ID KLK2_CAVPO Reviewed; 239 AA. AC P12323; DT 01-OCT-1989, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-1989, sequence version 1. DT 27-MAR-2024, entry version 99. DE RecName: Full=Glandular kallikrein, prostatic; DE EC=3.4.21.35; DE AltName: Full=Prostate esterase; DE AltName: Full=Tissue kallikrein; OS Cavia porcellus (Guinea pig). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Glires; Rodentia; Hystricomorpha; Caviidae; OC Cavia. OX NCBI_TaxID=10141; RN [1] RP PROTEIN SEQUENCE. RX PubMed=3307909; DOI=10.1021/bi00386a034; RA Dunbar J.C., Bradshaw R.A.; RT "Amino acid sequence of guinea pig prostate kallikrein."; RL Biochemistry 26:3471-3478(1987). 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 -!- 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 PIR; A27207; A27207. DR AlphaFoldDB; P12323; -. DR SMR; P12323; -. DR STRING; 10141.ENSCPOP00000005082; -. DR eggNOG; KOG3627; Eukaryota. DR InParanoid; P12323; -. DR Proteomes; UP000005447; Unassembled WGS sequence. DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:UniProtKB-EC. DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW. 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 1: Evidence at protein level; KW Direct protein sequencing; Disulfide bond; Glycoprotein; Hydrolase; KW Protease; Reference proteome; Serine protease. FT CHAIN 1..239 FT /note="Glandular kallikrein, prostatic" FT /id="PRO_0000088701" FT DOMAIN 1..236 FT /note="Peptidase S1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274" FT ACT_SITE 41 FT /note="Charge relay system" FT ACT_SITE 96 FT /note="Charge relay system" FT ACT_SITE 191 FT /note="Charge relay system" FT CARBOHYD 78 FT /note="N-linked (GlcNAc...) asparagine" FT CARBOHYD 169 FT /note="N-linked (GlcNAc...) asparagine" FT DISULFID 7..151 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274" FT DISULFID 26..42 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274" FT DISULFID 128..197 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274" FT DISULFID 162..176 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274" FT DISULFID 187..212 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274" FT VARIANT 50 FT /note="K -> W" SQ SEQUENCE 239 AA; 25989 MW; 56DC81BC10D49A64 CRC64; VIGGQECARD SHPWQAAVYY YSDIKCGGVL VDPQWVLTAA HCINDSNQVK LGRHNLFEDE DTAQHFLVSQ SVPHPDFNMS LLEPHNVLPN EDYSHDLMLL RLNQPAQITD SVQVMPLPTQ EVQVGTTCRA LGWGSIDPDP AHPVFPDELQ CVGLEILPSK NCDDAHIANV TGTMLCAGDL AGGKDTCVGD SGGPLICDGV LQGLTSWGDS PCGVAHSPSL YTKVIEYREW IERTMADNP //