DEFBL_ORNAN
ID DEFBL_ORNAN Reviewed; 68 AA.
AC P0C8B1;
DT 14-OCT-2008, integrated into UniProtKB/Swiss-Prot.
DT 14-OCT-2008, sequence version 1.
DT 03-AUG-2022, entry version 20.
DE RecName: Full=Venom-like beta-defensin {ECO:0000303|PubMed:18463304};
DE Short=DefB-vL {ECO:0000303|PubMed:18463304};
DE Short=Defensin-BvL {ECO:0000303|PubMed:18463304};
DE Short=OaDefB-vL {ECO:0000303|PubMed:18662710};
DE AltName: Full=Intermediate defensin-like peptide {ECO:0000303|PubMed:24694388};
DE Short=Int-DLP {ECO:0000303|PubMed:24694388};
DE AltName: Full=Ornithorhynchus venom defensin-like peptide {ECO:0000303|PubMed:18463304};
DE Short=OvDLP {ECO:0000303|PubMed:18463304, 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 SYNTHESIS OF 25-68.
RX PubMed=18463304; DOI=10.1101/gr.7149808;
RA Whittington C.M., Papenfuss A.T., Bansal P., Torres A.M., Wong E.S.,
RA Deakin J.E., Graves T., Alsop A., Schatzkamer K., Kremitzki C.,
RA Ponting C.P., Temple-Smith P., Warren W.C., Kuchel P.W., Belov K.;
RT "Defensins and the convergent evolution of platypus and reptile venom
RT genes.";
RL Genome Res. 18:986-994(2008).
RN [2]
RP TISSUE SPECIFICITY.
RC TISSUE=Brain, Kidney, Liver, Lung, Spleen, and Testis;
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 [3]
RP STRUCTURE BY NMR OF 25-68, DISULFIDE BOND, SYNTHESIS OF 25-68, FUNCTION,
RP AND MUTAGENESIS OF 25-ARG--ARG-28.
RX PubMed=24694388; DOI=10.1016/j.febslet.2014.03.044;
RA Torres A.M., Bansal P., Koh J.M., Pages G., Wu M.J., Kuchel P.W.;
RT "Structure and antimicrobial activity of platypus 'intermediate' defensin-
RT like peptide.";
RL FEBS Lett. 588:1821-1826(2014).
CC -!- FUNCTION: Potent antimicrobial peptide that displays activity against
CC S.aureus and P.aeruginosa (PubMed:24694388). Does not inhibit growth of
CC E.coli (PubMed:24694388). {ECO:0000269|PubMed:24694388}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Highly expressed in intestine, liver and spleen and
CC expressed at lower levels in brain, kidney, lung, testis and venom
CC gland. {ECO:0000269|PubMed:18662710}.
CC -!- DOMAIN: The 4 N-terminal Arg residues do not affect the overall fold,
CC but are important for the antimicrobial potency.
CC {ECO:0000269|PubMed:24694388}.
CC -!- WEB RESOURCE: Name=Platypus resources;
CC URL="https://www.twinkl.ch/search?q=platypus";
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; 2MN3; NMR; -; A=25-68.
DR PDBsum; 2MN3; -.
DR AlphaFoldDB; P0C8B1; -.
DR BMRB; P0C8B1; -.
DR SMR; P0C8B1; -.
DR Ensembl; ENSOANT00000060174; ENSOANP00000045696; ENSOANG00000047887.
DR Proteomes; UP000002279; Chromosome X2.
DR Bgee; ENSOANG00000047887; Expressed in liver and 2 other tissues.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0042742; P:defense response to bacterium; IEA:UniProtKB-KW.
DR Gene3D; 2.20.20.10; -; 1.
DR InterPro; IPR023355; Myo_ane_neurotoxin_sf.
PE 1: Evidence at protein level;
KW 3D-structure; Antibiotic; Antimicrobial; Defensin; Disulfide bond;
KW Reference proteome; Secreted; Signal.
FT SIGNAL 1..24
FT /evidence="ECO:0000305|PubMed:18463304,
FT ECO:0000305|PubMed:24694388"
FT CHAIN 25..68
FT /note="Venom-like beta-defensin"
FT /evidence="ECO:0000305|PubMed:18463304,
FT ECO:0000305|PubMed:24694388"
FT /id="PRO_0000352730"
FT DISULFID 33..60
FT /evidence="ECO:0000269|PubMed:24694388,
FT ECO:0000312|PDB:2MN3"
FT DISULFID 40..54
FT /evidence="ECO:0000269|PubMed:24694388,
FT ECO:0000312|PDB:2MN3"
FT DISULFID 47..61
FT /evidence="ECO:0000269|PubMed:24694388,
FT ECO:0000312|PDB:2MN3"
FT MUTAGEN 25..28
FT /note="Missing: Decrease in antimicrobial potency, but no
FT change in overall fold."
FT /evidence="ECO:0000269|PubMed:24694388"
FT HELIX 32..35
FT /evidence="ECO:0007829|PDB:2MN3"
FT STRAND 39..41
FT /evidence="ECO:0007829|PDB:2MN3"
FT STRAND 43..52
FT /evidence="ECO:0007829|PDB:2MN3"
FT STRAND 59..62
FT /evidence="ECO:0007829|PDB:2MN3"
SQ SEQUENCE 68 AA; 7455 MW; 6F73547C6E116277 CRC64;
MRLLILFLAV VTLLSLAGPG SAEVRRRRRR PPCEDVNGQC QPRGNPCLRL RGACPRGSRC
CMPTVAAH
