ID   BO8_BOMOR               Reviewed;          96 AA.
AC   Q5W280;
DT   12-DEC-2006, integrated into UniProtKB/Swiss-Prot.
DT   07-DEC-2004, sequence version 1.
DT   25-MAY-2022, entry version 46.
DE   RecName: Full=Prokineticin Bo8;
DE   Flags: Precursor;
OS   Bombina orientalis (Oriental fire-bellied toad).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Bombinatoridae; Bombina.
OX   NCBI_TaxID=8346;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 20-42, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Skin secretion;
RX   PubMed=15652643; DOI=10.1016/j.peptides.2004.10.021;
RA   Chen T., Xue Y., Zhou M., Shaw C.;
RT   "Molecular cloning of mRNA from toad granular gland secretion and
RT   lyophilized skin: identification of Bo8-a novel prokineticin from Bombina
RT   orientalis.";
RL   Peptides 26:377-383(2005).
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). {ECO:0000250|UniProtKB:Q9PW66}.
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- TISSUE SPECIFICITY: Expressed by the skin glands.
CC   -!- MASS SPECTROMETRY: Mass=7990.1; Method=MALDI;
CC       Evidence={ECO:0000269|PubMed:15652643};
CC   -!- SIMILARITY: Belongs to the AVIT (prokineticin) family. {ECO:0000305}.
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DR   EMBL; AJ812217; CAH23218.1; -; mRNA.
DR   AlphaFoldDB; Q5W280; -.
DR   SMR; Q5W280; -.
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:15652643"
FT   CHAIN           20..96
FT                   /note="Prokineticin Bo8"
FT                   /id="PRO_0000265778"
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;  10072 MW;  A7C98547544F7A1B CRC64;
     MKCFAQIVVL LLVIAFSHGA VITGACDRDV QCGSGTCCAA SAWSRNIRFC VPLGNSGEEC
     HPASHKVPYD GKRLSSLCPC KSGLTCSKSG AKFQCS