ID   DEF4_MACMU              Reviewed;          94 AA.
AC   P82319;
DT   21-NOV-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   25-MAY-2022, entry version 83.
DE   RecName: Full=Defensin alpha 4 {ECO:0000250|UniProtKB:P12838};
DE   AltName: Full=Neutrophil defensin 4 {ECO:0000303|PubMed:10531277};
DE   AltName: Full=RMAD-4 {ECO:0000303|PubMed:10531277};
DE   Contains:
DE     RecName: Full=Defensin alpha 5 {ECO:0000305};
DE     AltName: Full=Neutrophil defensin 5 {ECO:0000303|PubMed:10531277};
DE     AltName: Full=RMAD-5 {ECO:0000303|PubMed:10531277};
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], PROTEIN SEQUENCE OF 62-94, FUNCTION, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Bone marrow, and Leukocyte;
RX   PubMed=10531277; DOI=10.1128/iai.67.11.6139-6144.1999;
RA   Tang Y.Q., Yuan J., Miller C.J., Selsted M.E.;
RT   "Isolation, characterization, cDNA cloning, and antimicrobial properties of
RT   two distinct subfamilies of alpha-defensins from rhesus macaque
RT   leukocytes.";
RL   Infect. Immun. 67:6139-6144(1999).
CC   -!- FUNCTION: [Defensin alpha 4]: Exhibits bacteriostatic activity against
CC       Gram-positive bacteria S.aureus and L.monocytogenes and Gram-negative
CC       bacterium E.coli, antifungal activity against C.neoformans and
CC       microbicidial activity against Gram-positive bacteria S.aureus and
CC       L.monocytogenes. {ECO:0000269|PubMed:10531277}.
CC   -!- FUNCTION: [Defensin alpha 5]: Exhibits bacteriostatic activity against
CC       Gram-positive bacteria S.aureus and L.monocytogenes and Gram-negative
CC       bacterium E.coli, antifungal activity against C.neoformans and
CC       microbicidial activity against Gram-positive bacteria S.aureus and
CC       L.monocytogenes. {ECO:0000269|PubMed:10531277}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:Q01523}.
CC   -!- MASS SPECTROMETRY: [Defensin alpha 4]: Mass=3959.9; Method=MALDI;
CC       Evidence={ECO:0000269|PubMed:10531277};
CC   -!- MASS SPECTROMETRY: [Defensin alpha 5]: Mass=3802.6; Method=MALDI;
CC       Evidence={ECO:0000269|PubMed:10531277};
CC   -!- SIMILARITY: Belongs to the alpha-defensin family. {ECO:0000305}.
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DR   EMBL; AF188271; AAF06315.1; -; mRNA.
DR   PIR; D59076; D59076.
DR   PIR; E59076; E59076.
DR   PDB; 6KRA; NMR; -; A=62-94.
DR   PDBsum; 6KRA; -.
DR   AlphaFoldDB; P82319; -.
DR   SMR; P82319; -.
DR   eggNOG; ENOG502T2EX; Eukaryota.
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; IPR006081; Alpha-defensin_C.
DR   InterPro; IPR002366; Alpha-defensin_propep.
DR   InterPro; IPR006080; Defensin_beta/alpha.
DR   PANTHER; PTHR11876; PTHR11876; 1.
DR   Pfam; PF00323; Defensin_1; 1.
DR   Pfam; PF00879; Defensin_propep; 1.
DR   PIRSF; PIRSF001875; Alpha-defensin; 1.
DR   SMART; SM00048; DEFSN; 1.
DR   PROSITE; PS00269; DEFENSIN; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Antibiotic; Antimicrobial; Defensin;
KW   Direct protein sequencing; Disulfide bond; Fungicide; Reference proteome;
KW   Secreted; Signal.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000255"
FT   PROPEP          20..61
FT                   /evidence="ECO:0000269|PubMed:10531277"
FT                   /id="PRO_0000006799"
FT   PEPTIDE         62..94
FT                   /note="Defensin alpha 4"
FT                   /id="PRO_0000006800"
FT   PEPTIDE         63..94
FT                   /note="Defensin alpha 5"
FT                   /id="PRO_0000006801"
FT   DISULFID        65..93
FT                   /evidence="ECO:0000250|UniProtKB:P12838"
FT   DISULFID        67..82
FT                   /evidence="ECO:0000250|UniProtKB:P12838"
FT   DISULFID        72..92
FT                   /evidence="ECO:0000250|UniProtKB:P12838"
FT   STRAND          65..70
FT                   /evidence="ECO:0007829|PDB:6KRA"
FT   STRAND          76..84
FT                   /evidence="ECO:0007829|PDB:6KRA"
FT   STRAND          87..93
FT                   /evidence="ECO:0007829|PDB:6KRA"
SQ   SEQUENCE   94 AA;  10353 MW;  E06933B9BA1B0D62 CRC64;
     MRTIAILAAI LLFALLAQAK SLQETADDAA TQEQPGEDDQ DLAVSFEENG LSTLRASGSQ
     ARRTCRCRFG RCFRRESYSG SCNINGRIFS LCCR