ID   BM8C_BOMMX              Reviewed;          96 AA.
AC   Q8JFY1;
DT   12-DEC-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2002, sequence version 1.
DT   25-MAY-2022, entry version 46.
DE   RecName: Full=Prokineticin Bm8-c;
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].
RC   TISSUE=Skin secretion;
RX   PubMed=12413397; DOI=10.1042/bj20021343;
RA   Chen T., Farragher S.M., Bjourson A.J., Orr D.F., Rao P., Shaw C.;
RT   "Granular gland transcriptomes in stimulated amphibian skin secretions.";
RL   Biochem. J. 371:125-130(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). {ECO:0000250|UniProtKB:Q9PW66}.
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; AJ440232; CAD29342.1; -; mRNA.
DR   AlphaFoldDB; Q8JFY1; -.
DR   SMR; Q8JFY1; -.
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   2: Evidence at transcript level;
KW   Disulfide bond; G-protein coupled receptor impairing toxin; Secreted;
KW   Signal; Toxin.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000250|UniProtKB:Q9PW66"
FT   CHAIN           20..96
FT                   /note="Prokineticin Bm8-c"
FT                   /id="PRO_0000265774"
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;  10103 MW;  227EA1A5C49B18A6 CRC64;
     MKCFAQIVVL LLVIAFSHGA VITGVCDRDA QCGSGTCCAA SAFSRNVRFC VPLGNNGEEC
     HPASHKVPYN GKRLSSLCPC NTGLTCSKSG EKFQCS