ID   NATTP_THANI             Reviewed;          71 AA.
AC   Q66S08;
DT   01-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT   11-OCT-2004, sequence version 1.
DT   25-MAY-2022, entry version 31.
DE   RecName: Full=Natterin-P;
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   -!- SIMILARITY: Belongs to the natterin family. {ECO:0000305}.
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DR   EMBL; AY707912; AAU11826.1; -; mRNA.
DR   AlphaFoldDB; Q66S08; -.
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.
PE   3: Inferred from homology;
KW   Disulfide bond; Hydrolase; Secreted; Signal; Toxin.
FT   SIGNAL          1..18
FT                   /evidence="ECO:0000255"
FT   PROPEP          19..45
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000285221"
FT   PEPTIDE         46..71
FT                   /note="Natterin-P"
FT                   /id="PRO_5000093999"
FT   REGION          22..54
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        28..45
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   DISULFID        62..71
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   71 AA;  7890 MW;  4FDF7A527D6C541F CRC64;
     MKLLVLLVTL LVLSWTSAED LGDQEILENN EDNNHESELG EPAAQHTDDE TSQLGQALIP
     RCRKMPGVKM C