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FLASH GENE
Symbol LAMA5 contributors: mct/npt - updated : 28-01-2015
HGNC name laminin, alpha 5
HGNC id 6485
Location 20q13.33      Physical location : 60.884.122 - 60.942.368
Synonym name
  • laminin-3A32
  • laminin alpha-5 chain
  • laminin-10 subunit alpha
  • laminin-11 subunit alpha
  • laminin-15 subunit alpha
  • Synonym symbol(s) LMA5, KIAA0533, KIAA1907, Lm3A32, laminin-511
    DNA
    TYPE functioning gene
    STRUCTURE 58.25 kb     80 Exon(s)
    10 Kb 5' upstream gene genomic sequence study
    MAPPING cloned Y linked N status confirmed
    RNA
    TRANSCRIPTS type messenger
    identificationnb exonstypebpproduct
    ProteinkDaAAspecific expressionYearPubmed
    80 - 11426 - 3695 - 2009 19773554
    12 - - - - heart, placenta, kidney, spleen, prostate, colon 2009 19773554
  • also called LAMA5LN1
  • ex 1–11 + 11e
  • LaNt alpha51 (laminin N terminus)
  • may play important roles in regulating laminin matrix functions and its expression is up-regulated during wound healing
  • 12 - - - - kidney, spleen, small intestine 2009 19773554
  • also called LAMA5LN2
  • ex 1–11 + 12*
  • LaNt alpha52 (laminin N terminus)
  • may play important roles in regulating laminin matrix functions and its expression is up-regulated during wound healing
  • EXPRESSION
    Type widely
       expressed in (based on citations)
    organ(s)
    SystemOrgan level 1Organ level 2Organ level 3Organ level 4LevelPubmedSpeciesStageRna symbol
    Digestiveesophagus   highly Homo sapiens
    Nervousnerve   highly
    Reproductivefemale systembreast  highly Homo sapiens
    Respiratorylung   highly Homo sapiens
    Skin/Tegumentskin   highly Homo sapiens
    tissue
    SystemTissueTissue level 1Tissue level 2LevelPubmedSpeciesStageRna symbol
    Connectiveadipose  lowly
    Epithelialbarrier liningretinal pigment epithelium (RPE) moderately
    Muscularstriatumskeletal moderately
    cells
    SystemCellPubmedSpeciesStageRna symbol
    Skin/Tegumentkeratinocyte
    cell lineage
    cell lines
    fluid/secretion
    at STAGE
    physiological period embryo, pregnancy
    Text embryonic tissue at an highly level
    PROTEIN
    PHYSICAL PROPERTIES
    STRUCTURE
    motifs/domains
  • a N-terminal short arm allowing the self assembly of chains through interactions of the most terminal globular domain, with the N-terminal domains within the lamina densa (Rousselle 1997), with three globular domains (LN, L4a, and L4b) and three rodlike elements (LEa, LEb, and LEc)
  • 4 laminin A/neurexin/sex hormone-binding (LNS) globular domains
  • 22 EGF-like motifs
  • a long arm composed of hepstad repeats typical of a cell alpha helical coiled-coil protein
  • C-terminal G domain apposed to the hemidesmosomal integrin,
  • conjugated GlycoP
    mono polymer heteromer , trimer
    HOMOLOGY
    interspecies homolog to murine Lama5 (79.83 pc)
    homolog to rattus Lama5 (79.95 pc)
    Homologene
    FAMILY
    CATEGORY adhesion
    SUBCELLULAR LOCALIZATION extracellular
        intracellular
    intracellular,nucleus
    basic FUNCTION
  • binding to cells via a high affinity receptor
  • appears as a thin filament bridging the hemidesmosome with the anchoring fibrils (Rousselle 1997)
  • mediating the attachment, migration and organization of cells into tissues during embryonic development by interacting with other extracellular matrix components
  • important regulator of ADPKD cell proliferation and cystogenesis
  • stimulates osteogenic gene expression in mesenchymal stem cells, in the absence of any other osteogenic stimulus (Klees 2007)
  • activates extracellular matrix production and osteogenic gene focusing in human mesenchymal stem cells (Klees 2007)
  • in intact skin, provides essential links to both the hemidesmosomal alpha6beta4 integrin and the collagen type VII molecules which form the anchoring fibrils inserting into the dermis (Schneider 2007)
  • major contributions to the resistance of the epidermis against frictional stress but also for basement membrane regeneration and repair of damaged skin (Schneider 2007)
  • predominant role in blood lymphocyte biology and identifies lymph nodes laminins and their integrin receptors in blood lymphocytes (Gorfu 2008)
  • crucial motility-promoting factor for B-CLL lymphocytes and as a potential constituent favoring the dissemination of B-CLL lymphocytes through vascular basement membranes and possibly lymph node compartments (Spessotto 2007)
  • extracellular matrix protein containing multiple domains implicated in various biological processes, such as embryogenesis and renal function
  • plays a crucial role in both epithelial and mesenchymal cell behavior by inhibiting WNT and activating PI3K signaling
  • proper expression of LAMB3 and LAMA5 may regulate appropriate hair morphogenesis
  • CELLULAR PROCESS cell communication
    PHYSIOLOGICAL PROCESS
    PATHWAY
    metabolism
    signaling
    a component
  • constituent of basement membrane zone
  • LAMA5 heterotrimerization with beta-2 and gamma-3 chains conducing to Laminin 15
  • key component of the anchoring complex connecting keratinocytes to the underlying dermis (Schneider 2007)
  • heterotrimeric complexes of alpha, beta, and gamma chains, with each chain type representing a different subfamily of proteins
  • INTERACTION
    DNA
    RNA
    small molecule
    protein
  • binds the NH2-terminal NC1 domain of type VII collagen (Rousselle 1997)
  • BCAM is a specific receptor for LAMA5, a major component of basement membranes in various tissues
  • preferential binding of Lu/BCAM to LAMA5 promotes tumor cell migration
  • cell & other
    REGULATION
    ASSOCIATED DISORDERS
    corresponding disease(s)
    Other morbid association(s)
    TypeGene ModificationChromosome rearrangementProtein expressionProtein Function
    tumoral        
    null expression in prostate carcinoma
    constitutional     --other  
    aberrantly expressed in the pericystic ECM of AD polycystic kidneys
    constitutional       loss of function
    absence of functional LAMA5, leads to phenotype of Herlitz junctional epidermolysis bullosa (Schneider 2007)
    Susceptibility
    Variant & Polymorphism
    Candidate gene
    Marker
    Therapy target
    ANIMAL & CELL MODELS
  • mutation of the mouse laminin alpha5 gene results in a variety of developmental defects, including defects in kidney structure and function