P41219 · PERI_HUMAN
- ProteinPeripherin
- GenePRPH
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids470 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Class-III neuronal intermediate filament protein (By similarity).
May form an independent structural network without the involvement of other neurofilaments or may cooperate with the neuronal intermediate filament proteins NEFL, NEFH, NEFM and INA to form a filamentous network (PubMed:15322088, PubMed:15446584).
Assembly of the neuronal intermediate filaments may be regulated by RAB7A (By similarity).
Plays a role in the development of unmyelinated sensory neurons (By similarity).
May be involved in axon elongation and axon regeneration after injury (By similarity).
Inhibits neurite extension in type II spiral ganglion neurons in the cochlea (By similarity).
May form an independent structural network without the involvement of other neurofilaments or may cooperate with the neuronal intermediate filament proteins NEFL, NEFH, NEFM and INA to form a filamentous network (PubMed:15322088, PubMed:15446584).
Assembly of the neuronal intermediate filaments may be regulated by RAB7A (By similarity).
Plays a role in the development of unmyelinated sensory neurons (By similarity).
May be involved in axon elongation and axon regeneration after injury (By similarity).
Inhibits neurite extension in type II spiral ganglion neurons in the cochlea (By similarity).
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 | axon | |
Cellular Component | cytoplasm | |
Cellular Component | extracellular exosome | |
Cellular Component | intermediate filament | |
Cellular Component | membrane | |
Cellular Component | perikaryon | |
Cellular Component | plasma membrane | |
Cellular Component | type III intermediate filament | |
Molecular Function | structural molecule activity |
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended namePeripherin
- Alternative names
Gene names
Organism names
- Organism
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Hominidae > Homo
Accessions
- Primary accessionP41219
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Keywords
- Cellular component
Disease & Variants
Involvement in disease
Amyotrophic lateral sclerosis (ALS)
- Note
- DescriptionA neurodegenerative disorder affecting upper motor neurons in the brain and lower motor neurons in the brain stem and spinal cord, resulting in fatal paralysis. Sensory abnormalities are absent. The pathologic hallmarks of the disease include pallor of the corticospinal tract due to loss of motor neurons, presence of ubiquitin-positive inclusions within surviving motor neurons, and deposition of pathologic aggregates. The etiology of amyotrophic lateral sclerosis is likely to be multifactorial, involving both genetic and environmental factors. The disease is inherited in 5-10% of the cases.
- See alsoMIM:105400
Natural variants in ALS
Variant ID | Position(s) | Change | Description | |
---|---|---|---|---|
VAR_083259 | 133 | R>P | in ALS; uncertain significance; dbSNP:rs267607528 | |
VAR_083260 | 141 | D>Y | in ALS; uncertain significance; leads to filamentous aggregate formation; dbSNP:rs58599399 |
Features
Showing features for natural variant.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Natural variant | VAR_083259 | 133 | in ALS; uncertain significance; dbSNP:rs267607528 | |||
Sequence: R → P | ||||||
Natural variant | VAR_083260 | 141 | in ALS; uncertain significance; leads to filamentous aggregate formation; dbSNP:rs58599399 | |||
Sequence: D → Y |
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 589 variants from UniProt as well as other sources including ClinVar and dbSNP.
Keywords
- Disease
Organism-specific databases
Miscellaneous
Genetic variation databases
PTM/Processing
Features
Showing features for chain, modified residue, modified residue (large scale data).
Type | ID | Position(s) | Source | Description | |||
---|---|---|---|---|---|---|---|
Chain | PRO_0000063779 | 1-470 | UniProt | Peripherin | |||
Sequence: MSHHPSGLRAGFSSTSYRRTFGPPPSLSPGAFSYSSSSRFSSSRLLGSASPSSSVRLGSFRSPRAGAGALLRLPSERLDFSMAEALNQEFLATRSNEKQELQELNDRFANFIEKVRFLEQQNAALRGELSQARGQEPARADQLCQQELRELRRELELLGRERDRVQVERDGLAEDLAALKQRLEEETRKREDAEHNLVLFRKDVDDATLSRLELERKIESLMDEIEFLKKLHEEELRDLQVSVESQQVQQVEVEATVKPELTAALRDIRAQYESIAAKNLQEAEEWYKSKYADLSDAANRNHEALRQAKQEMNESRRQIQSLTCEVDGLRGTNEALLRQLRELEEQFALEAGGYQAGAARLEEELRQLKEEMARHLREYQELLNVKMALDIEIATYRKLLEGEESRISVPVHSFASLNIKTTVPEVEPPQDSHSRKTVLIKTIETRNGEVVTESQKEQRSELDKSSAHSY | |||||||
Modified residue | 17 | UniProt | 3'-nitrotyrosine | ||||
Sequence: Y | |||||||
Modified residue | 28 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 28 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 48 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 50 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 50 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 59 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 379 | UniProt | 3'-nitrotyrosine | ||||
Sequence: Y | |||||||
Modified residue | 470 | UniProt | Phosphotyrosine | ||||
Sequence: Y |
Post-translational modification
Phosphorylated; phosphorylation increases after nerve injury in regenerating neurons.
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Tissue specificity
Expressed in the neurons of the outer hair cells in the organ of Corti and to a lesser extent in type I spiral ganglion cells.
Gene expression databases
Organism-specific databases
Interaction
Subunit
Forms homodimers (in vitro) (By similarity).
Homopolymerizes into a filamentous network (in vitro) (PubMed:15446584).
Forms heterodimers with NEFL, NEFM or NEFH (in vitro) (By similarity).
Interacts with DST (via C-terminus) (By similarity).
Interacts with RAB7A; the interaction is direct (PubMed:23179371).
Interacts with PRKCE (via phorbol-ester/DAG-type 2 domain) (PubMed:18408015).
Homopolymerizes into a filamentous network (in vitro) (PubMed:15446584).
Forms heterodimers with NEFL, NEFM or NEFH (in vitro) (By similarity).
Interacts with DST (via C-terminus) (By similarity).
Interacts with RAB7A; the interaction is direct (PubMed:23179371).
Interacts with PRKCE (via phorbol-ester/DAG-type 2 domain) (PubMed:18408015).
Binary interactions
Protein-protein interaction databases
Miscellaneous
Structure
Family & Domains
Features
Showing features for region, domain, compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 1-99 | Head | ||||
Sequence: MSHHPSGLRAGFSSTSYRRTFGPPPSLSPGAFSYSSSSRFSSSRLLGSASPSSSVRLGSFRSPRAGAGALLRLPSERLDFSMAEALNQEFLATRSNEKQ | ||||||
Domain | 97-407 | IF rod | ||||
Sequence: EKQELQELNDRFANFIEKVRFLEQQNAALRGELSQARGQEPARADQLCQQELRELRRELELLGRERDRVQVERDGLAEDLAALKQRLEEETRKREDAEHNLVLFRKDVDDATLSRLELERKIESLMDEIEFLKKLHEEELRDLQVSVESQQVQQVEVEATVKPELTAALRDIRAQYESIAAKNLQEAEEWYKSKYADLSDAANRNHEALRQAKQEMNESRRQIQSLTCEVDGLRGTNEALLRQLRELEEQFALEAGGYQAGAARLEEELRQLKEEMARHLREYQELLNVKMALDIEIATYRKLLEGEESRI | ||||||
Region | 100-132 | Coil 1A | ||||
Sequence: ELQELNDRFANFIEKVRFLEQQNAALRGELSQA | ||||||
Region | 133-143 | Linker 1 | ||||
Sequence: RGQEPARADQL | ||||||
Region | 144-239 | Coil 1B | ||||
Sequence: CQQELRELRRELELLGRERDRVQVERDGLAEDLAALKQRLEEETRKREDAEHNLVLFRKDVDDATLSRLELERKIESLMDEIEFLKKLHEEELRDL | ||||||
Region | 240-262 | Linker 2 | ||||
Sequence: QVSVESQQVQQVEVEATVKPELT | ||||||
Region | 263-405 | Coil 2 | ||||
Sequence: AALRDIRAQYESIAAKNLQEAEEWYKSKYADLSDAANRNHEALRQAKQEMNESRRQIQSLTCEVDGLRGTNEALLRQLRELEEQFALEAGGYQAGAARLEEELRQLKEEMARHLREYQELLNVKMALDIEIATYRKLLEGEES | ||||||
Region | 406-470 | Tail | ||||
Sequence: RISVPVHSFASLNIKTTVPEVEPPQDSHSRKTVLIKTIETRNGEVVTESQKEQRSELDKSSAHSY | ||||||
Region | 447-470 | Disordered | ||||
Sequence: NGEVVTESQKEQRSELDKSSAHSY | ||||||
Compositional bias | 450-470 | Basic and acidic residues | ||||
Sequence: VVTESQKEQRSELDKSSAHSY |
Sequence similarities
Belongs to the intermediate filament family.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence & Isoform
- Sequence statusComplete
This entry describes 2 isoforms produced by Alternative splicing.
P41219-1
This isoform has been chosen as the canonical sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
- Name1
- Length470
- Mass (Da)53,651
- Last updated2006-10-31 v2
- Checksum4ABEAB96088719D6
P41219-2
- Name2
- NoteGene prediction based on similarity to orthologs.
- Differences from canonical
- 449-449: E → EQ
Computationally mapped potential isoform sequences
There are 2 potential isoforms mapped to this entry
Features
Showing features for sequence conflict, alternative sequence, compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Sequence conflict | 68 | in Ref. 1; AAA60190 | ||||
Sequence: G → R | ||||||
Alternative sequence | VSP_021159 | 449 | in isoform 2 | |||
Sequence: E → EQ | ||||||
Compositional bias | 450-470 | Basic and acidic residues | ||||
Sequence: VVTESQKEQRSELDKSSAHSY |
Keywords
- Coding sequence diversity
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
L14565 EMBL· GenBank· DDBJ | AAA60190.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AC125611 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
BC032703 EMBL· GenBank· DDBJ | AAH32703.1 EMBL· GenBank· DDBJ | mRNA |