Laminin subunit alpha-4 is a protein that in humans is encoded by the LAMA4 gene.[5][6]

LAMA4
Identifiers
AliasesLAMA4, CMD1JJ, LAMA3, LAMA4*-1, Laminin, alpha 4, laminin subunit alpha 4
External IDsOMIM: 600133; MGI: 109321; HomoloGene: 37604; GeneCards: LAMA4; OMA:LAMA4 - orthologs
Orthologs
SpeciesHumanMouse
Entrez
Ensembl
UniProt
RefSeq (mRNA)

NM_001105206
NM_001105207
NM_001105208
NM_001105209
NM_002290

NM_010681

RefSeq (protein)

NP_001098676
NP_001098677
NP_001098678
NP_001098679
NP_002281

NP_034811

Location (UCSC)Chr 6: 112.11 – 112.25 MbChr 10: 38.84 – 38.99 Mb
PubMed search[3][4]
Wikidata
View/Edit HumanView/Edit Mouse

Function

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Laminins, a family of extracellular matrix glycoproteins, are the major noncollagenous constituent of basement membranes. They have been implicated in a wide variety of biological processes including cell adhesion, differentiation, migration, signaling, neurite outgrowth and metastasis.

Laminins are composed of 3 non identical chains: laminin alpha, beta and gamma (formerly A, B1, and B2, respectively) and they form a cruciform structure consisting of 3 short arms, each formed by a different chain, and a long arm composed of all 3 chains. Each laminin chain is a multidomain protein encoded by a distinct gene. Several isoforms of each chain have been described. Different alpha, beta and gamma chain isomers combine to give rise to different heterotrimeric laminin isoforms which are designated by Arabic numerals in the order of their discovery, i.e. alpha1beta1gamma1 heterotrimer is laminin 1. The biological functions of the different chains and trimer molecules are largely unknown, but some of the chains have been shown to differ with respect to their tissue distribution, presumably reflecting diverse functions in vivo.

This gene encodes the alpha chain isoform laminin, alpha 4. The domain structure of alpha 4 is similar to that of alpha 3, both of which resemble truncated versions of alpha 1 and alpha 2, in that approximately 1,200 residues at the N-terminus (domains IV, V and VI) have been lost. Laminin, alpha 4 contains the C-terminal G domain which distinguishes all alpha chains from the beta and gamma chains. The RNA analysis from adult and fetal tissues revealed developmental regulation of expression, however, the exact function of laminin, alpha 4 is not known.[6]

Gene

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Tissue-specific utilization of alternative polyA-signal has been described in literature. Also, alternative splicing involving the first intron in the 5' UTR, and laminin alpha 4 like isoforms have been noted, however, the full-length nature of these products is not known.[6]

References

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  1. ^ a b c GRCh38: Ensembl release 89: ENSG00000112769Ensembl, May 2017
  2. ^ a b c GRCm38: Ensembl release 89: ENSMUSG00000019846Ensembl, May 2017
  3. ^ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  4. ^ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  5. ^ Richards AJ, al-Imara L, Carter NP, Lloyd JC, Leversha MA, Pope FM (Jul 1994). "Localization of the gene (LAMA4) to chromosome 6q21 and isolation of a partial cDNA encoding a variant laminin A chain". Genomics. 22 (1): 237–9. doi:10.1006/geno.1994.1372. PMID 7959779.
  6. ^ a b c "Entrez Gene: LAMA4 laminin, alpha 4".

Further reading

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