KLK2_BLABR
ID KLK2_BLABR Reviewed; 280 AA.
AC Q5FBW1;
DT 29-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 15-MAR-2005, sequence version 1.
DT 03-AUG-2022, entry version 48.
DE RecName: Full=Blarinasin-2;
DE EC=3.4.21.-;
DE AltName: Full=Kallikrein-2;
DE Flags: Precursor; Fragment;
GN Name=KLK2;
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].
RC TISSUE=Salivary gland;
RA Kita M., Nakamura Y., Kido H., Uemura D.;
RT "Blarina brevicauda kallikrein mRNA.";
RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: A kallikrein-like protease. It preferentially converts human
CC high-molecular-weight kininogen (HK) to bradykinin. Is not toxic to
CC mice (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Salivary glands.
CC -!- SIMILARITY: Belongs to the peptidase S1 family. Kallikrein subfamily.
CC {ECO:0000255|PROSITE-ProRule:PRU00274}.
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DR EMBL; AB105056; BAD89852.1; -; mRNA.
DR AlphaFoldDB; Q5FBW1; -.
DR SMR; Q5FBW1; -.
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 2: Evidence at transcript level;
KW Disulfide bond; Glycoprotein; Hydrolase; Protease; Secreted;
KW Serine protease; Signal; Zymogen.
FT SIGNAL <1..16
FT /evidence="ECO:0000255"
FT PROPEP 17..28
FT /id="PRO_0000288942"
FT CHAIN 29..280
FT /note="Blarinasin-2"
FT /id="PRO_0000288943"
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:0000255"
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; 31104 MW; 06D3B6F5AE354E36 CRC64;
YLLLLCLPLT LMGTGAVPPG PSIEIHPRIV GGWECDKHSQ PWQALLTFTN GLDGVCGGVL
VHPQWVLTAA HCIGDNYKIK LGLHDRFSKD DPFQEFQVSA SFPHPSYNMR LLKLLLSDEM
NDTYYYEIFP GADFSHDLMM MQLEKPVQLN DAVQVLDLPT QEPQVGSKCH ASGWGSMDPY
SRNFPRTGKL QCVDLTLMSN NECSRSHIFK ITDDMLCAGH IKGRKDTCGG DSGGPLICDG
VFQGTTSWGS YPCGKPRMPG VYVKIFSHVD WIREIIATHS