BNP_CRODO
ID BNP_CRODO Reviewed; 181 AA.
AC Q2PE51; Q2PE50;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 07-FEB-2006, sequence version 1.
DT 25-MAY-2022, entry version 47.
DE RecName: Full=Bradykinin-potentiating and C-type natriuretic peptides;
DE AltName: Full=Angiotensin converting enzyme inhibitor-CNP;
DE Short=ACEI-CNP;
DE AltName: Full=BPP-CNP;
DE Contains:
DE RecName: Full=Bradykinin-potentiating peptide-1;
DE Short=BPP-1;
DE Contains:
DE RecName: Full=Bradykinin-potentiating peptide-2;
DE Short=BPP-2;
DE Contains:
DE RecName: Full=Bradykinin inhibitor peptide homolog;
DE AltName: Full=Cdc peptide;
DE AltName: Full=Novel peptide;
DE Contains:
DE RecName: Full=C-type natriuretic peptide;
DE Short=CNP;
DE Flags: Precursor;
OS Crotalus durissus collilineatus (Brazilian rattlesnake).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC Serpentes; Colubroidea; Viperidae; Crotalinae; Crotalus.
OX NCBI_TaxID=221569;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 79-89, FUNCTION,
RP SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND MASS SPECTROMETRY.
RC TISSUE=Venom, and Venom gland;
RX PubMed=16979945; DOI=10.1016/j.cbpc.2006.04.006;
RA Higuchi S., Murayama N., Saguchi K., Ohi H., Fujita Y., da Silva N.J. Jr.,
RA de Siqueira R.J.B., Lahlou S., Aird S.D.;
RT "A novel peptide from the ACEI/BPP-CNP precursor in the venom of Crotalus
RT durissus collilineatus.";
RL Comp. Biochem. Physiol. 144C:107-121(2006).
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). {ECO:0000250}.
CC -!- FUNCTION: Bradykinin inhibitor peptide antagonizes the vasodilatory
CC actions of bradykinin at the B2 bradykinin receptor (By similarity).
CC Has no demonstrable hypotensive activity when injected intravenously in
CC rats. {ECO:0000250, ECO:0000269|PubMed:16979945}.
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:16979945}.
CC -!- TISSUE SPECIFICITY: Venom gland. {ECO:0000269|PubMed:16979945}.
CC -!- MASS SPECTROMETRY: [Bradykinin inhibitor peptide homolog]: Mass=1020.5;
CC Method=Electrospray; Evidence={ECO:0000269|PubMed:16979945};
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; AB246364; BAE73272.1; -; mRNA.
DR EMBL; AB246365; BAE73273.1; -; mRNA.
DR AlphaFoldDB; Q2PE51; -.
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..30
FT /evidence="ECO:0000255"
FT /id="PRO_0000335898"
FT PEPTIDE 31..40
FT /note="Bradykinin-potentiating peptide-1"
FT /id="PRO_0000335899"
FT PROPEP 41..43
FT /evidence="ECO:0000255"
FT /id="PRO_0000335900"
FT PEPTIDE 44..49
FT /note="Bradykinin-potentiating peptide-2"
FT /id="PRO_0000335901"
FT PROPEP 50..78
FT /evidence="ECO:0000255"
FT /id="PRO_0000335902"
FT PEPTIDE 79..89
FT /note="Bradykinin inhibitor peptide homolog"
FT /id="PRO_0000335903"
FT PROPEP 90..157
FT /evidence="ECO:0000255"
FT /id="PRO_0000335904"
FT PEPTIDE 160..181
FT /note="C-type natriuretic peptide"
FT /id="PRO_0000335905"
FT REGION 74..153
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 31
FT /note="Pyrrolidone carboxylic acid"
FT /evidence="ECO:0000250"
FT MOD_RES 44
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 2)"
FT VARIANT 36
FT /note="L -> P (in isoform 2)"
SQ SEQUENCE 181 AA; 18514 MW; CF5ADC5B93747C15 CRC64;
MFVSRLAASG LLLLALLAVS LDGKPLQQWS QRWPHLEIPP LVVQNWKSPT QLQARESPAG
GTTALREELS LGPEAALDTP PAGPDGGPRG SKAAAAAPQR LSKSKGASAT SAASRDLRTD
GKQARQNWGR LVSPDHHSAA GGGGGGGGGA RRLKGLAKKR AGNGCFGLKL DRIGSMSGLG
C
