A3LX75 · VPS27_PICST

Function

function

Component of the ESCRT-0 complex which is the sorting receptor for ubiquitinated cargo proteins at the multivesicular body (MVB) and recruits ESCRT-I to the MVB outer membrane.

Features

Showing features for binding site.

1732100200300400500600700
TypeIDPosition(s)Description
Binding site193Zn2+ 1 (UniProtKB | ChEBI)
Binding site196Zn2+ 1 (UniProtKB | ChEBI)
Binding site209Zn2+ 2 (UniProtKB | ChEBI)
Binding site212Zn2+ 2 (UniProtKB | ChEBI)
Binding site217Zn2+ 1 (UniProtKB | ChEBI)
Binding site220Zn2+ 1 (UniProtKB | ChEBI)
Binding site239Zn2+ 2 (UniProtKB | ChEBI)
Binding site242Zn2+ 2 (UniProtKB | ChEBI)

GO annotations

AspectTerm
Cellular Componentendosome membrane
Cellular ComponentESCRT-0 complex
Molecular Functionmetal ion binding
Molecular Functionphosphatidylinositol-3-phosphate binding
Molecular Functionubiquitin binding
Biological Processprotein targeting to vacuole
Biological Processprotein transport to vacuole involved in ubiquitin-dependent protein catabolic process via the multivesicular body sorting pathway

Keywords

Names & Taxonomy

Protein names

  • Recommended name
    Vacuolar protein sorting-associated protein 27

Gene names

    • Name
      VPS27
    • ORF names
      PICST_36619

Organism names

Accessions

  • Primary accession
    A3LX75

Proteomes

Subcellular Location

Endosome membrane
; Peripheral membrane protein

Keywords

PTM/Processing

Features

Showing features for chain.

TypeIDPosition(s)Description
ChainPRO_00002925221-732Vacuolar protein sorting-associated protein 27

Interaction

Subunit

Component of the ESCRT-0 complex composed of HSE1 and VPS27.

Protein-protein interaction databases

Structure

Family & Domains

Features

Showing features for domain, zinc finger, region, compositional bias.

Type
IDPosition(s)Description
Domain23-166VHS
Zinc finger187-247FYVE-type; atypical
Region245-272Disordered
Compositional bias246-263Polar residues
Domain271-290UIM 1
Region287-316Disordered
Domain313-332UIM 2
Region329-357Disordered
Region483-732Disordered
Compositional bias491-570Polar residues
Compositional bias590-633Polar residues
Compositional bias686-717Polar residues

Domain

The FYVE domain is involved in the binding to phosphatidylinositol 3-phosphate (PtdIns3P) which is required for the association to endosomal membranes.
Both IUM domains are necessary for efficient binding to ubiquitin.

Sequence similarities

Belongs to the VPS27 family.

Keywords

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    732
  • Mass (Da)
    83,145
  • Last updated
    2007-07-24 v2
  • MD5 Checksum
    8939CFF5F72216F7539E2DA57B47C4C1
MSWFGSSSDSTIELDNKIQEATSESIPNGELDLPLALEVTDLIRSKSLPPIQCMRSLKKRLGMTYSNPNLLSSTLKLVDLCIKNCGSHFLNEIASKEFMDYLVDFIFKVHYDTKNYQVRNSEAKMNVGELILSLIKEWSILFSNSSDLSYVTRCFERLESEAYNFPDFAETSALNSKFVDTEVPPDWVDDDKCMICYDKFSMINRKHHCRACGGVFCQTHSSNFIPLVSLGISKPVRACDNCLAKQKSKNKPSQHNSSSHSRGTSRVQEDDEDEMLRKAIELSLQDTQIPVSAPVARDAPTNSSQTKTITDEDDDEDLKAAIAASMKDYQDQERLREEQQKQWQQEQEEKHHQEEQSDFYNYSIPKPSNYSQQLPYVQSVASLTEEEEADINKFITLMYQVKNDQNISYARLHDEKLTDLHTKVCPLRSKVTKNLIYTVERQKAFTELNNKIAAITRLYEEHLDSKLKQTYGYQQSVPPVQLPEINDYMRGPQSNYEQSIPAQGTGYQQQAGYVHPETTGYPSYPGGQQPIPQQPIAQQPSGSRPSAQQAQKAPEQKHEQQQTSVPTFAYPPQESYPPEGEDDEEQSNFELPPLPNQAQNDFSYPPTQSYDSPSEPMYPNDSTDQQYNVYPPNGAGSEESKDEYSSGELQPVQPTREHVLRTRSSELPPHAVEQASARFPPIDTVEEEYQNSNNSSVPYPDVSFPIAPTQNLQPQQEPPKKFVPEPEPLIDI

Features

Showing features for compositional bias.

TypeIDPosition(s)Description
Compositional bias246-263Polar residues
Compositional bias491-570Polar residues
Compositional bias590-633Polar residues
Compositional bias686-717Polar residues

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
CP000500
EMBL· GenBank· DDBJ
ABN67754.2
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

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