DLP1_ORNAN
ID DLP1_ORNAN Reviewed; 66 AA.
AC P82172;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 14-OCT-2008, sequence version 2.
DT 03-AUG-2022, entry version 82.
DE RecName: Full=Defensin-like peptide 1 {ECO:0000303|PubMed:10417345};
DE Short=DLP-1 {ECO:0000303|PubMed:10417345};
DE AltName: Full=Ornithorhynchus venom defensin-like peptide C {ECO:0000303|PubMed:18662710};
DE Short=OvDLP-C {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, SYNTHESIS, 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).
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 intestine, kidney, spleen
CC and testis. {ECO:0000269|PubMed:10417345, ECO:0000269|PubMed:18662710}.
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";
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DR PDB; 1B8W; NMR; -; A=25-66.
DR PDBsum; 1B8W; -.
DR AlphaFoldDB; P82172; -.
DR SMR; P82172; -.
DR HOGENOM; CLU_2830578_0_0_1; -.
DR EvolutionaryTrace; P82172; -.
DR Proteomes; UP000002279; Chromosome X2.
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; Direct protein sequencing; Disulfide bond;
KW Reference proteome; Secreted; Signal; Toxin.
FT SIGNAL 1..24
FT /evidence="ECO:0000255"
FT CHAIN 25..66
FT /note="Defensin-like peptide 1"
FT /evidence="ECO:0000269|PubMed:10417345"
FT /id="PRO_0000079932"
FT DISULFID 33..63
FT /evidence="ECO:0000269|PubMed:10417345,
FT ECO:0000312|PDB:1B8W"
FT DISULFID 40..56
FT /evidence="ECO:0000269|PubMed:10417345,
FT ECO:0000312|PDB:1B8W"
FT DISULFID 48..64
FT /evidence="ECO:0000269|PubMed:10417345,
FT ECO:0000312|PDB:1B8W"
FT CONFLICT 60
FT /note="E -> G (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT HELIX 34..36
FT /evidence="ECO:0007829|PDB:1B8W"
FT STRAND 39..42
FT /evidence="ECO:0007829|PDB:1B8W"
FT STRAND 46..48
FT /evidence="ECO:0007829|PDB:1B8W"
FT STRAND 57..64
FT /evidence="ECO:0007829|PDB:1B8W"
SQ SEQUENCE 66 AA; 7518 MW; C338407A4788CB68 CRC64;
MRLAYLLLLL VAVLFQAGGG SVEAFVQHRP RDCESINGVC RHKDTVNCRE IFLADCYNDE
QKCCRK
