BPPEA_BOTJA
ID BPPEA_BOTJA Reviewed; 14 AA.
AC P85163; P85164;
DT 26-JUN-2007, integrated into UniProtKB/Swiss-Prot.
DT 26-JUN-2007, sequence version 1.
DT 29-SEP-2021, entry version 29.
DE RecName: Full=Bradykinin-potentiating peptide 14a;
DE Short=BPP-14a;
DE Contains:
DE RecName: Full=Bradykinin-potentiating peptide 11a;
DE Short=BPP-11a;
DE AltName: Full=Bradykinin-potentiating peptide V-2;
DE Short=BPPV-2;
DE Contains:
DE RecName: Full=Bradykinin-potentiating peptide 11a-F;
DE Short=BPP-11a-F;
DE Contains:
DE RecName: Full=Bradykinin-potentiating peptide 5b;
DE Short=BPP-5b;
OS Bothrops jararaca (Jararaca) (Bothrops jajaraca).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC Serpentes; Colubroidea; Viperidae; Crotalinae; Bothrops.
OX NCBI_TaxID=8724;
RN [1] {ECO:0000305}
RP PROTEIN SEQUENCE (BPP-11A AND BPP-14A), FUNCTION, SUBCELLULAR LOCATION,
RP TISSUE SPECIFICITY, MASS SPECTROMETRY, AND PYROGLUTAMATE FORMATION AT
RP GLN-1.
RC TISSUE=Venom {ECO:0000269|PubMed:15245866};
RX PubMed=15245866; DOI=10.1016/j.peptides.2004.04.006;
RA Ianzer D., Konno K., Marques-Porto R., Portaro F.C.V., Stoecklin R.,
RA de Camargo A.C.M., Pimenta D.C.;
RT "Identification of five new bradykinin potentiating peptides (BPPs) from
RT Bothrops jararaca crude venom by using electrospray ionization tandem mass
RT spectrometry after a two-step liquid chromatography.";
RL Peptides 25:1085-1092(2004).
RN [2]
RP PROTEIN SEQUENCE (BPP-11A AND BPP-14A), PYROGLUTAMATE FORMATION AT GLN-1
RP AND GLN-4, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC TISSUE=Venom;
RX PubMed=22869554; DOI=10.1074/mcp.m112.019331;
RA Tashima A.K., Zelanis A., Kitano E.S., Ianzer D., Melo R.L., Rioli V.,
RA Sant'anna S.S., Schenberg A.C., Camargo A.C., Serrano S.M.T.;
RT "Peptidomics of three Bothrops snake venoms: insights into the molecular
RT diversification of proteomes and peptidomes.";
RL Mol. Cell. Proteomics 11:1245-1262(2012).
RN [3]
RP PROTEIN SEQUENCE, PYROGLUTAMATE FORMATION AT GLN-1, DEVELOPMENTAL STAGE
RP (BPP-14A), AND IDENTIFICATION BY MASS SPECTROMETRY.
RC TISSUE=Venom;
RX PubMed=20146532; DOI=10.1021/pr901027r;
RA Zelanis A., Tashima A.K., Rocha M.M., Furtado M.F., Camargo A.C., Ho P.L.,
RA Serrano S.M.;
RT "Analysis of the ontogenetic variation in the venom proteome/peptidome of
RT Bothrops jararaca reveals different strategies to deal with prey.";
RL J. Proteome Res. 9:2278-2291(2010).
RN [4]
RP PROTEIN SEQUENCE OF 4-14 (BPP-11A), AND FUNCTION.
RC TISSUE=Venom;
RX PubMed=4334402; DOI=10.1021/bi00798a004;
RA Ondetti M.A., Williams N.J., Sabo E.F., Pluscec J., Weaver E.R., Kocy O.;
RT "Angiotensin-converting enzyme inhibitors from the venom of Bothrops
RT jararaca. Isolation, elucidation of structure, and synthesis.";
RL Biochemistry 10:4033-4039(1971).
RN [5]
RP PROTEIN SEQUENCE OF 4-14 (BPP-11A), SUBCELLULAR LOCATION, TISSUE
RP SPECIFICITY, MASS SPECTROMETRY, AND PYROGLUTAMATE FORMATION AT GLN-4.
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).
RN [6]
RP PROTEIN SEQUENCE OF 4-10 (BPP-11A-F), FUNCTION, SUBCELLULAR LOCATION,
RP TISSUE SPECIFICITY, MASS SPECTROMETRY, AND PYROGLUTAMATE FORMATION AT
RP GLN-4.
RC TISSUE=Venom;
RX PubMed=17315274; DOI=10.1002/rcm.2931;
RA Pimenta D.C., Prezoto B.C., Konno K., de Melo R.L., Furtado M.F.,
RA de Camargo A.C.M., Serrano S.M.T.;
RT "Mass spectrometric analysis of the individual variability of Bothrops
RT jararaca venom peptide fraction. Evidence for sex-based variation among the
RT bradykinin-potentiating peptides.";
RL Rapid Commun. Mass Spectrom. 21:1034-1042(2007).
CC -!- FUNCTION: This peptide both inhibits the activity of the angiotensin-
CC converting enzyme (ACE) and enhances the action of bradykinin by
CC inhibiting the peptidases that inactivate it. It acts as an indirect
CC hypotensive agent. Bradykinin-potentiating peptide 11a-F has much lower
CC activity than BPP-11a. {ECO:0000269|PubMed:15245866,
CC ECO:0000269|PubMed:17315274, ECO:0000269|PubMed:4334402}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:15245866,
CC ECO:0000269|PubMed:15912471, ECO:0000269|PubMed:17315274}.
CC -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC {ECO:0000269|PubMed:15245866, ECO:0000269|PubMed:15912471,
CC ECO:0000269|PubMed:17315274}.
CC -!- DEVELOPMENTAL STAGE: This protein seems to be found in both adult and
CC newborn B.jararaca venoms. {ECO:0000269|PubMed:20146532}.
CC -!- MASS SPECTROMETRY: [Bradykinin-potentiating peptide 5b]: Mass=665.6;
CC Method=Electrospray; Note=BPP-5b.;
CC Evidence={ECO:0000269|PubMed:15245866};
CC -!- MASS SPECTROMETRY: [Bradykinin-potentiating peptide 11a]: Mass=1299.5;
CC Method=Electrospray; Note=BPP-11a.;
CC Evidence={ECO:0000269|PubMed:15245866};
CC -!- MASS SPECTROMETRY: [Bradykinin-potentiating peptide 11a]: Mass=1299.75;
CC Method=MALDI; Note=BPP-11a.; Evidence={ECO:0000269|PubMed:15912471};
CC -!- MASS SPECTROMETRY: [Bradykinin-potentiating peptide 11a-F]:
CC Mass=863.43; Method=MALDI; Note=BPP-11a-F.;
CC Evidence={ECO:0000269|PubMed:17315274};
CC -!- MASS SPECTROMETRY: [Bradykinin-potentiating peptide 14a]: Mass=1683.85;
CC Method=Electrospray; Note=BPP-14a.;
CC Evidence={ECO:0000269|PubMed:15245866};
CC -!- MISCELLANEOUS: Bradykinin-potentiating peptide 11a-F is present only in
CC female snakes. {ECO:0000305|PubMed:17315274}.
CC -!- SIMILARITY: Belongs to the bradykinin-potentiating peptide family.
CC {ECO:0000305}.
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DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
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.
PE 1: Evidence at protein level;
KW Direct protein sequencing; Hypotensive agent; Metalloenzyme inhibitor;
KW Metalloprotease inhibitor; Protease inhibitor; Pyrrolidone carboxylic acid;
KW Secreted; Toxin.
FT PEPTIDE 1..14
FT /note="Bradykinin-potentiating peptide 14a"
FT /evidence="ECO:0000269|PubMed:15245866"
FT /id="PRO_0000292925"
FT PEPTIDE 4..14
FT /note="Bradykinin-potentiating peptide 11a"
FT /id="PRO_0000292917"
FT PEPTIDE 4..10
FT /note="Bradykinin-potentiating peptide 11a-F"
FT /id="PRO_0000292918"
FT PEPTIDE 4..8
FT /note="Bradykinin-potentiating peptide 5b"
FT /id="PRO_0000292919"
FT MOD_RES 1
FT /note="Pyrrolidone carboxylic acid"
FT /evidence="ECO:0000269|PubMed:15245866,
FT ECO:0000269|PubMed:20146532, ECO:0000269|PubMed:22869554"
FT MOD_RES 4
FT /note="Pyrrolidone carboxylic acid"
FT /evidence="ECO:0000269|PubMed:15912471,
FT ECO:0000269|PubMed:17315274, ECO:0000269|PubMed:22869554"
SQ SEQUENCE 14 AA; 1702 MW; 6824EF4381FEE274 CRC64;
QWAQWPRPTP QIPP
