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 05-MAY-2009, entry version 73. DE RecName: Full=Submandibular glandular kallikrein-9; DE EC=3.4.21.35; DE AltName: Full=Tissue kallikrein; DE AltName: Full=S3 kallikrein; DE AltName: Full=Submandibular enzymatic vasoconstrictor; DE Short=SEV; DE AltName: Full=KLK-S3; 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; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Rattus. OX NCBI_TaxID=10116; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RX MEDLINE=86051477; 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 RT project: 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 MEDLINE=91161590; PubMed=1900513; 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 MEDLINE=92250562; PubMed=1315752; 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 MEDLINE=92162030; PubMed=1536657; 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 CC in kininogen to release Lys-bradykinin. This enzyme has a CC vasoconstrictor activity. KLK-9 has both a chymotrypsin-like and a CC trypsin-like properties. CC -!- CATALYTIC ACTIVITY: Preferential cleavage of Arg-|-Xaa bonds in CC small molecule substrates. Highly selective action to release CC kallidin (lysyl-bradykinin) from kininogen involves hydrolysis of CC Met-|-Xaa or Leu-|-Xaa. 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 CC subfamily. CC -!- SIMILARITY: Contains 1 peptidase S1 domain. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; M11566; AAA41467.1; -; mRNA. DR EMBL; BC061771; AAH61771.1; -; mRNA. DR IPI; IPI00209517; -. DR PIR; D23863; D23863. DR RefSeq; NP_786935.1; -. DR UniGene; Rn.107068; -. DR HSSP; P00759; 1TON. DR SMR; P07647; 25-259. DR MEROPS; S01.407; -. DR Ensembl; ENSRNOG00000032857; Rattus norvegicus. DR GeneID; 292868; -. DR KEGG; rno:292868; -. DR RGD; 727805; Klks3. DR HOVERGEN; P07647; -. DR OMA; P07647; NENCAKV. DR BRENDA; 3.4.21.35; 248. DR NextBio; 634947; -. DR ArrayExpress; P07647; -. DR GermOnline; ENSRNOG00000032857; Rattus norvegicus. DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro. DR GO; GO:0045907; P:positive regulation of vasoconstriction; IDA:RGD. DR GO; GO:0006508; P:proteolysis; IEA:InterPro. DR InterPro; IPR018114; Peptidase_S1/S6_AS. DR InterPro; IPR001254; Peptidase_S1_S6. DR InterPro; IPR001314; Peptidase_S1A. DR Pfam; PF00089; Trypsin; 1. DR PRINTS; PR00722; CHYMOTRYPSIN. DR SMART; SM00020; Tryp_SPc; 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; Serine protease; Signal; Zymogen. FT SIGNAL 1 18 Probable. FT PROPEP 19 24 Activation peptide. FT /FTId=PRO_0000028009. FT CHAIN 25 259 Submandibular glandular kallikrein-9. FT /FTId=PRO_0000028010. FT CHAIN 25 111 Submandibular glandular kallikrein-9 FT light chain. FT /FTId=PRO_0000028011. FT CHAIN 112 259 Submandibular glandular kallikrein-9 FT heavy chain. FT /FTId=PRO_0000028012. FT DOMAIN 25 256 Peptidase S1. FT ACT_SITE 63 63 Charge relay system. FT ACT_SITE 118 118 Charge relay system. FT ACT_SITE 211 211 Charge relay system. FT CARBOHYD 106 106 N-linked (GlcNAc...) (Probable). FT DISULFID 31 171 By similarity. FT DISULFID 48 64 By similarity. FT DISULFID 150 217 By similarity. FT DISULFID 182 196 By similarity. FT DISULFID 207 232 By similarity. 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 //