BNP_SISCA
ID BNP_SISCA Reviewed; 201 AA.
AC B0VXV8;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 08-APR-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 10c;
DE Short=BPP-10c;
DE Short=BPP-2;
DE AltName: 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 Contains:
DE RecName: Full=C-type natriuretic peptide;
DE Short=CNP;
DE Flags: Precursor;
OS Sistrurus catenatus edwardsii (Desert massasauga) (Crotalophorus
OS edwardsii).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC Serpentes; Colubroidea; Viperidae; Crotalinae; Sistrurus.
OX NCBI_TaxID=8762;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Venom gland;
RX PubMed=18096037; DOI=10.1186/1471-2199-8-115;
RA Pahari S., Mackessy S.P., Kini R.M.;
RT "The venom gland transcriptome of the Desert Massasauga rattlesnake
RT (Sistrurus catenatus edwardsii): towards an understanding of venom
RT composition among advanced snakes (Superfamily Colubroidea).";
RL BMC Mol. Biol. 8:115-115(2007).
RN [2]
RP SYNTHESIS OF 48-57, AND FUNCTION.
RX PubMed=11994001; DOI=10.1021/bi012121x;
RA Cotton J., Hayashi M.A., Cuniasse P., Vazeux G., Ianzer D.,
RA De Camargo A.C., Dive V.;
RT "Selective inhibition of the C-domain of angiotensin I converting enzyme by
RT bradykinin potentiating peptides.";
RL Biochemistry 41:6065-6071(2002).
CC -!- FUNCTION: [Bradykinin-potentiating peptide 10c]: Inhibits the activity
CC of the angiotensin-converting enzyme (ACE) by a preferential
CC interaction with its C-domain. May also potentiate the hypotensive
CC effects of bradykinin. {ECO:0000269|PubMed:11994001}.
CC -!- FUNCTION: [Bradykinin inhibitor peptide homolog]: Antagonizes the
CC vasodilatory actions of bradykinin at the B2 bradykinin receptor.
CC {ECO:0000250}.
CC -!- FUNCTION: [C-type natriuretic peptide]: 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: Venom gland.
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:0000305}.
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DR EMBL; DQ464265; ABG26994.1; -; mRNA.
DR AlphaFoldDB; B0VXV8; -.
DR PRIDE; B0VXV8; -.
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 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..47
FT /evidence="ECO:0000255"
FT /id="PRO_0000335915"
FT PEPTIDE 48..57
FT /note="Bradykinin-potentiating peptide 10c"
FT /evidence="ECO:0000250"
FT /id="PRO_0000335916"
FT PROPEP 58..60
FT /evidence="ECO:0000255"
FT /id="PRO_0000335917"
FT PEPTIDE 61..66
FT /note="Bradykinin-potentiating peptide-2"
FT /evidence="ECO:0000250"
FT /id="PRO_0000335918"
FT PROPEP 67..95
FT /evidence="ECO:0000255"
FT /id="PRO_0000335919"
FT PEPTIDE 96..106
FT /note="Bradykinin inhibitor peptide homolog"
FT /evidence="ECO:0000250"
FT /id="PRO_0000335920"
FT PROPEP 107..177
FT /evidence="ECO:0000255"
FT /id="PRO_0000335921"
FT PEPTIDE 180..201
FT /note="C-type natriuretic peptide"
FT /evidence="ECO:0000250"
FT /id="PRO_0000335922"
FT REGION 90..172
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 119..133
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 48
FT /note="Pyrrolidone carboxylic acid"
FT /evidence="ECO:0000250"
FT MOD_RES 61
FT /note="Pyrrolidone carboxylic acid"
FT /evidence="ECO:0000250"
FT DISULFID 185..201
FT /evidence="ECO:0000250"
SQ SEQUENCE 201 AA; 20896 MW; AB4258B899E4EDF4 CRC64;
MFVSRLAASG LLLLALLAVS LDGKPVQQWS QNWPGPKVPP LVVQQWSQNW PHPQIPPLVV
QNWKSPTQLQ PRESPAGGTT ALREELSLGP DAALDTPPAG PDVGPRGSKA AAAPQRLSKS
KGASATSTAS RPMRDLRTDG KQARQNWGRM LNPDHHSAPG GGGGGGGGGA RRLKGLAKKR
AGSGCFGLKL DRIGSMSGLG C
