Contents

Laminin subunit gamma-3

Protein-coding gene in the species Homo sapiens

LAMC3
Identifiers
Aliases	LAMC3, OCCM, laminin subunit gamma 3
External IDs	OMIM: 604349; MGI: 1344394; HomoloGene: 21222; GeneCards: LAMC3; OMA:LAMC3 - orthologs
Gene location (Human) Chr. Chromosome 9 (human)[1] Band 9q34.12 Start 131,009,174 bp[1] End 131,094,473 bp[1]
Gene location (Mouse) Chr. Chromosome 2 (mouse)[2] Band 2|2 B Start 31,777,303 bp[2] End 31,836,551 bp[2]
RNA expression pattern Bgee Human Mouse (ortholog) Top expressed in canal of the cervix right lung left testis upper lobe of left lung anterior pituitary right adrenal cortex ectocervix right testis left adrenal gland left adrenal cortex Top expressed in ascending aorta aortic valve lip lumbar subsegment of spinal cord spermatid right kidney visual cortex dentate gyrus of hippocampal formation granule cell Gonadal ridge superior frontal gyrus More reference expression data BioGPS n/a
Gene ontology Molecular function structural molecule activity Cellular component extracellular region basement membrane membrane extracellular matrix Biological process astrocyte development cell morphogenesis involved in differentiation cell adhesion extracellular matrix organization retina development in camera-type eye visual perception animal organ morphogenesis tissue development cell migration substrate adhesion-dependent cell spreading Sources:Amigo / QuickGO
Orthologs Species Human Mouse Entrez 10319 23928 Ensembl ENSG00000050555 ENSMUSG00000026840 UniProt Q9Y6N6 Q9R0B6 RefSeq (mRNA) NM_006059 NM_011836 RefSeq (protein) NP_006050 NP_035966 Location (UCSC) Chr 9: 131.01 – 131.09 Mb Chr 2: 31.78 – 31.84 Mb PubMed search [3] [4]
Wikidata
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Laminin subunit gamma-3 also known as LAMC3 is a protein that in humans is encoded by the LAMC3 gene.^[5][6]

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 gamma chain isoform laminin, gamma 3. The gamma 3 chain is most similar to the gamma 1 chain, and contains all the 6 domains expected of the gamma chain. It is a component of laminin 12. The gamma 3 chain is broadly expressed in skin, heart, lung, and the reproductive tracts. In skin, it is seen within the basement membrane of the dermoepidermal junction at points of nerve penetration. However, it was also found that the gamma 3 is a prominent element of the apical surface of ciliated epithelial cells of lung, oviduct, epididymis, ductus deferens, and seminiferous tubules. The distribution of gamma 3-containing laminins along ciliated epithelial surfaces suggests that the apical laminins are important in the morphogenesis and structural stability of the ciliated processes of these cells.^[6]

A recent study found that LAMC3 plays a critical role in forming the convolution of the cerebral cortex. Particularly LAMC3 is expressed during the embryonic period, which contributes the formation of dendrites.^[7]

• LAMC3 human gene location in the UCSC Genome Browser.
• LAMC3 human gene details in the UCSC Genome Browser.

This article incorporates text from the United States National Library of Medicine, which is in the public domain.