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-MAR-2009, entry version 56.
DE   RecName: Full=Kallikrein-1;
DE            EC=3.4.21.35;
DE   AltName: Full=Tissue kallikrein;
DE   AltName: Full=Kidney/pancreas/salivary gland kallikrein;
DE   Flags: Precursor;
GN   Name=KLK1;
OS   Macaca fascicularis (Crab eating macaque) (Cynomolgus monkey).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Cercopithecidae; Cercopithecinae; Macaca.
OX   NCBI_TaxID=9541;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   MEDLINE=93305727; 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.,
RA   Herrera C., Jones T., Chao J., Chao L.;
RT   "Molecular cloning and sequence analysis of the monkey and human
RT   tissue kallikrein genes.";
RL   Biochim. Biophys. Acta 1173:325-328(1993).
CC   -!- FUNCTION: Glandular kallikreins cleave Met-Lys and Arg-Ser bonds
CC       in kininogen to release Lys-bradykinin.
CC   -!- CATALYTIC ACTIVITY: Preferential cleavage of Arg-|-Xaa bonds in
CC       small molecule substrates. Highly selective action to release
CC       kallidin (lysyl-bradykinin) from kininogen involves hydrolysis of
CC       Met-|-Xaa or Leu-|-Xaa.
CC   -!- SIMILARITY: Belongs to the peptidase S1 family. Kallikrein
CC       subfamily.
CC   -!- SIMILARITY: Contains 1 peptidase S1 domain.
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DR   EMBL; L10039; AAA36853.1; -; mRNA.
DR   PIR; S33772; S33772.
DR   HSSP; P00746; 1FDP.
DR   SMR; Q07276; 25-257.
DR   MEROPS; S01.160; -.
DR   HOVERGEN; Q07276; -.
DR   BRENDA; 3.4.21.35; 3438.
DR   GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
DR   GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR   InterPro; IPR018114; Peptidase_S1/S6_AS.
DR   InterPro; IPR001254; Peptidase_S1_S6.
DR   InterPro; IPR001314; Peptidase_S1A.
DR   Pfam; PF00089; Trypsin; 1.
DR   PRINTS; PR00722; CHYMOTRYPSIN.
DR   SMART; SM00020; Tryp_SPc; 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; Serine protease;
KW   Signal; Zymogen.
FT   SIGNAL        1     18       By similarity.
FT   PROPEP       19     24       Activation peptide (Probable).
FT                                /FTId=PRO_0000027925.
FT   CHAIN        25    257       Kallikrein-1.
FT                                /FTId=PRO_0000027926.
FT   DOMAIN       25    254       Peptidase S1.
FT   ACT_SITE     62     62       Charge relay system (By similarity).
FT   ACT_SITE    116    116       Charge relay system (By similarity).
FT   ACT_SITE    209    209       Charge relay system (By similarity).
FT   CARBOHYD     90     90       O-linked (GalNAc...) (By similarity).
FT   CARBOHYD     99     99       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    101    101       O-linked (GalNAc...) (By similarity).
FT   CARBOHYD    105    105       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    160    160       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    162    162       O-linked (GalNAc...) (By similarity).
FT   DISULFID     31    169       By similarity.
FT   DISULFID     47     63       By similarity.
FT   DISULFID    148    215       By similarity.
FT   DISULFID    180    194       By similarity.
FT   DISULFID    205    230       By similarity.
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
//