about 35 amino acids each that are separated by a hydrophilic loop of about 60 amino acids.The C terminus of FAM134B contains a coiled-coil domain.
PTMs Phosphorylation on Thr and Ser
Significance of PTMs Mass spectrometry analysis resulted in the identification of serine 149, 151, and 153 (S149, S151, S153) as potential FAM134B phosphorylation sites and all of these three residues reside within RTND.Under ER-stress conditions, activated CAMK2B phosphorylates the reticulon-homology domain of FAM134B, which enhances FAM134B oligomerization and activity in membrane fragmentation to accommodate high demand for ERphagy.
Linking IDs Bomi8721
Bibliography 1.Kurth, I., Pamminger, T., Hennings, J. C., Soehendra, D., Huebner, A. K., Rotthier, A., Baets, J., Senderek, J., Topaloglu, H., Farrell, S. A., Nurnberg, G., Nurnberg, P., De Jonghe, P., Gal, A., Kaether, C., Timmerman, V., Hubner, C. A. Mutations in FAM134B, encoding a newly identified Golgi protein, cause severe sensory and autonomic neuropathy. Nature Genet. 41: 1179-1181, 2009. 2.Islam, F., Gopalan, V., & Lam, A. K. (2018). RETREG1 (FAM134B): A new player in human diseases: 15 years after the discovery in cancer. Journal of cellular physiology, 233(6), 4479–4489. https://doi.org/10.1002/jcp.26384 3.Jiang X, Wang X, Ding X, Du M, Li B, Weng X, Zhang J, Li L, Tian R, Zhu Q, Chen S, Wang L, Liu W, Fang L, Neculai D, Sun Q. FAM134B oligomerization drives endoplasmic reticulum membrane scission for ER-phagy. EMBO J. 2020 Mar 2;39(5):e102608. doi: 10.15252/embj.2019102608. Epub 2020 Jan 13. PMID: 31930741; PMCID: PMC7049798.
Protein Function It is an autophagy receptor anchoroed to ER.RETREG1 participates in the formation of the mitophagophore by interacting with OPA1 and is responsible for delivering ER into lysosomes through sequestration into autophagosomes.
Biochemical Properties LC3 binding motif of RETREG1 is essential for autophagic degradation of AMFR.The reticulon homology domain provides capacity to bend the membrane and promotes ER scission.Structure analysis showed that the N-terminal half of FAM134B has 2 unusually long hydrophobic segments of about 35 amino acids each that are separated by a hydrophilic loop of about 60 amino acids.The C terminus of FAM134B contains a coiled-coil domain.
PTMs Phosphorylation on Thr and Ser
Site(s) of PTM(s)

N-glycosylation, O-glycosylation,
Phosphorylation
>sp|Q5E9K8|RETR1_BOVIN Reticulophagy regulator 1 OS=Bos taurus OX=9913 GN=RETREG1 PE=2 SV=2 MASPAPPEPAEQGSPALAAAPQAPPPPTRAPPEEPEGAAPPEEGAAAGAGRQVEEAAGGV AAVVTWLLGEPALWLGGRADELLSWKRPLHSLLAFVGANLVFWFLALTPWRVYHLISVMI LTRVIMQIIKDMILSRTRGAQLWRSLSESWEVINSKPDERPGFSHCLAESWMNFSIFLQE MSVFKQQSPGKFCLLVCSVCTFFTILGSYIPGVILSYLLLLCAFLCPLFKCNDIGQKIYS KIKSCLLKLDFGIREYINQKKRERSEADKEKSHKDDSELDFSALCPKISLTTAAKELSVS DTDVSEVSWTDNGTFNLSEGYTPQTDTSDDLDRPSEEVFSRDLSDFPSLENGT*353GTNDEDE LSLGLPTELKRKKEQLDGGPRRSTEKKSAAGLSLPLSSDQTLHLMSDLAGDVITAAVTAA VKDQLAGVRQALSQAAPSLGEDTDTEEGDDFELLDQSELDQIESELGLSQDQEAEAQQNK KSSGFLSNLLGGH
Predicted Disorder Regions 5 disordered segments; (1-54), (263-276), (313-363), (366-400), (415-493)
DisProt Annotation
TM Helix Prediction 2 TMHs;( 100-122) and ( 192-214)
Significance of PTMs Mass spectrometry analysis resulted in the identification of serine 149, 151, and 153 (S149, S151, S153) as potential FAM134B phosphorylation sites and all of these three residues reside within RTND.Under ER-stress conditions, activated CAMK2B phosphorylates the reticulon-homology domain of FAM134B, which enhances FAM134B oligomerization and activity in membrane fragmentation to accommodate high demand for ERphagy.
Linking IDs
Bibliography 1.Kurth, I., Pamminger, T., Hennings, J. C., Soehendra, D., Huebner, A. K., Rotthier, A., Baets, J., Senderek, J., Topaloglu, H., Farrell, S. A., Nurnberg, G., Nurnberg, P., De Jonghe, P., Gal, A., Kaether, C., Timmerman, V., Hubner, C. A. Mutations in FAM134B, encoding a newly identified Golgi protein, cause severe sensory and autonomic neuropathy. Nature Genet. 41: 1179-1181, 2009. 2.Islam, F., Gopalan, V., & Lam, A. K. (2018). RETREG1 (FAM134B): A new player in human diseases: 15 years after the discovery in cancer. Journal of cellular physiology, 233(6), 4479–4489. https://doi.org/10.1002/jcp.26384 3.Jiang X, Wang X, Ding X, Du M, Li B, Weng X, Zhang J, Li L, Tian R, Zhu Q, Chen S, Wang L, Liu W, Fang L, Neculai D, Sun Q. FAM134B oligomerization drives endoplasmic reticulum membrane scission for ER-phagy. EMBO J. 2020 Mar 2;39(5):e102608. doi: 10.15252/embj.2019102608. Epub 2020 Jan 13. PMID: 31930741; PMCID: PMC7049798.