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FLASH GENE
Symbol KLK7 contributors: mct/npt - updated : 10-07-2018
HGNC name kallikrein-related peptidase 7
HGNC id 6368
Location 19q13.33      Physical location : 51.479.729 - 51.487.150
Synonym name
  • stratum corneum chymotryptic enzyme
  • kallikrein 7 (chymotryptic, stratum corneum)
  • protease, serine, 6
  • Synonym symbol(s) SCCE, PRSS6, hK7
    EC.number 3.4.21.117
    DNA
    TYPE functioning gene
    SPECIAL FEATURE component of a cluster
    text tightly clustered multigene family on chromosome 19q13.4
    STRUCTURE 7.59 kb     6 Exon(s)
    10 Kb 5' upstream gene genomic sequence study
    MAPPING cloned Y linked N status provisional
    regionally located clustered with kallikrein gene family
    RNA
    TRANSCRIPTS type messenger
    identificationnb exonstypebpproduct
    ProteinkDaAAspecific expressionYearPubmed
    6 splicing 1927 27.4 253 - 2008 18627343
  • 6 exons
  • differing in the 5' UTR compared to variant 2
  • both variants encode the same protein
  • 6 splicing 1927 27.4 253 - 2008 18627343
  • 6 exons
  • differing in the 5' UTR compared to variant 1
  • both variants encode the same protein
  • 5 - 1956 - 246 - 2008 18627343
    5 - 1973 - 161 - 2008 18627343
    EXPRESSION
    Type restricted
       expressed in (based on citations)
    organ(s)
    SystemOrgan level 1Organ level 2Organ level 3Organ level 4LevelPubmedSpeciesStageRna symbol
    Cardiovascularheart     Homo sapiens
    Digestiveesophagus     Homo sapiens
     liver     Homo sapiens
    Lymphoid/Immunetonsils   highly Homo sapiens
    Skin/Tegumentskin appendageshairfollicle   Homo sapiens
    Urinarykidneytubule  highly
    tissue
    SystemTissueTissue level 1Tissue level 2LevelPubmedSpeciesStageRna symbol
    Epithelialbarrier/liningepidermisstratum corneumhighly Homo sapiens
    skin tegumentdermis   
    cells
    SystemCellPubmedSpeciesStageRna symbol
    Skin/Tegumentkeratinocyte
    cell lineage
    cell lines
    fluid/secretion
    at STAGE
    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