ID   VNP_BUNMU               Reviewed;         210 AA.
AC   P0DMD5;
DT   19-FEB-2014, integrated into UniProtKB/Swiss-Prot.
DT   19-FEB-2014, sequence version 1.
DT   25-MAY-2022, entry version 17.
DE   RecName: Full=Natriuretic peptide BM026;
DE            Short=NP;
DE   Flags: Precursor;
OS   Bungarus multicinctus (Many-banded krait).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC   Serpentes; Colubroidea; Elapidae; Bungarinae; Bungarus.
OX   NCBI_TaxID=8616;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Venom gland;
RX   PubMed=21194499; DOI=10.1186/1471-2164-12-1;
RA   Jiang Y., Li Y., Lee W., Xu X., Zhang Y., Zhao R., Zhang Y., Wang W.;
RT   "Venom gland transcriptomes of two elapid snakes (Bungarus multicinctus and
RT   Naja atra) and evolution of toxin genes.";
RL   BMC Genomics 12:1-1(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   AlphaFoldDB; P0DMD5; -.
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_0000425577"
FT   CHAIN           156..200
FT                   /note="Natriuretic peptide BM026"
FT                   /id="PRO_0000425578"
FT   PROPEP          201..210
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000425579"
FT   REGION          83..99
FT                   /note="Natriuretic peptide domain 1"
FT                   /evidence="ECO:0000250"
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                   /evidence="ECO:0000250"
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