RILP
Rab-interacting lysosomal protein
Also known as: FLJ31193, RILP_HUMAN
Cross-references: UniProt · Ensembl · Human Protein Atlas · GeneCards · NCBI Gene
Protein identityUniProt · HPA
- UniProt accession
- Q96NA2
- Gene
- RILP
- Ensembl
- ENSG00000167705
- Chromosome
- 17
- Canonical length
- 401 aa
- Protein class
- Predicted intracellular proteins
- Quaternary structure
- Homodimer
OverviewNCBI Gene
This gene encodes a lysosomal protein that interacts with RAB7, a small GTPase that controls transport to endocytic degradative compartments. Studies using mutant forms of the two proteins suggest that this protein represents a downstream effector for RAB7, and both proteins act together in the regulation of late endocytic traffic. A unique region of this protein has also been shown to be involved in the regulation of lysosomal morphology. [provided by RefSeq, Sep 2011]
Canonical amino-acid sequenceUniProt
401 residues, UniProt reviewed canonical sequence.
>Q96NA2|RILP
1 MEPRRAAPGV PGWGSREAAG SASAAELVYH LAGALGTELQ DLARRFGPEA AAGLVPLVVR
61 ALELLEQAAV GPAPDSLQVS AQPAEQELRR LREENERLRR ELRAGPQEER ALLRQLKEVT
121 DRQRDELRAH NRDLRQRGQE TEALQEQLQR LLLVNAELRH KLAAMQTQLR AAQDRERERQ
181 QPGEAATPQA KERARGQAGR PGHQHGQEPE WATAGAGAPG NPEDPAEAAQ QLGRPSEAGQ
241 CRFSREEFEQ ILQERNELKA KVFLLKEELA YFQRELLTDH RVPGLLLEAM KVAVRKQRKK
301 IKAKMLGTPE EAESSEDEAG PWILLSDDKG DHPPPPESKI QSFFGLWYRG KAESSEDETS
361 SPAPSKLGGE EEAQPQSPAP DPPCSALHEH LCLGASAAPE ALocalizationUniProt · AlphaFold · HPA
Whether an antibody against RILP can act on the native protein depends on physical access: surface and secreted proteins are reachable by circulating antibodies, intracellular proteins usually are not.
- Antibody reachability
- Other membrane
- Secreted
- No
- Transmembrane segments
- 0
- Mean surface accessibility (rSASA)
- 0.56
- Highest tissue expression
- 65 nTPM
Expression across tissuesHPA
Tissue
- heart muscle: 65 nTPM
- skeletal muscle: 52 nTPM
- liver: 33 nTPM
- thyroid gland: 31 nTPM
- adrenal gland: 20 nTPM
- adipose tissue: 18 nTPM
Single-cell type
- renal collecting duct intercalated cells: 14 nCPM
- distal convoluted tubule cells: 11 nCPM
- choroid plexus epithelial cells: 8.3 nCPM
- renal connecting tubule cells: 7.2 nCPM
- proximal tubule cells: 6.6 nCPM
- loop of henle epithelial cells: 5.5 nCPM
Immune cell
- classical monocyte: 3.5 nTPM
- neutrophil: 3.4 nTPM
- myeloid DC: 2.4 nTPM
- plasmacytoid DC: 1.3 nTPM
- intermediate monocyte: 1.2 nTPM
- eosinophil: 1 nTPM
Brain region
- choroid plexus: 22 nTPM
- cerebral cortex: 9.1 nTPM
- thalamus: 7.1 nTPM
- medulla oblongata: 6.6 nTPM
- amygdala: 6 nTPM
- midbrain: 6 nTPM
Genetic constraint and essentialitygnomAD · DepMap
Does the body need this protein intact? Low LOEUF or a strong DepMap dependency means loss or blockade of the protein is likely to be felt.
- gnomAD LOEUF (loss-of-function intolerance)
- 1.69
- gnomAD pLI
- 0
- gnomAD missense Z
- -0.02
- DepMap mean gene effect
- -0.31
- DepMap dependency class
- selective
Cancer expressionTCGA
Across TCGA tumor cohorts, this protein is over-expressed in roughly 4% of surveyed tumor types (aggregate summary; per-cohort expression, alteration, and survival load in the interactive view).
OntologyGO
Biological processes
- cilium assembly
- early endosome to late endosome transport
- endosome to lysosome transport
- endosome transport via multivesicular body sorting pathway
- intralumenal vesicle formation
- negative regulation of protein catabolic process
- positive regulation of protein catabolic process
- protein transport
Molecular functions
Cellular components
Protein domainsUniProt · Pfam · InterPro
KeywordsUniProt
InteractionsUniProt · HPA
Protein binding partners of RILP in the human serome: UniProt-annotated complex subunits plus reported interactors. Each links to its own Seroatlas record.
Antibody and autoantibody relevanceSeroatlas analysis
Seroatlas reads RILP as an antibody target. Whether an autoantibody or antibody against RILP could matter depends on whether native RILP is physically reachable, whether the body needs it intact, and whether it acts in a disease-relevant tissue.
RILP is annotated as predominantly intracellular. Intracellular proteins are common autoantibody markers, becoming visible to the immune system after cell injury or altered processing, but are usually markers of disease rather than direct drivers.
Annotation status
The present source text does not explicitly label RILP as an autoantigen. Seroatlas presents hypothesis context only and does not manufacture a known-serology claim.
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