Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

Q5R658 (VPS4B_PONAB) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 59. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Vacuolar protein sorting-associated protein 4B

EC=3.6.4.6
Gene names
Name:VPS4B
OrganismPongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii) [Reference proteome]
Taxonomic identifier9601 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaePongo

Protein attributes

Sequence length444 AA.
Sequence statusComplete.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

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) By similarity.

Catalytic activity

ATP + H2O = ADP + phosphate.

Subunit structure

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. In vitro, associates on the inside of a helical tubular structure formed by a CHMP2A-CHMP3 polymer. Interacts with CHMP1A, CHMP1B, CHMP2A, CHMP4B and CHMP6. Interacts with VPS4A; the interaction suggests a heteromeric assembly with VPS4A. Interacts with VTA1 By similarity.

Subcellular location

Prevacuolar compartment membrane; Peripheral membrane protein By similarity. Late endosome membrane; Peripheral membrane protein By similarity. Note: Membrane-associated in the prevacuolar endosomal compartment By similarity.

Sequence similarities

Belongs to the AAA ATPase family.

Contains 1 MIT domain.

Ontologies

Keywords
   Biological processCell cycle
Cell division
Protein transport
Transport
   Cellular componentEndosome
Membrane
   DomainCoiled coil
   LigandATP-binding
Nucleotide-binding
   Molecular functionHydrolase
   PTMPhosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processcell cycle

Inferred from electronic annotation. Source: UniProtKB-KW

cell division

Inferred from electronic annotation. Source: UniProtKB-KW

protein transport

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentlate endosome membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

nucleoside-triphosphatase activity

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 444444Vacuolar protein sorting-associated protein 4B
PRO_0000331379

Regions

Domain4 – 8279MIT
Nucleotide binding174 – 1818ATP Potential
Coiled coil19 – 8264 Potential

Amino acid modifications

Modified residue931Phosphoserine By similarity
Modified residue1021Phosphoserine By similarity
Modified residue1081Phosphoserine By similarity

Sequences

Sequence LengthMass (Da)Tools
Q5R658 [UniParc].

Last modified December 21, 2004. Version 1.
Checksum: B6549F4E19C210F4

FASTA44449,330
        10         20         30         40         50         60 
MSSTSPNLQK AIDLASKAAQ EDKAGNYEEA LQLYQHAVQY FLHVVKYEAQ GDKAKQSIRA 

        70         80         90        100        110        120 
QCTEYLDRAE KLKEYLKNKE KKAQKPVKEG QPSPADEKGN DSDGEGESDD PEKKKLQNQL 

       130        140        150        160        170        180 
QGAIVIERPN VKWSDVAGLE GAKEALKEAV ILPIKFPHLF TGKRTPWRGI LLFGPPGTGK 

       190        200        210        220        230        240 
SYLAKAVATE ANNSTFFSIS SSDLVSKWLG ESEKLVKNLF QLARENKPSI IFIDEIDSLC 

       250        260        270        280        290        300 
GSRSENESEA ARRIKTEFLV QMRGVGVDND GILVLGATNI PWVLDSAIRR RFEKRIYIPL 

       310        320        330        340        350        360 
PEPHARAAMF KLHLGTTQNS LTEADFRELG RKTDGYSGAD ISIIVRDALM QPVRKVQSAT 

       370        380        390        400        410        420 
HFKKVRGPSR ADPNHLVDDL LTPCSPGDPG AIEMTWMDVP GDKLLEPVVS MSDMLRSLSN 

       430        440 
TKPTVNEHDL LKLKKFTEDF GQEG 

« Hide

References

[1]The German cDNA consortium
Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Brain cortex.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CR860638 mRNA. Translation: CAH92758.1.
RefSeqNP_001126608.1. NM_001133136.1.

3D structure databases

ProteinModelPortalQ5R658.
SMRQ5R658. Positions 6-108, 123-444.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID100173605.
KEGGpon:100173605.

Organism-specific databases

CTD9525.

Phylogenomic databases

HOGENOMHOG000225146.
HOVERGENHBG057074.
InParanoidQ5R658.
KOK12196.

Family and domain databases

Gene3D1.20.58.280. 1 hit.
3.40.50.300. 1 hit.
InterProIPR003593. AAA+_ATPase.
IPR003959. ATPase_AAA_core.
IPR003960. ATPase_AAA_CS.
IPR007330. MIT.
IPR027417. P-loop_NTPase.
IPR015415. Vps4_C.
[Graphical view]
PfamPF00004. AAA. 1 hit.
PF04212. MIT. 1 hit.
PF09336. Vps4_C. 1 hit.
[Graphical view]
SMARTSM00382. AAA. 1 hit.
SM00745. MIT. 1 hit.
[Graphical view]
SUPFAMSSF116846. SSF116846. 1 hit.
SSF52540. SSF52540. 1 hit.
PROSITEPS00674. AAA. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameVPS4B_PONAB
AccessionPrimary (citable) accession number: Q5R658
Entry history
Integrated into UniProtKB/Swiss-Prot: April 29, 2008
Last sequence update: December 21, 2004
Last modified: April 16, 2014
This is version 59 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families