ID KLK3_RAT Reviewed; 188 AA.
AC P15950;
DT 01-APR-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1994, sequence version 2.
DT 24-JAN-2024, entry version 130.
DE RecName: Full=Glandular kallikrein-3, submandibular;
DE Short=rGK-3;
DE EC=3.4.21.35;
DE AltName: Full=RSGK-50;
DE AltName: Full=S1 kallikrein;
DE AltName: Full=Tissue kallikrein;
DE Flags: Fragment;
GN Name=Klk3; Synonyms=Klk-3;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2550051; DOI=10.1021/bi00439a005;
RA Shai S.Y., Woodley-Miller C., Chao J., Chao L.;
RT "Characterization of genes encoding rat tonin and a kallikrein-like serine
RT protease.";
RL Biochemistry 28:5334-5343(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 33-188.
RX PubMed=2998455; DOI=10.1021/bi00338a005;
RA Ashley P.L., MacDonald R.J.;
RT "Kallikrein-related mRNAs of the rat submaxillary gland: nucleotide
RT sequences of four distinct types including tonin.";
RL Biochemistry 24:4512-4520(1985).
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; M26534; AAA42080.1; -; Genomic_DNA.
DR EMBL; M11564; AAA41465.1; -; mRNA.
DR PIR; B23863; B23863.
DR PIR; B32340; B32340.
DR AlphaFoldDB; P15950; -.
DR SMR; P15950; -.
DR MEROPS; S01.411; -.
DR GlyCosmos; P15950; 2 sites, No reported glycans.
DR GlyGen; P15950; 2 sites.
DR PhosphoSitePlus; P15950; -.
DR PaxDb; 10116-ENSRNOP00000025777; -.
DR AGR; RGD:735032; -.
DR eggNOG; KOG3627; Eukaryota.
DR InParanoid; P15950; -.
DR PhylomeDB; P15950; -.
DR TreeFam; TF331065; -.
DR BRENDA; 3.4.21.77; 5301.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0030141; C:secretory granule; IBA:GO_Central.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:UniProtKB-EC.
DR GO; GO:0003073; P:regulation of systemic arterial blood pressure; IBA:GO_Central.
DR GO; GO:0031638; P:zymogen activation; IBA:GO_Central.
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; 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; PS00135; TRYPSIN_SER; 1.
PE 2: Evidence at transcript level;
KW Disulfide bond; Glycoprotein; Hydrolase; Protease; Reference proteome;
KW Serine protease.
FT CHAIN <1..188
FT /note="Glandular kallikrein-3, submandibular"
FT /id="PRO_0000088702"
FT DOMAIN <1..185
FT /note="Peptidase S1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT ACT_SITE 47
FT /note="Charge relay system"
FT ACT_SITE 140
FT /note="Charge relay system"
FT CARBOHYD 10
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 36
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 79..146
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT DISULFID 111..125
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT DISULFID 136..161
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT CONFLICT 34..35
FT /note="MR -> IW (in Ref. 2; AAA41465)"
FT /evidence="ECO:0000305"
FT CONFLICT 42
FT /note="K -> G (in Ref. 2; AAA41465)"
FT /evidence="ECO:0000305"
FT CONFLICT 186
FT /note="E -> K (in Ref. 1; AAA42080)"
FT /evidence="ECO:0000305"
FT NON_TER 1
SQ SEQUENCE 188 AA; 20986 MW; B3ECEC65582EB1E9 CRC64;
NYHVLLGQNN LSEDVQHRLV SQSFRHPDYK PFLMRNHTRK PKDYSNDLML LHLSEPADIT
DGVKVIDLPT KEPKVGSTCL VSGWGSTNPS EWEFPDDLQC VNIHLLSNEK CIKAYKEKVT
DLMLCAGELE GGKDTCRGDS GGPLICDGVL QGITSWGSVP CGEPNKPGIY TKLIKFTSWI
KEVMKENP
//
