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   24-JAN-2024, entry version 161.
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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
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   GlyCosmos; Q61759; 1 site, No reported glycans.
DR   GlyGen; Q61759; 1 site.
DR   PaxDb; 10090-ENSMUSP00000082582; -.
DR   ProteomicsDB; 268930; -.
DR   DNASU; 16616; -.
DR   Ensembl; ENSMUST00000085455.6; ENSMUSP00000082582.5; ENSMUSG00000066516.6.
DR   GeneID; 16616; -.
DR   KEGG; mmu:16616; -.
DR   UCSC; uc009goh.1; mouse.
DR   AGR; MGI:892022; -.
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; ETMSANS; -.
DR   OrthoDB; 4629979at2759; -.
DR   PhylomeDB; Q61759; -.
DR   TreeFam; TF331065; -.
DR   BioGRID-ORCS; 16616; 3 hits in 50 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 cell types or tissues.
DR   ExpressionAtlas; Q61759; 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; 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; 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; Q61759; MM.
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
//