K1KB9_MOUSE
ID K1KB9_MOUSE Reviewed; 261 AA.
AC P15949;
DT 01-APR-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-APR-1990, sequence version 1.
DT 03-AUG-2022, entry version 174.
DE RecName: Full=Kallikrein 1-related peptidase b9;
DE EC=3.4.21.35;
DE AltName: Full=Epidermal growth factor-binding protein type C;
DE Short=EGF-BP C;
DE AltName: Full=Glandular kallikrein K9;
DE Short=mGK-9;
DE AltName: Full=Tissue kallikrein-9;
DE Flags: Precursor;
GN Name=Klk1b9; Synonyms=Egfbp3, Klk-9, Klk9;
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=3322386; DOI=10.1021/bi00395a025;
RA Blaber M., Isackson P.J., Bradshaw R.A.;
RT "A complete cDNA sequence for the major epidermal growth factor binding
RT protein in the male mouse submandibular gland.";
RL Biochemistry 26:6742-6749(1987).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=BALB/cJ; TISSUE=Salivary gland;
RX PubMed=3322387; DOI=10.1021/bi00395a026;
RA Drinkwater C.C., Evans B.A., Richards R.I.;
RT "Mouse glandular kallikrein genes: identification and characterization of
RT the genes encoding the epidermal growth factor binding proteins.";
RL Biochemistry 26:6750-6756(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).
RN [4]
RP NUCLEOTIDE SEQUENCE OF 16-54 AND 70-122.
RC STRAIN=BALB/cJ; TISSUE=Liver;
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; M17962; AAA37541.1; -; mRNA.
DR EMBL; M17985; AAA37681.1; -; Genomic_DNA.
DR EMBL; M17983; AAA37681.1; JOINED; Genomic_DNA.
DR EMBL; M17984; AAA37681.1; JOINED; Genomic_DNA.
DR EMBL; BC024624; AAH24624.1; -; mRNA.
DR EMBL; BC048869; AAH48869.1; -; mRNA.
DR EMBL; M18588; AAA39350.1; ALT_SEQ; Genomic_DNA.
DR EMBL; M18608; AAA39351.1; -; Genomic_DNA.
DR CCDS; CCDS21191.1; -.
DR PIR; C29746; A29745.
DR PIR; I70014; I70014.
DR RefSeq; NP_034246.1; NM_010116.1.
DR AlphaFoldDB; P15949; -.
DR SMR; P15949; -.
DR STRING; 10090.ENSMUSP00000080133; -.
DR MEROPS; S01.071; -.
DR GlyGen; P15949; 1 site.
DR MaxQB; P15949; -.
DR PaxDb; P15949; -.
DR PRIDE; P15949; -.
DR ProteomicsDB; 269141; -.
DR DNASU; 13648; -.
DR Ensembl; ENSMUST00000081399; ENSMUSP00000080133; ENSMUSG00000059042.
DR GeneID; 13648; -.
DR KEGG; mmu:13648; -.
DR UCSC; uc009god.1; mouse.
DR CTD; 13648; -.
DR MGI; MGI:95293; Klk1b9.
DR VEuPathDB; HostDB:ENSMUSG00000059042; -.
DR eggNOG; KOG3627; Eukaryota.
DR GeneTree; ENSGT01020000230389; -.
DR HOGENOM; CLU_006842_1_1_1; -.
DR InParanoid; P15949; -.
DR OMA; WLENDIS; -.
DR OrthoDB; 1314811at2759; -.
DR PhylomeDB; P15949; -.
DR TreeFam; TF331065; -.
DR BRENDA; 3.4.21.B40; 3474.
DR Reactome; R-MMU-1592389; Activation of Matrix Metalloproteinases.
DR BioGRID-ORCS; 13648; 3 hits in 70 CRISPR screens.
DR ChiTaRS; Klk1b9; mouse.
DR PRO; PR:P15949; -.
DR Proteomes; UP000000589; Chromosome 7.
DR RNAct; P15949; protein.
DR Bgee; ENSMUSG00000059042; Expressed in male reproductive system and 10 other tissues.
DR Genevisible; P15949; 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:0008233; F:peptidase activity; IDA: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; IDA:MGI.
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; 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 /id="PRO_0000027979"
FT CHAIN 25..261
FT /note="Kallikrein 1-related peptidase b9"
FT /id="PRO_0000027980"
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; 28900 MW; 796FD4DAE56020D7 CRC64;
MRFLILFLAL SLGGIDAAPP VHSRIVGGFK CEKNSQPWHV AVYRYNEYIC GGVLLDANWV
LTAAHCYYEE NKVSLGKNNL YEEEPSAQHR LVSKSFLHPG YNRSLHRNHI RHPEYDYSND
LMLLRLSKPA DITDVVKPIA LPTEEPKLGS TCLASGWGST TPFKFQNAKD LQCVNLKLLP
NEDCGKAHIE KVTDVMLCAG ETDGGKDTCK GDSGGPLICD GVLQGITSWG FTPCGEPKKP
GVYTKLIKFT SWIKDTMAKN L
