ID   NATT4_THANI             Reviewed;         387 AA.
AC   Q66S13;
DT   01-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT   11-OCT-2004, sequence version 1.
DT   25-MAY-2022, entry version 54.
DE   RecName: Full=Natterin-4;
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].
RC   TISSUE=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:0000305|PubMed:16054523}.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC       {ECO:0000305|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; AY707911; AAU11825.1; -; mRNA.
DR   AlphaFoldDB; Q66S13; -.
DR   SMR; Q66S13; -.
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   2: Evidence at transcript level;
KW   Disulfide bond; Hydrolase; Secreted; Signal; Toxin.
FT   SIGNAL          1..18
FT                   /evidence="ECO:0000255"
FT   PROPEP          19..46
FT                   /evidence="ECO:0000305|PubMed:16054523"
FT                   /id="PRO_0000285220"
FT   CHAIN           48..387
FT                   /note="Natterin-4"
FT                   /evidence="ECO:0000305|PubMed:16054523"
FT                   /id="PRO_5000093998"
FT   REGION          31..57
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   387 AA;  43357 MW;  22F5ABE818494EDF CRC64;
     MKLLVLLVTL LVLSWTSAED VGDQEILQQH NEDNNHKSEL GEAAPQRTDN ETSQLGQETP
     TIRVARAYEF SSKSNLEWVR WNGHIPSNAV KISNTYVGRE DYVCRVGCEA GYYTPKKGPS
     CFYPYGFTEQ HSKMFHILVN RDNFEILEWK WKTGGEVPEN AVKACRDLYV AKNKYGLGKL
     HQSHHVFYLP WKGTEYKYNE YYVLNVNMDV VEQKITNVRY NMKGVEVHKD KPETLRSTSV
     KNYQCREATK QVTLEKSTET SQSWDVSNSI TLGVSTEVSA GIPNIADVSV AVSAETSVEI
     SHGTSKTEST SHSLSVSATI PPNSSCSITM EGCTFKANIP FTGRLTRKYS NGKVTSSSVK
     GIYKKVQVGE IQAVLHRCDK IADAKPC