ID   K1KB1_MOUSE             Reviewed;         261 AA.
AC   P00755;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   21-JUL-1986, sequence version 1.
DT   27-MAR-2024, entry version 178.
DE   RecName: Full=Kallikrein 1-related peptidase b1;
DE            EC=3.4.21.35;
DE   AltName: Full=Glandular kallikrein K1;
DE            Short=mGK-1;
DE   AltName: Full=Tissue kallikrein-1;
DE   Flags: Precursor;
GN   Name=Klk1b1; Synonyms=Klk-1, Klk1;
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=Quakenbush inbred;
RX   PubMed=6602295; DOI=10.1038/303300a0;
RA   Mason A.J., Evans B.A., Cox D.R., Shine J., Richards R.I.;
RT   "Structure of mouse kallikrein gene family suggests a role in specific
RT   processing of biologically active peptides.";
RL   Nature 303:300-307(1983).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
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).
RN   [3]
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).
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; V00829; CAA24213.1; -; Genomic_DNA.
DR   EMBL; J00390; AAA39349.1; -; Genomic_DNA.
DR   EMBL; BC026378; AAH26378.1; -; mRNA.
DR   CCDS; CCDS21190.1; -.
DR   PIR; A00941; KQMS1.
DR   RefSeq; NP_034775.1; NM_010645.3.
DR   AlphaFoldDB; P00755; -.
DR   SMR; P00755; -.
DR   STRING; 10090.ENSMUSP00000077879; -.
DR   MEROPS; S01.164; -.
DR   GlyCosmos; P00755; 1 site, No reported glycans.
DR   GlyGen; P00755; 1 site.
DR   iPTMnet; P00755; -.
DR   PhosphoSitePlus; P00755; -.
DR   MaxQB; P00755; -.
DR   PaxDb; 10090-ENSMUSP00000077879; -.
DR   ProteomicsDB; 269139; -.
DR   DNASU; 16623; -.
DR   Ensembl; ENSMUST00000078835.3; ENSMUSP00000077879.3; ENSMUSG00000063133.3.
DR   GeneID; 16623; -.
DR   KEGG; mmu:16623; -.
DR   UCSC; uc009goc.1; mouse.
DR   AGR; MGI:892019; -.
DR   CTD; 16623; -.
DR   MGI; MGI:892019; Klk1b1.
DR   VEuPathDB; HostDB:ENSMUSG00000063133; -.
DR   eggNOG; KOG3627; Eukaryota.
DR   GeneTree; ENSGT01020000230389; -.
DR   HOGENOM; CLU_006842_1_1_1; -.
DR   InParanoid; P00755; -.
DR   OMA; MQNNICI; -.
DR   OrthoDB; 4629979at2759; -.
DR   PhylomeDB; P00755; -.
DR   TreeFam; TF331065; -.
DR   BRENDA; 3.4.21.35; 3474.
DR   BioGRID-ORCS; 16623; 3 hits in 80 CRISPR screens.
DR   ChiTaRS; Klk1b1; mouse.
DR   PRO; PR:P00755; -.
DR   Proteomes; UP000000589; Chromosome 7.
DR   RNAct; P00755; Protein.
DR   Bgee; ENSMUSG00000063133; Expressed in submandibular gland and 8 other cell types or tissues.
DR   ExpressionAtlas; P00755; baseline and differential.
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:0002936; P:bradykinin biosynthetic process; IMP:MGI.
DR   GO; GO:0060048; P:cardiac muscle contraction; IMP:MGI.
DR   GO; GO:0003220; P:left ventricular cardiac muscle tissue morphogenesis; IMP:MGI.
DR   GO; GO:0003073; P:regulation of systemic arterial blood pressure; IMP:MGI.
DR   GO; GO:0002255; P:tissue kallikrein-kinin cascade; IMP:MGI.
DR   GO; GO:0042311; P:vasodilation; IMP:MGI.
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; P00755; 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_0000027966"
FT   CHAIN           25..261
FT                   /note="Kallikrein 1-related peptidase b1"
FT                   /id="PRO_0000027967"
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;  29022 MW;  15DC946600AF1604 CRC64;
     MWFLILFLAL SLGGIDAAPP VQSRIVGGFK CEKNSQPWHV AVYRYKEYIC GGVLLDANWV
     LTAAHCYYEK NNVWLGKNNL YQDEPSAQHR LVSKSFLHPC YNMSLHRNRI QNPQDDYSYD
     LMLLRLSKPA DITDVVKPIA LPTEEPKLGS TCLASGWGSI IPVKFQYAKD LQCVNLKLLP
     NEDCDKAYVQ KVTDVMLCAG VKGGGKDTCK GDSGGPLICD GVLQGLTSWG YNPCGEPKKP
     GVYTKLIKFT SWIKDTLAQN P
//