K1B27_MOUSE
ID K1B27_MOUSE Reviewed; 263 AA.
AC Q9JM71; A2RSF8;
DT 24-MAY-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 138.
DE RecName: Full=Kallikrein 1-related peptidase b27;
DE EC=3.4.21.-;
DE AltName: Full=Glandular kallikrein K27;
DE Short=mGK-27;
DE AltName: Full=Tissue kallikrein 27;
DE Short=mKlk27;
DE Flags: Precursor;
GN Name=Klk1b27; Synonyms=Klk-27, Klk27;
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:BAA92318.1};
RN [1] {ECO:0000305}
RP NUCLEOTIDE SEQUENCE [MRNA], CATALYTIC ACTIVITY, TISSUE SPECIFICITY,
RP DEVELOPMENTAL STAGE, AND MUTAGENESIS OF GLY-209.
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]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain;
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).
CC -!- FUNCTION: Serine protease with chymotrypsin-like cleavage specificity.
CC Shows activity towards casein, gelatin, IGFBP3 and fibronectin but not
CC towards laminin or collagens I and IV. Does not hydrolyze kininogin to
CC release Lys-bradykinin.
CC -!- ACTIVITY REGULATION: Strongly inhibited by protease inhibitors
CC diisopropyl fluorophosphate, phenylmethanesulfonyl fluoride and SBTI.
CC {ECO:0000269|PubMed:11082197}.
CC -!- TISSUE SPECIFICITY: Expressed in testis and submaxillary gland. Not
CC expressed in heart, brain, spleen, lung, liver, muscle, kidney and
CC ovary. In the testis, expression localized specifically to Leydig cells
CC in the interstitial tissues. {ECO:0000269|PubMed:11082197}.
CC -!- DEVELOPMENTAL STAGE: Detectable in testis 4 weeks after birth, becoming
CC more prominent thereafter. {ECO:0000269|PubMed:11082197}.
CC -!- SIMILARITY: Belongs to the peptidase S1 family. Kallikrein subfamily.
CC {ECO:0000255|PROSITE-ProRule:PRU00274}.
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DR EMBL; AB039275; BAA92318.1; -; mRNA.
DR EMBL; BC132090; AAI32091.1; -; mRNA.
DR EMBL; BC132665; AAI32666.1; -; mRNA.
DR CCDS; CCDS21194.1; -.
DR RefSeq; NP_064664.1; NM_020268.3.
DR AlphaFoldDB; Q9JM71; -.
DR SMR; Q9JM71; -.
DR BioGRID; 200982; 3.
DR STRING; 10090.ENSMUSP00000078786; -.
DR MEROPS; S01.073; -.
DR GlyGen; Q9JM71; 2 sites.
DR MaxQB; Q9JM71; -.
DR PaxDb; Q9JM71; -.
DR PRIDE; Q9JM71; -.
DR ProteomicsDB; 269137; -.
DR DNASU; 16619; -.
DR Ensembl; ENSMUST00000079859; ENSMUSP00000078786; ENSMUSG00000063177.
DR GeneID; 16619; -.
DR KEGG; mmu:16619; -.
DR UCSC; uc009gog.1; mouse.
DR CTD; 16619; -.
DR MGI; MGI:891980; Klk1b27.
DR VEuPathDB; HostDB:ENSMUSG00000063177; -.
DR eggNOG; KOG3627; Eukaryota.
DR GeneTree; ENSGT01020000230389; -.
DR HOGENOM; CLU_006842_1_1_1; -.
DR InParanoid; Q9JM71; -.
DR OrthoDB; 1314811at2759; -.
DR PhylomeDB; Q9JM71; -.
DR TreeFam; TF331065; -.
DR Reactome; R-MMU-1592389; Activation of Matrix Metalloproteinases.
DR BioGRID-ORCS; 16619; 3 hits in 73 CRISPR screens.
DR PRO; PR:Q9JM71; -.
DR Proteomes; UP000000589; Chromosome 7.
DR RNAct; Q9JM71; protein.
DR Bgee; ENSMUSG00000063177; Expressed in submandibular gland and 10 other tissues.
DR Genevisible; Q9JM71; MM.
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; IDA:UniProtKB.
DR GO; GO:0008236; F:serine-type peptidase activity; ISO:MGI.
DR GO; GO:0006508; P:proteolysis; IDA:UniProtKB.
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 1: Evidence at protein 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_0000027995"
FT CHAIN 25..263
FT /note="Kallikrein 1-related peptidase b27"
FT /id="PRO_0000027996"
FT DOMAIN 25..260
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 122
FT /note="Charge relay system"
FT /evidence="ECO:0000250|UniProtKB:P36368"
FT ACT_SITE 215
FT /note="Charge relay system"
FT /evidence="ECO:0000250|UniProtKB:P36368"
FT CARBOHYD 69
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000305"
FT CARBOHYD 105
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000305"
FT DISULFID 31..175
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 154..221
FT /evidence="ECO:0000250|UniProtKB:P36368,
FT ECO:0000255|PROSITE-ProRule:PRU00274"
FT DISULFID 186..200
FT /evidence="ECO:0000250|UniProtKB:P36368,
FT ECO:0000255|PROSITE-ProRule:PRU00274"
FT DISULFID 211..236
FT /evidence="ECO:0000250|UniProtKB:P36368,
FT ECO:0000255|PROSITE-ProRule:PRU00274"
FT MUTAGEN 209
FT /note="G->D: Loss of chymotryptic specificity and
FT acquisition of trypsin-like cleavage specificity."
FT /evidence="ECO:0000269|PubMed:11082197"
SQ SEQUENCE 263 AA; 28742 MW; 2B396C2DD3B359FB CRC64;
MRFLILFLAL SLGGIDAAPP VQSRIIGGFK CKKNSQPWHV AVLRSNKYIC GGVLLDPNWV
LTAAHCYGND TSQHNVWLGK NKLFQREPSA QHRWVSKSFP HPDYNMSLLN DHIPHPEDKS
NDLMLLRLSK PADITDAVKP IDLPTEEPKL GSTCLASGWG SITPTKYQIP NDLQCVFIKL
LPNENCAKAY VHKVTDVMLC VGETGGGKGT CKGDSGGPLI CDGVLHGITS WGSIPCAKPN
APGVFTKLIK FTSWIKDTMA KNP
