ID KLK_PIG Reviewed; 246 AA. AC P00752; DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot. DT 27-MAR-2002, sequence version 4. DT 24-JAN-2024, entry version 144. DE RecName: Full=Glandular kallikrein; DE EC=3.4.21.35; DE AltName: Full=Tissue kallikrein; DE Flags: Precursor; OS Sus scrofa (Pig). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus. OX NCBI_TaxID=9823; RN [1] RP PROTEIN SEQUENCE OF 1-15 AND 95-102. RX PubMed=3246048; DOI=10.1248/cpb.36.4891; RA Kamada M., Aoki K., Ikekita M., Kizuki K., Moriya H., Kamo M., Tsugita A.; RT "Generation of alpha- and beta-kallikreins from porcine pancreatic RT prokallikrein by the action of trypsin."; RL Chem. Pharm. Bull. 36:4891-4899(1988). RN [2] RP PROTEIN SEQUENCE OF 8-87 AND 95-246. RC TISSUE=Pancreas; RA Tschesche H., Mair G., Godec G., Fiedler F., Ehret W., Hirschauer C., RA Lemon M., Fritz H., Schmidt-Kastner G., Kutzbach C.; RT "The primary structure of porcine glandular kallikreins."; RL Adv. Exp. Med. Biol. 120:245-260(1979). RN [3] RP PROTEIN SEQUENCE OF 8-87; 95-127 AND 176-246. RC TISSUE=Pancreas; RA Ehret W.; RT "The primary structure of the kallikrein from porcine pancreas."; RL Thesis (1976), University of Munich, Germany. RN [4] RP PROTEIN SEQUENCE OF 84-98. RX PubMed=2379280; DOI=10.1248/cpb.38.1053; RA Kamada M., Ikekita M., Kurahashi T., Aoki K., Kizuki K., Moriya H., RA Sweeley C.C., Kamo M., Tsugita A.; RT "Generation of a different type of beta-kallikrein from porcine pancreatic RT alpha-kallikrein by the action of chymotrypsin -- observation of RT proteolytic processing occurring around 'kallikrein autolysis loop' RT region."; RL Chem. Pharm. Bull. 38:1053-1057(1990). RN [5] RP PROTEIN SEQUENCE OF 128-175. RC TISSUE=Pancreas; RA Ehret W.; RT "Investigation of the sequence of amino acid residues 127 to 174 of the RT kallikrein from porcine pancreas."; RL Thesis (1978), University of Munich, Germany. RN [6] RP REVIEW. RX PubMed=7043199; DOI=10.1016/s0076-6879(81)80042-0; RA Fiedler F., Fink E., Tschesche H., Fritz H.; RT "Porcine glandular kallikreins."; RL Methods Enzymol. 80:493-532(1981). RN [7] RP X-RAY CRYSTALLOGRAPHY (2 ANGSTROMS), AND SEQUENCE REVISION. RX PubMed=6551452; DOI=10.1016/0022-2836(83)90077-3; RA Bode W., Chen Z., Bartels K., Kutzbach C., Schmidt-Kastner G., Bartunik H.; RT "Refined 2-A X-ray crystal structure of porcine pancreatic kallikrein A, a RT specific trypsin-like serine proteinase. Crystallization, structure RT determination, crystallographic refinement, structure and its comparison RT with bovine trypsin."; RL J. Mol. Biol. 164:237-282(1983). RN [8] RP X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF COMPLEX WITH BOVINE PANCREATIC RP TRYPSIN INHIBITOR. RX PubMed=6188842; DOI=10.1016/0022-2836(83)90078-5; RA Chen Z., Bode W.; RT "Refined 2.5 A X-ray crystal structure of the complex formed by porcine RT kallikrein A and the bovine pancreatic trypsin inhibitor. Crystallization, RT Patterson search, structure determination, refinement, structure and RT comparison with its components and with the bovine trypsin-pancreatic RT trypsin inhibitor complex."; RL J. Mol. Biol. 164:283-311(1983). RN [9] RP X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF COMPLEX WITH HIRUSTASIN. RX PubMed=9032072; DOI=10.1016/s0969-2126(97)00183-4; RA Mittl P.R.E., di Marco S., Fendrich G., Pohlig G., Heim J., Sommerhoff C., RA Fritz H., Priestle J.P., Gruetter M.G.; RT "A new structural class of serine protease inhibitors revealed by the RT structure of the hirustasin-kallikrein complex."; RL Structure 5:253-264(1997). RN [10] RP ERRATUM OF PUBMED:9032072. RA Mittl P.R.E., di Marco S., Fendrich G., Pohlig G., Heim J., Sommerhoff C., RA Fritz H., Priestle J.P., Gruetter M.G.; RL Structure 5:585-585(1997). RN [11] RP STRUCTURE OF CARBOHYDRATES. RX PubMed=3196708; DOI=10.1021/bi00418a072; RA Tomiya N., Yamaguchi T., Awaya J., Kurono M., Endo S., Arata Y., RA Takahashi N., Ishihara H., Mori M., Tejima S.; RT "Structural analyses of asparagine-linked oligosaccharides of porcine RT pancreatic kallikrein."; RL Biochemistry 27:7146-7154(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 -!- SUBUNIT: Monomer. CC -!- SIMILARITY: Belongs to the peptidase S1 family. Kallikrein subfamily. CC {ECO:0000255|PROSITE-ProRule:PRU00274}. CC -!- CAUTION: Native porcine kallikrein is a monomer. Chains of the CC pancreatic beta-kallikrein are heterogeneous artifacts of proteolytic CC degradation during isolation. {ECO:0000305}. 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; A00938; KQPG. DR PDB; 1HIA; X-ray; 2.40 A; A/X=8-87, B/Y=95-246. DR PDB; 2KAI; X-ray; 2.50 A; A=8-87, B=95-246. DR PDB; 2PKA; X-ray; 2.05 A; A/X=8-87, B/Y=95-246. DR PDBsum; 1HIA; -. DR PDBsum; 2KAI; -. DR PDBsum; 2PKA; -. DR SMR; P00752; -. DR STRING; 9823.ENSSSCP00000055845; -. DR BindingDB; P00752; -. DR ChEMBL; CHEMBL3243909; -. DR PaxDb; 9823-ENSSSCP00000027121; -. DR eggNOG; KOG3627; Eukaryota. DR InParanoid; P00752; -. DR EvolutionaryTrace; P00752; -. DR Proteomes; UP000008227; Unplaced. DR Proteomes; UP000314985; Unplaced. DR Proteomes; UP000694570; Unplaced. DR Proteomes; UP000694571; Unplaced. DR Proteomes; UP000694720; Unplaced. DR Proteomes; UP000694722; Unplaced. DR Proteomes; UP000694723; Unplaced. DR Proteomes; UP000694724; Unplaced. DR Proteomes; UP000694725; Unplaced. DR Proteomes; UP000694726; Unplaced. DR Proteomes; UP000694727; Unplaced. DR Proteomes; UP000694728; Unplaced. DR GO; GO:0030141; C:secretory granule; IBA:GO_Central. DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:UniProtKB-EC. 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 1: Evidence at protein level; KW 3D-structure; Direct protein sequencing; Disulfide bond; Glycoprotein; KW Hydrolase; Protease; Reference proteome; Serine protease; Zymogen. FT PROPEP 1..7 FT /evidence="ECO:0000269|Ref.2, ECO:0000269|Ref.3" FT /id="PRO_0000027964" FT CHAIN 8..246 FT /note="Glandular kallikrein" FT /id="PRO_0000027965" FT DOMAIN 8..243 FT /note="Peptidase S1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274" FT REGION 85..104 FT /note="Kallikrein (autolysis) loop" FT ACT_SITE 48 FT /note="Charge relay system" FT ACT_SITE 103 FT /note="Charge relay system" FT ACT_SITE 198 FT /note="Charge relay system" FT CARBOHYD 85 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 239 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT DISULFID 14..158 FT DISULFID 33..49 FT DISULFID 135..204 FT DISULFID 169..183 FT DISULFID 194..219 FT STRAND 22..27 FT /evidence="ECO:0007829|PDB:2PKA" FT STRAND 30..39 FT /evidence="ECO:0007829|PDB:2PKA" FT STRAND 42..45 FT /evidence="ECO:0007829|PDB:2PKA" FT HELIX 47..49 FT /evidence="ECO:0007829|PDB:2PKA" FT STRAND 55..59 FT /evidence="ECO:0007829|PDB:2PKA" FT STRAND 61..65 FT /evidence="ECO:0007829|PDB:1HIA" FT STRAND 71..80 FT /evidence="ECO:0007829|PDB:2PKA" FT TURN 82..86 FT /evidence="ECO:0007829|PDB:2PKA" FT STRAND 105..111 FT /evidence="ECO:0007829|PDB:2PKA" FT STRAND 134..141 FT /evidence="ECO:0007829|PDB:2PKA" FT STRAND 157..164 FT /evidence="ECO:0007829|PDB:2PKA" FT HELIX 166..170 FT /evidence="ECO:0007829|PDB:2PKA" FT STRAND 181..185 FT /evidence="ECO:0007829|PDB:2PKA" FT STRAND 201..204 FT /evidence="ECO:0007829|PDB:2PKA" FT STRAND 207..212 FT /evidence="ECO:0007829|PDB:2PKA" FT STRAND 226..230 FT /evidence="ECO:0007829|PDB:2PKA" FT HELIX 231..234 FT /evidence="ECO:0007829|PDB:2PKA" FT HELIX 235..244 FT /evidence="ECO:0007829|PDB:2PKA" SQ SEQUENCE 246 AA; 27172 MW; 5991CEDE406A19A1 CRC64; APPIQSRIIG GRECEKNSHP WQVAIYHYSS FQCGGVLVNP KWVLTAAHCK NDNYEVWLGR HNLFENENTA QFFGVTADFP HPGFNLSLLK XHTKADGKDY SHDLMLLRLQ SPAKITDAVK VLELPTQEPE LGSTCEASGW GSIEPGPDBF EFPDEIQCVQ LTLLQNTFCA BAHPBKVTES MLCAGYLPGG KDTCMGDSGG PLICNGMWQG ITSWGHTPCG SANKPSIYTK LIFYLDWIND TITENP //