ID   NATT3_THANI             Reviewed;         364 AA.
AC   Q66S17;
DT   01-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT   11-OCT-2004, sequence version 1.
DT   25-MAY-2022, entry version 70.
DE   RecName: Full=Natterin-3;
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 109-118; 177-189; 193-206;
RP   312-316 AND 342-349, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND
RP   IDENTIFICATION BY 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:0000250|UniProtKB:Q66S25}.
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:0000250|UniProtKB:Q66S25}.
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; AY707910; AAU11824.1; -; mRNA.
DR   AlphaFoldDB; Q66S17; -.
DR   SMR; Q66S17; -.
DR   TCDB; 1.C.4.6.1; the aerolysin channel-forming toxin (aerolysin) family.
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..42
FT                   /evidence="ECO:0000305|PubMed:16054523"
FT                   /id="PRO_0000285219"
FT   CHAIN           43..364
FT                   /note="Natterin-3"
FT                   /evidence="ECO:0000305|PubMed:16054523"
FT                   /id="PRO_5000093997"
SQ   SEQUENCE   364 AA;  39806 MW;  DC36A0DE0DE09022 CRC64;
     MKLSVLVVTL LAVSWTSAQP ETFSIQTKEA NMNPEPANIR VARSSSAQSN LQWNYWDGQG
     AVPDGAVSIW NGEEKRTDYV CSCGCSSGFY STKTGANCHY AYGETEKTCS GFSILVNRDN
     FENLEWKGGS DGSVPKNAVE VCEKVYVGKN KYGLGKVHTK HEALFLPWHG EEHWYKDYEV
     LTVNDDVVKQ ELTQVNYKLD AAHPIKNPPE TLRRSSASNS QCRPITKTVA LEKAIQTEQS
     WDVTSTVTFG VESSITAGIP DIASATVSVS VETSLSVSLG STTTKTTTHT VSVIVTVPPN
     HYCPVTMVAT KYTADIPFTG KMTRTYRNGQ KRTTSITGTY RAIQVGEIRA DVQRCSEIAG
     AKPC