ID 3NO25_NAJNA Reviewed; 62 AA. AC P29179; DT 01-DEC-1992, integrated into UniProtKB/Swiss-Prot. DT 01-DEC-1992, sequence version 1. DT 18-SEP-2019, entry version 80. DE RecName: Full=Weak neurotoxin 5 {ECO:0000305|PubMed:2060629}; OS Naja naja (Indian cobra). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; OC Toxicofera; Serpentes; Colubroidea; Elapidae; Elapinae; Naja. OX NCBI_TaxID=35670; RN [1] RP PROTEIN SEQUENCE, AND SUBCELLULAR LOCATION. RC TISSUE=Venom; RX PubMed=2060629; DOI=10.1016/0014-5793(91)80764-t; RA Shafqat J., Siddiqi A.R., Zaidi Z.H., Joernvall H.; RT "Extensive multiplicity of the miscellaneous type of neurotoxins from RT the venom of the cobra Naja naja naja and structural characterization RT of major components."; RL FEBS Lett. 284:70-72(1991). RN [2] RP 3D-STRUCTURE MODELING. RA Bano A., Salim A., Abbasi A., Zaidi Z.H.; RT "3d-structure of a complex of alpha short chain neurotoxin and human RT acetylcholine receptor peptide by homology modeling."; RL Submitted (MAY-2002) to the PDB data bank. CC -!- FUNCTION: Binds with low affinity to muscular (alpha-1-beta-1- CC delta-epsilon/CHRNA1-CHRNB1-CHRND-CHRNE) and very low affinity to CC neuronal (alpha-7/CHRNA7) nicotinic acetylcholine receptor CC (nAChR). {ECO:0000250|UniProtKB:O42255}. CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:2060629}. CC -!- TISSUE SPECIFICITY: Expressed by the venom gland. CC {ECO:0000305|PubMed:2060629}. CC -!- SIMILARITY: Belongs to the snake three-finger toxin family. Non- CC conventional subfamily. Orphan group II sub-subfamily. CC {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 PIR; S15871; S15871. DR PDB; 1LN7; Model; -; A=1-62. DR PDB; 1XVZ; Model; -; A=1-62. DR PDBsum; 1LN7; -. DR PDBsum; 1XVZ; -. DR SMR; P29179; -. DR PRIDE; P29179; -. DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell. DR GO; GO:0090729; F:toxin activity; IEA:UniProtKB-KW. DR CDD; cd00206; snake_toxin; 1. DR InterPro; IPR003571; Snake_3FTx. DR InterPro; IPR018354; Snake_toxin_con_site. DR InterPro; IPR035076; Toxin/TOLIP. DR Pfam; PF00087; Toxin_TOLIP; 1. DR PROSITE; PS00272; SNAKE_TOXIN; 1. PE 1: Evidence at protein level; KW 3D-structure; Direct protein sequencing; Disulfide bond; Secreted; KW Toxin. FT CHAIN 1 62 Weak neurotoxin 5. FT {ECO:0000269|PubMed:2060629}. FT /FTId=PRO_0000093637. FT DISULFID 3 24 {ECO:0000250|UniProtKB:Q8AY51}. FT DISULFID 6 11 {ECO:0000250|UniProtKB:Q8AY51}. FT DISULFID 17 40 {ECO:0000250|UniProtKB:Q8AY51}. FT DISULFID 44 54 {ECO:0000250|UniProtKB:Q8AY51}. FT DISULFID 55 60 {ECO:0000250|UniProtKB:Q8AY51}. SQ SEQUENCE 62 AA; 6943 MW; 2BA3EB6FDF2BDCF9 CRC64; LTCLICPEKY CNKVHTCLNG ENICFKRFNR ILGKRYDLGC AATCPTVKTG IVQCCSTDKC NH //