ID   DEF1_DERVA              Reviewed;          74 AA.
AC   Q86QI5;
DT   24-OCT-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   25-MAY-2022, entry version 60.
DE   RecName: Full=Defensin;
DE   AltName: Full=Varisin A1;
DE   Flags: Precursor;
GN   Name=VSNA1;
OS   Dermacentor variabilis (American dog tick).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Chelicerata; Arachnida; Acari;
OC   Parasitiformes; Ixodida; Ixodoidea; Ixodidae; Rhipicephalinae; Dermacentor.
OX   NCBI_TaxID=34621 {ECO:0000312|EMBL:AAO24323.1};
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Hemocyte;
RX   PubMed=14563361; DOI=10.1016/s0965-1748(03)00122-x;
RA   Ceraul S.M., Sonenshine D.E., Ratzlaff R.E., Hynes W.L.;
RT   "An arthropod defensin expressed by the hemocytes of the American dog tick,
RT   Dermacentor variabilis (Acari: Ixodidae).";
RL   Insect Biochem. Mol. Biol. 33:1099-1103(2003).
RN   [2] {ECO:0000305}
RP   PROTEIN SEQUENCE OF 37-66, FUNCTION, SUBCELLULAR LOCATION, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Hemolymph {ECO:0000269|PubMed:11439245};
RX   PubMed=11439245; DOI=10.1016/s0965-1748(01)00031-5;
RA   Johns R., Sonenshine D.E., Hynes W.L.;
RT   "Identification of a defensin from the hemolymph of the American dog tick,
RT   Dermacentor variabilis.";
RL   Insect Biochem. Mol. Biol. 31:857-865(2001).
CC   -!- FUNCTION: Antibacterial activity against Gram-positive and Gram-
CC       negative bacteria. {ECO:0000269|PubMed:11439245}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:11439245}.
CC   -!- TISSUE SPECIFICITY: Hemolymph.
CC   -!- MASS SPECTROMETRY: Mass=4228.66; Method=MALDI;
CC       Evidence={ECO:0000269|PubMed:11439245};
CC   -!- SIMILARITY: Belongs to the invertebrate defensin family. Type 2
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; AY181027; AAO24323.1; -; mRNA.
DR   AlphaFoldDB; Q86QI5; -.
DR   SMR; Q86QI5; -.
DR   GO; GO:0005576; C:extracellular region; IDA:UniProtKB.
DR   GO; GO:0050829; P:defense response to Gram-negative bacterium; IDA:UniProtKB.
DR   GO; GO:0050830; P:defense response to Gram-positive bacterium; IDA:UniProtKB.
DR   Gene3D; 3.30.30.10; -; 1.
DR   InterPro; IPR001542; Defensin_invertebrate/fungal.
DR   InterPro; IPR036574; Scorpion_toxin-like_sf.
DR   Pfam; PF01097; Defensin_2; 1.
DR   SUPFAM; SSF57095; SSF57095; 1.
DR   PROSITE; PS51378; INVERT_DEFENSINS; 1.
PE   1: Evidence at protein level;
KW   Antibiotic; Antimicrobial; Cleavage on pair of basic residues; Defensin;
KW   Direct protein sequencing; Disulfide bond; Secreted; Signal.
FT   SIGNAL          1..22
FT                   /evidence="ECO:0000255"
FT   PROPEP          23..36
FT                   /evidence="ECO:0000305|PubMed:11439245"
FT                   /id="PRO_0000006760"
FT   CHAIN           37..74
FT                   /note="Defensin"
FT                   /evidence="ECO:0000305|PubMed:11439245"
FT                   /id="PRO_0000006761"
FT   DISULFID        40..61
FT                   /evidence="ECO:0000250|UniProtKB:I1T3C7"
FT   DISULFID        47..69
FT                   /evidence="ECO:0000250|UniProtKB:I1T3C7"
FT   DISULFID        51..71
FT                   /evidence="ECO:0000250|UniProtKB:I1T3C7"
FT   CONFLICT        63
FT                   /note="G -> Q (in Ref. 2; AA sequence)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   74 AA;  8040 MW;  A5A29AF4E70DD0BB CRC64;
     MRGLCICLVF LLVCGLVSAT AAAPAESEVA HLRVRRGFGC PLNQGACHNH CRSIRRRGGY
     CSGIIKQTCT CYRN