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FLASH GENE
Symbol KLK14 contributors: mct - updated : 22-04-2020
HGNC name kallikrein-related peptidase 14
HGNC id 6362
PROTEIN
PHYSICAL PROPERTIES
STRUCTURE
motifs/domains
  • trypsin-like substrate specificity
  • signal sequence and catalytic domains
    • HOMOLOGY
    Homologene
    FAMILY
  • kallikrein family
  • peptidase S1 family
    • CATEGORY enzyme
    SUBCELLULAR LOCALIZATION extracellular
        intracellular
    intracellular,cytoplasm,cytosolic,granule
    text localized in the cytoplasm of epithelial cells of normal bronchus
    basic FUNCTION
  • involved in carcinogenesis
  • may participate in desquamation through cleavage of desmoglein 1 and regulation by LEKTI
  • may be a major contributor to trypsin-like proteolytic activity in stratum corneum, and key trypsin-like proteases involved in skin desquamation
  • playing a potential role in seminal plasma
  • exerting a significant and dose-dependent effect in the process of semen liquefaction
  • might function as a key factor in the proteolytic cascade in seminal plasma, regulating major seminal KLKs, including KLK1, KLK3, and KLK11
  • as other KLKs may participate in desquamation through cleavage of desmoglein 1 and regulation by LEKTI
  • activating KLK proteolytic cascade, including KLK3, KLK11 and KLK1
  • estrogen-sensitive kallikreins with KLK11, and KLK10, all synergistically enhanced and upregulated by androgens in breast cancer cells via a membrane bound androgen receptor
  • KLK14 promotes tumourigenesis by activating proteinase-activated receptors
  • is a serine protease linked to several pathologies including prostate cancer
  • HPN and TMPRSS2 colocalize on the cell surface with the secreted serine proteases KLK4 and KLK14, only in membrane protrusions, suggesting that reciprocal proteolytic interactions occur in defined cellular structures that are important during cancer dissemination for cell migration, invasion and survival
  • 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
  • cleaving semenogelins (SEMG1 and SEMG2 were able to reverse KLK14 inhibition by Zn2+, providing a novel regulatory mechanism for KLK14 activity)
  • KLK14, acting via F2RL1, represents an autocrine/paracrine regulator of colon tumorigenesis
  • KLK14 is a second KLK protease to be inhibited by SERPINA12
  • in contrast with HPN, TMPRSS2 degrades KLK14 and TMPRSS2 cleavage is mediated by KLK14
  • kinin B1 receptor agonist induces secretion of KLK1, KLK6, KLK10, KLK13 and KLK14 into the medium nof neutrophils
    • cell & other
    REGULATION
    activated by citrate
    inhibited by by autolytic cleavage
    zinc ions
    Other regulated by the inhibitory serpins alpha1-antitrypsin, alpha2-antiplasmin, antithrombin III, alpha1-antichymotrypsin and plasminogen activator inhibitor-1
    regulated by androgens and progestins
    ASSOCIATED DISORDERS
    corresponding disease(s)
    Other morbid association(s)
    TypeGene ModificationChromosome rearrangementProtein expressionProtein Function
    tumoral     --low  
    in testicular and ovarian cancer
    tumoral     --over  
    in invasive breast carcinomas compared to normal breast tissues, associated with higher tumour grade and size
    constitutional     --other  
    differentially expressed in asthenospermic cases
    tumoral     --over  
    during Prostate carcinoma development, and in advanced PCa, and particularly in metastasis
    Susceptibility
    Variant & Polymorphism
    Candidate gene
    Marker
  • its expression could be evaluated as a putative independent diagnostic biomarker in breast tumour biopsies
  • may be a promising new biomarker in salivary gland tumors
  • 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
  • therapeutic induction of the seminal proteolytic cascade can be utilized to supplement the current clinical treatment of male subfertility and conversely, targeted inhibition of key components of the cascade may have potential pharmaceutical utility as a novel topical contraceptive strategy
  • potential target for the treatment of skin disorders in which KLK activity is elevated
    • ANIMAL & CELL MODELS