ID   K1B26_MOUSE             Reviewed;         261 AA.
AC   P36369; B9EI06; P00753; P00754;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-1994, sequence version 1.
DT   24-JAN-2024, entry version 180.
DE   RecName: Full=Kallikrein 1-related peptidase b26;
DE            EC=3.4.21.35;
DE   AltName: Full=Glandular kallikrein K26;
DE            Short=mGK-26;
DE   AltName: Full=Prorenin-converting enzyme 2;
DE            Short=PRECE-2;
DE   AltName: Full=Tissue kallikrein 26;
DE   Flags: Precursor;
GN   Name=Klk1b26; Synonyms=Klk-26, Klk26;
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 [MRNA].
RC   STRAIN=ICR; TISSUE=Submandibular gland;
RX   PubMed=1959648; DOI=10.1016/0014-5793(91)81171-4;
RA   Kim W.S., Nakayama K., Murakami K.;
RT   "The presence of two types of prorenin converting enzymes in the mouse
RT   submandibular gland.";
RL   FEBS Lett. 293:142-144(1991).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=NMRI;
RX   PubMed=6330081; DOI=10.1016/s0021-9258(17)42861-4;
RA   Lundgren S., Ronne H., Rask L., Peterson P.A.;
RT   "Sequence of an epidermal growth factor-binding protein.";
RL   J. Biol. Chem. 259:7780-7784(1984).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=FVB/N; TISSUE=Brain, and Salivary gland;
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]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 113-261.
RC   STRAIN=Quakenbush inbred;
RX   PubMed=6174512; DOI=10.1016/s0021-9258(19)81027-x;
RA   Richards R.I., Catanzaro D.F., Mason A.J., Morris B.J., Baxter J.D.,
RA   Shine J.;
RT   "Mouse glandular kallikrein genes. Nucleotide sequence of cloned cDNA
RT   coding for a member of the kallikrein arginyl esteropeptidase group of
RT   serine proteases.";
RL   J. Biol. Chem. 257:2758-2761(1982).
CC   -!- FUNCTION: Glandular kallikreins cleave Met-Lys and Arg-Ser bonds in
CC       kininogen to release Lys-bradykinin.
CC   -!- FUNCTION: Prorenin-converting enzyme cleaves mouse REN-2 prorenin at a
CC       dibasic site to yield mature renin.
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; K01831; AAA37540.1; -; mRNA.
DR   EMBL; X63327; CAA44931.1; -; mRNA.
DR   EMBL; BC024688; AAH24688.1; -; mRNA.
DR   EMBL; BC138704; AAI38705.1; -; mRNA.
DR   EMBL; V00828; CAA24211.1; -; mRNA.
DR   CCDS; CCDS39938.1; -.
DR   PIR; A00940; EGMSB.
DR   RefSeq; NP_034774.1; NM_010644.3.
DR   AlphaFoldDB; P36369; -.
DR   SMR; P36369; -.
DR   STRING; 10090.ENSMUSP00000047488; -.
DR   MEROPS; S01.070; -.
DR   MEROPS; S01.173; -.
DR   GlyCosmos; P36369; 1 site, No reported glycans.
DR   GlyGen; P36369; 1 site.
DR   MaxQB; P36369; -.
DR   PaxDb; 10090-ENSMUSP00000047488; -.
DR   ProteomicsDB; 268931; -.
DR   DNASU; 16618; -.
DR   Ensembl; ENSMUST00000048945.6; ENSMUSP00000047488.5; ENSMUSG00000053719.11.
DR   GeneID; 16618; -.
DR   KEGG; mmu:16618; -.
DR   UCSC; uc009gof.3; mouse.
DR   AGR; MGI:891981; -.
DR   CTD; 16618; -.
DR   MGI; MGI:891981; Klk1b26.
DR   VEuPathDB; HostDB:ENSMUSG00000053719; -.
DR   eggNOG; KOG3627; Eukaryota.
DR   GeneTree; ENSGT01020000230389; -.
DR   HOGENOM; CLU_006842_1_1_1; -.
DR   InParanoid; P36369; -.
DR   OrthoDB; 2495122at2759; -.
DR   PhylomeDB; P36369; -.
DR   TreeFam; TF331065; -.
DR   BioGRID-ORCS; 16618; 3 hits in 77 CRISPR screens.
DR   PRO; PR:P36369; -.
DR   Proteomes; UP000000589; Chromosome 7.
DR   RNAct; P36369; Protein.
DR   Bgee; ENSMUSG00000053719; Expressed in submandibular gland and 39 other cell types or tissues.
DR   ExpressionAtlas; P36369; 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:0002035; P:brain renin-angiotensin system; IDA: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; 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; P36369; MM.
PE   2: Evidence at transcript level;
KW   Disulfide bond; Glycoprotein; Hydrolase; Protease; Reference proteome;
KW   Serine protease; Signal; Zymogen.
FT   SIGNAL          1..18
FT                   /evidence="ECO:0000305"
FT   PROPEP          19..24
FT                   /note="Activation peptide"
FT                   /id="PRO_0000027993"
FT   CHAIN           25..261
FT                   /note="Kallikrein 1-related peptidase b26"
FT                   /id="PRO_0000027994"
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   ACT_SITE        120
FT                   /note="Charge relay system"
FT   ACT_SITE        213
FT                   /note="Charge relay system"
FT   CARBOHYD        102
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000305"
FT   DISULFID        31..173
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT   DISULFID        50..66
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT   DISULFID        152..219
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT   DISULFID        184..198
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT   DISULFID        209..234
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT   CONFLICT        114..115
FT                   /note="GA -> EY (in Ref. 4)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        117
FT                   /note="F -> Y (in Ref. 4)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        144
FT                   /note="K -> E (in Ref. 4; CAA24211)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        148
FT                   /note="P -> L (in Ref. 4; CAA24211)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   261 AA;  28463 MW;  55DCE378F4B007C5 CRC64;
     MWFLILFPAL SLGGIDAAPP LQSRVVGGFN CEKNSQPWQV AVYYQKEHIC GGVLLDRNWV
     LTAAHCYVDQ YEVWLGKNKL FQEEPSAQHR LVSKSFPHPG FNMSLLMLQT TPPGADFSND
     LMLLRLSKPA DITDVVKPIA LPTKEPKPGS TCLASGWGSI TPTRWQKSDD LQCVFITLLP
     NENCAKVYLQ KVTDVMLCAG EMGGGKDTCA GDSGGPLICD GILQGTTSNG PEPCGKPGVP
     AIYTNLIKFN SWIKDTMMKN A
//