ID   VNP_OPHHA               Reviewed;         210 AA.
AC   D9IX98;
DT   11-JAN-2011, integrated into UniProtKB/Swiss-Prot.
DT   05-OCT-2010, sequence version 1.
DT   25-MAY-2022, entry version 23.
DE   RecName: Full=Natriuretic peptide Oh-NP;
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 [MRNA].
RC   TISSUE=Venom gland;
RX   PubMed=21334357; DOI=10.1016/j.toxicon.2011.02.016;
RA   Lei W., Zhang Y., Yu G., Jiang P., He Y., Lee W., Zhang Y.;
RT   "Cloning and sequence analysis of an Ophiophagus hannah cDNA encoding a
RT   precursor of two natriuretic peptide domains.";
RL   Toxicon 57:811-816(2011).
CC   -!- FUNCTION: Snake venom natriuretic peptide that exhibits hypotensive and
CC       vasodepressor activity. Acts by activating natriuretic receptors (NPR1
CC       and/or NPR2 and/or NPR3) (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC   -!- SIMILARITY: Belongs to the natriuretic peptide family. {ECO:0000305}.
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DR   EMBL; HM217216; ADK12002.1; -; mRNA.
DR   AlphaFoldDB; D9IX98; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0005179; F:hormone activity; IEA:InterPro.
DR   GO; GO:0090729; F:toxin activity; IEA:UniProtKB-KW.
DR   GO; GO:0008217; P:regulation of blood pressure; IEA:UniProtKB-KW.
DR   GO; GO:0042311; P:vasodilation; IEA:UniProtKB-KW.
DR   InterPro; IPR000663; Natr_peptide.
DR   InterPro; IPR030480; Natr_peptide_CS.
DR   Pfam; PF00212; ANP; 2.
DR   SMART; SM00183; NAT_PEP; 2.
DR   PROSITE; PS00263; NATRIURETIC_PEPTIDE; 1.
PE   2: Evidence at transcript level;
KW   Disulfide bond; Hypotensive agent; Secreted; Signal; Toxin; Vasoactive;
KW   Vasodilator.
FT   SIGNAL          1..26
FT                   /evidence="ECO:0000255"
FT   PROPEP          27..155
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000403805"
FT   CHAIN           156..200
FT                   /note="Natriuretic peptide Oh-NP"
FT                   /id="PRO_0000403806"
FT   PROPEP          201..210
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000403807"
FT   REGION          83..99
FT                   /note="Natriuretic peptide domain 1"
FT   REGION          122..210
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          166..182
FT                   /note="Natriuretic peptide domain 2"
FT   COMPBIAS        154..180
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   DISULFID        83..99
FT                   /evidence="ECO:0000250"
FT   DISULFID        166..182
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   210 AA;  21600 MW;  4C1095FC5E983B9E CRC64;
     MVGPSRLAGG GLLLLLLALL PVALDGKPAP PSQALHKAPA GGTKASQIMQ VLLPESKKSW
     AARDRMVGPY NPAGGGGGHP SSCFGHKIDR ISHSSGMGCG RRPNAPAGGT KASQIMQVLL
     PESKKSRAAR DRMVGPDNRA GGGGGGGGGD SSRQQELAKK DQHNNCFGRR IDRISHSTDL
     GCRRRPNPPP APTAAPLAVA QFNSKSSQVA