ID   BM8X_BOMMX              Reviewed;          96 AA.
AC   Q8JFQ0;
DT   12-DEC-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2002, sequence version 1.
DT   25-MAY-2022, entry version 47.
DE   RecName: Full=Prokineticin Bv8-like peptide 2;
DE            Short=Bv8-LP2;
DE   Flags: Precursor;
OS   Bombina maxima (Giant fire-bellied toad) (Chinese red belly toad).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Bombinatoridae; Bombina.
OX   NCBI_TaxID=161274;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 20-45, AND FUNCTION.
RC   TISSUE=Skin secretion;
RX   PubMed=12628381; DOI=10.1016/s1096-4959(02)00294-4;
RA   Lai R., Liu H., Lee W.H., Zhang Y.;
RT   "Two novel Bv8-like peptides from skin secretions of the toad Bombina
RT   maxima.";
RL   Comp. Biochem. Physiol. 134B:509-514(2003).
CC   -!- FUNCTION: Potent agonist for both PKR1/PROKR1 and PKR2/PROKR2, and
CC       inducer of a potent and long-lasting hyperalgesia. Also potentiates
CC       capsaicin-induced TRPV1 current when tested on DRG neurons. At
CC       subnanomolar concentrations, this protein both induces potent
CC       chemotaxis of macrophages and stimulates LPS-induced production of the
CC       pro-inflammatory cytokines IL-1 and IL-12. In vivo, potently stimulates
CC       the contraction of the guinea-pig gastrointestinal (GI) smooth muscle
CC       (nanomolar concentration) and rabbit aortic rings (PubMed:12628381).
CC       {ECO:0000250|UniProtKB:Q9PW66, ECO:0000269|PubMed:12628381}.
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- TISSUE SPECIFICITY: Expressed by the skin glands.
CC   -!- SIMILARITY: Belongs to the AVIT (prokineticin) family. {ECO:0000305}.
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DR   EMBL; AF411091; AAN03822.1; -; mRNA.
DR   AlphaFoldDB; Q8JFQ0; -.
DR   SMR; Q8JFQ0; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0090729; F:toxin activity; IEA:UniProtKB-KW.
DR   InterPro; IPR009523; Prokineticin.
DR   InterPro; IPR023569; Prokineticin_domain.
DR   PANTHER; PTHR18821; PTHR18821; 1.
DR   Pfam; PF06607; Prokineticin; 1.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; Disulfide bond;
KW   G-protein coupled receptor impairing toxin; Secreted; Signal; Toxin.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000269|PubMed:12628381"
FT   CHAIN           20..96
FT                   /note="Prokineticin Bv8-like peptide 2"
FT                   /id="PRO_0000265772"
FT   DISULFID        26..38
FT                   /evidence="ECO:0000250|UniProtKB:Q9PW66"
FT   DISULFID        32..50
FT                   /evidence="ECO:0000250|UniProtKB:Q9PW66"
FT   DISULFID        37..78
FT                   /evidence="ECO:0000250|UniProtKB:Q9PW66"
FT   DISULFID        60..86
FT                   /evidence="ECO:0000250|UniProtKB:Q9PW66"
FT   DISULFID        80..95
FT                   /evidence="ECO:0000250|UniProtKB:Q9PW66"
SQ   SEQUENCE   96 AA;  10198 MW;  EC4EAA5EFE49B2F0 CRC64;
     MKCFAQIVVL LLVIAFSHGA VITGACDRDV QCGSGTCCAA SLWSRNIRFC VPLGNNGEEC
     HPASHKVPYN GKRLSSLCPC KSGLTCSKSG EKFQCS