BNP_PROFL
ID BNP_PROFL Reviewed; 193 AA.
AC P0C7P5;
DT 01-JUL-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-2008, sequence version 1.
DT 25-MAY-2022, entry version 36.
DE RecName: Full=Bradykinin-potentiating and C-type natriuretic peptides;
DE AltName: Full=BPP-CNP;
DE Contains:
DE RecName: Full=Bradykinin-potentiating peptide Tf1;
DE Contains:
DE RecName: Full=Bradykinin-potentiating peptide Tf2;
DE Contains:
DE RecName: Full=Bradykinin-potentiating peptide Tf3;
DE Contains:
DE RecName: Full=C-type natriuretic peptide Tf-CNP;
DE Contains:
DE RecName: Full=C-type natriuretic peptide Tf-CNP(3-22);
DE Contains:
DE RecName: Full=C-type natriuretic peptide Tf-CNP(6-22);
DE Flags: Precursor;
OS Protobothrops flavoviridis (Habu) (Trimeresurus flavoviridis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC Serpentes; Colubroidea; Viperidae; Crotalinae; Protobothrops.
OX NCBI_TaxID=88087;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Venom gland;
RX PubMed=10604536; DOI=10.1016/s0162-3109(99)00119-8;
RA Higuchi S., Murayama N., Saguchi K., Ohi H., Fujita Y., de Camargo A.C.M.,
RA Ogawa T., Deshimaru M., Ohno M.;
RT "Bradykinin-potentiating peptides and C-type natriuretic peptides from
RT snake venom.";
RL Immunopharmacology 44:129-135(1999).
RN [2]
RP PROTEIN SEQUENCE OF 174-193 (TF-CNP(3-22) AND TF-CNP(6-22)), AND SYNTHESIS
RP OF TF-CNP.
RC TISSUE=Venom;
RX PubMed=10876042; DOI=10.1016/s0196-9781(00)00203-5;
RA Michel G.H., Murayama N., Sada T., Nozaki M., Saguchi K., Ohi H.,
RA Fujita Y., Koike H., Higuchi S.;
RT "Two N-terminally truncated forms of C-type natriuretic peptide from habu
RT snake venom.";
RL Peptides 21:609-615(2000).
RN [3]
RP SYNTHESIS OF 28-39 AND 44-57, AND FUNCTION.
RX PubMed=17714693; DOI=10.1016/j.bcp.2007.07.014;
RA Gomes C.L., Konno K., Conceicao I.M., Ianzer D., Yamanouye N.,
RA Prezoto B.C., Assakura M.T., Radis-Baptista G., Yamane T., Santos R.A.,
RA de Camargo A.C.M., Hayashi M.A.F.;
RT "Identification of novel bradykinin-potentiating peptides (BPPs) in the
RT venom gland of a rattlesnake allowed the evaluation of the structure-
RT function relationship of BPPs.";
RL Biochem. Pharmacol. 74:1350-1360(2007).
CC -!- FUNCTION: Bradykinin-potentiating peptide both inhibits the activity of
CC the angiotensin-converting enzyme (ACE) and enhances the action of
CC bradykinin by inhibiting the peptidases that inactivate it. It acts as
CC an indirect hypotensive agent (By similarity). Neither synthetic Tf1,
CC nor synthetic Tf2 show bradykinin-potentiating effects. {ECO:0000250,
CC ECO:0000269|PubMed:17714693}.
CC -!- FUNCTION: [C-type natriuretic peptide Tf-CNP]: Has a vasorelaxant
CC activity in rat aortic strips and a diuretic potency in anesthetized
CC rats. {ECO:0000269|PubMed:17714693}.
CC -!- FUNCTION: [C-type natriuretic peptide Tf-CNP(6-22)]: Has a vasorelaxant
CC activity in rat aortic strips and a diuretic potency in anesthetized
CC rats. Is as potent as Tf-CNP. {ECO:0000269|PubMed:17714693}.
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC -!- SIMILARITY: In the N-terminal section; belongs to the bradykinin-
CC potentiating peptide family. {ECO:0000305}.
CC -!- SIMILARITY: In the C-terminal section; belongs to the natriuretic
CC peptide family. {ECO:0000305}.
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DR AlphaFoldDB; P0C7P5; -.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0005179; F:hormone activity; IEA:InterPro.
DR GO; GO:0008191; F:metalloendopeptidase inhibitor 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 PRINTS; PR00710; NATPEPTIDES.
DR SMART; SM00183; NAT_PEP; 1.
DR PROSITE; PS00263; NATRIURETIC_PEPTIDE; 1.
PE 1: Evidence at protein level;
KW Cleavage on pair of basic residues; Direct protein sequencing;
KW Disulfide bond; Hypotensive agent; Metalloenzyme inhibitor;
KW Metalloprotease inhibitor; Protease inhibitor; Pyrrolidone carboxylic acid;
KW Secreted; Signal; Toxin; Vasoactive; Vasodilator.
FT SIGNAL 1..23
FT /evidence="ECO:0000255"
FT PROPEP 24..27
FT /evidence="ECO:0000250"
FT /id="PRO_0000342439"
FT PEPTIDE 28..39
FT /note="Bradykinin-potentiating peptide Tf1"
FT /evidence="ECO:0000250"
FT /id="PRO_0000342440"
FT PROPEP 40..43
FT /evidence="ECO:0000250"
FT /id="PRO_0000342441"
FT PEPTIDE 44..57
FT /note="Bradykinin-potentiating peptide Tf2"
FT /evidence="ECO:0000250"
FT /id="PRO_0000342442"
FT PROPEP 58..64
FT /evidence="ECO:0000250"
FT /id="PRO_0000342443"
FT PEPTIDE 65..74
FT /note="Bradykinin-potentiating peptide Tf3"
FT /evidence="ECO:0000250"
FT /id="PRO_0000342444"
FT PROPEP 75..169
FT /evidence="ECO:0000250"
FT /id="PRO_0000342445"
FT PEPTIDE 172..193
FT /note="C-type natriuretic peptide Tf-CNP"
FT /id="PRO_0000342446"
FT PEPTIDE 174..193
FT /note="C-type natriuretic peptide Tf-CNP(3-22)"
FT /id="PRO_0000342447"
FT PEPTIDE 177..193
FT /note="C-type natriuretic peptide Tf-CNP(6-22)"
FT /id="PRO_0000342448"
FT REGION 25..173
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 127..144
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 28
FT /note="Pyrrolidone carboxylic acid"
FT /evidence="ECO:0000250"
FT MOD_RES 65
FT /note="Pyrrolidone carboxylic acid"
FT /evidence="ECO:0000250"
FT DISULFID 177..193
SQ 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
