ID   MCDP_APIME              Reviewed;          50 AA.
AC   P01499;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 2.
DT   25-MAY-2022, entry version 103.
DE   RecName: Full=Mast cell degranulating peptide;
DE            Short=MCD peptide;
DE            Short=MCDP;
DE   AltName: Full=Peptide 401;
DE   Flags: Precursor;
OS   Apis mellifera (Honeybee).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Hymenoptera; Apocrita; Aculeata; Apoidea; Apidae;
OC   Apis.
OX   NCBI_TaxID=7460;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND AMIDATION AT ASN-49.
RC   TISSUE=Venom gland;
RX   PubMed=7759523; DOI=10.1074/jbc.270.21.12704;
RA   Gmachl M., Kreil G.;
RT   "The precursors of the bee venom constituents apamin and MCD peptide are
RT   encoded by two genes in tandem which share the same 3'-exon.";
RL   J. Biol. Chem. 270:12704-12708(1995).
RN   [2]
RP   PROTEIN SEQUENCE OF 28-49.
RC   TISSUE=Venom;
RX   PubMed=5789872;
RA   Haux P.;
RT   "Amino acid sequence of MCD-peptide, a specific mast cell-degranulating
RT   peptide from bee venom.";
RL   Hoppe-Seyler's Z. Physiol. Chem. 350:536-546(1969).
RN   [3]
RP   PARTIAL PROTEIN SEQUENCE, FORMYLATION AT LYS-29; LYS-44 AND LYS-48, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY.
RA   Doonan S., Garman A.J., Hanson J.M., Loudon A.G., Vernon C.A.;
RT   "Identification by mass spectrometry of N(epsilon)-formyl-lysine.";
RL   J. Chem. Soc. Perkin Trans. I 12:1157-1160(1978).
RN   [4]
RP   DISULFIDE BONDS.
RX   PubMed=4582672; DOI=10.1038/245163a0;
RA   Billingham M.E.J., Morley J., Hanson J.M., Shipolini R.A., Vernon C.A.;
RT   "An anti-inflammatory peptide from bee venom.";
RL   Nature 245:163-164(1973).
RN   [5]
RP   REVIEW.
RX   PubMed=1703229; DOI=10.1111/j.2042-7158.1990.tb06595.x;
RA   Ziai M.R., Russek S., Wang H.-C., Beer B., Blume A.J.;
RT   "Mast cell degranulating peptide: a multi-functional neurotoxin.";
RL   J. Pharm. Pharmacol. 42:457-461(1990).
CC   -!- FUNCTION: Potent anti-inflammatory agent. At low concentrations,
CC       mediates the degranulation of mast cells thus evoking an inflammatory
CC       response. Also acts as a neurotoxin capable of blocking a class of
CC       voltage-gated potassium channels.
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom gland.
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DR   EMBL; S78459; AAB34403.1; -; mRNA.
DR   PIR; B56710; MDHB.
DR   RefSeq; NP_001011611.2; NM_001011611.2.
DR   AlphaFoldDB; P01499; -.
DR   STRING; 7460.GB40696-PA; -.
DR   PaxDb; P01499; -.
DR   GeneID; 406134; -.
DR   KEGG; ame:406134; -.
DR   CTD; 406134; -.
DR   Proteomes; UP000005203; Unplaced.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0015459; F:potassium channel regulator activity; IEA:UniProtKB-KW.
DR   GO; GO:0090729; F:toxin activity; IEA:UniProtKB-KW.
DR   GO; GO:0043303; P:mast cell degranulation; IEA:UniProtKB-KW.
DR   InterPro; IPR035361; Bee_toxin.
DR   Pfam; PF17454; Bee_toxin; 1.
PE   1: Evidence at protein level;
KW   Amidation; Direct protein sequencing; Disulfide bond; Formylation;
KW   Ion channel impairing toxin; Mast cell degranulation; Neurotoxin;
KW   Potassium channel impairing toxin; Reference proteome; Secreted; Signal;
KW   Toxin.
FT   SIGNAL          1..27
FT                   /evidence="ECO:0000269|PubMed:5789872"
FT   PEPTIDE         28..49
FT                   /note="Mast cell degranulating peptide"
FT                   /evidence="ECO:0000269|PubMed:5789872"
FT                   /id="PRO_0000018613"
FT   MOD_RES         29
FT                   /note="N6-formyllysine; partial"
FT                   /evidence="ECO:0000269|Ref.3"
FT   MOD_RES         44
FT                   /note="N6-formyllysine; partial"
FT                   /evidence="ECO:0000269|Ref.3"
FT   MOD_RES         48
FT                   /note="N6-formyllysine; partial"
FT                   /evidence="ECO:0000269|Ref.3"
FT   MOD_RES         49
FT                   /note="Asparagine amide"
FT                   /evidence="ECO:0000269|PubMed:7759523"
FT   DISULFID        30..42
FT                   /evidence="ECO:0000269|PubMed:4582672"
FT   DISULFID        32..46
FT                   /evidence="ECO:0000269|PubMed:4582672"
SQ   SEQUENCE   50 AA;  5781 MW;  FB9A61F8A68B17AA CRC64;
     MISMLRCTFF FLSVILITSY FVTPTMSIKC NCKRHVIKPH ICRKICGKNG