ID   NATT1_THANI             Reviewed;         355 AA.
AC   Q66S25;
DT   01-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT   11-OCT-2004, sequence version 1.
DT   25-MAY-2022, entry version 52.
DE   RecName: Full=Natterin-1;
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; 89-111;
RP   136-179; 214-226; 262-269 AND 287-310, FUNCTION, ACTIVITY REGULATION,
RP   SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND IDENTIFICATION BY MASS
RP   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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AY707908; AAU11822.1; -; mRNA.
DR   AlphaFoldDB; Q66S25; -.
DR   SMR; Q66S25; -.
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_0000285217"
FT   CHAIN           29..355
FT                   /note="Natterin-1"
FT                   /evidence="ECO:0000305|PubMed:16054523"
FT                   /id="PRO_5000093994"
SQ   SEQUENCE   355 AA;  38994 MW;  CF4AFB2F0F328028 CRC64;
     MIPSVLLVTL LLLSWTSAEK DLKVRVARST NDETNLHWVK CGGSVPDGAV SIQNTYVSPA
     RTEYVCKSNC EAGYYSTKDS KCHYPFGRVE QTTSVCEILV NRDNFELLEW KEGYAGSLPA
     NAVSTCKTNR IYVGKGAYGL GKIEPAHHCL YYGWNGAETW TKTYQALTVN KDVIEQTMKD
     VKYQTEGVTV IQGKPEVMRK STVNNKQCKE VTKTVTLSKD ISTEERWDVT NSVTFGVTTT
     VTAGIPDVAS ASLAVSMEAR RDFAHGASKT ESQSYMVTVS VPVPPKQSCT VSMVAQVNKA
     DVPFTATLIR TYRGGKKTQT TTKGVYRTTQ VAETHADVEQ CTIIGDEKDC PKASK