ID   NATT2_THANI             Reviewed;         376 AA.
AC   Q66S21;
DT   01-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT   11-OCT-2004, sequence version 1.
DT   25-MAY-2022, entry version 65.
DE   RecName: Full=Natterin-2;
DE            EC=3.4.-.-;
DE   Flags: Precursor;
OS   Thalassophryne nattereri (Copper Joe toadfish).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Batrachoidaria; Batrachoididae; Thalassophryne.
OX   NCBI_TaxID=289382;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 29-40; 54-67; 104-111;
RP   137-143; 164-180; 184-200; 215-220; 263-270 AND 288-300, FUNCTION, ACTIVITY
RP   REGULATION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY.
RC   TISSUE=Venom, and Venom gland;
RX   PubMed=16054523; DOI=10.1016/j.biochi.2005.03.016;
RA   Magalhaes G.S., Lopes-Ferreira M., Junqueira-de-Azevedo I.L.M.,
RA   Spencer P.J., Araujo M.S., Portaro F.C.V., Ma L., Valente R.H., Juliano L.,
RA   Fox J.W., Ho P.L., Moura-da-Silva A.M.;
RT   "Natterins, a new class of proteins with kininogenase activity
RT   characterized from Thalassophryne nattereri fish venom.";
RL   Biochimie 87:687-699(2005).
CC   -!- FUNCTION: Shows nociceptive, edema-inducing and kininogenase activity
CC       with release of kallidin from low molecular weight kininogen. The
CC       cleavage occurs at Met-Lys bonds. {ECO:0000269|PubMed:16054523}.
CC   -!- ACTIVITY REGULATION: Inhibited by tissue-kallikrein inhibitor TKI and
CC       trasylol. Plasma kallikrein inhibitor PKSI527 and classical inhibitors
CC       of serine-, metallo-, thiol- or aspartate-peptidases evokes a minor
CC       inhibition of the peptide digestion. {ECO:0000269|PubMed:16054523}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:16054523}.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC       {ECO:0000269|PubMed:16054523}.
CC   -!- PTM: Contains 4 disulfide bonds. {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the natterin family. {ECO:0000305}.
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DR   EMBL; AY707909; AAU11823.1; -; mRNA.
DR   AlphaFoldDB; Q66S21; -.
DR   SMR; Q66S21; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR   GO; GO:0090729; F:toxin activity; IEA:UniProtKB-KW.
DR   InterPro; IPR006616; DM9_repeat.
DR   InterPro; IPR024518; DUF3421.
DR   Pfam; PF11901; DUF3421; 1.
DR   SMART; SM00696; DM9; 1.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; Disulfide bond; Hydrolase; Secreted; Signal;
KW   Toxin.
FT   SIGNAL          1..18
FT                   /evidence="ECO:0000255"
FT   PROPEP          19..27
FT                   /evidence="ECO:0000305|PubMed:16054523"
FT                   /id="PRO_0000285218"
FT   CHAIN           29..376
FT                   /note="Natterin-2"
FT                   /evidence="ECO:0000305|PubMed:16054523"
FT                   /id="PRO_5000093996"
SQ   SEQUENCE   376 AA;  41327 MW;  9D64F34CB55F51C2 CRC64;
     MNLSVLLVTL LLLSWTSAEK DLKVRVARST NDETNLHWVK CGGSVPDGAV SIRNTYVSPA
     RTEYVCKCFC QAGYYSTKDS KCHYPYGTKE MATSTNCYIL VNRDNFELLE WKDGYAGSVP
     DNAVSTCKTN KIYVGKGAYG LGKIEPANHC LYYVWDGAET WTKTYQALTM NKDVIEQAMK
     DVKYQTEGVT VIKGKPEVMR RSTVNNQHCK EVTKTVTLTK DISTDERWDV TNSVTFGVTT
     TVTAGIPDVS SASLEISMQA TMDFAHGASK TETQSYMVTV SVPVPPKQSC TVSMVAQVNK
     ADIPFTATLI RTYRGGKKTQ TTTKGVYRTI QVAETHADVE QCTIIGDAKD CPNASSTITT
     LRPKLKSKKP AKPAGK