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 08-NOV-2023, entry version 130. 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 GlyCosmos; P36376; 2 sites, No reported glycans. DR GlyGen; P36376; 2 sites. DR PaxDb; 10116-ENSRNOP00000025631; -. DR UCSC; RGD:1303192; rat. DR AGR; RGD:1303192; -. DR RGD; 1303192; Klk12. DR eggNOG; KOG3627; Eukaryota. DR InParanoid; P36376; -. DR PhylomeDB; P36376; -. 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; 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. 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 //