DEFA1_ORNAN
ID DEFA1_ORNAN Reviewed; 98 AA.
AC P0C8A1;
DT 14-OCT-2008, integrated into UniProtKB/Swiss-Prot.
DT 14-OCT-2008, sequence version 1.
DT 03-AUG-2022, entry version 28.
DE RecName: Full=Defensin-A1 {ECO:0000305|PubMed:18463304, ECO:0000305|PubMed:18662710};
DE Short=DefA1 {ECO:0000303|PubMed:18463304};
DE Short=OaDefA1 {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].
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.
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).
CC -!- FUNCTION: Has antimicrobial activity. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Highly expressed in intestine, and expressed at
CC lower levels in lung and spleen. {ECO:0000269|PubMed:18662710}.
CC -!- SIMILARITY: Belongs to the alpha-defensin family. {ECO:0000305}.
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 AlphaFoldDB; P0C8A1; -.
DR SMR; P0C8A1; -.
DR Ensembl; ENSOANT00000040883; ENSOANP00000031636; ENSOANG00000031301.
DR GeneTree; ENSGT01000000220353; -.
DR Proteomes; UP000002279; Chromosome X2.
DR Bgee; ENSOANG00000031301; Expressed in testis.
DR GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR GO; GO:0019731; P:antibacterial humoral response; IBA:GO_Central.
DR GO; GO:0061844; P:antimicrobial humoral immune response mediated by antimicrobial peptide; IBA:GO_Central.
DR GO; GO:0071222; P:cellular response to lipopolysaccharide; IBA:GO_Central.
DR GO; GO:0050829; P:defense response to Gram-negative bacterium; IBA:GO_Central.
DR GO; GO:0050830; P:defense response to Gram-positive bacterium; IBA:GO_Central.
DR GO; GO:0002227; P:innate immune response in mucosa; IBA:GO_Central.
DR GO; GO:0051673; P:membrane disruption in another organism; IBA:GO_Central.
DR InterPro; IPR016327; Alpha-defensin.
DR InterPro; IPR006081; Alpha-defensin_C.
DR PANTHER; PTHR11876; PTHR11876; 1.
DR PIRSF; PIRSF001875; Alpha-defensin; 1.
DR PROSITE; PS00269; DEFENSIN; 1.
PE 2: Evidence at transcript level;
KW Antibiotic; Antimicrobial; Cleavage on pair of basic residues; Defensin;
KW Disulfide bond; Reference proteome; Secreted; Signal.
FT SIGNAL 1..19
FT /evidence="ECO:0000255"
FT PROPEP 20..62
FT /evidence="ECO:0000255"
FT /id="PRO_0000352681"
FT PEPTIDE 63..94
FT /note="Defensin-A1"
FT /id="PRO_0000352682"
FT PROPEP 97..98
FT /evidence="ECO:0000255"
FT /id="PRO_0000352683"
FT DISULFID 67..94
FT /evidence="ECO:0000250"
FT DISULFID 69..83
FT /evidence="ECO:0000250"
FT DISULFID 73..93
FT /evidence="ECO:0000250"
SQ SEQUENCE 98 AA; 10460 MW; 4625C607ED11C9E0 CRC64;
MQTLSFLLAL LFLVAQTPAQ PTGEGEKGGT IQEPEATEAQ DTAAVLMAAG AADGDDSDTK
QLDTTFCRCR VSCNILEKYS GKCELSGRTA RICCRKIK