ID   PROTO_ICASP             Reviewed;          13 AA.
AC   P17237;
DT   01-AUG-1990, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1990, sequence version 1.
DT   29-SEP-2021, entry version 49.
DE   RecName: Full=Chemotactic peptide {ECO:0000303|Ref.1};
DE            Short=I-CP {ECO:0000303|Ref.1};
OS   Icaria sp. (Ropalidian wasp).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Hymenoptera; Apocrita; Aculeata; Vespoidea;
OC   Vespidae; Polistinae; Ropalidiini; Icaria; unclassified Icaria.
OX   NCBI_TaxID=7495;
RN   [1]
RP   PROTEIN SEQUENCE, AMIDATION AT THR-13, AND SUBCELLULAR LOCATION.
RC   TISSUE=Venom;
RA   Yasuhara T., Itokawa H., Suzuki N., Nakamura H., Nakajima T.;
RL   (In) Izumiya N. (eds.);
RL   Peptide chemistry 1984, pp.177-182, Protein Research Foundation, Osaka
RL   (1985).
CC   -!- FUNCTION: Mast cell degranulating peptide. Induces the chemotaxis of
CC       neutrophils.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|Ref.1}.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom gland. {ECO:0000305|Ref.1}.
CC   -!- SIMILARITY: Belongs to the MCD family. Protonectin subfamily.
CC       {ECO:0000305}.
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DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0006935; P:chemotaxis; IEA:UniProtKB-KW.
DR   GO; GO:0043303; P:mast cell degranulation; IEA:UniProtKB-KW.
PE   1: Evidence at protein level;
KW   Amidation; Chemotaxis; Direct protein sequencing; Mast cell degranulation;
KW   Secreted.
FT   PEPTIDE         1..13
FT                   /note="Chemotactic peptide"
FT                   /evidence="ECO:0000269|Ref.1"
FT                   /id="PRO_0000044043"
FT   MOD_RES         13
FT                   /note="Threonine amide"
FT                   /evidence="ECO:0000269|Ref.1"
SQ   SEQUENCE   13 AA;  1353 MW;  348DBC7AA30A3768 CRC64;
     IVPFLGPLLG LLT