DLP2_ORNAN
ID DLP2_ORNAN Reviewed; 66 AA.
AC P82140;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 14-OCT-2008, sequence version 2.
DT 03-AUG-2022, entry version 85.
DE RecName: Full=Defensin-like peptide 2/4 {ECO:0000303|PubMed:10417345};
DE Short=DLP-2/DLP-4 {ECO:0000303|PubMed:10417345};
DE AltName: Full=Ornithorhynchus venom defensin-like peptide B {ECO:0000303|PubMed:18662710};
DE Short=OvDLP-B {ECO:0000303|PubMed:18662710};
DE Flags: Precursor;
OS Ornithorhynchus anatinus (Duckbill platypus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Monotremata; Ornithorhynchidae; Ornithorhynchus.
OX NCBI_TaxID=9258;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RX PubMed=18662710; DOI=10.1016/j.toxicon.2008.07.002;
RA Whittington C.M., Papenfuss A.T., Kuchel P.W., Belov K.;
RT "Expression patterns of platypus defensin and related venom genes across a
RT range of tissue types reveal the possibility of broader functions for
RT OvDLPs than previously suspected.";
RL Toxicon 52:559-565(2008).
RN [2]
RP PROTEIN SEQUENCE OF 25-66, FUNCTION, SUBCELLULAR LOCATION, TISSUE
RP SPECIFICITY, STRUCTURE BY NMR OF 25-66, AND DISULFIDE BOND.
RC TISSUE=Venom, and Venom gland;
RX PubMed=10417345; DOI=10.1042/bj3410785;
RA Torres A.M., Wang X., Fletcher J.I., Alewood D., Alewood P.F., Smith R.,
RA Simpson R.J., Nicholson G.M., Sutherland S.K., Gallagher C.H., King G.F.,
RA Kuchel P.W.;
RT "Solution structure of a defensin-like peptide from platypus venom.";
RL Biochem. J. 341:785-794(1999).
RN [3]
RP PROTEIN SEQUENCE OF 25-66, STRUCTURE BY NMR OF 25-66, AND DISULFIDE BOND.
RC TISSUE=Venom;
RX PubMed=10839998; DOI=10.1042/bj3480649;
RA Torres A.M., de Plater G.M., Doverskog M., Birinyi-Strachan L.C.,
RA Nicholson G.M., Gallagher C.H., Kuchel P.W.;
RT "Defensin-like peptide-2 from platypus venom: member of a class of peptides
RT with a distinct structural fold.";
RL Biochem. J. 348:649-656(2000).
RN [4]
RP D-AMINO ACID AT MET-26, TISSUE SPECIFICITY, STRUCTURE BY NMR OF 25-66, AND
RP DISULFIDE BOND.
RX PubMed=16033333; DOI=10.1042/bj20050900;
RA Torres A.M., Tsampazi C., Geraghty D.P., Bansal P.S., Alewood P.F.,
RA Kuchel P.W.;
RT "D-amino acid residue in a defensin-like peptide from platypus venom:
RT effect on structure and chromatographic properties.";
RL Biochem. J. 391:215-220(2005).
CC -!- FUNCTION: Does not show antimicrobial, myotoxic, hemolytic and cell-
CC promoting activities. {ECO:0000269|PubMed:10417345}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:10417345}.
CC -!- TISSUE SPECIFICITY: Produced by the crural gland and detected in venom
CC from the spur located on each male hind leg. Is also widely expressed
CC in both male and female tissues, including brain, intestine, kidney,
CC lung, spleen and testis. {ECO:0000269|PubMed:10417345,
CC ECO:0000269|PubMed:16033333, ECO:0000269|PubMed:18662710}.
CC -!- PTM: Stereoinversion of L-Met-26 (in DLP-4) to D-Met-26 (in DLP-2).
CC {ECO:0000269|PubMed:16033333}.
CC -!- WEB RESOURCE: Name=Platypus resources;
CC URL="https://www.twinkl.ch/search?q=platypus";
CC -!- WEB RESOURCE: Name=Protein Spotlight; Note=Platypus poison - Issue 29
CC of December 2002;
CC URL="https://web.expasy.org/spotlight/back_issues/029";
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 PDB; 1D6B; NMR; -; A=25-66.
DR PDB; 1ZUE; NMR; -; A=25-66.
DR PDB; 1ZUF; NMR; -; A=25-66.
DR PDBsum; 1D6B; -.
DR PDBsum; 1ZUE; -.
DR PDBsum; 1ZUF; -.
DR AlphaFoldDB; P82140; -.
DR SMR; P82140; -.
DR Ensembl; ENSOANT00000002832; ENSOANP00000002831; ENSOANG00000001780.
DR HOGENOM; CLU_2830578_0_0_1; -.
DR EvolutionaryTrace; P82140; -.
DR Proteomes; UP000002279; Chromosome X2.
DR Bgee; ENSOANG00000001780; Expressed in testis and 4 other tissues.
DR GO; GO:0005576; C:extracellular region; IDA:UniProtKB.
DR GO; GO:0090729; F:toxin activity; IEA:UniProtKB-KW.
DR Gene3D; 2.20.20.10; -; 1.
DR InterPro; IPR012553; Defensin_3.
DR InterPro; IPR023355; Myo_ane_neurotoxin_sf.
DR Pfam; PF08131; Defensin_3; 1.
PE 1: Evidence at protein level;
KW 3D-structure; D-amino acid; Direct protein sequencing; Disulfide bond;
KW Reference proteome; Secreted; Signal; Toxin.
FT SIGNAL 1..22
FT /evidence="ECO:0000255"
FT PROPEP 23..24
FT /evidence="ECO:0000269|PubMed:10417345,
FT ECO:0000269|PubMed:10839998"
FT /id="PRO_0000352673"
FT CHAIN 25..66
FT /note="Defensin-like peptide 2/4"
FT /evidence="ECO:0000269|PubMed:10417345,
FT ECO:0000269|PubMed:10839998"
FT /id="PRO_0000079933"
FT MOD_RES 26
FT /note="D-methionine; in form DLP-2"
FT /evidence="ECO:0000269|PubMed:16033333"
FT DISULFID 33..63
FT /evidence="ECO:0000269|PubMed:10417345,
FT ECO:0000269|PubMed:10839998, ECO:0000269|PubMed:16033333,
FT ECO:0000312|PDB:1D6B, ECO:0000312|PDB:1ZUE,
FT ECO:0000312|PDB:1ZUF"
FT DISULFID 40..56
FT /evidence="ECO:0000269|PubMed:10417345,
FT ECO:0000269|PubMed:10839998, ECO:0000269|PubMed:16033333,
FT ECO:0000312|PDB:1D6B, ECO:0000312|PDB:1ZUE,
FT ECO:0000312|PDB:1ZUF"
FT DISULFID 48..64
FT /evidence="ECO:0000269|PubMed:10417345,
FT ECO:0000269|PubMed:10839998, ECO:0000269|PubMed:16033333,
FT ECO:0000312|PDB:1D6B, ECO:0000312|PDB:1ZUE,
FT ECO:0000312|PDB:1ZUF"
FT STRAND 30..32
FT /evidence="ECO:0007829|PDB:1ZUF"
FT HELIX 33..36
FT /evidence="ECO:0007829|PDB:1D6B"
FT STRAND 39..42
FT /evidence="ECO:0007829|PDB:1D6B"
FT STRAND 53..55
FT /evidence="ECO:0007829|PDB:1ZUF"
FT STRAND 61..64
FT /evidence="ECO:0007829|PDB:1D6B"
SQ SEQUENCE 66 AA; 7599 MW; 1825CB894D077B7B CRC64;
MRLAYLLLLL VAVLFQAGGG SAKPIMFFEM QACWSHSGVC RDKSERNCKP MAWTYCENRN
QKCCEY
