K1B22_MOUSE
ID K1B22_MOUSE Reviewed; 259 AA.
AC P15948;
DT 01-APR-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-APR-1990, sequence version 1.
DT 03-AUG-2022, entry version 165.
DE RecName: Full=Kallikrein 1-related peptidase b22;
DE EC=3.4.21.35;
DE AltName: Full=Beta-NGF-endopeptidase;
DE AltName: Full=Epidermal growth factor-binding protein type A;
DE Short=EGF-BP A;
DE AltName: Full=Glandular kallikrein K22;
DE Short=mGK-22;
DE AltName: Full=Nerve growth factor beta chain endopeptidase;
DE AltName: Full=Tissue kallikrein 22;
DE Flags: Precursor;
GN Name=Klk1b22; Synonyms=Klk-22, Klk22;
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=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 [2]
RP PROTEIN SEQUENCE OF 25-54.
RX PubMed=2012805; DOI=10.1021/bi00228a014;
RA Fahnestock M., Woo J.E., Lopez G.A., Snow J., Walz D.A., Arici M.J.,
RA Mobley W.C.;
RT "Beta-NGF-endopeptidase: structure and activity of a kallikrein encoded by
RT the gene mGK-22.";
RL Biochemistry 30:3443-3450(1991).
RN [3]
RP PROTEIN SEQUENCE OF 25-41.
RC TISSUE=Submandibular gland;
RX PubMed=1639762; DOI=10.1093/oxfordjournals.jbchem.a123812;
RA Peters J., Takahashi S., Tada M., Miyake Y.;
RT "mGK-6-derived true tissue kallikrein is synthesized, processed, and
RT targeted through a regulated secretory pathway in mouse pituitary AtT-20
RT cells.";
RL J. Biochem. 111:643-648(1992).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 17-54 AND 70-120.
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; M17979; AAA37682.1; ALT_SEQ; Genomic_DNA.
DR EMBL; M17977; AAA37682.1; JOINED; Genomic_DNA.
DR EMBL; M17978; AAA37682.1; JOINED; Genomic_DNA.
DR EMBL; M18598; AAA39361.1; -; Genomic_DNA.
DR EMBL; M18618; AAA39362.1; -; Genomic_DNA.
DR CCDS; CCDS21196.1; -.
DR PIR; A29746; A29746.
DR RefSeq; NP_034244.1; NM_010114.2.
DR AlphaFoldDB; P15948; -.
DR SMR; P15948; -.
DR STRING; 10090.ENSMUSP00000076733; -.
DR MEROPS; S01.039; -.
DR GlyGen; P15948; 1 site.
DR PaxDb; P15948; -.
DR PRIDE; P15948; -.
DR ProteomicsDB; 269136; -.
DR DNASU; 13646; -.
DR Ensembl; ENSMUST00000077528; ENSMUSP00000076733; ENSMUSG00000060177.
DR GeneID; 13646; -.
DR KEGG; mmu:13646; -.
DR UCSC; uc009goi.1; mouse.
DR CTD; 13646; -.
DR MGI; MGI:95291; Klk1b22.
DR VEuPathDB; HostDB:ENSMUSG00000060177; -.
DR eggNOG; KOG3627; Eukaryota.
DR GeneTree; ENSGT01020000230389; -.
DR HOGENOM; CLU_006842_1_1_1; -.
DR InParanoid; P15948; -.
DR OMA; CADAHIQ; -.
DR OrthoDB; 1314811at2759; -.
DR PhylomeDB; P15948; -.
DR TreeFam; TF331065; -.
DR Reactome; R-MMU-1592389; Activation of Matrix Metalloproteinases.
DR BioGRID-ORCS; 13646; 3 hits in 74 CRISPR screens.
DR ChiTaRS; Klk1b22; mouse.
DR PRO; PR:P15948; -.
DR Proteomes; UP000000589; Chromosome 7.
DR RNAct; P15948; protein.
DR Bgee; ENSMUSG00000060177; Expressed in right kidney and 9 other tissues.
DR ExpressionAtlas; P15948; baseline and differential.
DR Genevisible; P15948; 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 1: Evidence at protein level;
KW Direct protein sequencing; Disulfide bond; Glycoprotein; Hydrolase;
KW Protease; Reference proteome; Serine protease; Signal; Zymogen.
FT SIGNAL 1..17
FT PROPEP 18..24
FT /note="Activation peptide"
FT /evidence="ECO:0000269|PubMed:1639762,
FT ECO:0000269|PubMed:2012805"
FT /id="PRO_0000027989"
FT CHAIN 25..259
FT /note="Kallikrein 1-related peptidase b22"
FT /id="PRO_0000027990"
FT DOMAIN 25..256
FT /note="Peptidase S1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT ACT_SITE 65
FT /note="Charge relay system"
FT ACT_SITE 118
FT /note="Charge relay system"
FT ACT_SITE 211
FT /note="Charge relay system"
FT CARBOHYD 102
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000305"
FT DISULFID 31..171
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT DISULFID 50..66
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT DISULFID 150..217
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT DISULFID 182..196
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT DISULFID 207..232
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
SQ SEQUENCE 259 AA; 28384 MW; D7745794D8A87B9C CRC64;
MRFLILFLTL SLGGIDAAPP VQSRILGGFK CEKNSQPWQV AVYYLDEYLC GGVLLDRNWV
LTAAHCYEDK YNIWLGKNKL FQDEPSAQHR LVSKSFPHPD FNMSLLQSVP TGADLSNDLM
LLRLSKPADI TDVVKPIDLP TTEPKLGSTC LASGWGSINQ LIYQNPNDLQ CVSIKLHPNE
VCVKAHILKV TDVMLCAGEM NGGKDTCKGD SGGPLICDGV LQGITSWGST PCGEPNAPAI
YTKLIKFTSW IKDTMAKNP
