vacuolar protein sorting 11 [Drosophila melanogaster]
Protein Classification
RING-H2_Vps11 domain-containing protein( domain architecture ID 11616313)
RING-H2_Vps11 domain-containing protein
List of domain hits
| Name | Accession | Description | Interval | E-value | ||
| RING-H2_Vps11 | cd16688 | RING finger, H2 subclass, found in vacuolar protein sorting-associated protein 11 homolog ... |
731-777 | 2.67e-15 | ||
RING finger, H2 subclass, found in vacuolar protein sorting-associated protein 11 homolog (Vps11) and similar proteins; Vps11, also known as RING finger protein 108 (RNF108), is a soluble protein involved in regulation of glycolipid degradation and retrograde toxin transport. It is highly expressed in heart and pancreas. Vps11 associates with Vps16, Vps18, and Vps33 to form a Class C Vps core complex that is required for soluble N-ethylmaleimide-sensitive factor attachment protein receptors (SNARE)-mediated membrane fusion at the lysosome-like yeast vacuole. The core complex, together with two additional compartment-specific subunits, forms the tethering complexes HOPS (homotypic vacuole fusion and protein sorting) and CORVET (class C core vacuole/endosome transport). CORVET contains the additional Vps3 and Vps8 subunits. It operates at endosomes, controls traffic into late endosomes and interacts with the Rab5/Vps21-GTP form. HOPS contains the additional Vps39 and Vps41 subunits. It operates at the lysosomal vacuole, controls all traffic from late endosomes into the vacuole and interacts with the Rab7/Ypt7-GTP form. Vps11 is a central scaffold protein upon which both HOPS and CORVET assemble. The HOPS and CORVET complexes disassemble in the absence of Vps11, resulting in massive fragmentation of vacuoles. Vps11 contains a clathrin repeat domain and a C-terminal C3H2C3-type RING-H2 finger. This subfamily also includes Vps11 homologs found in fungi, such as Saccharomyces cerevisiae vacuolar membrane protein Pep5p, also known as carboxypeptidase Y-deficient protein 5, vacuolar morphogenesis protein 1, or vacuolar biogenesis protein END1. Pep5p is essential for vacuolar biogenesis. It associates with Pep3p to form a core Pep3p/Pep5p complex that promotes vesicular docking/fusion reactions in conjunction with SNARE proteins at multiple steps in transport routes to the vacuole. : Pssm-ID: 438349 [Multi-domain] Cd Length: 44 Bit Score: 70.45 E-value: 2.67e-15
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| Name | Accession | Description | Interval | E-value | ||
| RING-H2_Vps11 | cd16688 | RING finger, H2 subclass, found in vacuolar protein sorting-associated protein 11 homolog ... |
731-777 | 2.67e-15 | ||
RING finger, H2 subclass, found in vacuolar protein sorting-associated protein 11 homolog (Vps11) and similar proteins; Vps11, also known as RING finger protein 108 (RNF108), is a soluble protein involved in regulation of glycolipid degradation and retrograde toxin transport. It is highly expressed in heart and pancreas. Vps11 associates with Vps16, Vps18, and Vps33 to form a Class C Vps core complex that is required for soluble N-ethylmaleimide-sensitive factor attachment protein receptors (SNARE)-mediated membrane fusion at the lysosome-like yeast vacuole. The core complex, together with two additional compartment-specific subunits, forms the tethering complexes HOPS (homotypic vacuole fusion and protein sorting) and CORVET (class C core vacuole/endosome transport). CORVET contains the additional Vps3 and Vps8 subunits. It operates at endosomes, controls traffic into late endosomes and interacts with the Rab5/Vps21-GTP form. HOPS contains the additional Vps39 and Vps41 subunits. It operates at the lysosomal vacuole, controls all traffic from late endosomes into the vacuole and interacts with the Rab7/Ypt7-GTP form. Vps11 is a central scaffold protein upon which both HOPS and CORVET assemble. The HOPS and CORVET complexes disassemble in the absence of Vps11, resulting in massive fragmentation of vacuoles. Vps11 contains a clathrin repeat domain and a C-terminal C3H2C3-type RING-H2 finger. This subfamily also includes Vps11 homologs found in fungi, such as Saccharomyces cerevisiae vacuolar membrane protein Pep5p, also known as carboxypeptidase Y-deficient protein 5, vacuolar morphogenesis protein 1, or vacuolar biogenesis protein END1. Pep5p is essential for vacuolar biogenesis. It associates with Pep3p to form a core Pep3p/Pep5p complex that promotes vesicular docking/fusion reactions in conjunction with SNARE proteins at multiple steps in transport routes to the vacuole. Pssm-ID: 438349 [Multi-domain] Cd Length: 44 Bit Score: 70.45 E-value: 2.67e-15
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| zf-RING_5 | pfam14634 | zinc-RING finger domain; |
732-776 | 8.99e-04 | ||
zinc-RING finger domain; Pssm-ID: 434085 [Multi-domain] Cd Length: 43 Bit Score: 37.79 E-value: 8.99e-04
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| Name | Accession | Description | Interval | E-value | ||
| RING-H2_Vps11 | cd16688 | RING finger, H2 subclass, found in vacuolar protein sorting-associated protein 11 homolog ... |
731-777 | 2.67e-15 | ||
RING finger, H2 subclass, found in vacuolar protein sorting-associated protein 11 homolog (Vps11) and similar proteins; Vps11, also known as RING finger protein 108 (RNF108), is a soluble protein involved in regulation of glycolipid degradation and retrograde toxin transport. It is highly expressed in heart and pancreas. Vps11 associates with Vps16, Vps18, and Vps33 to form a Class C Vps core complex that is required for soluble N-ethylmaleimide-sensitive factor attachment protein receptors (SNARE)-mediated membrane fusion at the lysosome-like yeast vacuole. The core complex, together with two additional compartment-specific subunits, forms the tethering complexes HOPS (homotypic vacuole fusion and protein sorting) and CORVET (class C core vacuole/endosome transport). CORVET contains the additional Vps3 and Vps8 subunits. It operates at endosomes, controls traffic into late endosomes and interacts with the Rab5/Vps21-GTP form. HOPS contains the additional Vps39 and Vps41 subunits. It operates at the lysosomal vacuole, controls all traffic from late endosomes into the vacuole and interacts with the Rab7/Ypt7-GTP form. Vps11 is a central scaffold protein upon which both HOPS and CORVET assemble. The HOPS and CORVET complexes disassemble in the absence of Vps11, resulting in massive fragmentation of vacuoles. Vps11 contains a clathrin repeat domain and a C-terminal C3H2C3-type RING-H2 finger. This subfamily also includes Vps11 homologs found in fungi, such as Saccharomyces cerevisiae vacuolar membrane protein Pep5p, also known as carboxypeptidase Y-deficient protein 5, vacuolar morphogenesis protein 1, or vacuolar biogenesis protein END1. Pep5p is essential for vacuolar biogenesis. It associates with Pep3p to form a core Pep3p/Pep5p complex that promotes vesicular docking/fusion reactions in conjunction with SNARE proteins at multiple steps in transport routes to the vacuole. Pssm-ID: 438349 [Multi-domain] Cd Length: 44 Bit Score: 70.45 E-value: 2.67e-15
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| zf-RING_5 | pfam14634 | zinc-RING finger domain; |
732-776 | 8.99e-04 | ||
zinc-RING finger domain; Pssm-ID: 434085 [Multi-domain] Cd Length: 43 Bit Score: 37.79 E-value: 8.99e-04
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| zf-C3HC4_2 | pfam13923 | Zinc finger, C3HC4 type (RING finger); |
732-774 | 1.19e-03 | ||
Zinc finger, C3HC4 type (RING finger); Pssm-ID: 404756 [Multi-domain] Cd Length: 40 Bit Score: 37.42 E-value: 1.19e-03
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| RING-H2_Vps18 | cd16689 | RING finger, H2 subclass, found in vacuolar protein sorting-associated protein 18 (Vps18) and ... |
731-758 | 1.91e-03 | ||
RING finger, H2 subclass, found in vacuolar protein sorting-associated protein 18 (Vps18) and similar proteins; Vps18 is an ubiquitin ligase E3 that is highly expressed in heart. It induces the ubiquitylation and degradation of serum-inducible kinase. Vps18 associates with Vps11, Vps16, and Vps33 to form a Class C Vps core complex that is required for soluble N-ethylmaleimide-sensitive factor attachment protein receptors (SNARE)-mediated membrane fusion at the lysosome-like yeast vacuole. The core complex, together with two additional compartment-specific subunits, forms the tethering complexes HOPS (homotypic vacuole fusion and protein sorting) and CORVET (class C core vacuole/endosome transport). CORVET contains the additional Vps3 and Vps8 subunits. It operates at endosomes, controls traffic into late endosomes and interacts with the Rab5/Vps21-GTP form. HOPS contains the additional Vps39 and Vps41 subunits. It operates at the lysosomal vacuole, controls all traffic from late endosomes into the vacuole and interacts with the Rab7/Ypt7-GTP form. Vps18 deficiency inhibits dendritogenesis in Purkinje cells by blocking the lysosomal degradation of lysyl oxidase. Vps18 contains a clathrin heavy chain repeat, a coiled-coil domain, and a C3H2C3-type RING-H2 finger domain close to its C-terminus. This subfamily also includes Vps18 homologs found in insects and fungi, such as Drosophila melanogaster protein Dor (encoded by deep orange (dor) gene), and Saccharomyces cerevisiae vacuolar membrane protein Pep3p, also known as carboxypeptidase Y-deficient protein 3, or vacuolar morphogenesis protein 8. Drosophila Dor is part of a protein complex, that also includes the Sep1p homolog carnation (car), which localizes to endosomal compartments and is required not only for the biogenesis of pigment granules but also for the normal delivery of proteins to lysosomes. Pep3p is a vacuolar peripheral membrane protein that is required for vacuolar biogenesis in Saccharomyces cerevisiae. Pep3p associates with Pep5p to form a core Pep3p/Pep5p complex that promotes vesicular docking/fusion reactions in conjunction with SNARE proteins at multiple steps in transport routes to the vacuole. Pssm-ID: 438350 Cd Length: 45 Bit Score: 36.69 E-value: 1.91e-03
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| RING-H2_Pep3p-like | cd16462 | RING finger, H2 subclass, found in Saccharomyces cerevisiae vacuolar membrane protein PEP3 ... |
731-758 | 3.41e-03 | ||
RING finger, H2 subclass, found in Saccharomyces cerevisiae vacuolar membrane protein PEP3 (Pep3p) and similar proteins; Pep3p, also known as carboxypeptidase Y-deficient protein 3, vacuolar morphogenesis protein 8, vacuolar protein sorting-associated protein 18 (Vps18p), or vacuolar protein-targeting protein 18, is a vacuolar membrane protein that affects late Golgi functions required for vacuolar protein sorting and efficient alpha-factor prohormone maturation. It is required for vacuolar biogenesis and for trafficking of hydrolase precursors to the vacuole. The disruption of PEP3 may cause hypersensitivity to heat shock and ethanol stresses, probably due to disappearance of normal vacuoles. As a component of the homotypic fusion and vacuole protein sorting (HOPS) and class C core vacuole/endosome tethering (CORVET) complexes, its overexpression shortens lag phase but does not alter growth rate in Saccharomyces cerevisiae exposed to acetic acid stress. Moreover, Pep3p forms the Class C Vps protein complex (C-Vps complex) with Pep5p (also known as Vps11), Vps16, and Vps33, and is necessary for trafficking of hydrolase precursors to the vacuole by promoting vesicular docking reactions with SNARE proteins. Pep3p contains a C3H2C3-type RING-H2 finger at the C-terminus. Pssm-ID: 438125 [Multi-domain] Cd Length: 50 Bit Score: 36.12 E-value: 3.41e-03
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| zf-RING_UBOX | pfam13445 | RING-type zinc-finger; This zinc-finger is a typical RING-type of plant ubiquitin ligases. |
733-771 | 4.86e-03 | ||
RING-type zinc-finger; This zinc-finger is a typical RING-type of plant ubiquitin ligases. Pssm-ID: 463881 [Multi-domain] Cd Length: 38 Bit Score: 35.45 E-value: 4.86e-03
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