Q8R361 · RFIP5_MOUSE
- ProteinRab11 family-interacting protein 5
- GeneRab11fip5
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids645 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
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 annotations | all molecular function | virus receptor activity | dna binding | rna binding | cytoskeletal motor activity | catalytic activity | gtpase activity | structural molecule activity | transporter activity | cytoskeletal protein binding | lipid binding | cyclase activity | antioxidant activity | oxidoreductase activity | transferase activity | hydrolase activity | lyase activity | isomerase activity | ligase activity | protein tag activity | cargo receptor activity | histone binding | protein folding chaperone | translation regulator activity | nutrient reservoir activity | receptor ligand activity | molecular transducer activity | molecular adaptor activity | toxin activity | cell adhesion mediator activity | molecular function regulator activity | virus coreceptor activity | catalytic activity, acting on a protein | catalytic activity, acting on dna | catalytic activity, acting on rna | molecular carrier activity | transcription regulator activity | general transcription initiation factor activity | molecular sensor activity | molecular sequestering activity | atp-dependent activity | other molecular function | all biological process | mitotic cell cycle | cytokinesis | cytoplasmic translation | immune system process | muscle system process | circulatory system process | renal system process | respiratory system process | carbohydrate metabolic process | generation of precursor metabolites and energy | dna replication | dna repair | dna recombination | chromatin organization | dna-templated transcription | regulation of dna-templated transcription | trna metabolic process | protein folding | protein glycosylation | amino acid metabolic process | modified amino acid metabolic process | lipid metabolic process | vitamin metabolic process | sulfur compound metabolic process | intracellular protein transport | nucleocytoplasmic transport | autophagy | inflammatory response | mitochondrion organization | cytoskeleton organization | microtubule-based movement | peroxisome organization | lysosome organization | chromosome segregation | cell adhesion | establishment or maintenance of cell polarity | programmed cell death | photosynthesis | mrna metabolic process | snrna metabolic process | vesicle-mediated transport | reproductive process | digestive system process | signaling | cell differentiation | protein catabolic process | extracellular matrix organization | regulatory ncrna-mediated gene silencing | telomere organization | cell junction organization | wound healing | ribosome biogenesis | cilium organization | anatomical structure development | cell motility | nervous system process | endocrine process | protein maturation | transmembrane transport | nucleobase-containing small molecule metabolic process | hepaticobiliary system process | membrane organization | protein-containing complex assembly | cell wall organization or biogenesis | nitrogen cycle metabolic process | protein localization to plasma membrane | defense response to other organism | detoxification | meiotic nuclear division | mitotic nuclear division | mitochondrial gene expression | carbohydrate derivative metabolic process | other biological process | all cellular component | nuclear chromosome | extracellular region | extracellular space | cell wall | nucleus | nuclear envelope | nucleoplasm | chromosome | nucleolus | mitochondrion | lysosome | endosome | vacuole | peroxisome | endoplasmic reticulum | golgi apparatus | lipid droplet | microtubule organizing center | cytosol | ribosome | cytoskeleton | plasma membrane | cilium | plastid | thylakoid | external encapsulating structure | extracellular matrix | cytoplasmic vesicle | organelle | other cellular component | |||
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Aspect | Term | |
---|---|---|
Cellular Component | early endosome | |
Cellular Component | early endosome membrane | |
Cellular Component | Golgi apparatus | |
Cellular Component | Golgi membrane | |
Cellular Component | mitochondrial outer membrane | |
Cellular Component | mitochondrion | |
Cellular Component | phagocytic vesicle | |
Cellular Component | postsynapse | |
Cellular Component | recycling endosome | |
Cellular Component | recycling endosome membrane | |
Cellular Component | secretory granule | |
Cellular Component | transport vesicle membrane | |
Molecular Function | gamma-tubulin binding | |
Molecular Function | small GTPase binding | |
Biological Process | cellular response to type II interferon | |
Biological Process | insulin secretion involved in cellular response to glucose stimulus | |
Biological Process | postsynaptic neurotransmitter receptor internalization | |
Biological Process | regulated exocytosis |
Keywords
- Biological process
Names & Taxonomy
Protein names
- Recommended nameRab11 family-interacting protein 5
- Short namesRab11-FIP5
- Alternative names
Gene names
Organism names
- Organism
- Strains
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Glires > Rodentia > Myomorpha > Muroidea > Muridae > Murinae > Mus > Mus
Accessions
- Primary accessionQ8R361
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
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
- Cellular component
PTM/Processing
Features
Showing features for chain, modified residue.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000097308 | 1-645 | Rab11 family-interacting protein 5 | |||
Sequence: MALVRDPEPAAGSSRWLPTHVQVTVLRASGLRGKSSGAGSTSDAYTVIQVGREKYSTSVVEKTQGCPEWCEECSFELPPGALDGLLRAQEADAGPAPWASGPNAACELVLTTMHRSLIGVDKFLGRATVALDEVFRAGRAQHTQWYRLHSKPGKKEKERGEIQVTIQFTRNNLSASMFDLSMKDKPRSPFSKLKDRVKGKKKYDLESASAILPSSALEDPELGSLGKMGKAKGFFLRNKLRKSSLTQSNTSLGSDSTLSSTSGSLVYQGPGAELLTRSPSHSSWLSTEGGRDSIQSPKLLTHKRTYSDEASQLRAAPPRALLELQGHLDGASRSSLCVNGSHVYNEEPQPPLRHRSSISGPFPPSSSLHSVPPRSSEEGSRSSDDSWGRGSHGTSSSEAVPGQEELSKQAKGASCSGEEEGARLPEGKPVQVATPMVASSEAVAAEKDRKPRMGLFHHHHHQGLSRSEQGRRGSVGEKGSPSLGASPHHSSTGEEKAKSSWFGLRESKEPTQKPSPHPVKPLTAAPVEASPDRKQPRTSLSTALSSGLERLKTVTSGGIQSVLPASQLGSSVDTKRPKDSAVLDQSAKYYHLTHDELIGLLLQRERELSQRDEHVQELESYIDRLLVRIMETSPTLLQISPGPPK | ||||||
Modified residue | 176 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 283 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 286 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 307 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 357 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 367 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 391 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 395 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 486 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 530 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 539 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 545 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 640 | Phosphoserine | ||||
Sequence: S |
Post-translational modification
Phosphorylated on serine and threonine residues. Phosphorylation at Ser-357 is PKA-dependent.
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Gene expression databases
Structure
Family & Domains
Features
Showing features for domain, region, compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 1-146 | C2 | ||||
Sequence: MALVRDPEPAAGSSRWLPTHVQVTVLRASGLRGKSSGAGSTSDAYTVIQVGREKYSTSVVEKTQGCPEWCEECSFELPPGALDGLLRAQEADAGPAPWASGPNAACELVLTTMHRSLIGVDKFLGRATVALDEVFRAGRAQHTQWY | ||||||
Region | 271-299 | Disordered | ||||
Sequence: GAELLTRSPSHSSWLSTEGGRDSIQSPKL | ||||||
Compositional bias | 275-294 | Polar residues | ||||
Sequence: LTRSPSHSSWLSTEGGRDSI | ||||||
Region | 341-550 | Disordered | ||||
Sequence: SHVYNEEPQPPLRHRSSISGPFPPSSSLHSVPPRSSEEGSRSSDDSWGRGSHGTSSSEAVPGQEELSKQAKGASCSGEEEGARLPEGKPVQVATPMVASSEAVAAEKDRKPRMGLFHHHHHQGLSRSEQGRRGSVGEKGSPSLGASPHHSSTGEEKAKSSWFGLRESKEPTQKPSPHPVKPLTAAPVEASPDRKQPRTSLSTALSSGLER | ||||||
Compositional bias | 359-377 | Polar residues | ||||
Sequence: SGPFPPSSSLHSVPPRSSE | ||||||
Compositional bias | 386-403 | Polar residues | ||||
Sequence: SWGRGSHGTSSSEAVPGQ | ||||||
Compositional bias | 534-550 | Polar residues | ||||
Sequence: KQPRTSLSTALSSGLER | ||||||
Domain | 578-640 | FIP-RBD | ||||
Sequence: KDSAVLDQSAKYYHLTHDELIGLLLQRERELSQRDEHVQELESYIDRLLVRIMETSPTLLQIS |
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 statusComplete
- Length645
- Mass (Da)69,553
- Last updated2003-08-22 v2
- ChecksumCBA713E9E68A042A
Computationally mapped potential isoform sequences
There is 1 potential isoform mapped to this entry
Entry | Entry name | Gene name | Length | ||
---|---|---|---|---|---|
A0A0N4SW73 | A0A0N4SW73_MOUSE | Rab11fip5 | 1318 |
Features
Showing features for compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 275-294 | Polar residues | ||||
Sequence: LTRSPSHSSWLSTEGGRDSI | ||||||
Compositional bias | 359-377 | Polar residues | ||||
Sequence: SGPFPPSSSLHSVPPRSSE | ||||||
Compositional bias | 386-403 | Polar residues | ||||
Sequence: SWGRGSHGTSSSEAVPGQ | ||||||
Compositional bias | 534-550 | Polar residues | ||||
Sequence: KQPRTSLSTALSSGLER |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
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 |