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Bradykinin-potentiating and C-type natriuretic peptides (BPP-CNP) [Cleaved into: Bradykinin-potentiating peptide Tg1 (BPP); C-type natriuretic peptide (CNP)]

 BNP_TRIGA               Reviewed;         210 AA.
P0C7P6;
01-JUL-2008, integrated into UniProtKB/Swiss-Prot.
01-JUL-2008, sequence version 1.
22-NOV-2017, entry version 26.
RecName: Full=Bradykinin-potentiating and C-type natriuretic peptides;
AltName: Full=BPP-CNP;
Contains:
RecName: Full=Bradykinin-potentiating peptide Tg1;
Short=BPP;
Contains:
RecName: Full=C-type natriuretic peptide;
Short=CNP;
Flags: Precursor;
Trimeresurus gramineus (Bamboo pit viper) (Indian green tree viper).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata;
Toxicofera; Serpentes; Colubroidea; Viperidae; Crotalinae;
Trimeresurus.
NCBI_TaxID=8767;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Venom gland;
PubMed=10604536; DOI=10.1016/S0162-3109(99)00119-8;
Higuchi S., Murayama N., Saguchi K., Ohi H., Fujita Y.,
de Camargo A.C.M., Ogawa T., Deshimaru M., Ohno M.;
"Bradykinin-potentiating peptides and C-type natriuretic peptides from
snake venom.";
Immunopharmacology 44:129-135(1999).
[2]
SYNTHESIS OF 27-38, AND FUNCTION.
PubMed=17714693; DOI=10.1016/j.bcp.2007.07.014;
Gomes C.L., Konno K., Conceicao I.M., Ianzer D., Yamanouye N.,
Prezoto B.C., Assakura M.T., Radis-Baptista G., Yamane T.,
Santos R.A., de Camargo A.C.M., Hayashi M.A.F.;
"Identification of novel bradykinin-potentiating peptides (BPPs) in
the venom gland of a rattlesnake allowed the evaluation of the
structure-function relationship of BPPs.";
Biochem. Pharmacol. 74:1350-1360(2007).
-!- FUNCTION: Bradykinin-potentiating peptide both inhibits the
activity of the angiotensin-converting enzyme (ACE) and enhances
the action of bradykinin by inhibiting the peptidases that
inactivate it. It acts as an indirect hypotensive agent (By
similarity). Tg1 does not show bradykinin-potentiating effects.
{ECO:0000250, ECO:0000269|PubMed:17714693}.
-!- FUNCTION: Snake venom natriuretic peptide that exhibits
hypotensive and vasodepressor activity. Acts by activating
natriuretic receptors (NPR1 and/or NPR2 and/or NPR3) (By
similarity). {ECO:0000250}.
-!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
-!- TISSUE SPECIFICITY: Expressed by the venom gland.
-!- SIMILARITY: In the N-terminal section; belongs to the bradykinin-
potentiating peptide family. {ECO:0000305}.
-!- SIMILARITY: In the C-terminal section; belongs to the natriuretic
peptide family. {ECO:0000305}.
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SMR; P0C7P6; -.
HOVERGEN; HBG073115; -.
GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
GO; GO:0005179; F:hormone activity; IEA:InterPro.
GO; GO:0008191; F:metalloendopeptidase inhibitor activity; IEA:UniProtKB-KW.
GO; GO:0090729; F:toxin activity; IEA:UniProtKB-KW.
GO; GO:0008217; P:regulation of blood pressure; IEA:UniProtKB-KW.
GO; GO:0042311; P:vasodilation; IEA:UniProtKB-KW.
InterPro; IPR000663; Natr_peptide.
InterPro; IPR030480; Natr_peptide_CS.
Pfam; PF00212; ANP; 1.
SMART; SM00183; NAT_PEP; 1.
PROSITE; PS00263; NATRIURETIC_PEPTIDE; 1.
2: Evidence at transcript level;
Cleavage on pair of basic residues; Disulfide bond; Hypotensive agent;
Metalloenzyme inhibitor; Metalloprotease inhibitor;
Protease inhibitor; Pyrrolidone carboxylic acid; Secreted; Signal;
Toxin; Vasoactive; Vasodilator.
SIGNAL 1 23 {ECO:0000255}.
PROPEP 24 26 {ECO:0000250}.
/FTId=PRO_0000342449.
PEPTIDE 27 38 Bradykinin-potentiating peptide Tg1.
{ECO:0000250}.
/FTId=PRO_0000342450.
PROPEP 39 186 {ECO:0000250}.
/FTId=PRO_0000342451.
PEPTIDE 189 210 C-type natriuretic peptide.
{ECO:0000250}.
/FTId=PRO_0000342452.
COMPBIAS 25 78 Pro-rich.
COMPBIAS 170 178 Poly-Gly.
MOD_RES 27 27 Pyrrolidone carboxylic acid.
{ECO:0000250}.
DISULFID 194 210 {ECO:0000250}.
SEQUENCE 210 AA; 21905 MW; D90F280019954650 CRC64;
MFVSRLAASG LLLLALLALS LDGKPVQEKP GRSPPISPLL VPPPPPPPHW PPPHHIPPLS
VQKFPPGWKP THPHHIPPLE VQQWSQGGPR SELVQPHESP AGGTTAFREE LSLGPEAASG
PAAPQRLPKR KGASATSAAS RSMRDLRADG KQARQKWGRM VQPDHHAAPG GGGGGGGGAR
RLKGLAKKAV GKGCFGLPLD RIGSMSGMGC


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