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 |