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Bradykinin-potentiating and C-type natriuretic peptides (BPP-CNP) [Cleaved into: Bradykinin-potentiating peptide Tf1; Bradykinin-potentiating peptide Tf2; Bradykinin-potentiating peptide Tf3; C-type natriuretic peptide Tf-CNP; C-type natriuretic peptide Tf-CNP(3-22); C-type natriuretic peptide Tf-CNP(6-22)]

 BNP_PROFL               Reviewed;         193 AA.
P0C7P5;
01-JUL-2008, integrated into UniProtKB/Swiss-Prot.
01-JUL-2008, sequence version 1.
10-MAY-2017, entry version 27.
RecName: Full=Bradykinin-potentiating and C-type natriuretic peptides;
AltName: Full=BPP-CNP;
Contains:
RecName: Full=Bradykinin-potentiating peptide Tf1;
Contains:
RecName: Full=Bradykinin-potentiating peptide Tf2;
Contains:
RecName: Full=Bradykinin-potentiating peptide Tf3;
Contains:
RecName: Full=C-type natriuretic peptide Tf-CNP;
Contains:
RecName: Full=C-type natriuretic peptide Tf-CNP(3-22);
Contains:
RecName: Full=C-type natriuretic peptide Tf-CNP(6-22);
Flags: Precursor;
Protobothrops flavoviridis (Habu) (Trimeresurus flavoviridis).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata;
Toxicofera; Serpentes; Colubroidea; Viperidae; Crotalinae;
Protobothrops.
NCBI_TaxID=88087;
[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]
PROTEIN SEQUENCE OF 174-193 (TF-CNP(3-22) AND TF-CNP(6-22)), AND
SYNTHESIS OF TF-CNP.
TISSUE=Venom;
PubMed=10876042; DOI=10.1016/S0196-9781(00)00203-5;
Michel G.H., Murayama N., Sada T., Nozaki M., Saguchi K., Ohi H.,
Fujita Y., Koike H., Higuchi S.;
"Two N-terminally truncated forms of C-type natriuretic peptide from
habu snake venom.";
Peptides 21:609-615(2000).
[3]
SYNTHESIS OF 28-39 AND 44-57, 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). Neither synthetic Tf1, nor synthetic Tf2 show
bradykinin-potentiating effects. {ECO:0000250,
ECO:0000269|PubMed:17714693}.
-!- FUNCTION: C-type natriuretic peptide Tf-CNP: has a vasorelaxant
activity in rat aortic strips and a diuretic potency in
anesthetized rats. {ECO:0000269|PubMed:17714693}.
-!- FUNCTION: C-type natriuretic peptide Tf-CNP(6-22): has a
vasorelaxant activity in rat aortic strips and a diuretic potency
in anesthetized rats. Is as potent as Tf-CNP.
{ECO:0000269|PubMed:17714693}.
-!- SUBCELLULAR LOCATION: Secreted.
-!- 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; P0C7P5; -.
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: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.
PRINTS; PR00710; NATPEPTIDES.
SMART; SM00183; NAT_PEP; 1.
PROSITE; PS00263; NATRIURETIC_PEPTIDE; 1.
1: Evidence at protein level;
Cleavage on pair of basic residues; Direct protein sequencing;
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 27 {ECO:0000250}.
/FTId=PRO_0000342439.
PEPTIDE 28 39 Bradykinin-potentiating peptide Tf1.
{ECO:0000250}.
/FTId=PRO_0000342440.
PROPEP 40 43 {ECO:0000250}.
/FTId=PRO_0000342441.
PEPTIDE 44 57 Bradykinin-potentiating peptide Tf2.
{ECO:0000250}.
/FTId=PRO_0000342442.
PROPEP 58 64 {ECO:0000250}.
/FTId=PRO_0000342443.
PEPTIDE 65 74 Bradykinin-potentiating peptide Tf3.
{ECO:0000250}.
/FTId=PRO_0000342444.
PROPEP 75 169 {ECO:0000250}.
/FTId=PRO_0000342445.
PEPTIDE 172 193 C-type natriuretic peptide Tf-CNP.
/FTId=PRO_0000342446.
PEPTIDE 174 193 C-type natriuretic peptide Tf-CNP(3-22).
/FTId=PRO_0000342447.
PEPTIDE 177 193 C-type natriuretic peptide Tf-CNP(6-22).
/FTId=PRO_0000342448.
COMPBIAS 31 111 Pro-rich.
COMPBIAS 153 161 Poly-Gly.
MOD_RES 28 28 Pyrrolidone carboxylic acid.
{ECO:0000250}.
MOD_RES 65 65 Pyrrolidone carboxylic acid.
{ECO:0000250}.
DISULFID 177 193
SEQUENCE 193 AA; 20051 MW; 4B240B7BE52BF504 CRC64;
MFVSRLAASG LLLLALLALS LDGKPVHQSK PGRSPPISPL SAQQWMPEGR PPHPIPPLSV
QQWSQGRPRS EVPPVVVQPH ESPAGGTTAF REELSPGPEA ASGPAAPHRL PKSKGASATS
AASRPMRDLR TDGKQERQKW GRMVQPDHHA APGGGGGGGG GARRMKGLAK KAMGKGCFGH
KLDRIGSTSG LGC


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