UniProt functional annotation for P15379



	UniProt functional annotation for P15379

UniProt code: P15379.

Organism: Mus musculus (Mouse).

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

Function: Cell-surface receptor that plays a role in cell-cell interactions, cell adhesion and migration, helping them to sense and respond to changes in the tissue microenvironment. Participates thereby in a wide variety of cellular functions including the activation, recirculation and homing of T-lymphocytes, hematopoiesis, inflammation and response to bacterial infection. Engages, through its ectodomain, extracellular matrix components such as hyaluronan/HA, collagen, growth factors, cytokines or proteases and serves as a platform for signal transduction by assembling, via its cytoplasmic domain, protein complexes containing receptor kinases and membrane proteases (PubMed:8343954, PubMed:25065622). Such effectors include PKN2, the RhoGTPases RAC1 and RHOA, Rho-kinases and phospholipase C that coordinate signaling pathways promoting calcium mobilization and actin- mediated cytoskeleton reorganization essential for cell migration and adhesion (By similarity). {ECO:0000250|UniProtKB:P16070, ECO:0000269|PubMed:25065622, ECO:0000269|PubMed:8343954}.

Subunit: Interacts with PKN2 (PubMed:17403031). Interacts with TIAM1 and TIAM2 (PubMed:19893486). Interacts with HA, as well as other glycosaminoglycans, collagen, laminin, and fibronectin via its N- terminal segment (PubMed:24606063). Interacts with UNC119. Interacts with PDPN (via extracellular domain); this interaction is required for PDPN-mediated directional migration and regulation of lamellipodia extension/stabilization during cell spreading and migration (By similarity). Interacts with RDX, EZR and MSN (via FERM domain) (PubMed:9472040, PubMed:18753140). Interacts with EGFR (By similarity). Interacts with CD74; this complex is essential for the MIF-induced signaling cascade that results in B cell survival (PubMed:8343954). {ECO:0000250|UniProtKB:P16070, ECO:0000269|PubMed:17403031, ECO:0000269|PubMed:18753140, ECO:0000269|PubMed:19893486, ECO:0000269|PubMed:24606063, ECO:0000269|PubMed:8343954, ECO:0000269|PubMed:9472040}.

Subcellular location: Cell membrane {ECO:0000269|PubMed:17403031, ECO:0000269|PubMed:25065622}; Single-pass type I membrane protein {ECO:0000269|PubMed:17403031}. Cell projection, microvillus {ECO:0000269|PubMed:9472040}. Note=Colocalizes with actin in membrane protrusionFs at wounding edges. Co-localizes with RDX, EZR and MSN in microvilli. {ECO:0000269|PubMed:17403031, ECO:0000269|PubMed:9472040}.

Domain: The lectin-like LINK domain is responsible for hyaluronan binding.

Ptm: N-glycosylated. {ECO:0000250|UniProtKB:P16070}.

Ptm: O-glycosylated; contains chondroitin sulfate glycans which can be more or less sulfated. {ECO:0000250|UniProtKB:P16070}.

Ptm: Phosphorylated; activation of PKC results in the dephosphorylation of Ser-742 (constitutive phosphorylation site), and the phosphorylation of Ser-708. {ECO:0000250}.

Polymorphism: Two allelic forms of this glycoprotein, PGP-1.1 and PGP- 1.2, have been reported. The expressed product is PGP-1.1 (Ly-24.1).

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:		Cell-surface receptor that plays a role in cell-cell interactions, cell adhesion and migration, helping them to sense and respond to changes in the tissue microenvironment. Participates thereby in a wide variety of cellular functions including the activation, recirculation and homing of T-lymphocytes, hematopoiesis, inflammation and response to bacterial infection. Engages, through its ectodomain, extracellular matrix components such as hyaluronan/HA, collagen, growth factors, cytokines or proteases and serves as a platform for signal transduction by assembling, via its cytoplasmic domain, protein complexes containing receptor kinases and membrane proteases (PubMed:8343954, PubMed:25065622). Such effectors include PKN2, the RhoGTPases RAC1 and RHOA, Rho-kinases and phospholipase C that coordinate signaling pathways promoting calcium mobilization and actin- mediated cytoskeleton reorganization essential for cell migration and adhesion (By similarity). {ECO:0000250\|UniProtKB:P16070, ECO:0000269\|PubMed:25065622, ECO:0000269\|PubMed:8343954}.


Subunit:		Interacts with PKN2 (PubMed:17403031). Interacts with TIAM1 and TIAM2 (PubMed:19893486). Interacts with HA, as well as other glycosaminoglycans, collagen, laminin, and fibronectin via its N- terminal segment (PubMed:24606063). Interacts with UNC119. Interacts with PDPN (via extracellular domain); this interaction is required for PDPN-mediated directional migration and regulation of lamellipodia extension/stabilization during cell spreading and migration (By similarity). Interacts with RDX, EZR and MSN (via FERM domain) (PubMed:9472040, PubMed:18753140). Interacts with EGFR (By similarity). Interacts with CD74; this complex is essential for the MIF-induced signaling cascade that results in B cell survival (PubMed:8343954). {ECO:0000250\|UniProtKB:P16070, ECO:0000269\|PubMed:17403031, ECO:0000269\|PubMed:18753140, ECO:0000269\|PubMed:19893486, ECO:0000269\|PubMed:24606063, ECO:0000269\|PubMed:8343954, ECO:0000269\|PubMed:9472040}.
Subcellular location:		Cell membrane {ECO:0000269\|PubMed:17403031, ECO:0000269\|PubMed:25065622}; Single-pass type I membrane protein {ECO:0000269\|PubMed:17403031}. Cell projection, microvillus {ECO:0000269\|PubMed:9472040}. Note=Colocalizes with actin in membrane protrusionFs at wounding edges. Co-localizes with RDX, EZR and MSN in microvilli. {ECO:0000269\|PubMed:17403031, ECO:0000269\|PubMed:9472040}.
Domain:		The lectin-like LINK domain is responsible for hyaluronan binding.
Ptm:		N-glycosylated. {ECO:0000250\|UniProtKB:P16070}.
Ptm:		O-glycosylated; contains chondroitin sulfate glycans which can be more or less sulfated. {ECO:0000250\|UniProtKB:P16070}.
Ptm:		Phosphorylated; activation of PKC results in the dephosphorylation of Ser-742 (constitutive phosphorylation site), and the phosphorylation of Ser-708. {ECO:0000250}.
Polymorphism:		Two allelic forms of this glycoprotein, PGP-1.1 and PGP- 1.2, have been reported. The expressed product is PGP-1.1 (Ly-24.1).