Carmil2 Gene Summary [Rat]
Predicted to enable phospholipid binding activity. Predicted to be involved in several processes, including actin filament network formation; positive regulation of cellular component organization; and wound healing, spreading of cells. Predicted to act upstream of or within several processes, including T cell receptor signaling pathway; positive regulation of T cell activation; and positive regulation of cytokine production. Predicted to be located in several cellular components, including cytoskeleton; immunological synapse; and macropinosome. Predicted to be part of F-actin capping protein complex. Predicted to be active in lamellipodium and plasma membrane. Human ortholog(s) of this gene implicated in immunodeficiency 58. Orthologous to human CARMIL2 (capping protein regulator and myosin 1 linker 2). [provided by Alliance of Genome Resources, Jul 2025]
Details
| Type | Protein Coding |
| Official Symbol | Carmil2 |
| Official Name | capping protein regulator and myosin 1 linker 2 [Source:RGD Symbol;Acc:1562390] |
| Ensembl ID | ENSRNOG00000024452 |
| Bio databases IDs | |
| Aliases | capping protein regulator and myosin 1 linker 2 |
| Synonyms | capping protein regulator and myosin 1 linker 2, CARMIL2b, CG1399-PB, D130029J02, D130029J02Rik, Gm585, IMD58, LRRC16C, RGD1562390, RLTPR |
| Species | Rat, Rattus norvegicus |
| Orthologies |
Protein Domains
A protein domain is a distinct structural or functional region within a protein that can evolve, function, and exist independently of the rest of the protein chain. These domains in rat Carmil2 often fold into stable, three-dimensional structures and are associated with specific biological functions, such as binding to DNA, other proteins, or small molecules.
- phospholipid binding
- Carmil pleckstrin homology domain
- CARMIL C-terminus
- protein phosphatase 1 regulatory subunit 42
- binding protein
- Leucine rich repeat, ribonuclease inhibitor type
- Leucine rich repeat
- protein binding
Top Findings
The most significant associations for this gene, including commonly observed domains, pathway involvement, and functional highlights based on current data.
disease
- T-cell non-Hodgkin disease
- mature T-cell neoplasia
- skin cancer
- combined immunodeficiency
- severe combined immunodeficiency
- tonsillitis
- immunodeficiency type 58
- myopia
- cutaneous T-cell lymphoma
- diabetic nephropathy
regulated by
- tetradecanoylphorbol acetate
- ionomycin
- CARMIL2
- FIRRE
- pervanadate
role in cell
- proliferation
- production in
- binding in
- migration
- organization
- differentiation
- assembly
- disassembly
- network formation
Subcellular Expression
Locations within the cell where the protein is known or predicted to be active, providing insight into its function and cellular context.
- Plasma Membrane
- intermediate filament cytoskeleton
- ruffle
- Cytoplasm
- actin cytoskeleton
- intercellular junctions
- immunological synapses
- cell membrane leading edge
- lamellipodia
- macropinosomes
Gene Ontology Annotations
Describes the biological processes, cellular components, and molecular functions associated with the rat Carmil2 gene, providing context for its role in the cell.
Biological Process
Functions and activities the gene product is involved in
- wound healing, spreading of cells
- positive regulation of lamellipodium assembly
- positive regulation of extracellular matrix disassembly
- negative regulation of barbed-end actin filament capping
- establishment or maintenance of cell polarity
- establishment or maintenance of monopolar cell polarity
- actin filament network formation
- positive regulation of ruffle assembly
- cell migration
- regulation of Arp2/3 complex-mediated actin nucleation
- positive regulation of cell migration
Cellular Component
Where in the cell the gene product is active
- intermediate filament cytoskeleton
- cytoplasm
- cell leading edge
- membrane
- actin cytoskeleton
- ruffle
- macropinosome
- extrinsic to internal side of plasma membrane
- plasma membrane
- lamellipodium
Molecular Function
What the gene product does at the molecular level
- phospholipid binding