Member database | SMART |
SMART type | domain |
Short name | VPS10 |
Description Imported from IPR006581
Yeast Vps10p is a receptor for sorting and transport of the soluble vacuolar hydrolase carboxypeptidase Y to the lysosome-like vacuole
[3]. In mammalian cells, proteins containing this domain are involved in the transport of lipoproteins and sorting of endosomal proteins. They may also act as receptors for some neuropeptides.
The N terminus of murine brain SorCS contains two putative cleavage sites for the convertase furin which mark the beginning of the VPS10 domain, which is followed by a module of imperfect leucine-rich repeats and a transmembrane domain. The short intracellular C terminus contains consensus signals for rapid internalization. The identified putative binding motifs for SH2 and SH3 domains are unique in the family of VPS10 domain receptors. SorCS is predominantly expressed in brain, but also in heart, liver, and kidney. SorCS transcripts detected by in situ hybridization in the murine central nervous system point to a neuronal expression
[1, 2].
References Imported from IPR006581
1.Identification and characterization of SorCS, a third member of a novel receptor family. Hermey G, Riedel IB, Hampe W, Schaller HC, Hermans-Borgmeyer I. Biochem. Biophys. Res. Commun. 266, 347-51, (1999). View articlePMID: 10600506
2.Vps9p is a guanine nucleotide exchange factor involved in vesicle-mediated vacuolar protein transport. Hama H, Tall GG, Horazdovsky BF. J. Biol. Chem. 274, 15284-91, (1999). View articlePMID: 10329739
3.The yeast Vps10p cytoplasmic tail mediates lysosomal sorting in mammalian cells and interacts with human GGAs. Dennes A, Madsen P, Nielsen MS, Petersen CM, Pohlmann R. J. Biol. Chem. 277, 12288-93, (2002). View articlePMID: 11801606
Integrated to
External Links
Representative structure
3f6k: Crystal structure of the Vps10p domain of human sortilin/NTS3 in complex with neurotensin