BPP_BRAEP
ID BPP_BRAEP Reviewed; 8 AA.
AC P0DV72;
DT 25-MAY-2022, integrated into UniProtKB/Swiss-Prot.
DT 25-MAY-2022, sequence version 1.
DT 03-AUG-2022, entry version 2.
DE RecName: Full=Bradykinin-potentiating peptide Brachy {ECO:0000303|PubMed:26661890};
DE Short=BPP-Brachy {ECO:0000303|PubMed:26661890};
DE Short=BPP-BrachyNH2 {ECO:0000303|PubMed:26661890};
DE AltName: Full=Proline-rich oligopeptide {ECO:0000303|PubMed:26661890};
DE Short=PRO {ECO:0000303|PubMed:26661890};
DE Short=Proline-rich peptide {ECO:0000305};
OS Brachycephalus ephippium (Pumpkin toadlet) (Bufo ephippium).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Neobatrachia; Hyloidea; Brachycephalidae; Brachycephalus.
OX NCBI_TaxID=164302;
RN [1]
RP PROTEIN SEQUENCE, FUNCTION, SUBCELLULAR LOCATION, 3D-STRUCTURE MODELING OF
RP BPP-BRACHYNH2 IN COMPLEX WITH ACE, MASS SPECTROMETRY, PARTIAL AMIDATION AT
RP PRO-8, AND SYNTHESIS OF THE AMIDATED PEPTIDE.
RC TISSUE=Skin secretion;
RX PubMed=26661890; DOI=10.1371/journal.pone.0145071;
RA Arcanjo D.D., Vasconcelos A.G., Comerma-Steffensen S.G., Jesus J.R.,
RA Silva L.P., Pires Junior O.R., Costa-Neto C.M., Oliveira E.B., Migliolo L.,
RA Franco O.L., Restini C.B., Paulo M., Bendhack L.M., Bemquerer M.P.,
RA Oliveira A.P., Simonsen U., Leite J.R.;
RT "A novel vasoactive proline-rich oligopeptide from the skin secretion of
RT the frog Brachycephalus ephippium.";
RL PLoS ONE 10:e0145071-e0145071(2015).
CC -!- FUNCTION: The amidated peptide increases the release of nitric oxid
CC (NO) and that NO mediates the endothelium-dependent vasodilatation. In
CC addition, it inhibits efficiently angiotensin I-converting enzyme (ACE)
CC in rat serum (IC(50)=8.2 uM). 3D-structure modeling of this peptide in
CC complex with ACE suggests it acts by inhibiting the ACE C-terminal
CC catalytic site. {ECO:0000269|PubMed:26661890}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:26661890}.
CC -!- TISSUE SPECIFICITY: Expressed by the skin gland.
CC {ECO:0000305|PubMed:26661890}.
CC -!- PTM: Both amidated and non-amidated peptides have been observed in skin
CC secretions. {ECO:0000269|PubMed:26661890}.
CC -!- MASS SPECTROMETRY: Mass=907.37; Method=MALDI; Note=non-amidated.;
CC Evidence={ECO:0000269|PubMed:26661890};
CC -!- MASS SPECTROMETRY: Mass=906.36; Method=MALDI; Note=amidated.;
CC Evidence={ECO:0000269|PubMed:26661890};
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:0008217; P:regulation of blood pressure; IEA:UniProtKB-KW.
PE 1: Evidence at protein level;
KW Amidation; Direct protein sequencing; Hypotensive agent; Secreted;
KW Vasoactive.
FT PEPTIDE 1..8
FT /note="Bradykinin-potentiating peptide Brachy"
FT /evidence="ECO:0000269|PubMed:26661890"
FT /id="PRO_0000455436"
FT MOD_RES 8
FT /note="Proline amide; partial"
FT /evidence="ECO:0000269|PubMed:26661890"
SQ SEQUENCE 8 AA; 907 MW; 6C75A2C327777773 CRC64;
WPPPKVSP