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   03-AUG-2022, entry version 94.
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}.
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DR   PIR; A27207; A27207.
DR   AlphaFoldDB; P12323; -.
DR   SMR; P12323; -.
DR   STRING; 10141.ENSCPOP00000020997; -.
DR   eggNOG; KOG3627; Eukaryota.
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; -; 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   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