KLK_PIG
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 02-JUN-2021, entry version 137.
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.ENSSSCP00000027121; -.
DR BindingDB; P00752; -.
DR ChEMBL; CHEMBL3243909; -.
DR PaxDb; P00752; -.
DR eggNOG; KOG3627; Eukaryota.
DR EvolutionaryTrace; P00752; -.
DR Proteomes; UP000008227; Unplaced.
DR Proteomes; UP000314985; 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; -; 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 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
