ID   KLK6_RAT                Reviewed;         261 AA.
AC   P36374;
DT   01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-1994, sequence version 1.
DT   25-MAY-2022, entry version 121.
DE   RecName: Full=Prostatic glandular kallikrein-6;
DE            EC=3.4.21.35;
DE   AltName: Full=Glandular kallikrein-8;
DE            Short=rGK-8;
DE   AltName: Full=P1 kallikrein;
DE   AltName: Full=Tissue kallikrein;
DE   Flags: Precursor;
GN   Name=Klk6; Synonyms=Klk-8, Klk8;
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=2765531; DOI=10.1021/bi00438a043;
RA   Brady J.M., Wines D.R., MacDonald R.J.;
RT   "Expression of two kallikrein gene family members in the rat prostate.";
RL   Biochemistry 28:5203-5210(1989).
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; M27217; AAA42036.1; -; Genomic_DNA.
DR   EMBL; M27215; AAA42036.1; JOINED; Genomic_DNA.
DR   EMBL; M27216; AAA42036.1; JOINED; Genomic_DNA.
DR   PIR; A34079; A34079.
DR   AlphaFoldDB; P36374; -.
DR   SMR; P36374; -.
DR   STRING; 10116.ENSRNOP00000066639; -.
DR   MEROPS; S01.288; -.
DR   GlyGen; P36374; 1 site.
DR   PaxDb; P36374; -.
DR   UCSC; RGD:1305359; rat.
DR   RGD; 1305359; Klk6.
DR   eggNOG; KOG3627; Eukaryota.
DR   InParanoid; P36374; -.
DR   PhylomeDB; P36374; -.
DR   BRENDA; 3.4.21.118; 5301.
DR   Reactome; R-RNO-1592389; Activation of Matrix Metalloproteinases.
DR   Reactome; R-RNO-381426; Regulation of Insulin-like Growth Factor (IGF) transport and uptake by Insulin-like Growth Factor Binding Proteins (IGFBPs).
DR   PRO; PR:P36374; -.
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; 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   3: Inferred from homology;
KW   Disulfide bond; Glycoprotein; Hydrolase; Protease; Reference proteome;
KW   Serine protease; Signal; Zymogen.
FT   SIGNAL          1..18
FT                   /evidence="ECO:0000305"
FT   PROPEP          19..24
FT                   /note="Activation peptide"
FT                   /evidence="ECO:0000305"
FT                   /id="PRO_0000028007"
FT   CHAIN           25..261
FT                   /note="Prostatic glandular kallikrein-6"
FT                   /id="PRO_0000028008"
FT   DOMAIN          25..258
FT                   /note="Peptidase S1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT   ACT_SITE        65
FT                   /note="Charge relay system"
FT   ACT_SITE        120
FT                   /note="Charge relay system"
FT   ACT_SITE        213
FT                   /note="Charge relay system"
FT   CARBOHYD        108
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        31..173
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT   DISULFID        50..66
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT   DISULFID        152..219
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT   DISULFID        184..198
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT   DISULFID        209..234
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
SQ   SEQUENCE   261 AA;  29013 MW;  CA8F12151B04E337 CRC64;
     MWLLILFLIL SLGWNDAAPP GQSRIIGGFN CEKNSQPWQV AVYHFNEPQC GGVLIHPSWV
     ITAAHCYSVN YQVWLGRNNL LEDEPFAQHR LVSQSFPHPG FNLDIIKNHT RKPGNDYSND
     LMLLHLKTPA DITDGVKVID LPTEEPKVGS TCLTSGWGSI TPLKWEFPDD LQCVNIHLLS
     NEKCIKAYND EVTDVMLCAG EMDGGKDICK GDSGGPLICD GVLQGITSWG SMPCGEPNKP
     SVYTKLIKFT SWMKKVMKEN P