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DEFA2_ORNAN
ID   DEFA2_ORNAN             Reviewed;          97 AA.
AC   P0C8A2;
DT   14-OCT-2008, integrated into UniProtKB/Swiss-Prot.
DT   14-OCT-2008, sequence version 1.
DT   25-MAY-2022, entry version 23.
DE   RecName: Full=Defensin-A2 {ECO:0000305|PubMed:18463304, ECO:0000305|PubMed:18662710};
DE            Short=DefA2 {ECO:0000303|PubMed:18463304};
DE            Short=OaDefA2 {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, expressed at lower
CC       levels in spleen, and at very low levels in kidney and lung.
CC       {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";
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DR   AlphaFoldDB; P0C8A2; -.
DR   SMR; P0C8A2; -.
DR   Proteomes; UP000002279; Unplaced.
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   InterPro; IPR002366; Alpha-defensin_propep.
DR   PANTHER; PTHR11876; PTHR11876; 1.
DR   Pfam; PF00323; Defensin_1; 1.
DR   Pfam; PF00879; Defensin_propep; 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..61
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000352684"
FT   PEPTIDE         62..93
FT                   /note="Defensin-A2"
FT                   /id="PRO_0000352685"
FT   PROPEP          96..97
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000352686"
FT   DISULFID        66..93
FT                   /evidence="ECO:0000250"
FT   DISULFID        68..82
FT                   /evidence="ECO:0000250"
FT   DISULFID        72..92
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   97 AA;  10672 MW;  DF21F30C2022FE82 CRC64;
     MRTLSLLLAL LFLAAQTLAQ PIDEGAEEVI TEEPEITETQ DPTTIMLIER GIGGDSTDAT
     RSTITCYCRS RCRMLEKNSG TCRSSNCTYT LCCKKTS
 
 
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