| Entry information | 
|---|
 | Entry name | DNP_DENAN | 
 | Primary accession | P28374 | 
 | integrated into UniProtKB/Swiss-Prot | 01 December 1992 | 
 | sequence version 1 | 01 December 1992 | 
 | entry version 46 | 19 January 2010 | 
 | Name and origin of the protein | 
|---|
 | Protein name | Natriuretic peptide | 
 | DNP | 
 | From | Dendroaspis angusticeps (Eastern green mamba) (Taxon ID: 8618) | 
 | Taxonomy | Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Lepidosauria; Squamata; Scleroglossa; Serpentes; Colubroidea; Elapidae; Elapinae; Dendroaspis | 
 | Keywords | Direct protein sequencing; Disulfide bond; Ionic channel inhibitor; Potassium channel inhibitor; Secreted; Toxin; Vasoactive | 
 | References | 
|---|
 | 1 | Schweitz H., Vigne P., Moinier D., Frelin C., Lazdunski M.;  "A new member of the natriuretic peptide family is present in the venom of the green mamba (Dendroaspis angusticeps)."  J. Biol. Chem. 267:13928-13932(1992) 
 | MEDLINE | 92332489 |  | PubMed | 1352773 |  | Reference Position | protein sequence, function, subcellular location, and tissue specificity. |  | Reference Comment | tissue=venom | 
 | 
 | 2 | Lisy O., Jougasaki M., Heublein D.M., Schirger J.A., Chen H.H., Wennberg P.W., Burnett J.C.;  "Renal actions of synthetic dendroaspis natriuretic peptide."  Kidney Int. 56:502-508(1999) 
 | 
 | 3 | Collins E., Bracamonte M.P., Burnett J.C. Jr., Miller V.M.;  "Mechanism of relaxations to dendroaspis natriuretic peptide in canine coronary arteries."  J. Cardiovasc. Pharmacol. 35:614-618(2000) 
 | 
 | 4 | Lisy O., Lainchbury J.G., Leskinen H., Burnett J.C. Jr.;  "Therapeutic actions of a new synthetic vasoactive and natriuretic peptide, dendroaspis natriuretic peptide, in experimental severe congestive heart failure."  Hypertension 37:1089-1094(2001) 
 | PubMed | 11304508 |  | Reference Position | function. | 
 | 
 | 5 | Chai O.H., Kim E.K., Lee Y.H., Kim J.G., Baik B.J., Lee M.S., Han E.H., Kim H.T., Song C.H.;  "Histamine release induced by dendroaspis natriuretic peptide from rat mast cells."  Peptides 22:1421-1426(2001) 
 | 
 | 6 | Best P.J., Burnett J.C., Wilson S.H., Holmes D.R. Jr., Lerman A.;  "Dendroaspis natriuretic peptide relaxes isolated human arteries and veins."  Cardiovasc. Res. 55:375-384(2002) 
 | 
 | 7 | Chen H.H., Lainchbury J.G., Burnett J.C. Jr.;  "Natriuretic peptide receptors and neutral endopeptidase in mediating the renal actions of a new therapeutic synthetic natriuretic peptide dendroaspis natriuretic peptide."  J. Am. Coll. Cardiol. 40:1186-1191(2002) 
 | 
 | 8 | Singh G., Kuc R.E., Maguire J.J., Fidock M., Davenport A.P.;  "Novel snake venom ligand dendroaspis natriuretic peptide is selective for natriuretic peptide receptor-A in human heart: downregulation of natriuretic peptide receptor-A in heart failure."  Circ. Res. 99:183-190(2006) 
 | 
 | 9 | Johns D.G., Ao Z., Heidrich B.J., Hunsberger G.E., Graham T., Payne L., Elshourbagy N., Lu Q., Aiyar N., Douglas S.A.;  "Dendroaspis natriuretic peptide binds to the natriuretic peptide clearance receptor."  Biochem. Biophys. Res. Commun. 358:145-149(2007) 
 | 
 | 10 | Guo H.-S., Yang Y.-Z., Zou Y., Xu J., Cai Z.-X., Qi Q.-H.;  "Effects of dendroaspis natriuretic peptide on calcium-activated potassium current and its mechanism."  J. Physiol. Sci. 58:1-6(2008) 
 | 
 | Comments | 
|---|
 | function | Exhibits vasodilator, natriuretic and diuretic properties in animal models and human tissues. Acts by stimulating
 cGMP via the natriuretic peptide receptor A (NPR1). Is a poor
 agonist of the atrial natriuretic peptide receptor B (NPR2). Is
 not degradated by neutral endopeptidase (NEP / MME). Binds to
 atrial natriuretic peptide clearance receptor (NPR3 / NPR-C),
 which may be responsible of the removal of DNP from the
 circulation. Increases calcium uptake and induces histamine
 release from rat peritoneal mast cells. Increases calcium-
 activated potassium current in gastric antral circular smooth
 muscle cells by increasing cGMP production and activating inositol
 trisphosphate receptors (IP3Rs). | 
 | subcellular location | Secreted. | 
 | tissue specificity | Expressed by the venom gland. | 
 | similarity | Belongs to the natriuretic peptide family. | 
 | Copyright | 
|---|
 | Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms Distributed under the Creative Commons Attribution-NoDerivs License | 
 | Cross-references | 
|---|
 | PIR | A42974; A42974. | 
 | GO | ; C:extracellular region; IEA:UniProtKB-SubCell. | 
 | ; F:hormone activity; IEA:InterPro. | 
 | ; F:potassium channel inhibitor activity; IEA:UniProtKB-KW. | 
 | ; P:pathogenesis; IEA:UniProtKB-KW. | 
 | ; P:regulation of blood vessel size; IEA:UniProtKB-KW. | 
 | InterPro | IPR000663; Natr_peptide. | 
 | Pfam | PF00212; ANP; 1. | 
 | PROSITE | PS00263; NATRIURETIC_PEPTIDE; 1. | 
 | Features | 
|---|
 | | Key | From | To | Length | Description | 
|---|
 | peptide | 1 | 38 | 38 | Natriuretic peptide. /FTId=PRO_0000045068.
 |  | disulfid | 7 | 23 | 17 | By similarity. | 
 | 
 | Sequence information | 
|---|
 | Length: 38 aa, molecular weight 4193 Da, CRC64 checksum BCAD19AB95B52258 | 
 | EVKYDPCFGH KIDRINHVSN LGCPSLRDPR PNAPSTSA |