ID   APD22_APIME             Reviewed;         144 AA.
AC   P35581; P11525; P11526;
DT   01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-1994, sequence version 1.
DT   25-MAY-2022, entry version 79.
DE   RecName: Full=Apidaecins type 22;
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;
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 43-60; 71-88; 99-116 AND 127-144, AND SUBCELLULAR
RP   LOCATION.
RC   TISSUE=Hemolymph {ECO:0000303|PubMed:2676519};
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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; X72576; CAA51168.1; -; mRNA.
DR   PIR; S35331; S35331.
DR   RefSeq; NP_001011642.1; NM_001011642.1.
DR   AlphaFoldDB; P35581; -.
DR   GeneID; 494510; -.
DR   CTD; 494510; -.
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; 4.
PE   1: Evidence at protein level;
KW   Antibiotic; Antimicrobial; Cleavage on pair of basic residues;
KW   Direct protein sequencing; Immunity; Innate immunity; Reference proteome;
KW   Repeat; Secreted; Signal.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000255"
FT   PROPEP          20..42
FT                   /evidence="ECO:0000269|PubMed:2676519"
FT                   /id="PRO_0000004920"
FT   PEPTIDE         43..60
FT                   /note="Apidaecin-1B"
FT                   /id="PRO_0000004921"
FT   PROPEP          63..70
FT                   /evidence="ECO:0000269|PubMed:2676519"
FT                   /id="PRO_0000004922"
FT   PEPTIDE         71..88
FT                   /note="Apidaecin-1B"
FT                   /id="PRO_0000004923"
FT   PROPEP          91..98
FT                   /evidence="ECO:0000269|PubMed:2676519"
FT                   /id="PRO_0000004924"
FT   PEPTIDE         99..116
FT                   /note="Apidaecin-1B"
FT                   /id="PRO_0000004925"
FT   PROPEP          119..126
FT                   /evidence="ECO:0000269|PubMed:2676519"
FT                   /id="PRO_0000004926"
FT   PEPTIDE         127..144
FT                   /note="Apidaecin-1A"
FT                   /id="PRO_0000004927"
FT   REGION          20..144
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   144 AA;  16539 MW;  6FA1AD74CB77108D CRC64;
     MKNFALAILV VTFVVAVFGN TNLDPPTRPT RLRREAEPEA EPGNNRPVYI PQPRPPHPRL
     RREAEPEAEP GNNRPVYIPQ PRPPHPRLRR EAEPEAEPGN NRPVYIPQPR PPHPRLRREA
     EPEAEPGNNR PVYIPQPRPP HPRI