KLK14_MOUSE
ID KLK14_MOUSE Reviewed; 250 AA.
AC Q8CGR5;
DT 07-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 127.
DE RecName: Full=Kallikrein-14;
DE EC=3.4.21.-;
DE AltName: Full=Glandular kallikrein KLK14;
DE Short=mGK14;
DE AltName: Full=Kallikrein related-peptidase 14;
DE Flags: Precursor;
GN Name=Klk14; Synonyms=Gk14;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=12437987; DOI=10.1016/s0006-291x(02)02629-3;
RA Olsson A.Y., Lundwall A.;
RT "Organization and evolution of the glandular kallikrein locus in Mus
RT musculus.";
RL Biochem. Biophys. Res. Commun. 299:305-311(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
CC -!- FUNCTION: Serine-type endopeptidase with a dual trypsin-like and
CC chymotrypsin-like substrate specificity. May activate/inactivate the
CC proteinase-activated receptors F2R, F2RL1 and F2RL3 and other
CC kallikreins including KLK1, KLK3, KLK5 and KLK11. May function in
CC seminal clot liquefaction through direct cleavage of the semenogelin
CC SEMG1 and SEMG2 and activation of KLK3. May function through desmoglein
CC DSG1 cleavage in epidermal desquamation a process by which the most
CC superficial corneocytes are shed from the skin surface. May be involved
CC in several aspects of tumor progression including growth, invasion and
CC angiogenesis (By similarity). {ECO:0000250}.
CC -!- ACTIVITY REGULATION: Inhibited by SERPINA1, SERPINC1, SERPINE1,
CC SERPINF2, aprotinin, soybean, trypsin inhibitor and leupeptin.
CC Inhibited by serine protease inhibitor SPINK5. Has an autoproteolytic
CC activity which may have a regulatory effect. Activated by citrate and
CC inhibited by zinc and to a lower extent by manganese (By similarity).
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space {ECO:0000250}.
CC -!- PTM: Proteolytic cleavage of the activation peptide produces the active
CC enzyme. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the peptidase S1 family. Kallikrein subfamily.
CC {ECO:0000255|PROSITE-ProRule:PRU00274}.
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DR EMBL; AY152433; AAN78421.1; -; Genomic_DNA.
DR EMBL; BC128019; AAI28020.1; -; mRNA.
DR CCDS; CCDS21180.1; -.
DR RefSeq; NP_777355.1; NM_174866.3.
DR RefSeq; XP_006541018.1; XM_006540955.3.
DR AlphaFoldDB; Q8CGR5; -.
DR SMR; Q8CGR5; -.
DR BioGRID; 235057; 1.
DR STRING; 10090.ENSMUSP00000056935; -.
DR MEROPS; S01.029; -.
DR PhosphoSitePlus; Q8CGR5; -.
DR MaxQB; Q8CGR5; -.
DR PaxDb; Q8CGR5; -.
DR PRIDE; Q8CGR5; -.
DR ProteomicsDB; 263659; -.
DR Antibodypedia; 18986; 213 antibodies from 27 providers.
DR DNASU; 317653; -.
DR Ensembl; ENSMUST00000056329; ENSMUSP00000056935; ENSMUSG00000044737.
DR GeneID; 317653; -.
DR KEGG; mmu:317653; -.
DR UCSC; uc009gni.2; mouse.
DR CTD; 43847; -.
DR MGI; MGI:2447564; Klk14.
DR VEuPathDB; HostDB:ENSMUSG00000044737; -.
DR eggNOG; KOG3627; Eukaryota.
DR GeneTree; ENSGT01020000230389; -.
DR HOGENOM; CLU_006842_7_0_1; -.
DR InParanoid; Q8CGR5; -.
DR OMA; QECRQAY; -.
DR OrthoDB; 1314811at2759; -.
DR PhylomeDB; Q8CGR5; -.
DR TreeFam; TF331065; -.
DR BioGRID-ORCS; 317653; 2 hits in 72 CRISPR screens.
DR ChiTaRS; Klk14; mouse.
DR PRO; PR:Q8CGR5; -.
DR Proteomes; UP000000589; Chromosome 7.
DR RNAct; Q8CGR5; protein.
DR Bgee; ENSMUSG00000044737; Expressed in esophagus and 23 other tissues.
DR ExpressionAtlas; Q8CGR5; baseline and differential.
DR GO; GO:0005615; C:extracellular space; ISS:UniProtKB.
DR GO; GO:0030141; C:secretory granule; IBA:GO_Central.
DR GO; GO:0004252; F:serine-type endopeptidase activity; ISS:UniProtKB.
DR GO; GO:0048730; P:epidermis morphogenesis; ISS:UniProtKB.
DR GO; GO:0009566; P:fertilization; ISS:UniProtKB.
DR GO; GO:0045744; P:negative regulation of G protein-coupled receptor signaling pathway; ISS:UniProtKB.
DR GO; GO:0045745; P:positive regulation of G protein-coupled receptor signaling pathway; ISS:UniProtKB.
DR GO; GO:0006508; P:proteolysis; ISS:UniProtKB.
DR GO; GO:0070684; P:seminal clot liquefaction; ISS:UniProtKB.
DR CDD; cd00190; Tryp_SPc; 1.
DR Gene3D; 2.40.10.10; -; 2.
DR InterPro; IPR009003; Peptidase_S1_PA.
DR InterPro; IPR043504; Peptidase_S1_PA_chymotrypsin.
DR InterPro; IPR001314; Peptidase_S1A.
DR InterPro; IPR001254; Trypsin_dom.
DR InterPro; IPR018114; TRYPSIN_HIS.
DR InterPro; IPR033116; TRYPSIN_SER.
DR Pfam; PF00089; Trypsin; 1.
DR PRINTS; PR00722; CHYMOTRYPSIN.
DR SMART; SM00020; Tryp_SPc; 1.
DR SUPFAM; SSF50494; SSF50494; 1.
DR PROSITE; PS50240; TRYPSIN_DOM; 1.
DR PROSITE; PS00134; TRYPSIN_HIS; 1.
DR PROSITE; PS00135; TRYPSIN_SER; 1.
PE 2: Evidence at transcript level;
KW Disulfide bond; Hydrolase; Protease; Reference proteome; Secreted;
KW Serine protease; Signal; Zymogen.
FT SIGNAL 1..18
FT /evidence="ECO:0000250"
FT PROPEP 19..23
FT /note="Activation peptide"
FT /evidence="ECO:0000250"
FT /id="PRO_0000378340"
FT CHAIN 24..250
FT /note="Kallikrein-14"
FT /id="PRO_0000378341"
FT DOMAIN 24..248
FT /note="Peptidase S1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT ACT_SITE 66
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT ACT_SITE 110
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT ACT_SITE 203
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT DISULFID 51..67
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT DISULFID 142..209
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT DISULFID 174..188
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT DISULFID 199..224
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
SQ SEQUENCE 250 AA; 27016 MW; F62FEBF2290FEBE8 CRC64;
MFLLLIILQA LAVAIAQSQG DHKIIGGYRC VRNSQPWQVA LQAGPGHRFL CGGVLLSDQW
VITAAHCARP ILHVALGKHN IRRWEATQQV VRVARQVPHP QYQPQAHDND LMLLKLQKKV
RLGRAVKTIS VASSCASPGT PCRVSGWGTI ASPIARYPTA LQCVNVNIMS EQACHRAYPG
IITSGMVCAG VPEGGKDSCQ GDSGGPLVCG GQLQGLVSWG MERCAMPGYP GVYANLCNYH
SWIQRTMQSN
