KLK9_RAT
ID KLK9_RAT Reviewed; 259 AA.
AC P07647;
DT 01-APR-1988, integrated into UniProtKB/Swiss-Prot.
DT 01-APR-1988, sequence version 1.
DT 03-AUG-2022, entry version 147.
DE RecName: Full=Submandibular glandular kallikrein-9;
DE Short=rGK-9;
DE EC=3.4.21.35;
DE AltName: Full=KLK-S3;
DE AltName: Full=S3 kallikrein;
DE AltName: Full=Submandibular enzymatic vasoconstrictor;
DE Short=SEV;
DE AltName: Full=Tissue kallikrein;
DE Contains:
DE RecName: Full=Submandibular glandular kallikrein-9 light chain;
DE Contains:
DE RecName: Full=Submandibular glandular kallikrein-9 heavy chain;
DE Flags: Precursor;
GN Name=Klk9; Synonyms=Klk-9, Klks3;
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 [MRNA].
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).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Prostate;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [3]
RP PROTEIN SEQUENCE OF 25-36 AND 112-122.
RC TISSUE=Submandibular gland;
RX PubMed=1900513; DOI=10.1016/s0021-9258(19)67749-5;
RA Yamaguchi T., Carretero O.A., Scicli A.G.;
RT "A novel serine protease with vasoconstrictor activity coded by the
RT kallikrein gene S3.";
RL J. Biol. Chem. 266:5011-5017(1991).
RN [4]
RP PROTEIN SEQUENCE OF 25-47 AND 112-135, AND CHARACTERIZATION.
RX PubMed=1315752; DOI=10.1016/s0021-9258(19)50197-1;
RA Moreau T., Brillard-Bourdet M., Bouhnik J., Gauthier F.;
RT "Protein products of the rat kallikrein gene family. Substrate
RT specificities of kallikrein rK2 (tonin) and kallikrein rK9.";
RL J. Biol. Chem. 267:10045-10051(1992).
RN [5]
RP PROTEIN SEQUENCE OF 25-53 AND 112-130, AND CHARACTERIZATION.
RC TISSUE=Submandibular gland;
RX PubMed=1536657; DOI=10.1042/bj2810819;
RA Berg T., Schoeyen H., Wassdal I., Hull R., Gerskowitch V.P., Toft P.;
RT "Characterization of a new kallikrein-like enzyme (KLP-S3) of the rat
RT submandibular gland.";
RL Biochem. J. 281:819-828(1992).
CC -!- FUNCTION: Glandular kallikreins cleave Met-Lys and Arg-Ser bonds in
CC kininogen to release Lys-bradykinin. This enzyme has a vasoconstrictor
CC activity. KLK-9 has both a chymotrypsin-like and a trypsin-like
CC properties.
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 -!- SUBUNIT: Heterodimer of a light chain and heavy chain linked by a
CC disulfide bond.
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; M11566; AAA41467.1; -; mRNA.
DR EMBL; BC061771; AAH61771.1; -; mRNA.
DR PIR; D23863; D23863.
DR RefSeq; NP_786935.1; NM_175759.2.
DR AlphaFoldDB; P07647; -.
DR SMR; P07647; -.
DR STRING; 10116.ENSRNOP00000025723; -.
DR MEROPS; S01.407; -.
DR GlyGen; P07647; 1 site.
DR PaxDb; P07647; -.
DR PRIDE; P07647; -.
DR Ensembl; ENSRNOT00000025723; ENSRNOP00000025723; ENSRNOG00000067884.
DR GeneID; 292868; -.
DR KEGG; rno:292868; -.
DR UCSC; RGD:727805; rat.
DR CTD; 292868; -.
DR RGD; 727805; Klks3.
DR eggNOG; KOG3627; Eukaryota.
DR GeneTree; ENSGT01020000230389; -.
DR InParanoid; P07647; -.
DR OrthoDB; 1076876at2759; -.
DR PhylomeDB; P07647; -.
DR TreeFam; TF331065; -.
DR BRENDA; 3.4.21.B40; 5301.
DR Reactome; R-RNO-1592389; Activation of Matrix Metalloproteinases.
DR Reactome; R-RNO-381426; Regulation of Insulin-like Growth Factor (IGF) transport and uptake by Insulin-like Growth Factor Binding Proteins (IGFBPs).
DR PRO; PR:P07647; -.
DR Proteomes; UP000002494; Chromosome 1.
DR Bgee; ENSRNOG00000032857; Expressed in pancreas and 19 other tissues.
DR ExpressionAtlas; P07647; baseline and differential.
DR Genevisible; P07647; RN.
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:0045907; P:positive regulation of vasoconstriction; IDA:RGD.
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; -; 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; Reference proteome; Serine protease; Signal; Zymogen.
FT SIGNAL 1..18
FT /evidence="ECO:0000305"
FT PROPEP 19..24
FT /note="Activation peptide"
FT /evidence="ECO:0000269|PubMed:1315752,
FT ECO:0000269|PubMed:1536657, ECO:0000269|PubMed:1900513"
FT /id="PRO_0000028009"
FT CHAIN 25..259
FT /note="Submandibular glandular kallikrein-9"
FT /id="PRO_0000028010"
FT CHAIN 25..111
FT /note="Submandibular glandular kallikrein-9 light chain"
FT /id="PRO_0000028011"
FT CHAIN 112..259
FT /note="Submandibular glandular kallikrein-9 heavy chain"
FT /id="PRO_0000028012"
FT DOMAIN 25..256
FT /note="Peptidase S1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT ACT_SITE 63
FT /note="Charge relay system"
FT ACT_SITE 118
FT /note="Charge relay system"
FT ACT_SITE 211
FT /note="Charge relay system"
FT CARBOHYD 106
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000305"
FT DISULFID 31..171
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT DISULFID 48..64
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT DISULFID 150..217
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT DISULFID 182..196
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT DISULFID 207..232
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
SQ SEQUENCE 259 AA; 28368 MW; D167E8518BEC0791 CRC64;
MWFLILFLAL SLGQIDAAPP GQSRVVGGYN CETNSQPWQV AVIGTTFCGG VLIDPSWVIT
AAHCYSKNYR VLLGRNNLVK DEPFAQRRLV SQSFQHPDYI PVFMRNHTRQ RAYDHNNDLM
LLHLSKPADI TGGVKVIDLP TEEPKVGSIC LASGWGMTNP SEMKLSHDLQ CVNIHLLSNE
KCIETYKNIE TDVTLCAGEM DGGKDTCTGD SGGPLICDGV LQGLTSGGAT PCAKPKTPAI
YAKLIKFTSW IKKVMKENP
