[1]	NUCLEOTIDE SEQUENCE [MRNA]. DOI=10.1021/bi00338a005; PubMed=2998455 [NCBI, ExPASy, EBI, Israel, Japan] 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 [GENOMIC DNA]. PubMed=2708383 [NCBI, ExPASy, EBI, Israel, Japan] Wines D.R., Brady J.M., Pritchett D.B., Roberts J.L., MacDonald R.J.; "Organization and expression of the rat kallikrein gene family."; J. Biol. Chem. 264:7653-7662(1989).
[3]	NUCLEOTIDE SEQUENCE [GENOMIC DNA]. DOI=10.1021/bi00439a005; PubMed=2550051 [NCBI, ExPASy, EBI, Israel, Japan] Shai S.Y., Woodley-Miller C., Chao J., Chao L.; "Characterization of genes encoding rat tonin and a kallikrein-like serine protease."; Biochemistry 28:5334-5343(1989).
[4]	PROTEIN SEQUENCE OF 25-259. PubMed=3038148 [NCBI, ExPASy, EBI, Israel, Japan] Lazure C., Leduc R., Seidah N.G., Thibault G., Genest J., Chretien M.; "The complete amino acid sequence of rat submaxillary gland tonin does contain the aspartic acid at the active site: confirmation by protein sequence analysis."; Biochem. Cell Biol. 65:321-337(1987).
[5]	PROTEIN SEQUENCE OF 25-103 AND 120-259. DOI=10.1038/307555a0; PubMed=6320014 [NCBI, ExPASy, EBI, Israel, Japan] Lazure C., Leduc R., Seidah N.G., Thibault G., Genest J., Chretien M.; "Amino acid sequence of rat submaxillary tonin reveals similarities to serine proteases."; Nature 307:555-558(1984).
[6]	PROTEIN SEQUENCE OF 25-34. DOI=10.1016/0006-291X(90)91935-L; PubMed=2302205 [NCBI, ExPASy, EBI, Israel, Japan] Kamada M., Furuhata N., Yamaguchi T., Ikekita M., Kizuki K., Moriya H.; "Observation of tissue prokallikrein activation by some serine proteases, arginine esterases in rat submandibular gland."; Biochem. Biophys. Res. Commun. 166:231-237(1990).
[7]	PROTEIN SEQUENCE OF 25-50, AND CHARACTERIZATION. PubMed=1315752 [NCBI, ExPASy, EBI, Israel, Japan] 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).
[8]	X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS). DOI=10.1016/0022-2836(87)90658-9; PubMed=2821276 [NCBI, ExPASy, EBI, Israel, Japan] Fujinaga M., James M.N.G.; "Rat submaxillary gland serine protease, tonin. Structure solution and refinement at 1.8-A resolution."; J. Mol. Biol. 195:373-396(1987).

Comments

FUNCTION: This protein has both trypsin- and chymotrypsin-like activities, being able to release angiotensin II from angiotensin I or angiotensinogen.
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.
COFACTOR: Binds 1 zinc ion per subunit.
SUBUNIT: Monomer.
TISSUE SPECIFICITY: Found in submaxillary gland.
SIMILARITY: Belongs to the peptidase S1 family. Kallikrein subfamily [view classification].
SIMILARITY: Contains 1 peptidase S1 domain [view classification].

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

M11565; AAA41466.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
M23878; AAA42259.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
M23877; AAA42259.1; JOINED; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
M26533; AAA42081.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

B33359; KQRTTN.

NP_036809.1; -.

3D structure databases

PDB

1TON; X-ray; 1.80 A; A=25-259.

[ExPASy / RCSB / EBI]

PDBsum

1TON; -.

ModBase

P00759.

Protein family/group databases

MEROPS

S01.172; -.

Organism-specific databases

RGD

3888; Ton.

Gene expression databases

ArrayExpress

P00759; -.

GermOnline

ENSRNOG00000029237; Rattus norvegicus.

Ontologies

GO:0008270;	Molecular function: zinc ion binding (inferred from electronic annotation from UniProtKB-KW).
QuickGo view.

Family and domain databases

InterPro

IPR001254; Peptidase_S1_S6.
IPR001314; Peptidase_S1A.
Graphical view of domain structure.

Pfam

PF00089; Trypsin; 1.
Pfam graphical view of domain structure.

PRINTS

PR00722; CHYMOTRYPSIN.

SMART

SM00020; Tryp_SPc; 1.
SMART graphical view of domain structure.

PROSITE

PS50240; TRYPSIN_DOM; 1.
PS00134; TRYPSIN_HIS; 1.
PS00135; TRYPSIN_SER; 1.
PROSITE graphical view of domain structure (profiles).

Genome annotation databases

Ensembl

ENSRNOG00000029237; Rattus norvegicus. [Contig view]

GeneID

24841; -.

KEGG

rno:24841; -.

Phylogenomic databases

HOVERGEN

P00759; -.

Other

LinkHub

P00759; -.

NextBio

604592; -.

UniRef

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

3D-structure; Direct protein sequencing; Glycoprotein; Hydrolase; Metal-binding; Protease; Serine protease; Signal; Zinc; Zymogen.

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`SIGNAL`	`1 18`	`18`
`PROPEP`	`19 24`	`6`	`Activation peptide.`	`PRO_0000028003`
`CHAIN`	`25 259`	`235`	`Tonin.`	`PRO_0000028004`
`DOMAIN`	`25 256`	`232`	`Peptidase S1.`
`ACT_SITE`	`63 63`		`Charge relay system.`
`ACT_SITE`	`118 118`		`Charge relay system.`
`ACT_SITE`	`211 211`		`Charge relay system.`
`METAL`	`63 63`		`Zinc.`
`METAL`	`113 113`		`Zinc.`
`METAL`	`115 115`		`Zinc.`
`CARBOHYD`	`106 106`		`N-linked (GlcNAc...).`
`CARBOHYD`	`189 189`		`N-linked (GlcNAc...).`
`DISULFID`	`31 171`
`DISULFID`	`48 64`
`DISULFID`	`150 217`
`DISULFID`	`182 196`
`DISULFID`	`207 232`
`STRAND`	`39 54`	`16`
`STRAND`	`57 60`	`4`
`HELIX`	`62 64`	`3`
`STRAND`	`70 74`	`5`
`STRAND`	`86 88`	`3`
`STRAND`	`90 95`	`6`
`STRAND`	`120 126`	`7`
`STRAND`	`149 156`	`8`
`STRAND`	`158 162`	`5`
`STRAND`	`170 177`	`8`
`HELIX`	`179 181`	`3`
`HELIX`	`183 186`	`4`
`HELIX`	`190 193`	`4`
`STRAND`	`194 198`	`5`
`STRAND`	`214 217`	`4`
`STRAND`	`220 225`	`6`
`STRAND`	`239 243`	`5`
`HELIX`	`244 247`	`4`
`HELIX`	`248 257`	`10`

Sequence information

Length: 259 AA [This is the length of the unprocessed precursor]

Molecular weight: 28248 Da [This is the MW of the unprocessed precursor]

CRC64: 3D6E60D011F926B4 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MWLQILSLVL SVGRIDAAPP GQSRIVGGYK CEKNSQPWQV AVINEYLCGG VLIDPSWVIT 

        70         80         90        100        110        120 
AAHCYSNNYQ VLLGRNNLFK DEPFAQRRLV RQSFRHPDYI PLIVTNDTEQ PVHDHSNDLM 

       130        140        150        160        170        180 
LLHLSEPADI TGGVKVIDLP TKEPKVGSTC LASGWGSTNP SEMVVSHDLQ CVNIHLLSNE 

       190        200        210        220        230        240 
KCIETYKDNV TDVMLCAGEM EGGKDTCAGD SGGPLICDGV LQGITSGGAT PCAKPKTPAI 

       250 
YAKLIKFTSW IKKVMKENP

P00759 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools