ID   KLK1_CAVPO              Reviewed;          31 AA.
AC   P12322;
DT   01-OCT-1989, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1989, sequence version 1.
DT   03-AUG-2022, entry version 99.
DE   RecName: Full=Kallikrein-1;
DE            EC=3.4.21.35;
DE   AltName: Full=Glandular kallikrein, submandibular;
DE   AltName: Full=Tissue kallikrein;
DE   Flags: Fragment;
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=6552183; DOI=10.1042/bj2090125;
RA   Fiedler F., Lemon M.J.C., Hirschauer C., Leysath G., Lottspeich F.,
RA   Henschen A., Gau W., Bhoola K.D.;
RT   "Purification and properties of guinea-pig submandibular-gland
RT   kallikrein.";
RL   Biochem. J. 209:125-134(1983).
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; A18671; A18671.
DR   AlphaFoldDB; P12322; -.
DR   SMR; P12322; -.
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   Gene3D; 2.40.10.10; -; 1.
DR   InterPro; IPR009003; Peptidase_S1_PA.
DR   InterPro; IPR043504; Peptidase_S1_PA_chymotrypsin.
DR   InterPro; IPR001254; Trypsin_dom.
DR   Pfam; PF00089; Trypsin; 1.
DR   SUPFAM; SSF50494; SSF50494; 1.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; Hydrolase; Protease; Reference proteome;
KW   Serine protease.
FT   CHAIN           1..>31
FT                   /note="Kallikrein-1"
FT                   /id="PRO_0000088700"
FT   DOMAIN          1..>31
FT                   /note="Peptidase S1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT   NON_TER         31
SQ   SEQUENCE   31 AA;  3345 MW;  8FFFB84D46B8DC93 CRC64;
     VIGGQECARD SHPWQAAVYH FSDIECGGVL V