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FLASH GENE
Symbol KLK7 contributors: mct/npt - updated : 10-07-2018
HGNC name kallikrein-related peptidase 7
HGNC id 6368
PROTEIN
PHYSICAL PROPERTIES
STRUCTURE
motifs/domains
  • active site of serine proteinase
  • a potential N glycosylation site
  • a peptidase S1 domain
    • HOMOLOGY
    Homologene
    FAMILY
  • peptidase S1 family
  • kallikrein subfamily
    • CATEGORY enzyme
    SUBCELLULAR LOCALIZATION extracellular
    text
  • suprabasal keratinocytes
  • in the skin, SPINK5, KLK7, and KLK5 were all found in the lamellar granule (LG) system, but were separately localized
    • basic FUNCTION
  • may catalyze the degradation of intercellular cohesive structures in the cornified layer of the skin in the continuous shedding of cells from the skin surface
  • chymostatin-like serine protease, involved in desquamation cascade of the skin
  • playing a role in aiding tumor invasion via degradation of ECM proteins like fibronectin
  • participate in normal desquamation by facilitating cell shedding at the skin surface (Ramani 2008)
  • its aberrant expression and secretion in tumors may facilitate metastasis by directly degrading components of the extracellular matrix and may thus play an important role in tumorigenesis (Ramani 2008)
  • displays a unique chymotrypsin-like specificity for Tyr, which is also preferred at P2 (Debela 2008)
  • chymotryptic-like serine protease, that may play an important role in the activation of MMP9 in tumors that express high levels of both these proteases
  • KLK5, KLK7 and KLK14 are important proteases in skin desquamation
    • CELLULAR PROCESS protein, degradation
    PHYSIOLOGICAL PROCESS
    PATHWAY
    metabolism
    signaling
    a component
    INTERACTION
    DNA
    RNA
    small molecule
    protein
  • regulation of procaspase-14 maturation during keratinocyte terminal differentiation is a unique two-step process involving KLK7 and an activation intermediate of CASP14
  • proteolytic activation of CMKLR1 by KLK7 breaks an ionic linkage and results in C-terminal rearrangement
  • the actions of KLK7 are tightly controlled by PI3 and SPINK5, which also inhibits KLK5, localizing protease activity to the stratum corneum
  • KLK7 is the first protease target of vaspin (SERPINA12)
  • SPINK5 tightly controls the activities of serine proteases such as kallikrein-related peptidase KLK5 and KLK7 in the epidermis
    • cell & other
    REGULATION
    induced by estrogens and glucocorticoids in a breast carcinoma cell line
    inhibited by SERPINA12
    ASSOCIATED DISORDERS
    corresponding disease(s)
    Other morbid association(s)
    TypeGene ModificationChromosome rearrangementProtein expressionProtein Function
    tumoral     --low  
    in adenocarcinoma of the lung
    tumoral     --over  
    in pancreatic adenocarcinomas as well as other cancers
    tumoral     --over  
    in oral squamous cell carcinoma and may be implicated in malignant progression (Pettus 2009)
    tumoral     --over  
    in papillary renal cell carcinoma (Gabril 2010)
    tumoral     --low  
    in prostate and breast cancers (Li 2009)
    tumoral     --over  
    in colon cancer and its expression predicts poor prognosis for colon cancer patients (Galieri 2009)
    tumoral     --low  
    significantly decreased in prostate cancers compared with that in benign prostate epithelial cells (Xuan 2008)
    constitutional     --other  
    unregulated activities of KLK5 and KLK7 are responsible for Netherton syndrome (NS) development
    tumoral     --over  
    in human pancreatic ductal adenocarcinomas (PDACs)
    Susceptibility
    Variant & Polymorphism
    Candidate gene potential biomarkers for breast cancer (Li 2009)
    Marker
  • elevations in glioblastoma KLK6, KLK7 and KLK9 protein have utility as prognostic markers of patient survival
  • biomarker potential for chromophobe renal cell carcinoma
  • potential biomarker in colon adenocarcinoma
  • KLK7 and KLK14 gene expression can be regarded as markers of poor prognosis for Colon cancer (CC) patients with discriminating power between CC and adenoma patients
    • Therapy target
    SystemTypeDisorderPubmed
    cancerdigestivecolon
    may represent a potential therapeutic target for human colon tumorigenesis
    ANIMAL & CELL MODELS