VNP_DENAN
ID VNP_DENAN Reviewed; 38 AA.
AC P28374;
DT 01-DEC-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-1992, sequence version 1.
DT 03-AUG-2022, entry version 75.
DE RecName: Full=Natriuretic peptide DNP;
OS Dendroaspis angusticeps (Eastern green mamba) (Naja angusticeps).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC Serpentes; Colubroidea; Elapidae; Elapinae; Dendroaspis.
OX NCBI_TaxID=8618;
RN [1]
RP PROTEIN SEQUENCE, FUNCTION, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RC TISSUE=Venom;
RX PubMed=1352773; DOI=10.1016/s0021-9258(19)49658-0;
RA Schweitz H., Vigne P., Moinier D., Frelin C., Lazdunski M.;
RT "A new member of the natriuretic peptide family is present in the venom of
RT the green mamba (Dendroaspis angusticeps).";
RL J. Biol. Chem. 267:13928-13932(1992).
RN [2]
RP FUNCTION.
RX PubMed=10432389; DOI=10.1046/j.1523-1755.1999.00573.x;
RA Lisy O., Jougasaki M., Heublein D.M., Schirger J.A., Chen H.H.,
RA Wennberg P.W., Burnett J.C.;
RT "Renal actions of synthetic dendroaspis natriuretic peptide.";
RL Kidney Int. 56:502-508(1999).
RN [3]
RP FUNCTION.
RX PubMed=10774793; DOI=10.1097/00005344-200004000-00015;
RA Collins E., Bracamonte M.P., Burnett J.C. Jr., Miller V.M.;
RT "Mechanism of relaxations to dendroaspis natriuretic peptide in canine
RT coronary arteries.";
RL J. Cardiovasc. Pharmacol. 35:614-618(2000).
RN [4]
RP FUNCTION.
RX PubMed=11304508; DOI=10.1161/01.hyp.37.4.1089;
RA Lisy O., Lainchbury J.G., Leskinen H., Burnett J.C. Jr.;
RT "Therapeutic actions of a new synthetic vasoactive and natriuretic peptide,
RT dendroaspis natriuretic peptide, in experimental severe congestive heart
RT failure.";
RL Hypertension 37:1089-1094(2001).
RN [5]
RP FUNCTION.
RX PubMed=11514023; DOI=10.1016/s0196-9781(01)00483-1;
RA Chai O.H., Kim E.K., Lee Y.H., Kim J.G., Baik B.J., Lee M.S., Han E.H.,
RA Kim H.T., Song C.H.;
RT "Histamine release induced by dendroaspis natriuretic peptide from rat mast
RT cells.";
RL Peptides 22:1421-1426(2001).
RN [6]
RP FUNCTION.
RX PubMed=12123777; DOI=10.1016/s0008-6363(02)00402-9;
RA Best P.J., Burnett J.C., Wilson S.H., Holmes D.R. Jr., Lerman A.;
RT "Dendroaspis natriuretic peptide relaxes isolated human arteries and
RT veins.";
RL Cardiovasc. Res. 55:375-384(2002).
RN [7]
RP DEGRADATION OF DNP.
RX PubMed=12354448; DOI=10.1016/s0735-1097(02)02127-7;
RA Chen H.H., Lainchbury J.G., Burnett J.C. Jr.;
RT "Natriuretic peptide receptors and neutral endopeptidase in mediating the
RT renal actions of a new therapeutic synthetic natriuretic peptide
RT dendroaspis natriuretic peptide.";
RL J. Am. Coll. Cardiol. 40:1186-1191(2002).
RN [8]
RP FUNCTION, AND NPR1 BINDING.
RX PubMed=16778132; DOI=10.1161/01.res.0000232322.06633.d3;
RA Singh G., Kuc R.E., Maguire J.J., Fidock M., Davenport A.P.;
RT "Novel snake venom ligand dendroaspis natriuretic peptide is selective for
RT natriuretic peptide receptor-A in human heart: downregulation of
RT natriuretic peptide receptor-A in heart failure.";
RL Circ. Res. 99:183-190(2006).
RN [9]
RP FUNCTION, AND NPR3 BINDING.
RX PubMed=17475216; DOI=10.1016/j.bbrc.2007.04.079;
RA Johns D.G., Ao Z., Heidrich B.J., Hunsberger G.E., Graham T., Payne L.,
RA Elshourbagy N., Lu Q., Aiyar N., Douglas S.A.;
RT "Dendroaspis natriuretic peptide binds to the natriuretic peptide clearance
RT receptor.";
RL Biochem. Biophys. Res. Commun. 358:145-149(2007).
RN [10]
RP FUNCTION ON POTASSIUM CHANNEL.
RX PubMed=18096107; DOI=10.2170/physiolsci.rp010507;
RA Guo H.-S., Yang Y.-Z., Zou Y., Xu J., Cai Z.-X., Qi Q.-H.;
RT "Effects of dendroaspis natriuretic peptide on calcium-activated potassium
RT current and its mechanism.";
RL J. Physiol. Sci. 58:1-6(2008).
CC -!- FUNCTION: Exhibits vasodilator, natriuretic and diuretic properties in
CC animal models and human tissues. Acts by stimulating cGMP via the
CC natriuretic peptide receptor A (NPR1). Is a poor agonist of the atrial
CC natriuretic peptide receptor B (NPR2). Is not degraded by neutral
CC endopeptidase (NEP/MME). Binds to atrial natriuretic peptide clearance
CC receptor (NPR-C/NPR3), which may be responsible of the removal of DNP
CC from the circulation. Increases calcium uptake and induces histamine
CC release from rat peritoneal mast cells. Increases calcium-activated
CC potassium (KCa) current in gastric antral circular smooth muscle cells
CC by increasing cGMP production and activating inositol trisphosphate
CC receptors (IP3Rs). {ECO:0000269|PubMed:10432389,
CC ECO:0000269|PubMed:10774793, ECO:0000269|PubMed:11304508,
CC ECO:0000269|PubMed:11514023, ECO:0000269|PubMed:12123777,
CC ECO:0000269|PubMed:1352773, ECO:0000269|PubMed:16778132,
CC ECO:0000269|PubMed:17475216, ECO:0000269|PubMed:18096107}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:1352773}.
CC -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC {ECO:0000269|PubMed:1352773}.
CC -!- SIMILARITY: Belongs to the natriuretic peptide family. {ECO:0000305}.
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DR PIR; A42974; A42974.
DR PDB; 7BRI; X-ray; 2.45 A; L=1-38.
DR PDBsum; 7BRI; -.
DR AlphaFoldDB; P28374; -.
DR SMR; P28374; -.
DR PRIDE; P28374; -.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0005179; F:hormone activity; IEA:InterPro.
DR GO; GO:0015459; F:potassium channel regulator activity; IEA:UniProtKB-KW.
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; 1.
DR PROSITE; PS00263; NATRIURETIC_PEPTIDE; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Calcium-activated potassium channel impairing toxin;
KW Direct protein sequencing; Disulfide bond; Hypotensive agent;
KW Ion channel impairing toxin; Potassium channel impairing toxin; Secreted;
KW Toxin; Vasoactive; Vasodilator.
FT PEPTIDE 1..38
FT /note="Natriuretic peptide DNP"
FT /id="PRO_0000045068"
FT REGION 19..38
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 7..23
FT /evidence="ECO:0000250"
FT HELIX 14..17
FT /evidence="ECO:0007829|PDB:7BRI"
SQ SEQUENCE 38 AA; 4193 MW; BCAD19AB95B52258 CRC64;
EVKYDPCFGH KIDRINHVSN LGCPSLRDPR PNAPSTSA
