Q5M9G3 · CAPR1_RAT

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).

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

AspectTerm
Cellular Componentcell leading edge
Cellular Componentcytoplasm
Cellular Componentcytoplasmic stress granule
Cellular Componentcytosol
Cellular Componentdendrite
Cellular Componentglutamatergic synapse
Cellular Componentintracellular non-membrane-bounded organelle
Cellular Componentlamellipodium
Cellular ComponentP-body
Cellular Componentpostsynapse
Cellular Componentsynapse
Molecular FunctionATP binding
Molecular Functionmolecular condensate scaffold activity
Molecular Functionmolecular function activator activity
Molecular FunctionmRNA binding
Molecular FunctionRNA binding
Molecular Functionsignaling adaptor activity
Biological Processgeneration of neurons
Biological Processintracellular mRNA localization
Biological Processnegative regulation of translation
Biological Processnervous system development
Biological Processnon-membrane-bounded organelle assembly
Biological Processpositive regulation of dendrite morphogenesis
Biological Processpositive regulation of dendritic spine morphogenesis
Biological Processpositive regulation of stress granule assembly
Biological Processregulation of deadenylation-dependent decapping of nuclear-transcribed mRNA
Biological Processsynapse assembly
Biological Processsynapse organization

Keywords

Names & Taxonomy

Protein names

  • Recommended name
    Caprin-1
  • Alternative names
    • Cytoplasmic activation- and proliferation-associated protein 1
    • GPI-anchored protein p137 (GPI-p137; p137GPI)
    • RNA granule protein 105

Gene names

    • Name
      Caprin1
    • Synonyms
      Gpiap1, Rng105

Organism names

  • Taxonomic identifier
  • Strains
    • Brown Norway
    • Sprague-Dawley
  • Taxonomic lineage
    Eukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Glires > Rodentia > Myomorpha > Muroidea > Muridae > Murinae > Rattus

Accessions

  • Primary accession
    Q5M9G3
  • Secondary accessions
    • A9ZSZ9
    • Q6YF16

Proteomes

Organism-specific databases

Subcellular Location

Cytoplasm, cytosol
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

PTM/Processing

Features

Showing features for initiator methionine, modified residue, chain, glycosylation.

TypeIDPosition(s)Description
Initiator methionine1Removed
Modified residue2N-acetylproline
ChainPRO_00003272092-707Caprin-1
Modified residue10Phosphoserine
Modified residue113Phosphoserine
Modified residue163Omega-N-methylarginine
Modified residue333Phosphoserine
Modified residue341Phosphoserine
Modified residue623Phosphotyrosine
Modified residue624Omega-N-methylarginine
Modified residue631Omega-N-methylarginine
Modified residue634Phosphotyrosine
Modified residue637Phosphotyrosine
Modified residue638Omega-N-methylarginine
Glycosylation642O-linked (GlcNAc) serine
Glycosylation647O-linked (GlcNAc) serine
Modified residue649Phosphotyrosine
Modified residue660Phosphotyrosine
Modified residue663Phosphotyrosine
Modified residue668Phosphotyrosine
Modified residue696Asymmetric dimethylarginine; alternate
Modified residue696Omega-N-methylarginine; alternate

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

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.

TypeIDPosition(s)Description
Compositional bias1-22Polar residues
Region1-48Disordered
Coiled coil58-92
Coiled coil123-151
Compositional bias325-342Polar residues
Region325-347Disordered
Region358-379G3BP1-binding
Region412-443Disordered
Region523-558Disordered
Compositional bias530-558Polar residues
Compositional bias570-607Polar residues
Region570-620Disordered
Compositional bias641-677Polar residues
Region641-707Disordered

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

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    707
  • Mass (Da)
    78,121
  • Last updated
    2008-04-08 v2
  • Checksum
    3F0859BC83403242
MPSATSHSGSGSKSSGPPPPSGSSGSEAAAGAAAPASQHPATGTGAVQTEAMKQILGVIDKKLRNLEKKKGKLDDYQERMNKGERLNQDQLDAVSKYQEVTNNLEFAKELQRSFMALSQDIQKTIKKTARREQLMREEAEQKRLKTVLELQYVLDKLGDDDVRTDLKQGLSGVPILSEEELSLLDEFYKLVDPERDMSLRLNEQYEHASIHLWDLLEGKEKPVCGTTYKALKEIVERVFQSNYFDSTHNHQNGLCEEEEAASAPIVEDQVAEAEPEPTEEYTEQSEVESTEYVNRQFMAETQFSSGEKEQVDEWAVETVEVVNSLQQQPQAASPSVPEPHSLTPVAQSDPLVRRQRVQDLMAQMQGPYNFIQDSMLDFENQTLDPAIVSAQPMNPTQNMDMPQLVCPQVHSESRLAQSNQVPVQPEATQVPLVSSTSEGYTASQPLYQPSHAAEQRPQKEPIDQIQATISLNTEQTTASSSLPAASQPQVFQAGASKPLHSSGINVNAAPFQSMQTVFNMNAPVPPVNEPETLKQQSQYQASYNQSFSSQPHQVEQTELQQDQLQTVVGTYHGSQDQPHQVPGNHQQPPQQSTGFPRSSQPYYNSRGVSRGGSRGARGLMNGYRGPANGFRGGYDGYRSSFSNTPNSGYTQSQFNAPRDYSGYQRDGYQQNFKRGSGQSGPRGAPRGRGGPPRPNRGMPQMNTQQVN

Computationally mapped potential isoform sequences

There is 1 potential isoform mapped to this entry

View all
EntryEntry nameGene nameLength
A0A8L2Q6N7A0A8L2Q6N7_RATCaprin1720

Sequence caution

The sequence AAO21306.1 differs from that shown. Reason: Erroneous initiation Truncated N-terminus.

Features

Showing features for compositional bias, sequence conflict.

TypeIDPosition(s)Description
Compositional bias1-22Polar residues
Sequence conflict27in Ref. 4; AAO21306
Sequence conflict48in Ref. 4; AAO21306
Compositional bias325-342Polar residues
Sequence conflict372in Ref. 4; AAO21306
Sequence conflict396in Ref. 4; AAO21306
Compositional bias530-558Polar residues
Sequence conflict537in Ref. 4; AAO21306
Sequence conflict557in Ref. 4; AAO21306
Compositional bias570-607Polar residues
Sequence conflict571in Ref. 4; AAO21306
Sequence conflict582in Ref. 4; AAO21306
Sequence conflict587-588in Ref. 4; AAO21306
Compositional bias641-677Polar residues

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
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

Genome annotation databases

Similar Proteins

Disclaimer

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