ID   VESP_OPHHA              Reviewed;         190 AA.
AC   P83234; Q5QJD7;
DT   27-JUN-2003, integrated into UniProtKB/Swiss-Prot.
DT   17-OCT-2006, sequence version 2.
DT   25-MAY-2022, entry version 69.
DE   RecName: Full=Ohanin {ECO:0000303|PubMed:15668253, ECO:0000303|PubMed:16472942};
DE   Flags: Precursor;
OS   Ophiophagus hannah (King cobra) (Naja hannah).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC   Serpentes; Colubroidea; Elapidae; Elapinae; Ophiophagus.
OX   NCBI_TaxID=8665;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
RC   TISSUE=Liver, and Venom gland;
RX   PubMed=16472942; DOI=10.1016/j.gene.2005.12.002;
RA   Pung Y.F., Kumar S.V., Rajagopalan N., Fry B.G., Kumar P.P., Kini R.M.;
RT   "Ohanin, a novel protein from king cobra venom: its cDNA and genomic
RT   organization.";
RL   Gene 371:246-256(2006).
RN   [2]
RP   PROTEIN SEQUENCE OF 21-127, SYNTHESIS OF 21-127, FUNCTION, SUBCELLULAR
RP   LOCATION, AND MASS SPECTROMETRY.
RC   TISSUE=Venom;
RX   PubMed=15668253; DOI=10.1074/jbc.m414137200;
RA   Pung Y.F., Wong P.T.H., Kumar P.P., Hodgson W.C., Kini R.M.;
RT   "Ohanin, a novel protein from king cobra venom, induces hypolocomotion and
RT   hyperalgesia in mice.";
RL   J. Biol. Chem. 280:13137-13147(2005).
CC   -!- FUNCTION: Neurotoxin that produces dose-dependent hypolocomotion and
CC       hyperalgesia in mice. May directly act on the central nervous system,
CC       as it is 6500-fold more potent when administered
CC       intracerebroventricularly than intraperitoneal.
CC       {ECO:0000269|PubMed:15668253}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:15668253,
CC       ECO:0000305}.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC       {ECO:0000305|PubMed:15668253}.
CC   -!- MASS SPECTROMETRY: Mass=11951.47; Mass_error=0.67; Method=Electrospray;
CC       Evidence={ECO:0000269|PubMed:15668253};
CC   -!- SIMILARITY: Belongs to the ohanin/vespryn family. {ECO:0000305}.
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DR   EMBL; AY351433; AAR07992.2; -; mRNA.
DR   EMBL; DQ103590; AAZ15707.1; -; Genomic_DNA.
DR   AlphaFoldDB; P83234; -.
DR   SMR; P83234; -.
DR   TopDownProteomics; P83234; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0090729; F:toxin activity; IEA:UniProtKB-KW.
DR   Gene3D; 2.60.120.920; -; 1.
DR   InterPro; IPR001870; B30.2/SPRY.
DR   InterPro; IPR043136; B30.2/SPRY_sf.
DR   InterPro; IPR003879; Butyrophylin_SPRY.
DR   InterPro; IPR013320; ConA-like_dom_sf.
DR   InterPro; IPR006574; PRY.
DR   InterPro; IPR003877; SPRY_dom.
DR   Pfam; PF13765; PRY; 1.
DR   Pfam; PF00622; SPRY; 1.
DR   PRINTS; PR01407; BUTYPHLNCDUF.
DR   SMART; SM00589; PRY; 1.
DR   SUPFAM; SSF49899; SSF49899; 1.
DR   PROSITE; PS50188; B302_SPRY; 1.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; Neurotoxin; Secreted; Signal; Toxin.
FT   SIGNAL          1..20
FT                   /evidence="ECO:0000269|PubMed:15668253"
FT   CHAIN           21..127
FT                   /note="Ohanin"
FT                   /id="PRO_0000058036"
FT   PROPEP          128..190
FT                   /id="PRO_0000253029"
FT   DOMAIN          21..127
FT                   /note="B30.2/SPRY"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00548"
SQ   SEQUENCE   190 AA;  21174 MW;  55FDAADD714AE2BA CRC64;
     MLLFTLCFFA DQENGGKALA SPPGNWQKAD VTFDSNTAFE SLVVSPDKKT VENVGVPKGV
     PDSPERFSSS PCVLGSPGFR SGKHFFEVKY GTQREWAVGL AGKSVKRKGY LRLVPEERIW
     QKGLWWLRRL ETDSDKLQKG SGKIIVFLDY DEGKVIFDLD GEVTTIQANF NGEEVVPFYY
     IGARVSLANL