| UniProt functional annotation for Q60675 | |||
| UniProt code: Q60675. |
| Organism: | Mus musculus (Mouse). | |
| Taxonomy: | Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae; Murinae; Mus; Mus. | |
| Function: | Binding to cells via a high affinity receptor, laminin is thought to mediate the attachment, migration and organization of cells into tissues during embryonic development by interacting with other extracellular matrix components. | |
| Subunit: | Laminin is a complex glycoprotein, consisting of three different polypeptide chains (alpha, beta, gamma), which are bound to each other by disulfide bonds into a cross-shaped molecule comprising one long and three short arms with globules at each end. Alpha-2 is a subunit of laminin-2 (laminin-211 or merosin), laminin-4 (laminin-221 or S-merosin) and laminin-12 (laminin-213). Interacts with FBLN1, FBLN2 and NID2. {ECO:0000269|PubMed:10022829}. | |
| Subcellular location: | Secreted, extracellular space, extracellular matrix, basement membrane. Note=Major component. | |
| Domain: | The alpha-helical domains I and II are thought to interact with other laminin chains to form a coiled coil structure. | |
| Domain: | Domains VI, IV and G are globular. | |
| Disease: | Note=Defects in Lama2 are a cause of murine muscular dystrophy (dy2J). | |
| Sequence caution: | Sequence=AAC52165.1; Type=Frameshift; Evidence={ECO:0000305}; | |
Annotations taken from UniProtKB at the EBI.