K1B26_MOUSE
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 03-AUG-2022, entry version 172.
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 GlyGen; P36369; 1 site.
DR MaxQB; P36369; -.
DR PaxDb; P36369; -.
DR PRIDE; P36369; -.
DR ProteomicsDB; 268931; -.
DR DNASU; 16618; -.
DR Ensembl; ENSMUST00000048945; ENSMUSP00000047488; ENSMUSG00000053719.
DR GeneID; 16618; -.
DR KEGG; mmu:16618; -.
DR UCSC; uc009gof.3; mouse.
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; 1314811at2759; -.
DR PhylomeDB; P36369; -.
DR TreeFam; TF331065; -.
DR Reactome; R-MMU-1592389; Activation of Matrix Metalloproteinases.
DR BioGRID-ORCS; 16618; 3 hits in 72 CRISPR screens.
DR PRO; PR:P36369; -.
DR Proteomes; UP000000589; Chromosome 7.
DR RNAct; P36369; protein.
DR Bgee; ENSMUSG00000053719; Expressed in submandibular gland and 38 other tissues.
DR ExpressionAtlas; P36369; baseline and differential.
DR Genevisible; P36369; MM.
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: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; -; 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..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
