UniProt functional annotation for P26043



	UniProt functional annotation for P26043

UniProt code: P26043.

Organism: Mus musculus (Mouse).

Taxonomy: Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae; Murinae; Mus; Mus.

Function: Probably plays a crucial role in the binding of the barbed end of actin filaments to the plasma membrane.

Activity regulation: A head-to-tail association, of the N-terminal and C-terminal halves results in a closed conformation (inactive form) which is incapable of actin or membrane-binding. {ECO:0000250}.

Subunit: Interacts with CPNE1 (via VWFA domain) and CPNE4 (via VWFA domain) (PubMed:12522145). Binds SLC9A3R1 (By similarity). Interacts with LAYN (PubMed:15913605). Interacts with NHERF1 and NHERF2 (PubMed:16615918). Interacts with MME/NEP (PubMed:17459884). Interacts with ICAM2 (PubMed:12554651, PubMed:9472040). Interacts with SPN and CD44 (PubMed:9472040). {ECO:0000250|UniProtKB:P35241, ECO:0000269|PubMed:12522145, ECO:0000269|PubMed:12554651, ECO:0000269|PubMed:15913605, ECO:0000269|PubMed:16615918, ECO:0000269|PubMed:17459884, ECO:0000269|PubMed:9472040}.

Subcellular location: Cell membrane; Peripheral membrane protein; Cytoplasmic side. Cytoplasm, cytoskeleton. Cleavage furrow. Cell projection, microvillus {ECO:0000269|PubMed:9472040}. Note=Highly concentrated in the undercoat of the cell-to-cell adherens junction and the cleavage furrow in the interphase and mitotic phase, respectively.

Domain: The N-terminal domain interacts with the C-terminal domain of LAYN. An interdomain interaction between its N-terminal and C-terminal domains inhibits its ability to bind LAYN. In the presence of acidic phospholipids, the interdomain interaction is inhibited and this enhances binding to LAYN.

Ptm: Phosphorylated by tyrosine-protein kinases. Phosphorylation by ROCK2 suppresses the head-to-tail association of the N-terminal and C- terminal halves resulting in an opened conformation which is capable of actin and membrane-binding. {ECO:0000269|PubMed:8479753, ECO:0000269|PubMed:9456324}.

Annotations taken from UniProtKB at the EBI.


Organism:		Mus musculus (Mouse).
Taxonomy:		Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae; Murinae; Mus; Mus.



Function:		Probably plays a crucial role in the binding of the barbed end of actin filaments to the plasma membrane.


Activity regulation:		A head-to-tail association, of the N-terminal and C-terminal halves results in a closed conformation (inactive form) which is incapable of actin or membrane-binding. {ECO:0000250}.
Subunit:		Interacts with CPNE1 (via VWFA domain) and CPNE4 (via VWFA domain) (PubMed:12522145). Binds SLC9A3R1 (By similarity). Interacts with LAYN (PubMed:15913605). Interacts with NHERF1 and NHERF2 (PubMed:16615918). Interacts with MME/NEP (PubMed:17459884). Interacts with ICAM2 (PubMed:12554651, PubMed:9472040). Interacts with SPN and CD44 (PubMed:9472040). {ECO:0000250\|UniProtKB:P35241, ECO:0000269\|PubMed:12522145, ECO:0000269\|PubMed:12554651, ECO:0000269\|PubMed:15913605, ECO:0000269\|PubMed:16615918, ECO:0000269\|PubMed:17459884, ECO:0000269\|PubMed:9472040}.
Subcellular location:		Cell membrane; Peripheral membrane protein; Cytoplasmic side. Cytoplasm, cytoskeleton. Cleavage furrow. Cell projection, microvillus {ECO:0000269\|PubMed:9472040}. Note=Highly concentrated in the undercoat of the cell-to-cell adherens junction and the cleavage furrow in the interphase and mitotic phase, respectively.
Domain:		The N-terminal domain interacts with the C-terminal domain of LAYN. An interdomain interaction between its N-terminal and C-terminal domains inhibits its ability to bind LAYN. In the presence of acidic phospholipids, the interdomain interaction is inhibited and this enhances binding to LAYN.
Ptm:		Phosphorylated by tyrosine-protein kinases. Phosphorylation by ROCK2 suppresses the head-to-tail association of the N-terminal and C- terminal halves resulting in an opened conformation which is capable of actin and membrane-binding. {ECO:0000269\|PubMed:8479753, ECO:0000269\|PubMed:9456324}.