DEFI_APICA
ID DEFI_APICA Reviewed; 95 AA.
AC Q5J8R1;
DT 15-JUN-2010, integrated into UniProtKB/Swiss-Prot.
DT 15-FEB-2005, sequence version 1.
DT 25-MAY-2022, entry version 39.
DE RecName: Full=Defensin-1;
DE Flags: Precursor;
OS Apis mellifera carnica (Carniolan honeybee).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Hymenoptera; Apocrita; Aculeata; Apoidea; Apidae;
OC Apis.
OX NCBI_TaxID=88217;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND MASS SPECTROMETRY.
RC TISSUE=Head, and Royal jelly;
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).
CC -!- FUNCTION: Found in royal jelly and in hemolymph, potent antibacterial
CC protein against Gram-positive bacteria at low concentration.
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- MASS SPECTROMETRY: Mass=5515.5; Mass_error=3; Method=MALDI;
CC Evidence={ECO:0000269|PubMed:15607651};
CC -!- SIMILARITY: Belongs to the invertebrate defensin family. Type 1
CC subfamily. {ECO:0000255|PROSITE-ProRule:PRU00710}.
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; AY333923; AAR01214.1; -; mRNA.
DR AlphaFoldDB; Q5J8R1; -.
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; Disulfide bond; Immunity; Innate immunity; Secreted; Signal.
FT SIGNAL 1..19
FT /evidence="ECO:0000255"
FT PROPEP 20..43
FT /evidence="ECO:0000250"
FT /id="PRO_0000394507"
FT CHAIN 44..94
FT /note="Defensin-1"
FT /id="PRO_5000091845"
FT MOD_RES 94
FT /note="Phenylalanine amide"
FT /evidence="ECO:0000250"
FT DISULFID 46..74
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00710"
FT DISULFID 60..79
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00710"
FT DISULFID 64..81
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00710"
SQ SEQUENCE 95 AA; 10717 MW; 8689FDC5FC9C6F5A CRC64;
MKIYFIVGLL FMAMVAIMAA PVEDEFEPLE HFENEERADR HRRVTCDLLS FKGQVNDSAC
AANCLSLGKA GGHCEKGVCI CRKTSFKDLW DKRFG