ID   APD73_APIME             Reviewed;         283 AA.
AC   Q06602; P11525; P11526;
DT   01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-1994, sequence version 1.
DT   25-MAY-2022, entry version 76.
DE   RecName: Full=Apidaecins type 73;
DE   Contains:
DE     RecName: Full=Apidaecin;
DE   Contains:
DE     RecName: Full=Apidaecin-1B;
DE     AltName: Full=Apidaecin IB;
DE   Contains:
DE     RecName: Full=Apidaecin-1A;
DE     AltName: Full=Apidaecin IA;
DE   Flags: Precursor; Fragment;
GN   Name=APID73;
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].
RX   PubMed=8467807; DOI=10.1002/j.1460-2075.1993.tb05801.x;
RA   Casteels-Josson K., Capaci T., Casteels P., Tempst P.;
RT   "Apidaecin multipeptide precursor structure: a putative mechanism for
RT   amplification of the insect antibacterial response.";
RL   EMBO J. 12:1569-1578(1993).
RN   [2]
RP   PROTEIN SEQUENCE OF 42-59 AND 266-283, FUNCTION, AND SUBCELLULAR LOCATION.
RC   TISSUE=Hemolymph {ECO:0000303|PubMed:7929322};
RX   PubMed=2676519; DOI=10.1002/j.1460-2075.1989.tb08368.x;
RA   Casteels P., Ampe C., Jacobs F., Vaeck M., Tempst P.;
RT   "Apidaecins: antibacterial peptides from honeybees.";
RL   EMBO J. 8:2387-2391(1989).
RN   [3]
RP   FUNCTION OF APIDAECIN-1B, SUBCELLULAR LOCATION, AND MASS SPECTROMETRY.
RC   TISSUE=Hemolymph {ECO:0000303|PubMed:7929322};
RX   PubMed=7929322; DOI=10.1016/s0021-9258(18)47165-7;
RA   Casteels P., Romagnolo J., Castle M., Casteels-Josson K.,
RA   Erdjument-Bromage H., Tempst P.;
RT   "Biodiversity of apidaecin-type peptide antibiotics. Prospects of
RT   manipulating the antibacterial spectrum and combating acquired
RT   resistance.";
RL   J. Biol. Chem. 269:26107-26115(1994).
CC   -!- FUNCTION: Apidaecins have bactericidal activity; predominantly against
CC       Gram-negative bacteria (PubMed:2676519, PubMed:7929322). They seem to
CC       interfere with cell propagation (PubMed:2676519).
CC       {ECO:0000269|PubMed:2676519, ECO:0000269|PubMed:7929322}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:2676519,
CC       ECO:0000269|PubMed:7929322}.
CC   -!- MASS SPECTROMETRY: [Apidaecin-1B]: Mass=2110.0; Method=MALDI;
CC       Note=Apidaecin-1B.; Evidence={ECO:0000269|PubMed:7929322};
CC   -!- SIMILARITY: Belongs to the apidaecin family. {ECO:0000305}.
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DR   EMBL; X72577; CAA51169.1; -; mRNA.
DR   PIR; S06675; S06675.
DR   PIR; S35332; S35332.
DR   PDB; 4E81; X-ray; 1.90 A; C/D=268-279.
DR   PDBsum; 4E81; -.
DR   AlphaFoldDB; Q06602; -.
DR   SMR; Q06602; -.
DR   PaxDb; Q06602; -.
DR   Proteomes; UP000005203; Unplaced.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0042742; P:defense response to bacterium; IEA:UniProtKB-KW.
DR   GO; GO:0045087; P:innate immune response; IEA:UniProtKB-KW.
DR   InterPro; IPR004828; Apidaecin.
DR   Pfam; PF00807; Apidaecin; 9.
PE   1: Evidence at protein level;
KW   3D-structure; Antibiotic; Antimicrobial;
KW   Cleavage on pair of basic residues; Direct protein sequencing; Immunity;
KW   Innate immunity; Reference proteome; Repeat; Secreted; Signal.
FT   SIGNAL          <1..18
FT                   /evidence="ECO:0000255"
FT   PROPEP          19..41
FT                   /evidence="ECO:0000269|PubMed:2676519"
FT                   /id="PRO_0000004928"
FT   PEPTIDE         42..59
FT                   /note="Apidaecin-1B"
FT                   /id="PRO_0000004929"
FT   PROPEP          62..69
FT                   /id="PRO_0000004930"
FT   PEPTIDE         70..87
FT                   /note="Apidaecin-1B"
FT                   /id="PRO_0000004931"
FT   PROPEP          90..97
FT                   /id="PRO_0000004932"
FT   PEPTIDE         98..115
FT                   /note="Apidaecin"
FT                   /id="PRO_0000004933"
FT   PROPEP          118..125
FT                   /id="PRO_0000004934"
FT   PEPTIDE         126..143
FT                   /note="Apidaecin-1B"
FT                   /id="PRO_0000004935"
FT   PROPEP          146..153
FT                   /id="PRO_0000004936"
FT   PEPTIDE         154..171
FT                   /note="Apidaecin"
FT                   /id="PRO_0000004937"
FT   PROPEP          174..181
FT                   /id="PRO_0000004938"
FT   PEPTIDE         182..199
FT                   /note="Apidaecin-1B"
FT                   /id="PRO_0000004939"
FT   PROPEP          202..209
FT                   /id="PRO_0000004940"
FT   PEPTIDE         210..227
FT                   /note="Apidaecin-1B"
FT                   /id="PRO_0000004941"
FT   PROPEP          230..237
FT                   /id="PRO_0000004942"
FT   PEPTIDE         238..255
FT                   /note="Apidaecin-1B"
FT                   /id="PRO_0000004943"
FT   PROPEP          258..265
FT                   /evidence="ECO:0000269|PubMed:2676519"
FT                   /id="PRO_0000004944"
FT   PEPTIDE         266..283
FT                   /note="Apidaecin-1A"
FT                   /id="PRO_0000004945"
FT   REGION          19..283
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   NON_TER         1
SQ   SEQUENCE   283 AA;  32695 MW;  4EA5FEDECD5E142B CRC64;
     KNFALAILVV TFVVAVFGNT NLDPPTRPTR LRREAKPEAE PGNNRPVYIP QPRPPHPRLR
     REAEPEAEPG NNRPVYIPQP RPPHPRLRRE AELEAEPGNN RPVYISQPRP PHPRLRREAE
     PEAEPGNNRP VYIPQPRPPH PRLRREAELE AEPGNNRPVY ISQPRPPHPR LRREAEPEAE
     PGNNRPVYIP QPRPPHPRLR REAEPEAEPG NNRPVYIPQP RPPHPRLRRE AEPEAEPGNN
     RPVYIPQPRP PHPRLRREAK PEAKPGNNRP VYIPQPRPPH PRI