KLKR_MASNA
ID KLKR_MASNA Reviewed; 263 AA.
AC P32824;
DT 01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1993, sequence version 1.
DT 03-AUG-2022, entry version 85.
DE RecName: Full=Renal glandular kallikrein;
DE EC=3.4.21.35;
DE AltName: Full=Tissue kallikrein;
DE Flags: Precursor;
OS Mastomys natalensis (African soft-furred rat) (Praomys natalensis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mastomys.
OX NCBI_TaxID=10112;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Salivary gland;
RX PubMed=7909667; DOI=10.1089/dna.1994.13.293;
RA Fahnestock M.;
RT "Characterization of kallikrein cDNAs from the African rodent Mastomys.";
RL DNA Cell Biol. 13:293-300(1994).
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; X17352; CAA35232.1; -; mRNA.
DR PIR; I83227; S15686.
DR AlphaFoldDB; P32824; -.
DR SMR; P32824; -.
DR MEROPS; S01.290; -.
DR BRENDA; 3.4.21.35; 5009.
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; Serine protease; Signal;
KW Zymogen.
FT SIGNAL 1..18
FT /evidence="ECO:0000305"
FT PROPEP 19..24
FT /note="Activation peptide"
FT /evidence="ECO:0000305"
FT /id="PRO_0000027997"
FT CHAIN 25..263
FT /note="Renal glandular kallikrein"
FT /id="PRO_0000027998"
FT DOMAIN 25..260
FT /note="Peptidase S1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT ACT_SITE 65
FT /note="Charge relay system"
FT ACT_SITE 121
FT /note="Charge relay system"
FT ACT_SITE 215
FT /note="Charge relay system"
FT CARBOHYD 102
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000305"
FT DISULFID 31..175
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT DISULFID 50..66
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT DISULFID 153..221
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT DISULFID 186..200
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT DISULFID 211..236
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
SQ SEQUENCE 263 AA; 29130 MW; A8EB023B800337D5 CRC64;
MWFLILFLAL FLGGIDAAPP VQSRIIGGFN CEKNSQPWHV AVYRFARYQC GGVLLDANWV
LTAAHCYNDK YQVWLGKNNR FEDEPSAQHQ LISKAIPHPG FNMSLLNKDH TPHPEDDYSN
DLMLVRLKKP AEITDVVKPI DLPTEEPTVG SRCLASGWGS TTPTEEFEYS HDLQCVYLEL
LSNEVCAKAH TEKVTDTMLC AGEMDGGKDT CVGDSGGPLI CDGVLQGITS WGPTPCALPN
VPGIYTKLIE YRSWIKDVMA NNP
