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Tonin (EC 3.4.21.35) (Esterase 1) (Glandular kallikrein-2) (rGK-2) (RSKG-5) (S2 kallikrein)

 KLK2_RAT                Reviewed;         259 AA.
P00759;
21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
01-APR-1988, sequence version 1.
12-SEP-2018, entry version 151.
RecName: Full=Tonin;
EC=3.4.21.35;
AltName: Full=Esterase 1;
AltName: Full=Glandular kallikrein-2;
Short=rGK-2;
AltName: Full=RSKG-5;
AltName: Full=S2 kallikrein;
Flags: Precursor;
Name=Klk2; Synonyms=Klk-2, Ton;
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 [GENOMIC DNA].
PubMed=2708383;
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].
PubMed=2550051; DOI=10.1021/bi00439a005;
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;
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.
PubMed=6320014; DOI=10.1038/307555a0;
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.
PubMed=2302205; DOI=10.1016/0006-291X(90)91935-L;
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;
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).
PubMed=2821276; DOI=10.1016/0022-2836(87)90658-9;
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).
-!- 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:
Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
Note=Binds 1 zinc ion per subunit.;
-!- SUBUNIT: Monomer.
-!- TISSUE SPECIFICITY: Found in submaxillary gland.
-!- SIMILARITY: Belongs to the peptidase S1 family. Kallikrein
subfamily. {ECO:0000255|PROSITE-ProRule:PRU00274}.
-----------------------------------------------------------------------
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EMBL; M11565; AAA41466.1; -; mRNA.
EMBL; M23878; AAA42259.1; -; Genomic_DNA.
EMBL; M23877; AAA42259.1; JOINED; Genomic_DNA.
EMBL; M26533; AAA42081.1; -; Genomic_DNA.
PIR; B33359; KQRTTN.
RefSeq; NP_036809.1; NM_012677.1.
UniGene; Rn.9882; -.
PDB; 1TON; X-ray; 1.80 A; A=25-259.
PDBsum; 1TON; -.
ProteinModelPortal; P00759; -.
SMR; P00759; -.
STRING; 10116.ENSRNOP00000025701; -.
MEROPS; S01.172; -.
iPTMnet; P00759; -.
PaxDb; P00759; -.
PRIDE; P00759; -.
Ensembl; ENSRNOT00000025701; ENSRNOP00000025701; ENSRNOG00000029237.
GeneID; 24841; -.
KEGG; rno:24841; -.
UCSC; RGD:3888; rat.
CTD; 24841; -.
RGD; 3888; Ton.
eggNOG; KOG3627; Eukaryota.
eggNOG; COG5640; LUCA.
GeneTree; ENSGT00920000149111; -.
HOGENOM; HOG000251820; -.
HOVERGEN; HBG013304; -.
InParanoid; P00759; -.
KO; K01325; -.
OMA; GWECERH; -.
OrthoDB; EOG091G0DF7; -.
PhylomeDB; P00759; -.
TreeFam; TF331065; -.
EvolutionaryTrace; P00759; -.
PRO; PR:P00759; -.
Proteomes; UP000002494; Chromosome 1.
Bgee; ENSRNOG00000029237; Expressed in 1 organ(s), highest expression level in adult mammalian kidney.
Genevisible; P00759; RN.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
GO; GO:0008236; F:serine-type peptidase activity; 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;
3D-structure; Complete proteome; Direct protein sequencing;
Disulfide bond; Glycoprotein; Hydrolase; Metal-binding; Protease;
Reference proteome; Serine protease; Signal; Zinc; Zymogen.
SIGNAL 1 18
PROPEP 19 24 Activation peptide.
{ECO:0000269|PubMed:1315752,
ECO:0000269|PubMed:2302205,
ECO:0000269|PubMed:3038148,
ECO:0000269|PubMed:6320014}.
/FTId=PRO_0000028003.
CHAIN 25 259 Tonin.
/FTId=PRO_0000028004.
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.
METAL 63 63 Zinc.
METAL 113 113 Zinc.
METAL 115 115 Zinc.
CARBOHYD 106 106 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:3038148}.
CARBOHYD 189 189 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:3038148}.
DISULFID 31 171
DISULFID 48 64
DISULFID 150 217
DISULFID 182 196
DISULFID 207 232
STRAND 39 54 {ECO:0000244|PDB:1TON}.
STRAND 57 60 {ECO:0000244|PDB:1TON}.
HELIX 62 64 {ECO:0000244|PDB:1TON}.
STRAND 70 74 {ECO:0000244|PDB:1TON}.
STRAND 86 88 {ECO:0000244|PDB:1TON}.
STRAND 90 95 {ECO:0000244|PDB:1TON}.
STRAND 120 126 {ECO:0000244|PDB:1TON}.
STRAND 149 156 {ECO:0000244|PDB:1TON}.
STRAND 158 162 {ECO:0000244|PDB:1TON}.
STRAND 170 177 {ECO:0000244|PDB:1TON}.
HELIX 179 181 {ECO:0000244|PDB:1TON}.
HELIX 183 186 {ECO:0000244|PDB:1TON}.
HELIX 190 193 {ECO:0000244|PDB:1TON}.
STRAND 194 198 {ECO:0000244|PDB:1TON}.
STRAND 214 217 {ECO:0000244|PDB:1TON}.
STRAND 220 225 {ECO:0000244|PDB:1TON}.
STRAND 239 243 {ECO:0000244|PDB:1TON}.
HELIX 244 247 {ECO:0000244|PDB:1TON}.
HELIX 248 257 {ECO:0000244|PDB:1TON}.
SEQUENCE 259 AA; 28248 MW; 3D6E60D011F926B4 CRC64;
MWLQILSLVL SVGRIDAAPP GQSRIVGGYK CEKNSQPWQV AVINEYLCGG VLIDPSWVIT
AAHCYSNNYQ VLLGRNNLFK DEPFAQRRLV RQSFRHPDYI PLIVTNDTEQ PVHDHSNDLM
LLHLSEPADI TGGVKVIDLP TKEPKVGSTC LASGWGSTNP SEMVVSHDLQ CVNIHLLSNE
KCIETYKDNV TDVMLCAGEM EGGKDTCAGD SGGPLICDGV LQGITSGGAT PCAKPKTPAI
YAKLIKFTSW IKKVMKENP


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