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FLASH GENE
Symbol SFTPD contributors: mct - updated : 22-05-2018
HGNC name surfactant, pulmonary-associated protein D
HGNC id 10803
PROTEIN
PHYSICAL PROPERTIES
STRUCTURE
motifs/domains
  • a collagen-like region
  • carbohydrate recognition domains (CRD)
  • a neck domain plus CRD (NCRD)
  • a C-type lectin family domain
    • conjugated GlycoP
    HOMOLOGY
    Homologene
    FAMILY collectin family
    CATEGORY immunity/defense
    SUBCELLULAR LOCALIZATION extracellular
        intracellular
    intracellular,cytoplasm,organelle,lysosome
    intracellular,cytoplasm,cytosolic,vesicle
    basic FUNCTION
  • playing an important role in innate immunity by binding to specific carbohydrate structures found at the surface of pathogenic microorganisms
  • plays important roles in lipopolysaccharide (LPS) recognition
  • plays diverse and important roles in innate immunity and pulmonary homeostasis (Crouch 2010)
    • CELLULAR PROCESS
    PHYSIOLOGICAL PROCESS inflammation
    PATHWAY
    metabolism
    signaling
    a component
    INTERACTION
    DNA
    RNA
    small molecule
    protein
  • interacting with decorin, a SFTPD-binding protein (decorin core protein binds the collagen-like region of the SFTPD)
  • binds the extracellular domains of TLR2 and TLR4 through its CRD by a mechanism different from its binding to PI and LPS
  • putative binding motif for OSCAR within the SFTPD collagenous domain, and interaction is a potential therapeutic target in chronic inflammatory diseases of the lung as well as other diseases involving tissue accumulation of SFTPD, infiltration of inflammatory monocytes
    • cell & other
    REGULATION
    inhibited by MPO (Myeloperoxidase-dependent inactivation of surfactant protein D) (Crouch 2010)
    ASSOCIATED DISORDERS
    corresponding disease(s)
    Susceptibility
    Variant & Polymorphism
    Candidate gene
    Marker
    Therapy target
    ANIMAL & CELL MODELS
    Sftpd mutant lacking N-terminal cysteine residues and truncation mutants lacking the N-terminal domains were resistant to the oxidant-induced alterations in disulfide bonding (Crouch 2010)