RTD3_MACMU
ID RTD3_MACMU Reviewed; 76 AA.
AC Q9GLR2;
DT 19-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 25-MAY-2022, entry version 69.
DE RecName: Full=Demidefensin-3;
DE Flags: Precursor;
OS Macaca mulatta (Rhesus macaque).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Cercopithecinae; Macaca.
OX NCBI_TaxID=9544;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Bone marrow;
RX PubMed=11527997;
RA Leonova L., Kokryakov V.N., Aleshina G., Hong T., Nguyen T., Zhao C.,
RA Waring A.J., Lehrer R.I.;
RT "Circular minidefensins and posttranslational generation of molecular
RT diversity.";
RL J. Leukoc. Biol. 70:461-464(2001).
CC -!- FUNCTION: Has antimicrobial activities against bacteria and fungi.
CC {ECO:0000250}.
CC -!- SUBUNIT: Forms a cyclic homodimer; disulfide-linked. {ECO:0000250}.
CC -!- PTM: This is a cyclic peptide. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the alpha-defensin family. Theta subfamily.
CC {ECO:0000305}.
CC -!- CAUTION: The mature 9-residue peptide is expected to be found in 18-
CC residue cyclopeptides produced by combinatorial peptide splicing either
CC with itself or with other demidefensins. However among cyclopeptides
CC screened for antimicrobial activity, no peptides that would have been
CC produced from this sequence were detected. {ECO:0000305}.
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 EMBL; AF184158; AAG17204.1; -; mRNA.
DR RefSeq; NP_001027988.1; NM_001032816.1.
DR AlphaFoldDB; Q9GLR2; -.
DR STRING; 9544.ENSMMUP00000023401; -.
DR GeneID; 574121; -.
DR KEGG; mcc:574121; -.
DR CTD; 574121; -.
DR eggNOG; ENOG502TEA8; Eukaryota.
DR OrthoDB; 1874636at2759; -.
DR Proteomes; UP000006718; 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:0050832; P:defense response to fungus; IEA:UniProtKB-KW.
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:0031640; P:killing of cells of another organism; IEA:UniProtKB-KW.
DR GO; GO:0051673; P:membrane disruption in another organism; IBA:GO_Central.
DR InterPro; IPR016327; Alpha-defensin.
DR InterPro; IPR002366; Alpha-defensin_propep.
DR PANTHER; PTHR11876; PTHR11876; 1.
DR Pfam; PF00879; Defensin_propep; 1.
DR PIRSF; PIRSF001875; Alpha-defensin; 1.
PE 3: Inferred from homology;
KW Antibiotic; Antimicrobial; Defensin; Disulfide bond; Fungicide;
KW Reference proteome; Signal.
FT SIGNAL 1..22
FT /evidence="ECO:0000255"
FT PROPEP 23..64
FT /evidence="ECO:0000250"
FT /id="PRO_0000006877"
FT PEPTIDE 65..73
FT /note="Demidefensin-3"
FT /id="PRO_0000006878"
FT PROPEP 74..76
FT /evidence="ECO:0000250"
FT /id="PRO_0000006879"
FT REGION 25..45
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 66
FT /note="Interchain"
FT /evidence="ECO:0000250"
FT DISULFID 68..73
FT /evidence="ECO:0000250"
FT CONFLICT 4
FT /note="L -> F (in Ref. 1; published sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 49
FT /note="W -> R (in Ref. 1; published sequence)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 76 AA; 8209 MW; 54C8B19B8937D2FD CRC64;
MRTLALHTAM LLLVALHAQA EARQARADEA AAQQQPGADD QGMAHSFTWP ENAALPLSES
ERGLRCICVL GICRLL
