Q5M9G3 · CAPR1_RAT
- ProteinCaprin-1
- GeneCaprin1
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids707 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
mRNA-binding protein that acts as a regulator of mRNAs transport, translation and/or stability, and which is involved in neurogenesis, synaptic plasticity in neurons and cell proliferation and migration in multiple cell types (PubMed:15858068, PubMed:20516077).
Plays an essential role in cytoplasmic stress granule formation (By similarity).
Acts as an mRNA regulator by mediating formation of some phase-separated membraneless compartment: undergoes liquid-liquid phase separation upon binding to target mRNAs, leading to assemble mRNAs into cytoplasmic ribonucleoprotein granules that concentrate mRNAs with associated regulatory factors (By similarity).
Undergoes liquid-liquid phase separation following phosphorylation and interaction with FMR1, promoting formation of cytoplasmic ribonucleoprotein granules that concentrate mRNAs with factors that inhibit translation and mediate deadenylation of target mRNAs (By similarity).
In these cytoplasmic ribonucleoprotein granules, CAPRIN1 mediates recruitment of CNOT7 deadenylase, leading to mRNA deadenylation and degradation (By similarity).
Binds directly and selectively to MYC and CCND2 mRNAs (By similarity).
In neuronal cells, directly binds to several mRNAs associated with RNA granules, including BDNF, CAMK2A, CREB1, MAP2, NTRK2 mRNAs, as well as to GRIN1 and KPNB1 mRNAs, but not to rRNAs (By similarity).
Plays an essential role in cytoplasmic stress granule formation (By similarity).
Acts as an mRNA regulator by mediating formation of some phase-separated membraneless compartment: undergoes liquid-liquid phase separation upon binding to target mRNAs, leading to assemble mRNAs into cytoplasmic ribonucleoprotein granules that concentrate mRNAs with associated regulatory factors (By similarity).
Undergoes liquid-liquid phase separation following phosphorylation and interaction with FMR1, promoting formation of cytoplasmic ribonucleoprotein granules that concentrate mRNAs with factors that inhibit translation and mediate deadenylation of target mRNAs (By similarity).
In these cytoplasmic ribonucleoprotein granules, CAPRIN1 mediates recruitment of CNOT7 deadenylase, leading to mRNA deadenylation and degradation (By similarity).
Binds directly and selectively to MYC and CCND2 mRNAs (By similarity).
In neuronal cells, directly binds to several mRNAs associated with RNA granules, including BDNF, CAMK2A, CREB1, MAP2, NTRK2 mRNAs, as well as to GRIN1 and KPNB1 mRNAs, but not to rRNAs (By similarity).
Activity regulation
Ability to mediate liquid-liquid phase separation is regulated by ATP: moderate concentrations of ATP enhance phase separation, whereas high concentrations of ATP lead to inhibition of phase separation.
GO annotations
Keywords
- Molecular function
- Biological process
- Ligand
Names & Taxonomy
Protein names
- Recommended nameCaprin-1
- Alternative names
Gene names
Organism names
- Organism
- Strains
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Glires > Rodentia > Myomorpha > Muroidea > Muridae > Murinae > Rattus
Accessions
- Primary accessionQ5M9G3
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Note: Mediates formation and localizes to cytoplasmic ribonucleoprotein membraneless compartments. Associated with RNA granules. At the leading edge of migrating fibroblasts, colocalizes with DDX3X.
Keywords
- Cellular component
PTM/Processing
Features
Showing features for initiator methionine, modified residue, chain, glycosylation.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Initiator methionine | 1 | Removed | ||||
Sequence: M | ||||||
Modified residue | 2 | N-acetylproline | ||||
Sequence: P | ||||||
Chain | PRO_0000327209 | 2-707 | Caprin-1 | |||
Sequence: PSATSHSGSGSKSSGPPPPSGSSGSEAAAGAAAPASQHPATGTGAVQTEAMKQILGVIDKKLRNLEKKKGKLDDYQERMNKGERLNQDQLDAVSKYQEVTNNLEFAKELQRSFMALSQDIQKTIKKTARREQLMREEAEQKRLKTVLELQYVLDKLGDDDVRTDLKQGLSGVPILSEEELSLLDEFYKLVDPERDMSLRLNEQYEHASIHLWDLLEGKEKPVCGTTYKALKEIVERVFQSNYFDSTHNHQNGLCEEEEAASAPIVEDQVAEAEPEPTEEYTEQSEVESTEYVNRQFMAETQFSSGEKEQVDEWAVETVEVVNSLQQQPQAASPSVPEPHSLTPVAQSDPLVRRQRVQDLMAQMQGPYNFIQDSMLDFENQTLDPAIVSAQPMNPTQNMDMPQLVCPQVHSESRLAQSNQVPVQPEATQVPLVSSTSEGYTASQPLYQPSHAAEQRPQKEPIDQIQATISLNTEQTTASSSLPAASQPQVFQAGASKPLHSSGINVNAAPFQSMQTVFNMNAPVPPVNEPETLKQQSQYQASYNQSFSSQPHQVEQTELQQDQLQTVVGTYHGSQDQPHQVPGNHQQPPQQSTGFPRSSQPYYNSRGVSRGGSRGARGLMNGYRGPANGFRGGYDGYRSSFSNTPNSGYTQSQFNAPRDYSGYQRDGYQQNFKRGSGQSGPRGAPRGRGGPPRPNRGMPQMNTQQVN | ||||||
Modified residue | 10 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 113 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 163 | Omega-N-methylarginine | ||||
Sequence: R | ||||||
Modified residue | 333 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 341 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 623 | Phosphotyrosine | ||||
Sequence: Y | ||||||
Modified residue | 624 | Omega-N-methylarginine | ||||
Sequence: R | ||||||
Modified residue | 631 | Omega-N-methylarginine | ||||
Sequence: R | ||||||
Modified residue | 634 | Phosphotyrosine | ||||
Sequence: Y | ||||||
Modified residue | 637 | Phosphotyrosine | ||||
Sequence: Y | ||||||
Modified residue | 638 | Omega-N-methylarginine | ||||
Sequence: R | ||||||
Glycosylation | 642 | O-linked (GlcNAc) serine | ||||
Sequence: S | ||||||
Glycosylation | 647 | O-linked (GlcNAc) serine | ||||
Sequence: S | ||||||
Modified residue | 649 | Phosphotyrosine | ||||
Sequence: Y | ||||||
Modified residue | 660 | Phosphotyrosine | ||||
Sequence: Y | ||||||
Modified residue | 663 | Phosphotyrosine | ||||
Sequence: Y | ||||||
Modified residue | 668 | Phosphotyrosine | ||||
Sequence: Y | ||||||
Modified residue | 696 | Asymmetric dimethylarginine; alternate | ||||
Sequence: R | ||||||
Modified residue | 696 | Omega-N-methylarginine; alternate | ||||
Sequence: R |
Post-translational modification
Tyrosine phosphorylation by EPHA4 promotes interaction with FMR1 and liquid-liquid phase separation (LLPS) for the formation of a membraneless compartment that concentrates mRNAs with associated regulatory factors.
O-glycosylated (O-GlcNAcylated), in a cell cycle-dependent manner. O-glycosylation by OGT inhibit ability to undergo liquid-liquid phase separation (LLPS).
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Tissue specificity
Expressed in hippocampal and neocortical pyramidal neurons, but not in Purkinje cells.
Induction
Down-regulated by exposure to trichloroethylene (TCE) and dichloroethylene (DCE) in fetal heart.
Gene expression databases
Interaction
Subunit
May form homomultimers. Interacts with G3BP1; interaction is direct and promotes stress granule formation. Interacts with G3BP2; interaction is direct and promotes stress granule formation. Interacts with PQBP1. Interacts with DDX3X. Interacts (when phosphorylated by EPHA4) with FMR1; interaction with FMR1 promotes formation of a membraneless compartment.
Protein-protein interaction databases
Structure
Family & Domains
Features
Showing features for compositional bias, region, coiled coil.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 1-22 | Polar residues | ||||
Sequence: MPSATSHSGSGSKSSGPPPPSG | ||||||
Region | 1-48 | Disordered | ||||
Sequence: MPSATSHSGSGSKSSGPPPPSGSSGSEAAAGAAAPASQHPATGTGAVQ | ||||||
Coiled coil | 58-92 | |||||
Sequence: VIDKKLRNLEKKKGKLDDYQERMNKGERLNQDQLD | ||||||
Coiled coil | 123-151 | |||||
Sequence: KTIKKTARREQLMREEAEQKRLKTVLELQ | ||||||
Compositional bias | 325-342 | Polar residues | ||||
Sequence: LQQQPQAASPSVPEPHSL | ||||||
Region | 325-347 | Disordered | ||||
Sequence: LQQQPQAASPSVPEPHSLTPVAQ | ||||||
Region | 358-379 | G3BP1-binding | ||||
Sequence: QDLMAQMQGPYNFIQDSMLDFE | ||||||
Region | 412-443 | Disordered | ||||
Sequence: ESRLAQSNQVPVQPEATQVPLVSSTSEGYTAS | ||||||
Region | 523-558 | Disordered | ||||
Sequence: PVPPVNEPETLKQQSQYQASYNQSFSSQPHQVEQTE | ||||||
Compositional bias | 530-558 | Polar residues | ||||
Sequence: PETLKQQSQYQASYNQSFSSQPHQVEQTE | ||||||
Compositional bias | 570-607 | Polar residues | ||||
Sequence: TYHGSQDQPHQVPGNHQQPPQQSTGFPRSSQPYYNSRG | ||||||
Region | 570-620 | Disordered | ||||
Sequence: TYHGSQDQPHQVPGNHQQPPQQSTGFPRSSQPYYNSRGVSRGGSRGARGLM | ||||||
Compositional bias | 641-677 | Polar residues | ||||
Sequence: FSNTPNSGYTQSQFNAPRDYSGYQRDGYQQNFKRGSG | ||||||
Region | 641-707 | Disordered | ||||
Sequence: FSNTPNSGYTQSQFNAPRDYSGYQRDGYQQNFKRGSGQSGPRGAPRGRGGPPRPNRGMPQMNTQQVN |
Domain
The C-terminal disordered region undergoes liquid-liquid phase separation (LLPS) for the formation of a membraneless compartment that concentrates mRNAs with associated regulatory factors. CAPRIN1 molecules in the condensed phase are neutral. mRNA-binding promotes phase separation. Moderate concentrations of ATP enhance phase separation by reducing the electrostatic potential of CAPRIN1, thereby promoting intermolecular interactions. In contrast, high concentrations of ATP invert the electrostatic potential of CAPRIN1, so that CAPRIN1 molecules become negatively charged, lead to inhibition of phase separation.
Sequence similarities
Belongs to the caprin family.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length707
- Mass (Da)78,121
- Last updated2008-04-08 v2
- Checksum3F0859BC83403242
Computationally mapped potential isoform sequences
There is 1 potential isoform mapped to this entry
Entry | Entry name | Gene name | Length | ||
---|---|---|---|---|---|
A0A8L2Q6N7 | A0A8L2Q6N7_RAT | Caprin1 | 720 |
Sequence caution
Features
Showing features for compositional bias, sequence conflict.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 1-22 | Polar residues | ||||
Sequence: MPSATSHSGSGSKSSGPPPPSG | ||||||
Sequence conflict | 27 | in Ref. 4; AAO21306 | ||||
Sequence: E → K | ||||||
Sequence conflict | 48 | in Ref. 4; AAO21306 | ||||
Sequence: Q → E | ||||||
Compositional bias | 325-342 | Polar residues | ||||
Sequence: LQQQPQAASPSVPEPHSL | ||||||
Sequence conflict | 372 | in Ref. 4; AAO21306 | ||||
Sequence: Q → Y | ||||||
Sequence conflict | 396 | in Ref. 4; AAO21306 | ||||
Sequence: T → A | ||||||
Compositional bias | 530-558 | Polar residues | ||||
Sequence: PETLKQQSQYQASYNQSFSSQPHQVEQTE | ||||||
Sequence conflict | 537 | in Ref. 4; AAO21306 | ||||
Sequence: S → N | ||||||
Sequence conflict | 557 | in Ref. 4; AAO21306 | ||||
Sequence: T → Q | ||||||
Compositional bias | 570-607 | Polar residues | ||||
Sequence: TYHGSQDQPHQVPGNHQQPPQQSTGFPRSSQPYYNSRG | ||||||
Sequence conflict | 571 | in Ref. 4; AAO21306 | ||||
Sequence: Y → F | ||||||
Sequence conflict | 582 | in Ref. 4; AAO21306 | ||||
Sequence: P → L | ||||||
Sequence conflict | 587-588 | in Ref. 4; AAO21306 | ||||
Sequence: QP → AA | ||||||
Compositional bias | 641-677 | Polar residues | ||||
Sequence: FSNTPNSGYTQSQFNAPRDYSGYQRDGYQQNFKRGSG |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AB373991 EMBL· GenBank· DDBJ | BAF98181.1 EMBL· GenBank· DDBJ | mRNA | ||
AABR03028010 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
AABR03028081 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
AABR03029653 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
BC087123 EMBL· GenBank· DDBJ | AAH87123.1 EMBL· GenBank· DDBJ | mRNA | ||
AY155572 EMBL· GenBank· DDBJ | AAO21306.1 EMBL· GenBank· DDBJ | mRNA | Different initiation |