ID   KLK3_RAT                Reviewed;         188 AA.
AC   P15950;
DT   01-APR-1990, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-1994, sequence version 2.
DT   25-MAY-2022, entry version 124.
DE   RecName: Full=Glandular kallikrein-3, submandibular;
DE            Short=rGK-3;
DE            EC=3.4.21.35;
DE   AltName: Full=RSGK-50;
DE   AltName: Full=S1 kallikrein;
DE   AltName: Full=Tissue kallikrein;
DE   Flags: Fragment;
GN   Name=Klk3; Synonyms=Klk-3;
OS   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=2550051; DOI=10.1021/bi00439a005;
RA   Shai S.Y., Woodley-Miller C., Chao J., Chao L.;
RT   "Characterization of genes encoding rat tonin and a kallikrein-like serine
RT   protease.";
RL   Biochemistry 28:5334-5343(1989).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 33-188.
RX   PubMed=2998455; DOI=10.1021/bi00338a005;
RA   Ashley P.L., MacDonald R.J.;
RT   "Kallikrein-related mRNAs of the rat submaxillary gland: nucleotide
RT   sequences of four distinct types including tonin.";
RL   Biochemistry 24:4512-4520(1985).
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   EMBL; M26534; AAA42080.1; -; Genomic_DNA.
DR   EMBL; M11564; AAA41465.1; -; mRNA.
DR   PIR; B23863; B23863.
DR   PIR; B32340; B32340.
DR   AlphaFoldDB; P15950; -.
DR   SMR; P15950; -.
DR   STRING; 10116.ENSRNOP00000025777; -.
DR   MEROPS; S01.411; -.
DR   GlyGen; P15950; 2 sites.
DR   PaxDb; P15950; -.
DR   eggNOG; KOG3627; Eukaryota.
DR   InParanoid; P15950; -.
DR   PhylomeDB; P15950; -.
DR   TreeFam; TF331065; -.
DR   BRENDA; 3.4.21.77; 5301.
DR   Proteomes; UP000002494; 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; 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; PS00135; TRYPSIN_SER; 1.
PE   2: Evidence at transcript level;
KW   Disulfide bond; Glycoprotein; Hydrolase; Protease; Reference proteome;
KW   Serine protease.
FT   CHAIN           <1..188
FT                   /note="Glandular kallikrein-3, submandibular"
FT                   /id="PRO_0000088702"
FT   DOMAIN          <1..185
FT                   /note="Peptidase S1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT   ACT_SITE        47
FT                   /note="Charge relay system"
FT   ACT_SITE        140
FT                   /note="Charge relay system"
FT   CARBOHYD        10
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        36
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        79..146
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT   DISULFID        111..125
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT   DISULFID        136..161
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT   CONFLICT        34..35
FT                   /note="MR -> IW (in Ref. 2; AAA41465)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        42
FT                   /note="K -> G (in Ref. 2; AAA41465)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        186
FT                   /note="E -> K (in Ref. 1; AAA42080)"
FT                   /evidence="ECO:0000305"
FT   NON_TER         1
SQ   SEQUENCE   188 AA;  20986 MW;  B3ECEC65582EB1E9 CRC64;
     NYHVLLGQNN LSEDVQHRLV SQSFRHPDYK PFLMRNHTRK PKDYSNDLML LHLSEPADIT
     DGVKVIDLPT KEPKVGSTCL VSGWGSTNPS EWEFPDDLQC VNIHLLSNEK CIKAYKEKVT
     DLMLCAGELE GGKDTCRGDS GGPLICDGVL QGITSWGSVP CGEPNKPGIY TKLIKFTSWI
     KEVMKENP