ID   KLK12_RAT               Reviewed;         259 AA.
AC   P36376;
DT   01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-1994, sequence version 1.
DT   25-MAY-2022, entry version 124.
DE   RecName: Full=Glandular kallikrein-12, submandibular/renal;
DE            EC=3.4.21.35;
DE   AltName: Full=RSKG-3;
DE   AltName: Full=Tissue kallikrein;
DE   Flags: Precursor;
GN   Name=Klk12; Synonyms=Klk-12;
OS   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
RX   PubMed=2849988; DOI=10.1021/bi00419a005;
RA   Chen Y.-P., Chao J., Chao L.;
RT   "Molecular cloning and characterization of two rat renal kallikrein
RT   genes.";
RL   Biochemistry 27:7189-7196(1988).
CC   -!- FUNCTION: Glandular kallikreins cleave Met-Lys and Arg-Ser bonds in
CC       kininogen to release Lys-bradykinin.
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   -!- TISSUE SPECIFICITY: Kidney and submandibular gland.
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; M19648; AAA51640.1; -; Genomic_DNA.
DR   EMBL; M22922; AAA51640.1; JOINED; mRNA.
DR   PIR; B31136; B31136.
DR   AlphaFoldDB; P36376; -.
DR   SMR; P36376; -.
DR   STRING; 10116.ENSRNOP00000025631; -.
DR   MEROPS; S01.287; -.
DR   GlyGen; P36376; 2 sites.
DR   PaxDb; P36376; -.
DR   UCSC; RGD:1303192; rat.
DR   RGD; 1303192; Klk12.
DR   eggNOG; KOG3627; Eukaryota.
DR   InParanoid; P36376; -.
DR   PhylomeDB; P36376; -.
DR   Reactome; R-RNO-1592389; Activation of Matrix Metalloproteinases.
DR   Reactome; R-RNO-381426; Regulation of Insulin-like Growth Factor (IGF) transport and uptake by Insulin-like Growth Factor Binding Proteins (IGFBPs).
DR   PRO; PR:P36376; -.
DR   Proteomes; UP000002494; Unplaced.
DR   GO; GO:0030141; C:secretory granule; IBA:GO_Central.
DR   GO; GO:0004252; F:serine-type endopeptidase activity; TAS:RGD.
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   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                   /evidence="ECO:0000305"
FT                   /id="PRO_0000028017"
FT   CHAIN           25..259
FT                   /note="Glandular kallikrein-12, submandibular/renal"
FT                   /id="PRO_0000028018"
FT   DOMAIN          25..256
FT                   /note="Peptidase S1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT   ACT_SITE        63
FT                   /note="Charge relay system"
FT   ACT_SITE        118
FT                   /note="Charge relay system"
FT   ACT_SITE        211
FT                   /note="Charge relay system"
FT   CARBOHYD        91
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        106
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        31..171
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT   DISULFID        48..64
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT   DISULFID        150..217
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT   DISULFID        182..196
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT   DISULFID        207..232
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
SQ   SEQUENCE   259 AA;  28759 MW;  535A8EE25435144F CRC64;
     MWLQILFLVL SVGRIDAAPP GQSRVVGGYK CEKNSQPWQV AVINRYLCGG VLIDPSWVIT
     AAHCYSHNYH VLLGRNNLFK DEPFAQYRVV NQSFPHPDYN PFFMKNHTLF PGDDHSNDLM
     LLHLSEPADI TDGVKVIDLP TEEPKVGSTC LASGWSSTKP LEWEFPDDLQ CVNINILSNE
     KCIKAHTQMV TDVMLCAGEL EGGKDTCNGD SGGPLLCDGV LQGITSWSSV PCGETNRPAI
     YTKLIKFTSW IKEVMKENS