ID K1KB8_MOUSE Reviewed; 261 AA. AC P07628; DT 01-APR-1988, integrated into UniProtKB/Swiss-Prot. DT 01-APR-1988, sequence version 1. DT 24-JAN-2024, entry version 169. DE RecName: Full=Kallikrein 1-related peptidase b8; DE EC=3.4.21.35; DE AltName: Full=Glandular kallikrein K8; DE Short=mGK-8; DE AltName: Full=Tissue kallikrein-8; DE Flags: Precursor; GN Name=Klk1b8; Synonyms=Klk-8, Klk8; 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 [MRNA]. RX PubMed=3636812; DOI=10.1093/nar/14.12.4823; RA Fahnestock M., Brundage S., Shooter E.M.; RT "The sequence of a cDNA clone coding for a novel kallikrein from mouse RT submaxillary gland."; RL Nucleic Acids Res. 14:4823-4835(1986). RN [2] RP NUCLEOTIDE SEQUENCE OF 16-54 AND 70-122. 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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; X03994; CAA27630.1; -; mRNA. DR EMBL; M18587; AAA39347.1; -; Genomic_DNA. DR EMBL; M18607; AAA39348.1; -; Genomic_DNA. DR CCDS; CCDS21189.1; -. DR PIR; A24378; A24378. DR RefSeq; NP_032483.1; NM_008457.3. DR AlphaFoldDB; P07628; -. DR SMR; P07628; -. DR STRING; 10090.ENSMUSP00000072063; -. DR MEROPS; S01.067; -. DR GlyCosmos; P07628; 1 site, No reported glycans. DR GlyGen; P07628; 1 site. DR MaxQB; P07628; -. DR PaxDb; 10090-ENSMUSP00000072063; -. DR ProteomicsDB; 269167; -. DR DNASU; 16624; -. DR Ensembl; ENSMUST00000072204.5; ENSMUSP00000072063.5; ENSMUSG00000063089.5. DR GeneID; 16624; -. DR KEGG; mmu:16624; -. DR UCSC; uc009gob.1; mouse. DR AGR; MGI:892018; -. DR CTD; 16624; -. DR MGI; MGI:892018; Klk1b8. DR VEuPathDB; HostDB:ENSMUSG00000063089; -. DR eggNOG; KOG3627; Eukaryota. DR GeneTree; ENSGT01020000230389; -. DR HOGENOM; CLU_006842_1_1_1; -. DR InParanoid; P07628; -. DR OrthoDB; 2495122at2759; -. DR PhylomeDB; P07628; -. DR TreeFam; TF331065; -. DR BRENDA; 3.4.21.118; 3474. DR BioGRID-ORCS; 16624; 3 hits in 78 CRISPR screens. DR ChiTaRS; Klk1b8; mouse. DR PRO; PR:P07628; -. DR Proteomes; UP000000589; Chromosome 7. DR RNAct; P07628; Protein. DR Bgee; ENSMUSG00000063089; Expressed in submandibular gland and 134 other cell types or tissues. 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; ISO:MGI. DR GO; GO:0008236; F:serine-type peptidase activity; ISO: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. DR Genevisible; P07628; MM. 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_0000027977" FT CHAIN 25..261 FT /note="Kallikrein 1-related peptidase b8" FT /id="PRO_0000027978" 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; 28531 MW; D0174F7093137322 CRC64; MRFLILFLAL SLGGIDAAPP LQSRVVGGFN CEKNSQPWQV AVYDNKEHIC GGVLLERNWV LTAAHCYVDQ YEVWLGKNKL FQEEPSAQHR LVSKSFPHPG FNMSLLTLKE IPPGADFSND LMLLRLSKPA DITDAVKPIT LPTKESKLGS TCLASGWGSI TPTKWQKPDD LQCVFLKLLP IKNCIENHNV KVTDVMLCAG EMSGGKNICK GDSGGPLICD SVLQGITSTG PIPCGKPGVP AMYTNLIKFN SWIKDTMTKN S //