LAMA1

Domain

The alpha-helical domains I and II are thought to interact with other laminin chains to form a coiled coil structure.

Domains VI, IV and G are globular.

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.

Involvement in disease

Poretti-Boltshauser syndrome

PTBHS

An autosomal recessive disorder characterized by cerebellar dysplasia, cerebellar vermis atrophy, cerebellar cysts in most patients, high myopia, variable retinal dystrophy, and eye movement abnormalities including strabismus, ocular apraxia, nystagmus. Affected individuals have ataxia, delayed motor development, language impairment, and intellectual disability with variable severity.

None

The disease is caused by variants affecting the gene represented in this entry.

Post-translational modifications

Tyrosine phosphorylated by PKDCC/VLK.

Cellular localization

• Secreted
• Extracellular space
• Extracellular matrix
• Basement membrane
• Major component.

Alternative names

LAMA, LAMA1, Laminin subunit alpha-1, Laminin A chain, Laminin-1 subunit alpha, Laminin-3 subunit alpha, S-laminin subunit alpha, S-LAM alpha

Database links

swissprot:P25391 entrezGene:3912 entrezGene:3908 swissprot:Q9Y6N6 swissprot:P55268 swissprot:P24043 swissprot:P07942 omim:150320 entrezGene:3913 entrezGene:3915 entrezGene:3918 entrezGene:10319 entrezGene:284217