ID   BNP_TRIGA               Reviewed;         210 AA.
AC   P0C7P6;
DT   01-JUL-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-2008, sequence version 1.
DT   25-MAY-2022, entry version 34.
DE   RecName: Full=Bradykinin-potentiating and C-type natriuretic peptides;
DE   AltName: Full=BPP-CNP;
DE   Contains:
DE     RecName: Full=Bradykinin-potentiating peptide Tg1;
DE              Short=BPP;
DE   Contains:
DE     RecName: Full=C-type natriuretic peptide;
DE              Short=CNP;
DE   Flags: Precursor;
OS   Trimeresurus gramineus (Bamboo pit viper) (Indian green tree viper).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC   Serpentes; Colubroidea; Viperidae; Crotalinae; Trimeresurus.
OX   NCBI_TaxID=8767;
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   SYNTHESIS OF 27-38, 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). Tg1 does not show
CC       bradykinin-potentiating effects. {ECO:0000250,
CC       ECO:0000269|PubMed:17714693}.
CC   -!- FUNCTION: Snake venom natriuretic peptide that exhibits hypotensive and
CC       vasodepressor activity. Acts by activating natriuretic receptors (NPR1
CC       and/or NPR2 and/or NPR3) (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
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; P0C7P6; -.
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   SMART; SM00183; NAT_PEP; 1.
DR   PROSITE; PS00263; NATRIURETIC_PEPTIDE; 1.
PE   2: Evidence at transcript level;
KW   Cleavage on pair of basic residues; Disulfide bond; Hypotensive agent;
KW   Metalloenzyme inhibitor; Metalloprotease inhibitor; Protease inhibitor;
KW   Pyrrolidone carboxylic acid; Secreted; Signal; Toxin; Vasoactive;
KW   Vasodilator.
FT   SIGNAL          1..23
FT                   /evidence="ECO:0000255"
FT   PROPEP          24..26
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000342449"
FT   PEPTIDE         27..38
FT                   /note="Bradykinin-potentiating peptide Tg1"
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000342450"
FT   PROPEP          39..186
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000342451"
FT   PEPTIDE         189..210
FT                   /note="C-type natriuretic peptide"
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000342452"
FT   REGION          25..181
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        31..64
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        144..161
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         27
FT                   /note="Pyrrolidone carboxylic acid"
FT                   /evidence="ECO:0000250"
FT   DISULFID        194..210
FT                   /evidence="ECO:0000250"
SQ   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