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FLASH GENE
Symbol MATN3 contributors: mct/pgu - updated : 30-03-2016
HGNC name matrilin 3
HGNC id 6909
Corresponding disease
EDM5 epiphyseal dysplasia multiple 5
SEMD3 spondyloepimetaphyseal dysplasia, type 3
Location 2p24.1      Physical location : 20.191.813 - 20.212.455
DNA
TYPE functioning gene
STRUCTURE 20.64 kb     8 Exon(s)
10 Kb 5' upstream gene genomic sequence study
MAPPING cloned Y linked N status provisional
RNA
TRANSCRIPTS type messenger
EXPRESSION
Type restricted
   expressed in (based on citations)
organ(s)
SystemOrgan level 1Organ level 2Organ level 3Organ level 4LevelPubmedSpeciesStageRna symbol
Hearing/Equilibriumearinnercochlea  
Nervousnerve    
tissue
SystemTissueTissue level 1Tissue level 2LevelPubmedSpeciesStageRna symbol
Connectivebone   
Muscularstriatumskeletal  
cells
SystemCellPubmedSpeciesStageRna symbol
 chondroblast
 chondrocyte
cell lineage
cell lines
fluid/secretion
at STAGE
PROTEIN
PHYSICAL PROPERTIES
STRUCTURE
motifs/domains
  • a signal peptide,
  • a coiled-coil domain
  • a single A-domain (M3A), possessing metal ion-dependent adhesion site (MIDAS) motifs
  • four EGF-like repeats and an alpha helical region
  • a MATN3A domain, binding to other extracellular matrix proteins and exclusively through the COL3 domain of type IX collagen
  • conjugated PhosphoP
    mono polymer homomer , heteromer , oligo
    isoforms Precursor
    HOMOLOGY
    interspecies homolog to murine Matn3 (84.0pc)
    homolog to rattus Matn3 (82.6pc)
    intraspecies paralog to COL20A1
    Homologene
    FAMILY
  • Von Willebrand factor A domain containing protein family
  • CATEGORY structural protein
    SUBCELLULAR LOCALIZATION extracellular
    text
  • cartilage extracellular matrix
  • found mainly in the cartilage proliferation zone
  • basic FUNCTION
  • involved in the differentiation state of chondrocytes
  • playing with COMP an important role in matrix assembly
  • may play a role in the formation of extracellular filamentous networks
  • have a role in the development and homeostasis of cartilage and bone
  • mediate cell attachment, but the binding is clearly dose dependent and seen already at moderate coating concentrations
  • oligomeric extracellular matrix adaptor proteins mediating interactions between collagen fibrils and other matrix constituents
  • MATN1 and MATN3 modulate collagen fibrillogenesis in cartilage and provide evidence that biochemical compensation might exist between matrilins
  • activates the expression of osteoarthritis-associated genes in primary human chondrocytes
  • proteolytically-released MATN3 induces pro-inflammatory cytokines and ADMATS4/5 (via IL1-beta) which in turn cleave MATN3 and may release more MATN3 from the matrix
  • function for MATN1 and MATN3 to maintain and enhance chondrogenesis of mesenchymal fibroblasts initiated by TGF-beta
  • possible roles for MATN1/MATN3 hetero-oligomers could be to further bring this collagen type II and IX integrated meshwork together by increasing their affinities to interact with the extracellular matrix
  • MATN1, MATN2, MATN3, MATN4 are important to protect articular cartilage from deterioration and are involved in the specification of the vertebral column
  • CELLULAR PROCESS cell life, differentiation
    PHYSIOLOGICAL PROCESS development
    text
  • skeletal system development
  • PATHWAY
    metabolism
    signaling
    a component
  • can form homooligomers (mono/di/tri/tetramers)
  • form disulfide-bonded oligomers with matrilin-1
  • INTERACTION
    DNA
    RNA
    small molecule
    protein
  • MATN1
  • interacting with COMP
  • binding to type II and IX collagen and cartilage oligomeric matrix proteins in a Zn2+ dependent manner )
  • cell & other
    REGULATION
    Other
  • cleaved by ADAMTS4/5
  • ASSOCIATED DISORDERS
    corresponding disease(s) EDM5 , SEMD3
    Susceptibility to hand osteoarthritis (HOA)
    Variant & Polymorphism SNP T298M increased in hand osteoarthritis
    Candidate gene
    Marker
    Therapy target
    ANIMAL & CELL MODELS
    mice lacking both matrilin-1 and matrilin-3 develop an apparently normal skeleton, but exhibit biochemical and ultrastructural abnormalities of the knee joint cartilage