K1B11_MOUSE
ID K1B11_MOUSE Reviewed; 261 AA.
AC P15946;
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 b11;
DE EC=3.4.21.35;
DE AltName: Full=Glandular kallikrein K11;
DE Short=mGK-11;
DE AltName: Full=Tissue kallikrein-11;
DE Flags: Precursor;
GN Name=Klk1b11; Synonyms=Klk-11, Klk11;
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].
RX PubMed=3848399; DOI=10.1002/j.1460-2075.1985.tb02327.x;
RA Evans B.A., Richards R.I.;
RT "Genes for the alpha and gamma subunits of mouse nerve growth factor are
RT contiguous.";
RL EMBO J. 4:133-138(1985).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=BALB/cJ; TISSUE=Liver;
RX PubMed=3205728; DOI=10.1093/nar/16.22.10918;
RA Drinkwater C.C., Richards R.I.;
RT "Sequence of mGK-11, a mouse glandular kallikrein gene.";
RL Nucleic Acids Res. 16:10918-10918(1988).
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 [GENOMIC DNA] OF 16-54 AND 69-122.
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; X13215; CAA31604.3; -; Genomic_DNA.
DR EMBL; X13216; CAA31604.3; JOINED; Genomic_DNA.
DR EMBL; X13217; CAA31604.3; JOINED; Genomic_DNA.
DR EMBL; X13218; CAA31604.3; JOINED; Genomic_DNA.
DR EMBL; BC013660; AAH13660.1; -; mRNA.
DR EMBL; M18590; AAA39352.1; ALT_SEQ; Genomic_DNA.
DR EMBL; M18610; AAA39353.1; -; Genomic_DNA.
DR CCDS; CCDS21192.1; -.
DR PIR; I70022; I70022.
DR PIR; S01971; S01971.
DR RefSeq; NP_034770.1; NM_010640.2.
DR AlphaFoldDB; P15946; -.
DR SMR; P15946; -.
DR STRING; 10090.ENSMUSP00000007156; -.
DR MEROPS; S01.041; -.
DR GlyGen; P15946; 1 site.
DR MaxQB; P15946; -.
DR PaxDb; P15946; -.
DR PeptideAtlas; P15946; -.
DR PRIDE; P15946; -.
DR ProteomicsDB; 269438; -.
DR DNASU; 16613; -.
DR Ensembl; ENSMUST00000007156; ENSMUSP00000007156; ENSMUSG00000044485.
DR GeneID; 16613; -.
DR KEGG; mmu:16613; -.
DR UCSC; uc009goe.1; mouse.
DR CTD; 16613; -.
DR MGI; MGI:892023; Klk1b11.
DR VEuPathDB; HostDB:ENSMUSG00000044485; -.
DR eggNOG; KOG3627; Eukaryota.
DR GeneTree; ENSGT01020000230389; -.
DR HOGENOM; CLU_006842_1_1_1; -.
DR InParanoid; P15946; -.
DR OMA; ITAWGPI; -.
DR OrthoDB; 1314811at2759; -.
DR PhylomeDB; P15946; -.
DR TreeFam; TF331065; -.
DR BRENDA; 3.4.21.B42; 3474.
DR Reactome; R-MMU-1592389; Activation of Matrix Metalloproteinases.
DR BioGRID-ORCS; 16613; 3 hits in 74 CRISPR screens.
DR ChiTaRS; Klk1b11; mouse.
DR PRO; PR:P15946; -.
DR Proteomes; UP000000589; Chromosome 7.
DR RNAct; P15946; protein.
DR Bgee; ENSMUSG00000044485; Expressed in submandibular gland and 14 other tissues.
DR ExpressionAtlas; P15946; baseline and differential.
DR Genevisible; P15946; 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; -; 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 /evidence="ECO:0000305"
FT /id="PRO_0000027981"
FT CHAIN 25..261
FT /note="Kallikrein 1-related peptidase b11"
FT /id="PRO_0000027982"
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; 28727 MW; 8D32EFE8D835EA7B CRC64;
MWFLILFLAL SLGGIDAAPP VQSRIVGGFN CEKNSQPWHV AVYRYNKYIC GGVLLDRNWV
LTAAHCHVSQ YNVWLGKTKL FQREPSAQHR MVSKSFPHPD YNMSLLIIHN PEPEDDESND
LMLLRLSEPA DITDAVKPIA LPTEEPKLGS TCLVSGWGSI TPTKFQTPDD LQCVSIKLLP
NEVCVKNHNQ KVTDVMLCAG EMGGGKDTCK GDSGGPLICD GVLHGITAWG PIPCGKPNTP
GVYTKLIKFT NWIKDTMAKN P
