K1B21_MOUSE
ID K1B21_MOUSE Reviewed; 261 AA.
AC Q61759; Q61760; Q9JM70;
DT 07-JUN-2004, integrated into UniProtKB/Swiss-Prot.
DT 07-JUN-2004, sequence version 3.
DT 03-AUG-2022, entry version 153.
DE RecName: Full=Kallikrein 1-related peptidase b21;
DE EC=3.4.21.35;
DE AltName: Full=Glandular kallikrein K21;
DE Short=mGK-21;
DE AltName: Full=Tissue kallikrein 21;
DE Flags: Precursor;
GN Name=Klk1b21; Synonyms=Klk-21, Klk21;
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 {ECO:0000312|EMBL:BAA92319.1};
RN [1] {ECO:0000312|EMBL:BAA92319.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Testis {ECO:0000269|PubMed:11082197};
RX PubMed=11082197; DOI=10.1046/j.1432-1033.2000.01786.x;
RA Matsui H., Moriyama A., Takahashi T.;
RT "Cloning and characterization of mouse Klk27, a novel tissue kallikrein
RT expressed in testicular Leydig cells and exhibiting chymotrypsin-like
RT specificity.";
RL Eur. J. Biochem. 267:6858-6865(2000).
RN [2] {ECO:0000305}
RP NUCLEOTIDE SEQUENCE, FUNCTION, ACTIVITY REGULATION, TISSUE SPECIFICITY,
RP DEVELOPMENTAL STAGE, AND INDUCTION.
RC TISSUE=Testis {ECO:0000269|PubMed:11606460};
RX PubMed=11606460; DOI=10.1210/endo.142.11.8505;
RA Matsui H., Takahashi T.;
RT "Mouse testicular Leydig cells express Klk21, a tissue kallikrein that
RT cleaves fibronectin and IGF-binding protein-3.";
RL Endocrinology 142:4918-4929(2001).
RN [3] {ECO:0000312|EMBL:AAH12243.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N {ECO:0000312|EMBL:AAH12243.1};
RC TISSUE=Salivary gland {ECO:0000312|EMBL:AAH12243.1};
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] {ECO:0000305}
RP NUCLEOTIDE SEQUENCE OF 17-54 AND 70-122.
RC STRAIN=BALB/cJ {ECO:0000269|PubMed:3036794};
RC TISSUE=Liver {ECO:0000269|PubMed:3036794};
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. Displays trypsin-like substrate
CC specificity and shows activity towards casein, gelatin, fibronectin and
CC IGFBP3. {ECO:0000269|PubMed:11606460}.
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; Evidence={ECO:0000305};
CC -!- ACTIVITY REGULATION: Inhibited by protease inhibitors
CC diisopropylfluorophosphate, leupeptin, antipain, benzamidine,
CC phenylmethylsulfonyl fluoride and soybean trypsin inhibitor.
CC {ECO:0000269|PubMed:11606460}.
CC -!- TISSUE SPECIFICITY: Expressed in testis and submaxillary gland. In the
CC testis, expression localized specifically to Leydig cells in the
CC interstitial tissues. {ECO:0000269|PubMed:11606460}.
CC -!- DEVELOPMENTAL STAGE: Detectable in testis 4 weeks after birth, becoming
CC more prominent thereafter. {ECO:0000269|PubMed:11606460}.
CC -!- INDUCTION: By T protein. {ECO:0000269|PubMed:11606460}.
CC -!- SIMILARITY: Belongs to the peptidase S1 family. Kallikrein subfamily.
CC {ECO:0000255|PROSITE-ProRule:PRU00274}.
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DR EMBL; AB039276; BAA92319.1; -; mRNA.
DR EMBL; BC012243; AAH12243.1; -; mRNA.
DR EMBL; M18597; AAA39359.1; -; Genomic_DNA.
DR EMBL; M18617; AAA39360.1; -; Genomic_DNA.
DR CCDS; CCDS21195.1; -.
DR PIR; I70036; I70036.
DR PIR; I70037; I70037.
DR RefSeq; NP_034772.1; NM_010642.3.
DR AlphaFoldDB; Q61759; -.
DR SMR; Q61759; -.
DR STRING; 10090.ENSMUSP00000082582; -.
DR MEROPS; S01.038; -.
DR GlyGen; Q61759; 1 site.
DR PaxDb; Q61759; -.
DR PRIDE; Q61759; -.
DR ProteomicsDB; 268930; -.
DR DNASU; 16616; -.
DR Ensembl; ENSMUST00000085455; ENSMUSP00000082582; ENSMUSG00000066516.
DR GeneID; 16616; -.
DR KEGG; mmu:16616; -.
DR UCSC; uc009goh.1; mouse.
DR CTD; 16616; -.
DR MGI; MGI:892022; Klk1b21.
DR VEuPathDB; HostDB:ENSMUSG00000066516; -.
DR eggNOG; KOG3627; Eukaryota.
DR GeneTree; ENSGT01020000230389; -.
DR HOGENOM; CLU_006842_1_1_1; -.
DR InParanoid; Q61759; -.
DR OMA; PWLSLVY; -.
DR PhylomeDB; Q61759; -.
DR TreeFam; TF331065; -.
DR Reactome; R-MMU-1592389; Activation of Matrix Metalloproteinases.
DR BioGRID-ORCS; 16616; 3 hits in 45 CRISPR screens.
DR ChiTaRS; Klk1b21; mouse.
DR PRO; PR:Q61759; -.
DR Proteomes; UP000000589; Chromosome 7.
DR RNAct; Q61759; protein.
DR Bgee; ENSMUSG00000066516; Expressed in submandibular gland and 38 other tissues.
DR ExpressionAtlas; Q61759; baseline and differential.
DR Genevisible; Q61759; 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; IDA: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:0006508; P:proteolysis; IDA: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..17
FT /evidence="ECO:0000255"
FT PROPEP 18..24
FT /note="Activation peptide"
FT /evidence="ECO:0000250|UniProtKB:P36368"
FT /id="PRO_0000027987"
FT CHAIN 25..261
FT /note="Kallikrein 1-related peptidase b21"
FT /id="PRO_0000027988"
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 /evidence="ECO:0000250|UniProtKB:P36368"
FT ACT_SITE 120
FT /note="Charge relay system"
FT /evidence="ECO:0000250|UniProtKB:P36368"
FT ACT_SITE 213
FT /note="Charge relay system"
FT /evidence="ECO:0000250|UniProtKB:P36368"
FT CARBOHYD 102
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 31..173
FT /evidence="ECO:0000250|UniProtKB:P36368,
FT ECO:0000255|PROSITE-ProRule:PRU00274"
FT DISULFID 50..66
FT /evidence="ECO:0000250|UniProtKB:P36368,
FT ECO:0000255|PROSITE-ProRule:PRU00274"
FT DISULFID 152..219
FT /evidence="ECO:0000250|UniProtKB:P36368,
FT ECO:0000255|PROSITE-ProRule:PRU00274"
FT DISULFID 184..198
FT /evidence="ECO:0000250|UniProtKB:P36368,
FT ECO:0000255|PROSITE-ProRule:PRU00274"
FT DISULFID 209..234
FT /evidence="ECO:0000250|UniProtKB:P36368,
FT ECO:0000255|PROSITE-ProRule:PRU00274"
SQ SEQUENCE 261 AA; 28690 MW; 608B976BC78E03EE CRC64;
MRFLILFLAL SLGEIDAAPP VQSRIVGGFN CEKNSQPWHV AVFRYNKYIC GGVLLNPNWV
LTAAHCYGNQ YNVWLGKNKL FQHESSAQHR LVSKSFPHPD YNMSLMNDHT PHPEDDYSND
LMLLRLSKPA DITDAVKPID LPTEEPKLGS TCLASGWGSI TPTKWQIPND LQCGFIKPLP
NENCAKAYIH KVTDVMLCAG EMGGGKDTCA GDSGGPLICD GVLQGITSWG SIPCAKPNAP
AIYTKLIKFT SWIKDTMAKN P
