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}.
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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 Genevisible; P07628; 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; 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.
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
//
