Q0VD48 (VPS4B_BOVIN) Reviewed, UniProtKB/Swiss-Prot
Last modified May 14, 2014. Version 59. History...
Names and origin
|Protein names||Recommended name:|
Vacuolar protein sorting-associated protein 4B
|Organism||Bos taurus (Bovine) [Reference proteome]|
|Taxonomic identifier||9913 [NCBI]|
|Taxonomic lineage||Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Laurasiatheria › Cetartiodactyla › Ruminantia › Pecora › Bovidae › Bovinae › Bos|
|Sequence length||444 AA.|
|Protein existence||Evidence at transcript level|
General annotation (Comments)
Involved in late steps of the endosomal multivesicular bodies (MVB) pathway. Recognizes membrane-associated ESCRT-III assemblies and catalyzes their disassembly, possibly in combination with membrane fission. Redistributes the ESCRT-III components to the cytoplasm for further rounds of MVB sorting. MVBs contain intraluminal vesicles (ILVs) that are generated by invagination and scission from the limiting membrane of the endosome and mostly are delivered to lysosomes enabling degradation of membrane proteins, such as stimulated growth factor receptors, lysosomal enzymes and lipids. In conjunction with the ESCRT machinery also appears to function in topologically equivalent membrane fission events, such as the terminal stages of cytokinesis and enveloped virus budding (lentiviruses). Involved in cytokinesis By similarity.
ATP + H2O = ADP + phosphate.
Proposed to be monomeric or homodimeric in nucleotide-free form and to oligomerize upon binding to ATP to form two stacked hexameric or heptameric rings with a central pore through which ESCRT-III substrates are translocated in an ATP-dependent manner. Interacts with CHMP1A, CHMP1B, CHMP2A, CHMP2B, CHMP3, CHMP4A, CHMP4B, CHMP4C and CHMP6. Interacts with VPS4B; the interaction suggests a heteromeric assembly with VPS4B. Interacts with SPAST. Interacts with IST1 By similarity. with VTA1 By similarity.
Prevacuolar compartment membrane; Peripheral membrane protein. Late endosome membrane; Peripheral membrane protein By similarity. Note: Membrane-associated in the prevacuolar endosomal compartment. Localizes to the midbody of dividing cells. Localized in two distinct rings on either side of the Fleming body By similarity.
The MIT domain serves as an adapter for ESCRT-III proteins. It forms an asymmetric three-helix bundle that binds amphipathic MIM (MIT interacting motif) helices along the groove between MIT helices 2 and 3 present in a subset of ESCRT-III proteins thus establishing the canonical MIM-MIT interaction. In an extended conformation along the groove between helices 1 and 3, also binds to a type-2 MIT interacting motif (MIM2) By similarity.
Belongs to the AAA ATPase family.
Contains 1 MIT domain.
Sequence annotation (Features)
|Feature key||Position(s)||Length||Description||Graphical view||Feature identifier|
|Chain||1 – 444||444||Vacuolar protein sorting-associated protein 4B||PRO_0000331378|
|Domain||4 – 82||79||MIT|
|Nucleotide binding||174 – 181||8||ATP Potential|
|Coiled coil||19 – 82||64||Potential|
Amino acid modifications
|Modified residue||102||1||Phosphoserine By similarity|
|Modified residue||108||1||Phosphoserine By similarity|
|BC119836 mRNA. Translation: AAI19837.1.|
|RefSeq||NP_001069624.1. NM_001076156.1. |
3D structure databases
|SMR||Q0VD48. Positions 7-108, 123-444. |
Protein-protein interaction databases
Protocols and materials databases
Genome annotation databases
|Ensembl||ENSBTAT00000013862; ENSBTAP00000013862; ENSBTAG00000010492. |
Family and domain databases
|Gene3D||22.214.171.1240. 1 hit. |
126.96.36.1990. 1 hit.
|InterPro||IPR003593. AAA+_ATPase. |
|Pfam||PF00004. AAA. 1 hit. |
PF04212. MIT. 1 hit.
PF09336. Vps4_C. 1 hit.
|SMART||SM00382. AAA. 1 hit. |
SM00745. MIT. 1 hit.
|SUPFAM||SSF116846. SSF116846. 1 hit. |
SSF52540. SSF52540. 1 hit.
|PROSITE||PS00674. AAA. 1 hit. |
|Accession||Primary (citable) accession number: Q0VD48|
|Entry status||Reviewed (UniProtKB/Swiss-Prot)|
|Annotation program||Chordata Protein Annotation Program|
Index of protein domains and families