ID   VNHP_HELSC              Reviewed;         178 AA.
AC   C6EVG7;
DT   23-MAR-2010, integrated into UniProtKB/Swiss-Prot.
DT   01-SEP-2009, sequence version 1.
DT   25-MAY-2022, entry version 28.
DE   RecName: Full=Natriuretic and helokinestatin peptides {ECO:0000303|PubMed:19837656};
DE   Contains:
DE     RecName: Full=Helokinestatin-1 {ECO:0000303|PubMed:19837656};
DE              Short=HKS-1 {ECO:0000303|PubMed:19837656};
DE   Contains:
DE     RecName: Full=Helokinestatin-2 {ECO:0000303|PubMed:19837656};
DE              Short=HKS-2 {ECO:0000303|PubMed:19837656};
DE   Contains:
DE     RecName: Full=Helokinestatin-3 {ECO:0000303|PubMed:19837656};
DE              Short=HKS-3 {ECO:0000303|PubMed:19837656};
DE   Contains:
DE     RecName: Full=Helokinestatin-4 {ECO:0000303|PubMed:19837656};
DE              Short=HKS-4 {ECO:0000303|PubMed:19837656};
DE   Contains:
DE     RecName: Full=Natriuretic peptide {ECO:0000303|PubMed:19837656};
DE   Flags: Precursor;
OS   Heloderma suspectum cinctum (Banded Gila monster).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC   Anguimorpha; Neoanguimorpha; Helodermatidae; Heloderma.
OX   NCBI_TaxID=537493;
RN   [1] {ECO:0000305, ECO:0000312|EMBL:ACE95067.1}
RP   NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 59-68; 74-84; 90-102;
RP   113-122 AND 147-178, FUNCTION, SUBCELLULAR LOCATION, AND TISSUE
RP   SPECIFICITY.
RC   TISSUE=Venom {ECO:0000269|PubMed:19837656}, and
RC   Venom gland {ECO:0000312|EMBL:ACE95067.1};
RX   PubMed=19837656; DOI=10.1093/molbev/msp251;
RA   Fry B.G., Roelants K., Winter K., Hodgson W.C., Griesman L., Kwok H.F.,
RA   Scanlon D., Karas J., Shaw C., Wong L., Norman J.A.;
RT   "Novel venom proteins produced by differential domain-expression strategies
RT   in beaded lizards and gila monsters (genus Heloderma).";
RL   Mol. Biol. Evol. 27:395-407(2010).
CC   -!- FUNCTION: Helokinestatin antagonizes the vasodilatory actions of
CC       bradykinin at the B2 bradykinin receptor (BDKRB2), with helokinestatin-
CC       1 being the most potent antagonist. {ECO:0000269|PubMed:19837656}.
CC   -!- FUNCTION: Natriuretic peptide exhibits vasoactive properties and
CC       induces hypotension, possibly by binding to natriuretic peptide
CC       receptor NPR1. {ECO:0000269|PubMed:19837656}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:19837656}.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC       {ECO:0000269|PubMed:19837656}.
CC   -!- SIMILARITY: In the C-terminal section; belongs to the natriuretic
CC       peptide family. {ECO:0000255}.
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DR   EMBL; EU790965; ACE95067.1; -; mRNA.
DR   AlphaFoldDB; C6EVG7; -.
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   InterPro; IPR000663; Natr_peptide.
DR   InterPro; IPR030480; Natr_peptide_CS.
DR   InterPro; IPR002408; Natriuretic_peptide_brain.
DR   Pfam; PF00212; ANP; 1.
DR   PRINTS; PR00712; BNATPEPTIDE.
DR   SMART; SM00183; NAT_PEP; 1.
DR   PROSITE; PS00263; NATRIURETIC_PEPTIDE; 1.
PE   1: Evidence at protein level;
KW   Bradykinin receptor impairing toxin; Direct protein sequencing;
KW   Disulfide bond; G-protein coupled receptor impairing toxin;
KW   Hypotensive agent; Secreted; Signal; Toxin; Vasoactive.
FT   SIGNAL          1..25
FT                   /evidence="ECO:0000255"
FT   PROPEP          26..58
FT                   /evidence="ECO:0000269|PubMed:19837656"
FT                   /id="PRO_0000392454"
FT   PEPTIDE         59..68
FT                   /note="Helokinestatin-1"
FT                   /evidence="ECO:0000269|PubMed:19837656"
FT                   /id="PRO_0000392455"
FT   PROPEP          69..73
FT                   /evidence="ECO:0000269|PubMed:19837656"
FT                   /id="PRO_0000392456"
FT   PEPTIDE         74..84
FT                   /note="Helokinestatin-2"
FT                   /evidence="ECO:0000269|PubMed:19837656"
FT                   /id="PRO_0000392457"
FT   PROPEP          85..89
FT                   /evidence="ECO:0000269|PubMed:19837656"
FT                   /id="PRO_0000392458"
FT   PEPTIDE         90..102
FT                   /note="Helokinestatin-3"
FT                   /evidence="ECO:0000269|PubMed:19837656"
FT                   /id="PRO_0000392459"
FT   PROPEP          103..112
FT                   /evidence="ECO:0000269|PubMed:19837656"
FT                   /id="PRO_0000392460"
FT   PEPTIDE         113..122
FT                   /note="Helokinestatin-4"
FT                   /evidence="ECO:0000269|PubMed:19837656"
FT                   /id="PRO_0000392461"
FT   PROPEP          123..146
FT                   /evidence="ECO:0000269|PubMed:19837656"
FT                   /id="PRO_0000392462"
FT   PEPTIDE         147..178
FT                   /note="Natriuretic peptide"
FT                   /evidence="ECO:0000269|PubMed:19837656"
FT                   /id="PRO_0000392463"
FT   REGION          69..107
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          135..155
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   DISULFID        153..169
FT                   /evidence="ECO:0000250|UniProtKB:P83224"
SQ   SEQUENCE   178 AA;  19672 MW;  2B0F1F9895FBA88F CRC64;
     MNPRLACSTW LPLLLVLFTL DQGRANPVER GQEYRSLSKR FDDDSTELIL EPRASEENGP
     PYQPLVPRAS DENVPPAYVP LVPRASDENV PPPPLQMPLI PRASEQKGPP FNPPPFVDYE
     PRAANENALR KLIKRSFERS PGRNKRLSPG DGCFGQKIDR IGAVSGMGCN SVSSQGKK