ID   DEFI_APIME              Reviewed;          95 AA.
AC   P17722; C7AHT1; Q5MY57; Q9BMA5;
DT   01-AUG-1990, integrated into UniProtKB/Swiss-Prot.
DT   15-JUN-2010, sequence version 3.
DT   25-MAY-2022, entry version 110.
DE   RecName: Full=Defensin-1;
DE   AltName: Full=Royalisin;
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 [GENOMIC DNA], AND TISSUE SPECIFICITY.
RX   PubMed=15607651; DOI=10.1016/j.ibmb.2004.09.007;
RA   Klaudiny J., Albert S., Bachanova K., Kopernicky J., Simuth J.;
RT   "Two structurally different defensin genes, one of them encoding a novel
RT   defensin isoform, are expressed in honeybee Apis mellifera.";
RL   Insect Biochem. Mol. Biol. 35:11-22(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND AMIDATION AT PHE-94.
RC   TISSUE=Hemolymph;
RX   PubMed=7961803; DOI=10.1016/s0021-9258(19)61943-5;
RA   Casteels-Josson K., Zhang W., Capaci T., Casteels P., Tempst P.;
RT   "Acute transcriptional response of the honeybee peptide-antibiotics gene
RT   repertoire and required post-translational conversion of the precursor
RT   structures.";
RL   J. Biol. Chem. 269:28569-28575(1994).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 18-95.
RX   PubMed=19387012; DOI=10.1093/molbev/msp086;
RA   Viljakainen L., Evans J.D., Hasselmann M., Rueppell O., Tingek S.,
RA   Pamilo P.;
RT   "Rapid evolution of immune proteins in social insects.";
RL   Mol. Biol. Evol. 26:1791-1801(2009).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 26-82.
RC   TISSUE=Thorax;
RA   Lvov A.V., Nikolenko A.G., Chemeris A.V., Sabirganov B.E.;
RT   "Polymorphism defensin gene of South Ural honeybee Apis mellifera.";
RL   Submitted (FEB-2001) to the EMBL/GenBank/DDBJ databases.
RN   [5]
RP   PROTEIN SEQUENCE OF 44-94, AND DISULFIDE BONDS.
RC   TISSUE=Royal jelly;
RX   PubMed=2358464; DOI=10.1016/s0021-9258(19)38596-5;
RA   Fujiwara S., Imai J., Fujiwara M., Yaeshima T., Kawashima T., Kobayashi K.;
RT   "A potent antibacterial protein in royal jelly. Purification and
RT   determination of the primary structure of royalisin.";
RL   J. Biol. Chem. 265:11333-11337(1990).
CC   -!- FUNCTION: Found in royal jelly and in hemolymph, potent antibacterial
CC       protein against Gram-positive bacteria at low concentration.
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- TISSUE SPECIFICITY: High expression in head, hypopharyngeal gland, and
CC       mandibular gland. Low expression in thorax and thoracic salivary gland.
CC       {ECO:0000269|PubMed:15607651}.
CC   -!- SIMILARITY: Belongs to the invertebrate defensin family. Type 1
CC       subfamily. {ECO:0000255|PROSITE-ProRule:PRU00710}.
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DR   EMBL; AY496432; AAS75803.1; -; Genomic_DNA.
DR   EMBL; U15955; AAA67443.1; -; mRNA.
DR   EMBL; FJ546136; ACT66903.1; -; mRNA.
DR   EMBL; AJ308527; CAC33429.1; -; Genomic_DNA.
DR   PIR; C55392; C55392.
DR   RefSeq; NP_001011616.2; NM_001011616.2.
DR   AlphaFoldDB; P17722; -.
DR   STRING; 7460.GB41428-PA; -.
DR   PaxDb; P17722; -.
DR   EnsemblMetazoa; NM_001011616; NP_001011616; GeneID_406143.
DR   GeneID; 406143; -.
DR   KEGG; ame:406143; -.
DR   CTD; 406143; -.
DR   eggNOG; ENOG502T7DA; Eukaryota.
DR   HOGENOM; CLU_174272_0_0_1; -.
DR   InParanoid; P17722; -.
DR   OMA; ANEDGFM; -.
DR   OrthoDB; 1600872at2759; -.
DR   PhylomeDB; P17722; -.
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   Gene3D; 3.30.30.10; -; 1.
DR   InterPro; IPR017982; Defensin_insect.
DR   InterPro; IPR001542; Defensin_invertebrate/fungal.
DR   InterPro; IPR003614; Scorpion_toxin-like.
DR   InterPro; IPR036574; Scorpion_toxin-like_sf.
DR   Pfam; PF01097; Defensin_2; 1.
DR   PRINTS; PR00271; DEFENSIN.
DR   SMART; SM00505; Knot1; 1.
DR   SUPFAM; SSF57095; SSF57095; 1.
DR   PROSITE; PS51378; INVERT_DEFENSINS; 1.
PE   1: Evidence at protein level;
KW   Amidation; Antibiotic; Antimicrobial; Cleavage on pair of basic residues;
KW   Defensin; Direct protein sequencing; Disulfide bond; Immunity;
KW   Innate immunity; Reference proteome; Secreted; Signal.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000255"
FT   PROPEP          20..43
FT                   /evidence="ECO:0000269|PubMed:2358464"
FT                   /id="PRO_0000006740"
FT   CHAIN           44..94
FT                   /note="Defensin-1"
FT                   /id="PRO_0000006741"
FT   MOD_RES         94
FT                   /note="Phenylalanine amide"
FT                   /evidence="ECO:0000305|PubMed:7961803"
FT   DISULFID        46..74
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00710,
FT                   ECO:0000269|PubMed:2358464"
FT   DISULFID        60..79
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00710,
FT                   ECO:0000269|PubMed:2358464"
FT   DISULFID        64..81
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00710,
FT                   ECO:0000269|PubMed:2358464"
FT   CONFLICT        65
FT                   /note="L -> H (in Ref. 4; CAC33429)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        77..78
FT                   /note="GV -> VG (in Ref. 2; AAA67443)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        93
FT                   /note="R -> Y (in Ref. 5; AA sequence)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   95 AA;  10717 MW;  8689FDC5FC9C6F5A CRC64;
     MKIYFIVGLL FMAMVAIMAA PVEDEFEPLE HFENEERADR HRRVTCDLLS FKGQVNDSAC
     AANCLSLGKA GGHCEKGVCI CRKTSFKDLW DKRFG