ID KLK1_PAPHA Reviewed; 258 AA.
AC Q28773;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 22-FEB-2023, entry version 80.
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 Papio hamadryas (Hamadryas baboon).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Cercopithecinae; Papio.
OX NCBI_TaxID=9557;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Pancreas;
RA Perelygina L.M., Kammerer C.M., Henkel R.D.;
RT "Characterization of the baboon glandular kallikrein locus.";
RL Submitted (JUL-1995) to the EMBL/GenBank/DDBJ databases.
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; L43121; AAA73523.1; -; mRNA.
DR AlphaFoldDB; Q28773; -.
DR SMR; Q28773; -.
DR GlyCosmos; Q28773; 6 sites, No reported glycans.
DR BRENDA; 3.4.21.35; 4522.
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; Trypsin-like serine proteases; 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 PANTHER; PTHR24271:SF47; KALLIKREIN-1; 1.
DR PANTHER; PTHR24271; KALLIKREIN-RELATED; 1.
DR Pfam; PF00089; Trypsin; 1.
DR PRINTS; PR00722; CHYMOTRYPSIN.
DR SMART; SM00020; Tryp_SPc; 1.
DR SUPFAM; SSF50494; Trypsin-like serine proteases; 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; Signal;
KW Zymogen.
FT SIGNAL 1..18
FT /evidence="ECO:0000250"
FT PROPEP 19..24
FT /note="Activation peptide"
FT /evidence="ECO:0000305"
FT /id="PRO_0000027927"
FT CHAIN 25..258
FT /note="Kallikrein-1"
FT /id="PRO_0000027928"
FT DOMAIN 25..255
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 117
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT ACT_SITE 210
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 161
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 163
FT /note="O-linked (GalNAc...) serine"
FT /evidence="ECO:0000250"
FT DISULFID 31..170
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT DISULFID 47..63
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT DISULFID 149..216
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT DISULFID 181..195
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT DISULFID 206..231
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
SQ SEQUENCE 258 AA; 28339 MW; 8254BFEBC84F36E4 CRC64;
MWFLVLCLAL SLGGTGAAPP IQSRIVGGWE CSQPWQAALY HFSTFQCGGI LVHPQWVLTA
AHCIGDNYQL WLGRHNLFDD EDTAQFVHVS ESFPHPCFNM SLLKNHTRQA DEDYSHDLML
LRLTQPAEIT DAVQVVELPT QEPEVGSTCL ASGWGSIEPE NFSYPDDLQC VDLKILPNDK
CAKAHTQKVT EFMLCAGHLE GGKDTCVGDS GGPLTCDGVL QGVTSWGYIP CGSPNKPAVF
VRVLSYVKWI EDTIAENS
//
