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Kallikrein 1-related peptidase b21 (EC 3.4.21.35) (Glandular kallikrein K21) (mGK-21) (Tissue kallikrein 21)

 K1B21_MOUSE             Reviewed;         261 AA.
Q61759; Q61760; Q9JM70;
07-JUN-2004, integrated into UniProtKB/Swiss-Prot.
07-JUN-2004, sequence version 3.
25-OCT-2017, entry version 129.
RecName: Full=Kallikrein 1-related peptidase b21;
EC=3.4.21.35;
AltName: Full=Glandular kallikrein K21;
Short=mGK-21;
AltName: Full=Tissue kallikrein 21;
Flags: Precursor;
Name=Klk1b21; Synonyms=Klk-21, Klk21;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090 {ECO:0000312|EMBL:BAA92319.1};
[1] {ECO:0000312|EMBL:BAA92319.1}
NUCLEOTIDE SEQUENCE.
TISSUE=Testis {ECO:0000269|PubMed:11082197};
PubMed=11082197; DOI=10.1046/j.1432-1033.2000.01786.x;
Matsui H., Moriyama A., Takahashi T.;
"Cloning and characterization of mouse Klk27, a novel tissue
kallikrein expressed in testicular Leydig cells and exhibiting
chymotrypsin-like specificity.";
Eur. J. Biochem. 267:6858-6865(2000).
[2] {ECO:0000305}
NUCLEOTIDE SEQUENCE, FUNCTION, ENZYME REGULATION, TISSUE SPECIFICITY,
DEVELOPMENTAL STAGE, AND INDUCTION.
TISSUE=Testis {ECO:0000269|PubMed:11606460};
PubMed=11606460; DOI=10.1210/endo.142.11.8505;
Matsui H., Takahashi T.;
"Mouse testicular Leydig cells express Klk21, a tissue kallikrein that
cleaves fibronectin and IGF-binding protein-3.";
Endocrinology 142:4918-4929(2001).
[3] {ECO:0000312|EMBL:AAH12243.1}
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=FVB/N {ECO:0000312|EMBL:AAH12243.1};
TISSUE=Salivary gland {ECO:0000312|EMBL:AAH12243.1};
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[4] {ECO:0000305}
NUCLEOTIDE SEQUENCE OF 17-54 AND 70-122.
STRAIN=BALB/cJ {ECO:0000269|PubMed:3036794};
TISSUE=Liver {ECO:0000269|PubMed:3036794};
PubMed=3036794;
Evans B.A., Drinkwater C.C., Richards R.I.;
"Mouse glandular kallikrein genes. Structure and partial sequence
analysis of the kallikrein gene locus.";
J. Biol. Chem. 262:8027-8034(1987).
-!- FUNCTION: Glandular kallikreins cleave Met-Lys and Arg-Ser bonds
in kininogen to release Lys-bradykinin. Displays trypsin-like
substrate specificity and shows activity towards casein, gelatin,
fibronectin and IGFBP3. {ECO:0000269|PubMed:11606460}.
-!- CATALYTIC ACTIVITY: Preferential cleavage of Arg-|-Xaa bonds in
small molecule substrates. Highly selective action to release
kallidin (lysyl-bradykinin) from kininogen involves hydrolysis of
Met-|-Xaa or Leu-|-Xaa. {ECO:0000305}.
-!- ENZYME REGULATION: Inhibited by protease inhibitors
diisopropylfluorophosphate, leupeptin, antipain, benzamidine,
phenylmethylsulfonyl fluoride and soybean trypsin inhibitor.
{ECO:0000269|PubMed:11606460}.
-!- TISSUE SPECIFICITY: Expressed in testis and submaxillary gland. In
the testis, expression localized specifically to Leydig cells in
the interstitial tissues. {ECO:0000269|PubMed:11606460}.
-!- DEVELOPMENTAL STAGE: Detectable in testis 4 weeks after birth,
becoming more prominent thereafter. {ECO:0000269|PubMed:11606460}.
-!- INDUCTION: By T protein. {ECO:0000269|PubMed:11606460}.
-!- SIMILARITY: Belongs to the peptidase S1 family. Kallikrein
subfamily. {ECO:0000255|PROSITE-ProRule:PRU00274}.
-----------------------------------------------------------------------
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EMBL; AB039276; BAA92319.1; -; mRNA.
EMBL; BC012243; AAH12243.1; -; mRNA.
EMBL; M18597; AAA39359.1; -; Genomic_DNA.
EMBL; M18617; AAA39360.1; -; Genomic_DNA.
CCDS; CCDS21195.1; -.
PIR; I70036; I70036.
PIR; I70037; I70037.
RefSeq; NP_034772.1; NM_010642.3.
UniGene; Mm.443292; -.
ProteinModelPortal; Q61759; -.
SMR; Q61759; -.
STRING; 10090.ENSMUSP00000082582; -.
MEROPS; S01.038; -.
PaxDb; Q61759; -.
PRIDE; Q61759; -.
Ensembl; ENSMUST00000085455; ENSMUSP00000082582; ENSMUSG00000066516.
GeneID; 16616; -.
KEGG; mmu:16616; -.
UCSC; uc009goh.1; mouse.
CTD; 16616; -.
MGI; MGI:892022; Klk1b21.
eggNOG; KOG3627; Eukaryota.
eggNOG; COG5640; LUCA.
GeneTree; ENSGT00900000140952; -.
HOGENOM; HOG000251820; -.
HOVERGEN; HBG013304; -.
InParanoid; Q61759; -.
KO; K01325; -.
OMA; ANDVCAD; -.
OrthoDB; EOG091G0DF7; -.
PhylomeDB; Q61759; -.
TreeFam; TF331065; -.
Reactome; R-MMU-1592389; Activation of Matrix Metalloproteinases.
Reactome; R-MMU-381426; Regulation of Insulin-like Growth Factor (IGF) transport and uptake by Insulin-like Growth Factor Binding Proteins (IGFBPs).
PRO; PR:Q61759; -.
Proteomes; UP000000589; Chromosome 7.
Bgee; ENSMUSG00000066516; -.
CleanEx; MM_KLK1B21; -.
ExpressionAtlas; Q61759; baseline and differential.
Genevisible; Q61759; MM.
GO; GO:0070062; C:extracellular exosome; ISO:MGI.
GO; GO:0005615; C:extracellular space; IDA:MGI.
GO; GO:0005634; C:nucleus; ISO:MGI.
GO; GO:0043234; C:protein complex; ISO:MGI.
GO; GO:0004175; F:endopeptidase activity; ISO:MGI.
GO; GO:0016811; F:hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in linear amides; ISO:MGI.
GO; GO:0008233; F:peptidase activity; IDA:MGI.
GO; GO:0004252; F:serine-type endopeptidase activity; ISO:MGI.
GO; GO:0006508; P:proteolysis; IDA:MGI.
CDD; cd00190; Tryp_SPc; 1.
InterPro; IPR009003; Peptidase_S1_PA.
InterPro; IPR001314; Peptidase_S1A.
InterPro; IPR001254; Trypsin_dom.
InterPro; IPR018114; TRYPSIN_HIS.
InterPro; IPR033116; TRYPSIN_SER.
Pfam; PF00089; Trypsin; 1.
PRINTS; PR00722; CHYMOTRYPSIN.
SMART; SM00020; Tryp_SPc; 1.
SUPFAM; SSF50494; SSF50494; 1.
PROSITE; PS50240; TRYPSIN_DOM; 1.
PROSITE; PS00134; TRYPSIN_HIS; 1.
PROSITE; PS00135; TRYPSIN_SER; 1.
2: Evidence at transcript level;
Complete proteome; Disulfide bond; Glycoprotein; Hydrolase; Protease;
Reference proteome; Serine protease; Signal; Zymogen.
SIGNAL 1 17 {ECO:0000255}.
PROPEP 18 24 Activation peptide.
{ECO:0000250|UniProtKB:P36368}.
/FTId=PRO_0000027987.
CHAIN 25 261 Kallikrein 1-related peptidase b21.
/FTId=PRO_0000027988.
DOMAIN 25 258 Peptidase S1. {ECO:0000255|PROSITE-
ProRule:PRU00274}.
ACT_SITE 65 65 Charge relay system.
{ECO:0000250|UniProtKB:P36368}.
ACT_SITE 120 120 Charge relay system.
{ECO:0000250|UniProtKB:P36368}.
ACT_SITE 213 213 Charge relay system.
{ECO:0000250|UniProtKB:P36368}.
CARBOHYD 102 102 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 31 173 {ECO:0000250|UniProtKB:P36368,
ECO:0000255|PROSITE-ProRule:PRU00274}.
DISULFID 50 66 {ECO:0000250|UniProtKB:P36368,
ECO:0000255|PROSITE-ProRule:PRU00274}.
DISULFID 152 219 {ECO:0000250|UniProtKB:P36368,
ECO:0000255|PROSITE-ProRule:PRU00274}.
DISULFID 184 198 {ECO:0000250|UniProtKB:P36368,
ECO:0000255|PROSITE-ProRule:PRU00274}.
DISULFID 209 234 {ECO:0000250|UniProtKB:P36368,
ECO:0000255|PROSITE-ProRule:PRU00274}.
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


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