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Protein

Submandibular glandular kallikrein-9

Gene

Klk9

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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 activityi

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.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei63 – 631Charge relay system
Active sitei118 – 1181Charge relay system
Active sitei211 – 2111Charge relay system

GO - Molecular functioni

GO - Biological processi

  • positive regulation of vasoconstriction Source: RGD
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Protease, Serine protease

Enzyme and pathway databases

BRENDAi3.4.21.B40. 5301.

Protein family/group databases

MEROPSiS01.407.

Names & Taxonomyi

Protein namesi
Recommended name:
Submandibular glandular kallikrein-9 (EC:3.4.21.35)
Short name:
rGK-9
Alternative name(s):
KLK-S3
S3 kallikrein
Submandibular enzymatic vasoconstrictor
Short name:
SEV
Tissue kallikrein
Cleaved into the following 2 chains:
Gene namesi
Name:Klk9
Synonyms:Klk-9, Klks3
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
ProteomesiUP000002494 Componenti: Chromosome 1

Organism-specific databases

RGDi727805. Klks3.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 1818CuratedAdd
BLAST
Propeptidei19 – 246Activation peptide3 PublicationsPRO_0000028009
Chaini25 – 259235Submandibular glandular kallikrein-9PRO_0000028010Add
BLAST
Chaini25 – 11187Submandibular glandular kallikrein-9 light chainPRO_0000028011Add
BLAST
Chaini112 – 259148Submandibular glandular kallikrein-9 heavy chainPRO_0000028012Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi31 ↔ 171PROSITE-ProRule annotation
Disulfide bondi48 ↔ 64PROSITE-ProRule annotation
Glycosylationi106 – 1061N-linked (GlcNAc...)Curated
Disulfide bondi150 ↔ 217PROSITE-ProRule annotation
Disulfide bondi182 ↔ 196PROSITE-ProRule annotation
Disulfide bondi207 ↔ 232PROSITE-ProRule annotation

Keywords - PTMi

Disulfide bond, Glycoprotein, Zymogen

Proteomic databases

PRIDEiP07647.

Expressioni

Gene expression databases

GenevestigatoriP07647.

Interactioni

Subunit structurei

Heterodimer of a light chain and heavy chain linked by a disulfide bond.

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000025723.

Structurei

3D structure databases

ProteinModelPortaliP07647.
SMRiP07647. Positions 25-259.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini25 – 256232Peptidase S1PROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Belongs to the peptidase S1 family. Kallikrein subfamily.PROSITE-ProRule annotation
Contains 1 peptidase S1 domain.PROSITE-ProRule annotation

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiCOG5640.
GeneTreeiENSGT00760000118862.
HOGENOMiHOG000251820.
HOVERGENiHBG013304.
InParanoidiP07647.
OMAiNCETNSQ.
OrthoDBiEOG75B84T.
PhylomeDBiP07647.
TreeFamiTF331065.

Family and domain databases

InterProiIPR001254. Peptidase_S1.
IPR018114. Peptidase_S1_AS.
IPR001314. Peptidase_S1A.
IPR009003. Trypsin-like_Pept_dom.
[Graphical view]
PfamiPF00089. Trypsin. 1 hit.
[Graphical view]
PRINTSiPR00722. CHYMOTRYPSIN.
SMARTiSM00020. Tryp_SPc. 1 hit.
[Graphical view]
SUPFAMiSSF50494. SSF50494. 1 hit.
PROSITEiPS50240. TRYPSIN_DOM. 1 hit.
PS00134. TRYPSIN_HIS. 1 hit.
PS00135. TRYPSIN_SER. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P07647-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MWFLILFLAL SLGQIDAAPP GQSRVVGGYN CETNSQPWQV AVIGTTFCGG
60 70 80 90 100
VLIDPSWVIT AAHCYSKNYR VLLGRNNLVK DEPFAQRRLV SQSFQHPDYI
110 120 130 140 150
PVFMRNHTRQ RAYDHNNDLM LLHLSKPADI TGGVKVIDLP TEEPKVGSIC
160 170 180 190 200
LASGWGMTNP SEMKLSHDLQ CVNIHLLSNE KCIETYKNIE TDVTLCAGEM
210 220 230 240 250
DGGKDTCTGD SGGPLICDGV LQGLTSGGAT PCAKPKTPAI YAKLIKFTSW

IKKVMKENP
Length:259
Mass (Da):28,368
Last modified:April 1, 1988 - v1
Checksum:iD167E8518BEC0791
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M11566 mRNA. Translation: AAA41467.1.
BC061771 mRNA. Translation: AAH61771.1.
PIRiD23863.
RefSeqiNP_786935.1. NM_175759.2.
UniGeneiRn.224461.

Genome annotation databases

EnsembliENSRNOT00000025723; ENSRNOP00000025723; ENSRNOG00000032857.
GeneIDi292868.
KEGGirno:292868.
UCSCiRGD:727805. rat.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M11566 mRNA. Translation: AAA41467.1.
BC061771 mRNA. Translation: AAH61771.1.
PIRiD23863.
RefSeqiNP_786935.1. NM_175759.2.
UniGeneiRn.224461.

3D structure databases

ProteinModelPortaliP07647.
SMRiP07647. Positions 25-259.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000025723.

Protein family/group databases

MEROPSiS01.407.

Proteomic databases

PRIDEiP07647.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSRNOT00000025723; ENSRNOP00000025723; ENSRNOG00000032857.
GeneIDi292868.
KEGGirno:292868.
UCSCiRGD:727805. rat.

Organism-specific databases

CTDi292868.
RGDi727805. Klks3.

Phylogenomic databases

eggNOGiCOG5640.
GeneTreeiENSGT00760000118862.
HOGENOMiHOG000251820.
HOVERGENiHBG013304.
InParanoidiP07647.
OMAiNCETNSQ.
OrthoDBiEOG75B84T.
PhylomeDBiP07647.
TreeFamiTF331065.

Enzyme and pathway databases

BRENDAi3.4.21.B40. 5301.

Miscellaneous databases

NextBioi634947.
PROiP07647.

Gene expression databases

GenevestigatoriP07647.

Family and domain databases

InterProiIPR001254. Peptidase_S1.
IPR018114. Peptidase_S1_AS.
IPR001314. Peptidase_S1A.
IPR009003. Trypsin-like_Pept_dom.
[Graphical view]
PfamiPF00089. Trypsin. 1 hit.
[Graphical view]
PRINTSiPR00722. CHYMOTRYPSIN.
SMARTiSM00020. Tryp_SPc. 1 hit.
[Graphical view]
SUPFAMiSSF50494. SSF50494. 1 hit.
PROSITEiPS50240. TRYPSIN_DOM. 1 hit.
PS00134. TRYPSIN_HIS. 1 hit.
PS00135. TRYPSIN_SER. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Kallikrein-related mRNAs of the rat submaxillary gland: nucleotide sequences of four distinct types including tonin."
    Ashley P.L., MacDonald R.J.
    Biochemistry 24:4512-4520(1985) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Prostate.
  3. "A novel serine protease with vasoconstrictor activity coded by the kallikrein gene S3."
    Yamaguchi T., Carretero O.A., Scicli A.G.
    J. Biol. Chem. 266:5011-5017(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 25-36 AND 112-122.
    Tissue: Submandibular gland.
  4. "Protein products of the rat kallikrein gene family. Substrate specificities of kallikrein rK2 (tonin) and kallikrein rK9."
    Moreau T., Brillard-Bourdet M., Bouhnik J., Gauthier F.
    J. Biol. Chem. 267:10045-10051(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 25-47 AND 112-135, CHARACTERIZATION.
  5. "Characterization of a new kallikrein-like enzyme (KLP-S3) of the rat submandibular gland."
    Berg T., Schoeyen H., Wassdal I., Hull R., Gerskowitch V.P., Toft P.
    Biochem. J. 281:819-828(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 25-53 AND 112-130, CHARACTERIZATION.
    Tissue: Submandibular gland.

Entry informationi

Entry nameiKLK9_RAT
AccessioniPrimary (citable) accession number: P07647
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 1, 1988
Last sequence update: April 1, 1988
Last modified: April 29, 2015
This is version 114 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Peptidase families
    Classification of peptidase families and list of entries
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.