ID   KLK1_BLABR              Reviewed;         280 AA.
AC   Q5FBW2;
DT   29-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT   15-MAR-2005, sequence version 1.
DT   03-AUG-2022, entry version 50.
DE   RecName: Full=Blarinasin-1;
DE            EC=3.4.21.-;
DE   AltName: Full=Kallikrein-1;
DE   Flags: Precursor; Fragment;
GN   Name=KLK1;
OS   Blarina brevicauda (Northern short-tailed shrew).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Eulipotyphla; Soricidae; Soricinae; Blarina.
OX   NCBI_TaxID=9387;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 29-43, FUNCTION, CATALYTIC
RP   ACTIVITY, ACTIVITY REGULATION, BIOPHYSICOCHEMICAL PROPERTIES, SUBCELLULAR
RP   LOCATION, AND TISSUE SPECIFICITY.
RC   TISSUE=Saliva, and Salivary gland;
RX   PubMed=15843162; DOI=10.1515/bc.2005.022;
RA   Kita M., Okumura Y., Ohdachi S.D., Oba Y., Yoshikuni M., Nakamura Y.,
RA   Kido H., Uemura D.;
RT   "Purification and characterisation of blarinasin, a new tissue kallikrein-
RT   like protease from the short-tailed shrew Blarina brevicauda: comparative
RT   studies with blarina toxin.";
RL   Biol. Chem. 386:177-182(2005).
CC   -!- FUNCTION: A kallikrein-like protease. It preferentially converts human
CC       high-molecular-weight kininogen (HK) to bradykinin. Displays broad
CC       substrate specificity in vitro, with highest activity toward Boc-Val-
CC       Leu-Lys-MCA, Boc-Glu-Lys-Lys-MCA, Boc-Glu(OBzl)-Ala-Arg-MCA, Boc-Val-
CC       Pro-Arg-MCA, ZPhe-Arg-MCA and Pro-Phe-Arg-MCA. Has preference for Arg
CC       and Lys in position P1 and hydrophobic residues in position P2. Is not
CC       toxic to mice. {ECO:0000269|PubMed:15843162}.
CC   -!- ACTIVITY REGULATION: Strongly inhibited by aprotinin, moderately
CC       inhibited by secretory leukoprotease inhibitor (SLPI), leupeptin,
CC       benzamidine, and phenylmethanesulfonyl fluoride (PMSF), weakly
CC       inhibited by urinary trypsin inhibitor, and Kunitz-type soybean trypsin
CC       inhibitor and not inhibited by EDTA and alpha-1 protease inhibitor.
CC       {ECO:0000269|PubMed:15843162}.
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       pH dependence:
CC         Optimum pH is 8.5. {ECO:0000269|PubMed:15843162};
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:15843162}.
CC   -!- TISSUE SPECIFICITY: Submaxillary and sublingual salivary glands.
CC       {ECO:0000269|PubMed:15843162}.
CC   -!- SIMILARITY: Belongs to the peptidase S1 family. Kallikrein subfamily.
CC       {ECO:0000255|PROSITE-ProRule:PRU00274}.
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DR   EMBL; AB105055; BAD89851.1; -; mRNA.
DR   AlphaFoldDB; Q5FBW2; -.
DR   SMR; Q5FBW2; -.
DR   MEROPS; S01.452; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
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   1: Evidence at protein level;
KW   Direct protein sequencing; Disulfide bond; Glycoprotein; Hydrolase;
KW   Protease; Secreted; Serine protease; Signal; Zymogen.
FT   SIGNAL          <1..16
FT                   /evidence="ECO:0000255"
FT   PROPEP          17..28
FT                   /evidence="ECO:0000269|PubMed:15843162"
FT                   /id="PRO_0000288940"
FT   CHAIN           29..280
FT                   /note="Blarinasin-1"
FT                   /id="PRO_0000288941"
FT   DOMAIN          29..277
FT                   /note="Peptidase S1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT   ACT_SITE        71
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        137
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        232
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        99
FT                   /note="O-linked (GalNAc...) serine"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        121
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000305"
FT   DISULFID        35..192
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT   DISULFID        56..72
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT   DISULFID        169..238
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT   DISULFID        203..217
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT   DISULFID        228..253
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT   NON_TER         1
SQ   SEQUENCE   280 AA;  30963 MW;  38D91771767114A0 CRC64;
     YLLLLCLPLT LMGTGAVPPG PSIEIHPRIV GGWECDKHSQ PWQALLTFTN GLDGVCGGVL
     VHPQWVLTAA HCIGDNYKIK LGLHDRFSKD DPFQEFQVSA SFPHPSYNMR LLKLLLSDEL
     NDTYYDEISL GADFSHDLMM MQLEKPVQLN DAVQVLDLPT QEPQVGSKCH ASGWGSMDPY
     SRNFPRTGKL QCVDLTLMSN NECSRSHIFK ITDDMLCAGH IKGRKDTCGG DSGGPLICDG
     VFQGTTSWGS YPCGKPRTPG VYVKIFSHVD WIREIIATHS