BNP_CRODU
ID BNP_CRODU Reviewed; 181 AA.
AC Q90Y12; Q90Y11;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 25-MAY-2022, entry version 55.
DE RecName: Full=Bradykinin potentiating and C-type natriuretic peptides;
DE AltName: Full=BPP-CNP;
DE Contains:
DE RecName: Full=Bradykinin-potentiating peptide Cdt1a;
DE Contains:
DE RecName: Full=Bradykinin-potentiating peptide Cdt1b;
DE Contains:
DE RecName: Full=Bradykinin-potentiating peptide Cdt2;
DE Contains:
DE RecName: Full=Bradykinin inhibitor peptide Cdt3;
DE Contains:
DE RecName: Full=C-type natriuretic peptide;
DE Short=CNP;
DE Flags: Precursor;
OS Crotalus durissus terrificus (South American rattlesnake).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC Serpentes; Colubroidea; Viperidae; Crotalinae; Crotalus.
OX NCBI_TaxID=8732;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND SYNTHESIS OF 28-40; 31-40; 44-49
RP AND 53-58.
RC TISSUE=Venom gland;
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).
RN [2]
RP PROTEIN SEQUENCE OF 31-40, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, MASS
RP SPECTROMETRY, AND PYROGLUTAMATE FORMATION AT GLN-31.
RC TISSUE=Venom;
RX PubMed=15912471; DOI=10.1002/rcm.1973;
RA Wermelinger L.S., Dutra D.L., Oliveira-Carvalho A.L., Soares M.R.,
RA Bloch C. Jr., Zingali R.B.;
RT "Fast analysis of low molecular mass compounds present in snake venom:
RT identification of ten new pyroglutamate-containing peptides.";
RL Rapid Commun. Mass Spectrom. 19:1703-1708(2005).
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. Synthetic Cdt1a, Cdt1b and the short
CC hexapeptide Cdt3 are able to potentiate the hypotensive effect mediated
CC by Bk on the blood pressure of anesthetized rats.
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:0000269|PubMed:15912471}.
CC -!- TISSUE SPECIFICITY: Venom gland. {ECO:0000269|PubMed:15912471}.
CC -!- MASS SPECTROMETRY: [Bradykinin-potentiating peptide Cdt1b]:
CC Mass=1255.36; Method=MALDI; Evidence={ECO:0000269|PubMed:15912471};
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 EMBL; AF308593; AAL09426.1; -; mRNA.
DR EMBL; AF308594; AAL09427.1; -; mRNA.
DR AlphaFoldDB; Q90Y12; -.
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:0000255"
FT /id="PRO_0000335906"
FT PEPTIDE 28..40
FT /note="Bradykinin-potentiating peptide Cdt1a"
FT /evidence="ECO:0000250"
FT /id="PRO_0000335907"
FT PEPTIDE 31..40
FT /note="Bradykinin-potentiating peptide Cdt1b"
FT /id="PRO_0000335908"
FT PROPEP 41..43
FT /id="PRO_0000335909"
FT PEPTIDE 44..49
FT /note="Bradykinin-potentiating peptide Cdt2"
FT /evidence="ECO:0000250"
FT /id="PRO_0000335910"
FT PROPEP 50..52
FT /evidence="ECO:0000255"
FT /id="PRO_0000335911"
FT PEPTIDE 53..58
FT /note="Bradykinin inhibitor peptide Cdt3"
FT /evidence="ECO:0000250"
FT /id="PRO_0000335912"
FT PROPEP 59..157
FT /evidence="ECO:0000255"
FT /id="PRO_0000335913"
FT PEPTIDE 160..181
FT /note="C-type natriuretic peptide"
FT /evidence="ECO:0000250"
FT /id="PRO_0000335914"
FT REGION 74..150
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 103..117
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 28
FT /note="Pyrrolidone carboxylic acid"
FT /evidence="ECO:0000250"
FT MOD_RES 31
FT /note="Pyrrolidone carboxylic acid"
FT /evidence="ECO:0000269|PubMed:15912471"
FT MOD_RES 44
FT /note="Pyrrolidone carboxylic acid"
FT /evidence="ECO:0000250"
FT MOD_RES 53
FT /note="Pyrrolidone carboxylic acid"
FT /evidence="ECO:0000250"
FT DISULFID 165..181
FT /evidence="ECO:0000250"
FT VARIANT 31
FT /note="Q -> H (in isoform 1)"
FT VARIANT 36
FT /note="L -> P (in isoform 1)"
FT VARIANT 144
FT /note="C -> G (in isoform 1)"
SQ SEQUENCE 181 AA; 18560 MW; 7B5ADC5B9372D07F CRC64;
MFVSRLAASG LLLLALLAVS LDGKPLQQWS QRWPHLEIPP LVVQNWKSPT QLQARESPAG
GTTALREELS LGPEAALDTP PAGPDGGPRG SKAAAAAPQR LSKSKGASAT SAASRDLRTD
GKQARQNWGR LVSPDHHSAA GGGCGGGGGA RRLKGLAKKR AGNGCFGLKL DRIGSMSGLG
C
