Laminin, alpha 3

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Laminin, alpha 3
Identifiers
Symbols LAMA3 ; BM600; E170; LAMNA; LOCS; lama3a
External IDs OMIM600805 MGI99909 HomoloGene18279 GeneCards: LAMA3 Gene
RNA expression pattern
PBB GE LAMA3 203726 s at tn.png
PBB GE LAMA3 gnf1h02350 at tn.png
PBB GE LAMA3 gnf1h02351 s at tn.png
More reference expression data
Orthologs
Species Human Mouse
Entrez 3909 16774
Ensembl ENSG00000053747 ENSMUSG00000024421
UniProt Q16787 Q61789
RefSeq (mRNA) NM_000227 NM_010680
RefSeq (protein) NP_000218 NP_034810
Location (UCSC) Chr 18:
21.27 – 21.54 Mb
Chr 18:
12.33 – 12.58 Mb
PubMed search [1] [2]

Laminin subunit alpha-3 is a protein that in humans is encoded by the LAMA3 gene.[1][2]

Laminins are basement membrane components thought to mediate the attachment, migration and organization of cells into tissues during embryonic development by interacting with other extracellular matrix components. The protein encoded by this gene is the alpha-3 chain of laminin 5, which is a complex glycoprotein composed of three subunits (alpha, beta, and gamma). Laminin 5 is thought to be involved in cell adhesion, signal transduction and differentiation of keratinocytes. Mutations in this gene have been identified as the cause of Herlitz type junctional epidermolysis bullosa. Alternatively spliced transcript variants encoding different isoforms have been identified.[2]

It may be associated with Laryngoonychocutaneous syndrome.[3]

Interactions[edit]

Laminin, alpha 3 has been shown to interact with SDC2.[4]

References[edit]

  1. ^ Ryan MC, Tizard R, VanDevanter DR, Carter WG (Oct 1994). "Cloning of the LamA3 gene encoding the alpha 3 chain of the adhesive ligand epiligrin. Expression in wound repair". J Biol Chem 269 (36): 22779–87. PMID 8077230. 
  2. ^ a b "Entrez Gene: LAMA3 laminin, alpha 3". 
  3. ^ McLean WH, Irvine AD, Hamill KJ, et al. (September 2003). "An unusual N-terminal deletion of the laminin alpha3a isoform leads to the chronic granulation tissue disorder laryngo-onycho-cutaneous syndrome". Hum. Mol. Genet. 12 (18): 2395–409. doi:10.1093/hmg/ddg234. PMID 12915477. 
  4. ^ Utani, A; Nomizu M; Matsuura H; Kato K; Kobayashi T; Takeda U; Aota S; Nielsen P K; Shinkai H (Aug 2001). "A unique sequence of the laminin alpha 3 G domain binds to heparin and promotes cell adhesion through syndecan-2 and -4". J. Biol. Chem. (United States) 276 (31): 28779–88. doi:10.1074/jbc.M101420200. ISSN 0021-9258. PMID 11373281. 

Further reading[edit]