ID K1KB5_MOUSE Reviewed; 261 AA.
AC P15945; Q52KM1; Q565D7;
DT 01-APR-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-APR-1990, sequence version 1.
DT 24-JAN-2024, entry version 188.
DE RecName: Full=Kallikrein 1-related peptidase b5;
DE EC=3.4.21.35;
DE AltName: Full=Glandular kallikrein K5;
DE Short=mGK-5;
DE AltName: Full=Tissue kallikrein-5;
DE Flags: Precursor;
GN Name=Klk1b5; Synonyms=Klk-5, Klk5;
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].
RC STRAIN=BALB/cJ; TISSUE=Liver;
RX PubMed=3502721; DOI=10.1093/nar/15.23.10052;
RA Drinkwater C.C., Richards R.I.;
RT "Sequence of the mouse glandular kallikrein gene, mGK-5.";
RL Nucleic Acids Res. 15:10052-10052(1987).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N; TISSUE=Salivary gland;
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).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 17-54 AND 70-122.
RC STRAIN=BALB/cJ;
RX PubMed=3036794; DOI=10.1016/s0021-9258(18)47521-7;
RA Evans B.A., Drinkwater C.C., Richards R.I.;
RT "Mouse glandular kallikrein genes. Structure and partial sequence analysis
RT of the kallikrein gene locus.";
RL J. Biol. Chem. 262:8027-8034(1987).
CC -!- FUNCTION: Glandular kallikreins cleave Met-Lys and Arg-Ser bonds in
CC kininogen to release Lys-bradykinin.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Preferential cleavage of Arg-|-Xaa bonds in small molecule
CC substrates. Highly selective action to release kallidin (lysyl-
CC bradykinin) from kininogen involves hydrolysis of Met-|-Xaa or Leu-|-
CC Xaa.; EC=3.4.21.35;
CC -!- SIMILARITY: Belongs to the peptidase S1 family. Kallikrein subfamily.
CC {ECO:0000255|PROSITE-ProRule:PRU00274}.
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DR EMBL; Y00500; CAA68553.1; -; Genomic_DNA.
DR EMBL; BC013659; AAH13659.1; -; mRNA.
DR EMBL; BC094281; AAH94281.1; -; mRNA.
DR EMBL; M18584; AAX76511.1; -; Genomic_DNA.
DR EMBL; M18604; AAD15284.3; -; Genomic_DNA.
DR CCDS; CCDS21201.1; -.
DR PIR; S06305; TRMSM5.
DR RefSeq; NP_032482.1; NM_008456.4.
DR AlphaFoldDB; P15945; -.
DR SMR; P15945; -.
DR STRING; 10090.ENSMUSP00000073964; -.
DR BindingDB; P15945; -.
DR ChEMBL; CHEMBL5169118; -.
DR MEROPS; S01.037; -.
DR GlyCosmos; P15945; 1 site, No reported glycans.
DR GlyGen; P15945; 1 site.
DR iPTMnet; P15945; -.
DR PhosphoSitePlus; P15945; -.
DR CPTAC; non-CPTAC-3468; -.
DR MaxQB; P15945; -.
DR PaxDb; 10090-ENSMUSP00000073964; -.
DR PeptideAtlas; P15945; -.
DR ProteomicsDB; 269444; -.
DR DNASU; 16622; -.
DR Ensembl; ENSMUST00000074359.4; ENSMUSP00000073964.3; ENSMUSG00000066512.4.
DR GeneID; 16622; -.
DR KEGG; mmu:16622; -.
DR UCSC; uc009gon.1; mouse.
DR AGR; MGI:892020; -.
DR CTD; 16622; -.
DR MGI; MGI:892020; Klk1b5.
DR VEuPathDB; HostDB:ENSMUSG00000066512; -.
DR eggNOG; KOG3627; Eukaryota.
DR GeneTree; ENSGT01020000230389; -.
DR HOGENOM; CLU_006842_1_1_1; -.
DR InParanoid; P15945; -.
DR OMA; ERTMADN; -.
DR OrthoDB; 4629979at2759; -.
DR PhylomeDB; P15945; -.
DR TreeFam; TF331065; -.
DR BRENDA; 3.4.21.B39; 3474.
DR BioGRID-ORCS; 16622; 4 hits in 48 CRISPR screens.
DR ChiTaRS; Klk1b5; mouse.
DR PRO; PR:P15945; -.
DR Proteomes; UP000000589; Chromosome 7.
DR RNAct; P15945; Protein.
DR Bgee; ENSMUSG00000066512; Expressed in submandibular gland and 21 other cell types or tissues.
DR Genevisible; P15945; MM.
DR GO; GO:0001669; C:acrosomal vesicle; ISO:MGI.
DR GO; GO:0045177; C:apical part of cell; ISO:MGI.
DR GO; GO:0005615; C:extracellular space; ISO:MGI.
DR GO; GO:0005634; C:nucleus; ISO:MGI.
DR GO; GO:0032991; C:protein-containing complex; ISO:MGI.
DR GO; GO:0030141; C:secretory granule; IBA:GO_Central.
DR GO; GO:0004175; F:endopeptidase activity; ISO:MGI.
DR GO; GO:0016811; F:hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in linear amides; ISO:MGI.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IDA:MGI.
DR GO; GO:0008236; F:serine-type peptidase activity; ISO:MGI.
DR GO; GO:0006508; P:proteolysis; IDA:MGI.
DR GO; GO:0003073; P:regulation of systemic arterial blood pressure; IBA:GO_Central.
DR GO; GO:0031638; P:zymogen activation; IBA:GO_Central.
DR CDD; cd00190; Tryp_SPc; 1.
DR Gene3D; 2.40.10.10; Trypsin-like serine proteases; 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 PANTHER; PTHR24271:SF47; KALLIKREIN-1; 1.
DR PANTHER; PTHR24271; KALLIKREIN-RELATED; 1.
DR Pfam; PF00089; Trypsin; 1.
DR PRINTS; PR00722; CHYMOTRYPSIN.
DR SMART; SM00020; Tryp_SPc; 1.
DR SUPFAM; SSF50494; Trypsin-like serine proteases; 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; Glycoprotein; Hydrolase; Protease; Reference proteome;
KW Serine protease; Signal; Zymogen.
FT SIGNAL 1..18
FT /evidence="ECO:0000305"
FT PROPEP 19..24
FT /note="Activation peptide"
FT /evidence="ECO:0000305"
FT /id="PRO_0000027973"
FT CHAIN 25..261
FT /note="Kallikrein 1-related peptidase b5"
FT /id="PRO_0000027974"
FT DOMAIN 25..258
FT /note="Peptidase S1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT ACT_SITE 65
FT /note="Charge relay system"
FT ACT_SITE 120
FT /note="Charge relay system"
FT ACT_SITE 213
FT /note="Charge relay system"
FT CARBOHYD 102
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000305"
FT DISULFID 31..173
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT DISULFID 50..66
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT DISULFID 152..219
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT DISULFID 184..198
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT DISULFID 209..234
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
SQ SEQUENCE 261 AA; 28748 MW; 29B4D669335522D8 CRC64;
MWFLILFLAL SLGGIDAAPP VQSRIFGGFN CEKNSQPWQV AVYRFTKYQC GGVLLNANWV
LTAAHCHNDK YQVWLGKNNF FEDEPSAQHR LVSKAIPHPD FNMSLLNEHT PQPEDDYSND
LMLLRLKKPA DITDVVKPID LPTEEPKLGS TCLASGWGSI TPVIYEPADD LQCVNFKLLP
NEDCVKAHIE KVTDVMLCAG DMDGGKDTCM GDSGGPLICD GVLHGITSWG PSPCGKPNVP
GIYTKLIKFN SWIKDTIAKN A
//
