ID   KLK1_MACFA              Reviewed;         257 AA.
AC   Q07276;
DT   01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1994, sequence version 1.
DT   03-AUG-2022, entry version 94.
DE   RecName: Full=Kallikrein-1;
DE            EC=3.4.21.35;
DE   AltName: Full=Kidney/pancreas/salivary gland kallikrein;
DE   AltName: Full=Tissue kallikrein;
DE   Flags: Precursor;
GN   Name=KLK1;
OS   Macaca fascicularis (Crab-eating macaque) (Cynomolgus monkey).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC   Cercopithecidae; Cercopithecinae; Macaca.
OX   NCBI_TaxID=9541;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=7916636; DOI=10.1016/0167-4781(93)90131-v;
RA   Lin F.K., Lin C.H., Chou C., Chen K., Lu H.S., Bacheller B., Herrera C.,
RA   Jones T., Chao J., Chao L.;
RT   "Molecular cloning and sequence analysis of the monkey and human tissue
RT   kallikrein genes.";
RL   Biochim. Biophys. Acta 1173:325-328(1993).
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; L10039; AAA36853.1; -; mRNA.
DR   PIR; S33772; S33772.
DR   RefSeq; NP_001272131.1; NM_001285202.1.
DR   AlphaFoldDB; Q07276; -.
DR   SMR; Q07276; -.
DR   STRING; 9541.XP_005590094.1; -.
DR   GeneID; 102135781; -.
DR   eggNOG; KOG3627; Eukaryota.
DR   OrthoDB; 1314811at2759; -.
DR   BRENDA; 3.4.21.35; 1793.
DR   Proteomes; UP000233100; Unplaced.
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   2: Evidence at transcript level;
KW   Disulfide bond; Glycoprotein; Hydrolase; Protease; Reference proteome;
KW   Serine protease; Signal; Zymogen.
FT   SIGNAL          1..18
FT                   /evidence="ECO:0000250"
FT   PROPEP          19..24
FT                   /note="Activation peptide"
FT                   /evidence="ECO:0000305"
FT                   /id="PRO_0000027925"
FT   CHAIN           25..257
FT                   /note="Kallikrein-1"
FT                   /id="PRO_0000027926"
FT   DOMAIN          25..254
FT                   /note="Peptidase S1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT   ACT_SITE        62
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        116
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        209
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        90
FT                   /note="O-linked (GalNAc...) serine"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        99
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        101
FT                   /note="O-linked (GalNAc...) serine"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        105
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        160
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        162
FT                   /note="O-linked (GalNAc...) serine"
FT                   /evidence="ECO:0000250"
FT   DISULFID        31..169
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT   DISULFID        47..63
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT   DISULFID        148..215
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT   DISULFID        180..194
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT   DISULFID        205..230
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
SQ   SEQUENCE   257 AA;  28237 MW;  32774D4C069316A7 CRC64;
     MWFLVLCLAL SLGGTGRAPP IQSRIVGGWE CSQPWQAALY HFSTFQCGGI LVHPQWVLTA
     AHCISDNYQL WLGRHNLFDD EDTAQFVHVS ESFPHPGFNM SLLKNHTRQA DDYSHDLMLL
     RLTQPAEITD AVQVVELPTQ EPEVGSTCLA SGWGSIEPEN FSFPDDLQCV DLEILPNDEC
     AKAHTQKVTE FMLCAGHLEG GKDTCVGDSG GPLTCDGVLQ GVTSWGYIPC GSPNKPAVFV
     KVLSYVKWIE DTIAENS