Q8R361 · RFIP5_MOUSE

  • Protein
    Rab11 family-interacting protein 5
  • Gene
    Rab11fip5
  • Status
    UniProtKB reviewed (Swiss-Prot)
  • Amino acids
  • Protein existence
    Evidence at protein level
  • Annotation score
    5/5

Function

function

Rab effector involved in protein trafficking from apical recycling endosomes to the apical plasma membrane. Involved in insulin granule exocytosis. May regulate V-ATPase intracellular transport in response to extracellular acidosis.

GO annotations

all annotationsall molecular functionvirus receptor activitydna bindingrna bindingcytoskeletal motor activitycatalytic activitygtpase activitystructural molecule activitytransporter activitycytoskeletal protein bindinglipid bindingcyclase activityantioxidant activityoxidoreductase activitytransferase activityhydrolase activitylyase activityisomerase activityligase activityprotein tag activitycargo receptor activityhistone bindingprotein folding chaperonetranslation regulator activitynutrient reservoir activityreceptor ligand activitymolecular transducer activitymolecular adaptor activitytoxin activitycell adhesion mediator activitymolecular function regulator activityvirus coreceptor activitycatalytic activity, acting on a proteincatalytic activity, acting on dnacatalytic activity, acting on rnamolecular carrier activitytranscription regulator activitygeneral transcription initiation factor activitymolecular sensor activitymolecular sequestering activityatp-dependent activityother molecular functionall biological processmitotic cell cyclecytokinesiscytoplasmic translationimmune system processmuscle system processcirculatory system processrenal system processrespiratory system processcarbohydrate metabolic processgeneration of precursor metabolites and energydna replicationdna repairdna recombinationchromatin organizationdna-templated transcriptionregulation of dna-templated transcriptiontrna metabolic processprotein foldingprotein glycosylationamino acid metabolic processmodified amino acid metabolic processlipid metabolic processvitamin metabolic processsulfur compound metabolic processintracellular protein transportnucleocytoplasmic transportautophagyinflammatory responsemitochondrion organizationcytoskeleton organizationmicrotubule-based movementperoxisome organizationlysosome organizationchromosome segregationcell adhesionestablishment or maintenance of cell polarityprogrammed cell deathphotosynthesismrna metabolic processsnrna metabolic processvesicle-mediated transportreproductive processdigestive system processsignalingcell differentiationprotein catabolic processextracellular matrix organizationregulatory ncrna-mediated gene silencingtelomere organizationcell junction organizationwound healingribosome biogenesiscilium organizationanatomical structure developmentcell motilitynervous system processendocrine processprotein maturationtransmembrane transportnucleobase-containing small molecule metabolic processhepaticobiliary system processmembrane organizationprotein-containing complex assemblycell wall organization or biogenesisnitrogen cycle metabolic processprotein localization to plasma membranedefense response to other organismdetoxificationmeiotic nuclear divisionmitotic nuclear divisionmitochondrial gene expressioncarbohydrate derivative metabolic processother biological processall cellular componentnuclear chromosomeextracellular regionextracellular spacecell wallnucleusnuclear envelopenucleoplasmchromosomenucleolusmitochondrionlysosomeendosomevacuoleperoxisomeendoplasmic reticulumgolgi apparatuslipid dropletmicrotubule organizing centercytosolribosomecytoskeletonplasma membraneciliumplastidthylakoidexternal encapsulating structureextracellular matrixcytoplasmic vesicleorganelleother cellular component
Cell color indicative of number of GO terms
AspectTerm
Cellular Componentearly endosome
Cellular Componentearly endosome membrane
Cellular ComponentGolgi apparatus
Cellular ComponentGolgi membrane
Cellular Componentmitochondrial outer membrane
Cellular Componentmitochondrion
Cellular Componentphagocytic vesicle
Cellular Componentpostsynapse
Cellular Componentrecycling endosome
Cellular Componentrecycling endosome membrane
Cellular Componentsecretory granule
Cellular Componenttransport vesicle membrane
Molecular Functiongamma-tubulin binding
Molecular Functionsmall GTPase binding
Biological Processcellular response to type II interferon
Biological Processinsulin secretion involved in cellular response to glucose stimulus
Biological Processpostsynaptic neurotransmitter receptor internalization
Biological Processregulated exocytosis

Keywords

Names & Taxonomy

Protein names

  • Recommended name
    Rab11 family-interacting protein 5
  • Short names
    Rab11-FIP5
  • Alternative names
    • Rab11-interacting protein Rip11

Gene names

    • Name
      Rab11fip5
    • Synonyms
      D6Ertd32e
      , GAF1
      , Rip11

Organism names

  • Taxonomic identifier
  • Strains
    • C57BL/6J
    • FVB/N
    • OF1
  • Taxonomic lineage
    Eukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Glires > Rodentia > Myomorpha > Muroidea > Muridae > Murinae > Mus > Mus

Accessions

  • Primary accession
    Q8R361
  • Secondary accessions
    • C4IXU4

Proteomes

Organism-specific databases

Subcellular Location

Cytoplasm
Recycling endosome membrane
; Peripheral membrane protein
Early endosome membrane
; Peripheral membrane protein
Golgi apparatus membrane
; Peripheral membrane protein
Cytoplasmic vesicle, secretory vesicle membrane
; Peripheral membrane protein
Mitochondrion membrane
; Peripheral membrane protein

Keywords

PTM/Processing

Features

Showing features for chain, modified residue.

TypeIDPosition(s)Description
ChainPRO_00000973081-645Rab11 family-interacting protein 5
Modified residue176Phosphoserine
Modified residue283Phosphoserine
Modified residue286Phosphoserine
Modified residue307Phosphoserine
Modified residue357Phosphoserine
Modified residue367Phosphoserine
Modified residue391Phosphoserine
Modified residue395Phosphoserine
Modified residue486Phosphoserine
Modified residue530Phosphoserine
Modified residue539Phosphoserine
Modified residue545Phosphoserine
Modified residue640Phosphoserine

Post-translational modification

Phosphorylated on serine and threonine residues. Phosphorylation at Ser-357 is PKA-dependent.

Keywords

Proteomic databases

PTM databases

Expression

Gene expression databases

Interaction

Subunit

Interacts with RAB11FIP4 (By similarity).
Interacts with NAPG (By similarity).
Interacts with RO60 (By similarity).
Interacts with RAB11A that has been activated by GTP binding (By similarity).

Protein-protein interaction databases

Miscellaneous

Structure

Family & Domains

Features

Showing features for domain, region, compositional bias.

TypeIDPosition(s)Description
Domain1-146C2
Region271-299Disordered
Compositional bias275-294Polar residues
Region341-550Disordered
Compositional bias359-377Polar residues
Compositional bias386-403Polar residues
Compositional bias534-550Polar residues
Domain578-640FIP-RBD

Domain

Binds to vesicles enriched in neutral phospholipids via its C2 domain. The interaction is favored by Mg2+ rather than Ca2+ (By similarity).

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    645
  • Mass (Da)
    69,553
  • Last updated
    2003-08-22 v2
  • Checksum
    CBA713E9E68A042A
MALVRDPEPAAGSSRWLPTHVQVTVLRASGLRGKSSGAGSTSDAYTVIQVGREKYSTSVVEKTQGCPEWCEECSFELPPGALDGLLRAQEADAGPAPWASGPNAACELVLTTMHRSLIGVDKFLGRATVALDEVFRAGRAQHTQWYRLHSKPGKKEKERGEIQVTIQFTRNNLSASMFDLSMKDKPRSPFSKLKDRVKGKKKYDLESASAILPSSALEDPELGSLGKMGKAKGFFLRNKLRKSSLTQSNTSLGSDSTLSSTSGSLVYQGPGAELLTRSPSHSSWLSTEGGRDSIQSPKLLTHKRTYSDEASQLRAAPPRALLELQGHLDGASRSSLCVNGSHVYNEEPQPPLRHRSSISGPFPPSSSLHSVPPRSSEEGSRSSDDSWGRGSHGTSSSEAVPGQEELSKQAKGASCSGEEEGARLPEGKPVQVATPMVASSEAVAAEKDRKPRMGLFHHHHHQGLSRSEQGRRGSVGEKGSPSLGASPHHSSTGEEKAKSSWFGLRESKEPTQKPSPHPVKPLTAAPVEASPDRKQPRTSLSTALSSGLERLKTVTSGGIQSVLPASQLGSSVDTKRPKDSAVLDQSAKYYHLTHDELIGLLLQRERELSQRDEHVQELESYIDRLLVRIMETSPTLLQISPGPPK

Computationally mapped potential isoform sequences

There is 1 potential isoform mapped to this entry

View all
EntryEntry nameGene nameLength
A0A0N4SW73A0A0N4SW73_MOUSERab11fip51318

Features

Showing features for compositional bias.

TypeIDPosition(s)Description
Compositional bias275-294Polar residues
Compositional bias359-377Polar residues
Compositional bias386-403Polar residues
Compositional bias534-550Polar residues

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
AC153605
EMBL· GenBank· DDBJ
-Genomic DNA No translation available.
AC155728
EMBL· GenBank· DDBJ
-Genomic DNA No translation available.
BC026473
EMBL· GenBank· DDBJ
AAH26473.1
EMBL· GenBank· DDBJ
mRNA
BC044833
EMBL· GenBank· DDBJ
AAH44833.2
EMBL· GenBank· DDBJ
mRNA
BC051063
EMBL· GenBank· DDBJ
AAH51063.3
EMBL· GenBank· DDBJ
mRNA
BC141380
EMBL· GenBank· DDBJ
AAI41381.1
EMBL· GenBank· DDBJ
mRNA

Genome annotation databases

Similar Proteins

Disclaimer

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