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Natterin-1 (EC 3.4.-.-)

 NATT1_THANI             Reviewed;         355 AA.
Q66S25;
01-MAY-2007, integrated into UniProtKB/Swiss-Prot.
11-OCT-2004, sequence version 1.
23-MAY-2018, entry version 45.
RecName: Full=Natterin-1;
EC=3.4.-.-;
Flags: Precursor;
Thalassophryne nattereri (Copper Joe toadfish).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
Batrachoidaria; Batrachoididae; Thalassophryne.
NCBI_TaxID=289382;
[1]
NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 29-40; 54-67; 89-111;
136-179; 214-226; 262-269 AND 287-310, FUNCTION, ENZYME REGULATION,
SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND IDENTIFICATION BY MASS
SPECTROMETRY.
TISSUE=Venom, and Venom gland;
PubMed=16054523; DOI=10.1016/j.biochi.2005.03.016;
Magalhaes G.S., Lopes-Ferreira M., Junqueira-de-Azevedo I.L.M.,
Spencer P.J., Araujo M.S., Portaro F.C.V., Ma L., Valente R.H.,
Juliano L., Fox J.W., Ho P.L., Moura-da-Silva A.M.;
"Natterins, a new class of proteins with kininogenase activity
characterized from Thalassophryne nattereri fish venom.";
Biochimie 87:687-699(2005).
-!- FUNCTION: Shows nociceptive, edema-inducing and kininogenase
activity with release of kallidin from low molecular weight
kininogen. The cleavage occurs at Met-Lys bonds.
{ECO:0000269|PubMed:16054523}.
-!- ENZYME REGULATION: Inhibited by tissue-kallikrein inhibitor TKI
and trasylol. Plasma kallikrein inhibitor PKSI527 and classical
inhibitors of serine-, metallo-, thiol- or aspartate-peptidases
evokes a minor inhibition of the peptide digestion.
{ECO:0000269|PubMed:16054523}.
-!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:16054523}.
-!- TISSUE SPECIFICITY: Expressed by the venom gland.
{ECO:0000269|PubMed:16054523}.
-!- PTM: Contains four disulfide bonds. {ECO:0000305}.
-!- SIMILARITY: Belongs to the natterin family. {ECO:0000305}.
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EMBL; AY707908; AAU11822.1; -; mRNA.
ProteinModelPortal; Q66S25; -.
SMR; Q66S25; -.
PRIDE; Q66S25; -.
HOVERGEN; HBG097478; -.
GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
GO; GO:0090729; F:toxin activity; IEA:UniProtKB-KW.
InterPro; IPR006616; DM9_repeat.
InterPro; IPR024518; DUF3421.
Pfam; PF11901; DUF3421; 1.
SMART; SM00696; DM9; 1.
1: Evidence at protein level;
Direct protein sequencing; Disulfide bond; Hydrolase; Secreted;
Signal; Toxin.
SIGNAL 1 18 {ECO:0000255}.
PROPEP 19 27
/FTId=PRO_0000285217.
CHAIN 29 355 Natterin-1.
/FTId=PRO_5000093994.
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


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