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Submandibular glandular kallikrein-9 (rGK-9) (EC 3.4.21.35) (KLK-S3) (S3 kallikrein) (Submandibular enzymatic vasoconstrictor) (SEV) (Tissue kallikrein) [Cleaved into: Submandibular glandular kallikrein-9 light chain; Submandibular glandular kallikrein-9 heavy chain]

 KLK9_RAT                Reviewed;         259 AA.
P07647;
01-APR-1988, integrated into UniProtKB/Swiss-Prot.
01-APR-1988, sequence version 1.
10-MAY-2017, entry version 129.
RecName: Full=Submandibular glandular kallikrein-9;
Short=rGK-9;
EC=3.4.21.35;
AltName: Full=KLK-S3;
AltName: Full=S3 kallikrein;
AltName: Full=Submandibular enzymatic vasoconstrictor;
Short=SEV;
AltName: Full=Tissue kallikrein;
Contains:
RecName: Full=Submandibular glandular kallikrein-9 light chain;
Contains:
RecName: Full=Submandibular glandular kallikrein-9 heavy chain;
Flags: Precursor;
Name=Klk9; Synonyms=Klk-9, Klks3;
Rattus norvegicus (Rat).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Rattus.
NCBI_TaxID=10116;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=2998455; DOI=10.1021/bi00338a005;
Ashley P.L., MacDonald R.J.;
"Kallikrein-related mRNAs of the rat submaxillary gland: nucleotide
sequences of four distinct types including tonin.";
Biochemistry 24:4512-4520(1985).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Prostate;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[3]
PROTEIN SEQUENCE OF 25-36 AND 112-122.
TISSUE=Submandibular gland;
PubMed=1900513;
Yamaguchi T., Carretero O.A., Scicli A.G.;
"A novel serine protease with vasoconstrictor activity coded by the
kallikrein gene S3.";
J. Biol. Chem. 266:5011-5017(1991).
[4]
PROTEIN SEQUENCE OF 25-47 AND 112-135, AND CHARACTERIZATION.
PubMed=1315752;
Moreau T., Brillard-Bourdet M., Bouhnik J., Gauthier F.;
"Protein products of the rat kallikrein gene family. Substrate
specificities of kallikrein rK2 (tonin) and kallikrein rK9.";
J. Biol. Chem. 267:10045-10051(1992).
[5]
PROTEIN SEQUENCE OF 25-53 AND 112-130, AND CHARACTERIZATION.
TISSUE=Submandibular gland;
PubMed=1536657; DOI=10.1042/bj2810819;
Berg T., Schoeyen H., Wassdal I., Hull R., Gerskowitch V.P., Toft P.;
"Characterization of a new kallikrein-like enzyme (KLP-S3) of the rat
submandibular gland.";
Biochem. J. 281:819-828(1992).
-!- FUNCTION: Glandular kallikreins cleave Met-Lys and Arg-Ser bonds
in kininogen to release Lys-bradykinin. This enzyme has a
vasoconstrictor activity. KLK-9 has both a chymotrypsin-like and a
trypsin-like properties.
-!- CATALYTIC ACTIVITY: Preferential cleavage of Arg-|-Xaa bonds in
small molecule substrates. Highly selective action to release
kallidin (lysyl-bradykinin) from kininogen involves hydrolysis of
Met-|-Xaa or Leu-|-Xaa.
-!- SUBUNIT: Heterodimer of a light chain and heavy chain linked by a
disulfide bond.
-!- SIMILARITY: Belongs to the peptidase S1 family. Kallikrein
subfamily. {ECO:0000255|PROSITE-ProRule:PRU00274}.
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EMBL; M11566; AAA41467.1; -; mRNA.
EMBL; BC061771; AAH61771.1; -; mRNA.
PIR; D23863; D23863.
RefSeq; NP_786935.1; NM_175759.2.
UniGene; Rn.224461; -.
ProteinModelPortal; P07647; -.
SMR; P07647; -.
STRING; 10116.ENSRNOP00000025723; -.
MEROPS; S01.407; -.
PaxDb; P07647; -.
PRIDE; P07647; -.
Ensembl; ENSRNOT00000025723; ENSRNOP00000025723; ENSRNOG00000032857.
GeneID; 292868; -.
KEGG; rno:292868; -.
UCSC; RGD:727805; rat.
CTD; 292868; -.
RGD; 727805; Klks3.
eggNOG; KOG3627; Eukaryota.
eggNOG; COG5640; LUCA.
GeneTree; ENSGT00760000118862; -.
HOGENOM; HOG000251820; -.
HOVERGEN; HBG013304; -.
InParanoid; P07647; -.
PhylomeDB; P07647; -.
TreeFam; TF331065; -.
BRENDA; 3.4.21.B40; 5301.
PRO; PR:P07647; -.
Proteomes; UP000002494; Chromosome 1.
Bgee; ENSRNOG00000032857; -.
ExpressionAtlas; P07647; baseline and differential.
Genevisible; P07647; RN.
GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
GO; GO:0045907; P:positive regulation of vasoconstriction; IDA:RGD.
CDD; cd00190; Tryp_SPc; 1.
InterPro; IPR009003; Peptidase_S1_PA.
InterPro; IPR001314; Peptidase_S1A.
InterPro; IPR001254; Trypsin_dom.
InterPro; IPR018114; TRYPSIN_HIS.
InterPro; IPR033116; TRYPSIN_SER.
Pfam; PF00089; Trypsin; 1.
PRINTS; PR00722; CHYMOTRYPSIN.
SMART; SM00020; Tryp_SPc; 1.
SUPFAM; SSF50494; SSF50494; 1.
PROSITE; PS50240; TRYPSIN_DOM; 1.
PROSITE; PS00134; TRYPSIN_HIS; 1.
PROSITE; PS00135; TRYPSIN_SER; 1.
1: Evidence at protein level;
Complete proteome; Direct protein sequencing; Disulfide bond;
Glycoprotein; Hydrolase; Protease; Reference proteome;
Serine protease; Signal; Zymogen.
SIGNAL 1 18 {ECO:0000305}.
PROPEP 19 24 Activation peptide.
{ECO:0000269|PubMed:1315752,
ECO:0000269|PubMed:1536657,
ECO:0000269|PubMed:1900513}.
/FTId=PRO_0000028009.
CHAIN 25 259 Submandibular glandular kallikrein-9.
/FTId=PRO_0000028010.
CHAIN 25 111 Submandibular glandular kallikrein-9
light chain.
/FTId=PRO_0000028011.
CHAIN 112 259 Submandibular glandular kallikrein-9
heavy chain.
/FTId=PRO_0000028012.
DOMAIN 25 256 Peptidase S1. {ECO:0000255|PROSITE-
ProRule:PRU00274}.
ACT_SITE 63 63 Charge relay system.
ACT_SITE 118 118 Charge relay system.
ACT_SITE 211 211 Charge relay system.
CARBOHYD 106 106 N-linked (GlcNAc...) asparagine.
{ECO:0000305}.
DISULFID 31 171 {ECO:0000255|PROSITE-ProRule:PRU00274}.
DISULFID 48 64 {ECO:0000255|PROSITE-ProRule:PRU00274}.
DISULFID 150 217 {ECO:0000255|PROSITE-ProRule:PRU00274}.
DISULFID 182 196 {ECO:0000255|PROSITE-ProRule:PRU00274}.
DISULFID 207 232 {ECO:0000255|PROSITE-ProRule:PRU00274}.
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


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