BNP_LACMU
ID BNP_LACMU Reviewed; 239 AA.
AC Q27J49;
DT 31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 04-APR-2006, sequence version 1.
DT 25-MAY-2022, entry version 44.
DE RecName: Full=Bradykinin-potentiating and C-type natriuretic peptides;
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-potentiating peptide 3;
DE Short=BPP 3;
DE Contains:
DE RecName: Full=Bradykinin-potentiating peptide 4;
DE Short=BPP 4;
DE Contains:
DE RecName: Full=Bradykinin-potentiating peptide 5;
DE Short=BPP 5;
DE Contains:
DE RecName: Full=Bradykinin inhibitor peptide;
DE Short=BIP;
DE Contains:
DE RecName: Full=C-type natriuretic peptide;
DE Short=CNP;
DE Flags: Precursor;
OS Lachesis muta muta (Bushmaster).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC Serpentes; Colubroidea; Viperidae; Crotalinae; Lachesis.
OX NCBI_TaxID=8753;
RN [1] {ECO:0000305, ECO:0000312|EMBL:ABD52884.1}
RP NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 34-42; 50-61; 65-75; 83-94;
RP 98-108 AND 218-239, PYROGLUTAMATE FORMATION AT GLN-50; GLN-65; GLN-83 AND
RP GLN-98, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND MASS SPECTROMETRY.
RC TISSUE=Venom {ECO:0000269|PubMed:15876444}, and
RC Venom gland {ECO:0000269|PubMed:15876444};
RX PubMed=15876444; DOI=10.1016/j.toxicon.2005.03.006;
RA Soares M.R., Oliveira-Carvalho A.L., Wermelinger L.S., Zingali R.B.,
RA Ho P.L., Junqueira-de-Azevedo I.L.M., Diniz M.R.V.;
RT "Identification of novel bradykinin-potentiating peptides and C-type
RT natriuretic peptide from Lachesis muta venom.";
RL Toxicon 46:31-38(2005).
RN [2] {ECO:0000312|EMBL:ABD52884.1}
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Venom gland {ECO:0000269|PubMed:16582429};
RX PubMed=16582429; DOI=10.1534/genetics.106.056515;
RA Junqueira-de-Azevedo I.L.M., Ching A.T.C., Carvalho E., Faria F.,
RA Nishiyama M.Y. Jr., Ho P.L., Diniz M.R.V.;
RT "Lachesis muta (Viperidae) cDNAs reveal diverging pit viper molecules and
RT scaffolds typical of cobra (Elapidae) venoms: implications for snake toxin
RT repertoire evolution.";
RL Genetics 173:877-889(2006).
RN [3] {ECO:0000305}
RP PROTEIN SEQUENCE OF 137-147, FUNCTION, SUBCELLULAR LOCATION, AND MASS
RP SPECTROMETRY.
RC TISSUE=Venom {ECO:0000269|PubMed:16277978};
RX PubMed=16277978; DOI=10.1016/j.bbrc.2005.10.130;
RA Graham R.L.J., Graham C., McClean S., Chen T., O'Rourke M., Hirst D.,
RA Theakston D., Shaw C.;
RT "Identification and functional analysis of a novel bradykinin inhibitory
RT peptide in the venoms of new world crotalinae pit vipers.";
RL Biochem. Biophys. Res. Commun. 338:1587-1592(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 (By similarity). {ECO:0000250}.
CC -!- FUNCTION: Bradykinin inhibitor peptide antagonizes the vasodilatory
CC actions of bradykinin at the B2 bradykinin receptor.
CC {ECO:0000269|PubMed:16277978}.
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:15876444,
CC ECO:0000269|PubMed:16277978}.
CC -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC {ECO:0000269|PubMed:15876444}.
CC -!- MASS SPECTROMETRY: [Bradykinin-potentiating peptide 1]: Mass=1088.11;
CC Mass_error=0.02; Method=MALDI; Note=Bradykinin-potentiating peptide 1.;
CC Evidence={ECO:0000269|PubMed:15876444};
CC -!- MASS SPECTROMETRY: [Bradykinin-potentiating peptide 2]: Mass=1244.63;
CC Mass_error=0.02; Method=MALDI; Note=Bradykinin-potentiating peptide 2.;
CC Evidence={ECO:0000269|PubMed:15876444};
CC -!- MASS SPECTROMETRY: [Bradykinin-potentiating peptide 3]: Mass=1404.60;
CC Mass_error=0.02; Method=MALDI; Note=Bradykinin-potentiating peptide 3.;
CC Evidence={ECO:0000269|PubMed:15876444};
CC -!- MASS SPECTROMETRY: [Bradykinin-potentiating peptide 4]: Mass=1277.74;
CC Mass_error=0.02; Method=MALDI; Note=Bradykinin-potentiating peptide 4.;
CC Evidence={ECO:0000269|PubMed:15876444};
CC -!- MASS SPECTROMETRY: [Bradykinin-potentiating peptide 5]: Mass=1374.16;
CC Mass_error=0.02; Method=MALDI; Note=Bradykinin-potentiating peptide 5.;
CC Evidence={ECO:0000269|PubMed:15876444};
CC -!- MASS SPECTROMETRY: [Bradykinin inhibitor peptide]: Mass=1063.18;
CC Method=MALDI; Note=Bradykinin inhibitor peptide.;
CC Evidence={ECO:0000269|PubMed:16277978};
CC -!- SIMILARITY: In the N-terminal section; belongs to the bradykinin-
CC potentiating peptide family. {ECO:0000305}.
CC -!- SIMILARITY: In the central section; belongs to the bradykinin inhibitor
CC peptide family. {ECO:0000305}.
CC -!- SIMILARITY: In the C-terminal section; belongs to the natriuretic
CC peptide family. {ECO:0000255}.
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DR EMBL; DQ396475; ABD52884.1; -; mRNA.
DR AlphaFoldDB; Q27J49; -.
DR GO; GO:0005576; C:extracellular region; IDA:UniProtKB.
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..33
FT /evidence="ECO:0000255, ECO:0000269|PubMed:15876444"
FT /id="PRO_0000258024"
FT PEPTIDE 34..42
FT /note="Bradykinin-potentiating peptide 1"
FT /evidence="ECO:0000269|PubMed:15876444"
FT /id="PRO_0000258025"
FT PROPEP 43..49
FT /evidence="ECO:0000269|PubMed:15876444"
FT /id="PRO_0000258026"
FT PEPTIDE 50..61
FT /note="Bradykinin-potentiating peptide 2"
FT /evidence="ECO:0000269|PubMed:15876444"
FT /id="PRO_0000258027"
FT PROPEP 62..64
FT /evidence="ECO:0000269|PubMed:15876444"
FT /id="PRO_0000258028"
FT PEPTIDE 65..75
FT /note="Bradykinin-potentiating peptide 3"
FT /evidence="ECO:0000269|PubMed:15876444"
FT /id="PRO_0000258029"
FT PROPEP 76..82
FT /evidence="ECO:0000269|PubMed:15876444"
FT /id="PRO_0000258030"
FT PEPTIDE 83..94
FT /note="Bradykinin-potentiating peptide 4"
FT /evidence="ECO:0000269|PubMed:15876444"
FT /id="PRO_0000258031"
FT PROPEP 95..97
FT /evidence="ECO:0000269|PubMed:15876444"
FT /id="PRO_0000258032"
FT PEPTIDE 98..108
FT /note="Bradykinin-potentiating peptide 5"
FT /evidence="ECO:0000269|PubMed:15876444"
FT /id="PRO_0000258033"
FT PROPEP 109..136
FT /evidence="ECO:0000269|PubMed:15876444,
FT ECO:0000269|PubMed:16277978"
FT /id="PRO_0000258034"
FT PEPTIDE 137..147
FT /note="Bradykinin inhibitor peptide"
FT /evidence="ECO:0000269|PubMed:16277978"
FT /id="PRO_0000258035"
FT PROPEP 148..217
FT /evidence="ECO:0000269|PubMed:15876444,
FT ECO:0000269|PubMed:16277978"
FT /id="PRO_0000258036"
FT PEPTIDE 218..239
FT /note="C-type natriuretic peptide"
FT /evidence="ECO:0000269|PubMed:15876444"
FT /id="PRO_0000258037"
FT REGION 132..205
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 50
FT /note="Pyrrolidone carboxylic acid"
FT /evidence="ECO:0000269|PubMed:15876444"
FT MOD_RES 65
FT /note="Pyrrolidone carboxylic acid"
FT /evidence="ECO:0000269|PubMed:15876444"
FT MOD_RES 83
FT /note="Pyrrolidone carboxylic acid"
FT /evidence="ECO:0000269|PubMed:15876444"
FT MOD_RES 98
FT /note="Pyrrolidone carboxylic acid"
FT /evidence="ECO:0000269|PubMed:15876444"
FT DISULFID 223..239
FT /evidence="ECO:0000250"
SQ SEQUENCE 239 AA; 25453 MW; 8E7FCFFC2B587497 CRC64;
MFVSRLAASG LLLLALLAVS LDGKPVQQWS HKGWPPRPQI PPLVVQQWSQ KPWPPGHHIP
PVVVQEWPPG HHIPPLVVQQ WSQKKWPPGH HIPPLVVQKW DPPPISPPLL KPHESPAGGT
TALREELSLG PEAALDTPPA GPDVGPRGSK APAAPHRLPK SKGASATSAA SRPMRDLRTD
GKQARQNWGR MMNPDHHAVG GGGGGGGARR LKGLAKKRVG DGCFGLKLDR IGSMSGLGC
