ID   DEF4_PAPHA              Reviewed;          30 AA.
AC   P86724;
DT   05-OCT-2010, integrated into UniProtKB/Swiss-Prot.
DT   05-OCT-2010, sequence version 1.
DT   25-MAY-2022, entry version 17.
DE   RecName: Full=Alpha-defensin PhD-4 {ECO:0000303|PubMed:20155756};
OS   Papio hamadryas (Hamadryas baboon).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC   Cercopithecidae; Cercopithecinae; Papio.
OX   NCBI_TaxID=9557;
RN   [1] {ECO:0000305}
RP   PROTEIN SEQUENCE, FUNCTION, AND MASS SPECTROMETRY.
RC   TISSUE=Leukocyte {ECO:0000269|PubMed:20155756};
RX   PubMed=20155756; DOI=10.1002/rcm.4424;
RA   Stegemann C., Tsvetkova E.V., Aleshina G.M., Lehrer R.I., Kokryakov V.N.,
RA   Hoffmann R.;
RT   "De novo sequencing of two new cyclic theta-defensins from baboon (Papio
RT   hamadryas) leukocytes by matrix-assisted laser desorption/ionization mass
RT   spectrometry.";
RL   Rapid Commun. Mass Spectrom. 24:599-604(2010).
CC   -!- FUNCTION: In low salt conditions, has antibacterial activity against
CC       the Gram-negative bacterium E.coli ML35p (MIC=2.4 uM), the Gram-
CC       positive bacteria L.monocytogenes EGD (MIC=2.2 uM) and methicillin-
CC       resistant S.aureus ATCC 33591 (MIC=3.5 uM), and the fungus C.albicans
CC       820 (MIC=3.9 uM). At high physiological salt concentrations the
CC       antimicrobial activity decreases significantly: E.coli ML35p (MIC=7.1
CC       uM), L.monocytogenes EGD (MIC=1.8 uM), S.aureus ATCC 33591 (MIC=>50
CC       uM), and C.albicans 820 (MIC=>50 uM). {ECO:0000269|PubMed:20155756}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:P59665}.
CC   -!- MASS SPECTROMETRY: Mass=3478.5; Method=MALDI;
CC       Evidence={ECO:0000269|PubMed:20155756};
CC   -!- SIMILARITY: Belongs to the alpha-defensin family. {ECO:0000255}.
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DR   AlphaFoldDB; P86724; -.
DR   SMR; P86724; -.
DR   GO; GO:0005615; C:extracellular space; IEA:InterPro.
DR   GO; GO:0042742; P:defense response to bacterium; IEA:UniProtKB-KW.
DR   GO; GO:0050832; P:defense response to fungus; IEA:UniProtKB-KW.
DR   GO; GO:0031640; P:killing of cells of another organism; IEA:UniProtKB-KW.
DR   InterPro; IPR016327; Alpha-defensin.
DR   InterPro; IPR006081; Alpha-defensin_C.
DR   InterPro; IPR006080; Defensin_beta/alpha.
DR   PANTHER; PTHR11876; PTHR11876; 1.
DR   Pfam; PF00323; Defensin_1; 1.
DR   SMART; SM00048; DEFSN; 1.
DR   PROSITE; PS00269; DEFENSIN; 1.
PE   1: Evidence at protein level;
KW   Antibiotic; Antimicrobial; Defensin; Direct protein sequencing;
KW   Disulfide bond; Fungicide; Secreted.
FT   PEPTIDE         1..30
FT                   /note="Alpha-defensin PhD-4"
FT                   /evidence="ECO:0000269|PubMed:20155756"
FT                   /id="PRO_0000399454"
FT   DISULFID        2..30
FT                   /evidence="ECO:0000250|UniProtKB:P59665"
FT   DISULFID        4..19
FT                   /evidence="ECO:0000250|UniProtKB:P59665"
FT   DISULFID        9..29
FT                   /evidence="ECO:0000250|UniProtKB:P59665"
SQ   SEQUENCE   30 AA;  3487 MW;  D752D040888A809F CRC64;
     ACYCRIPACF AGERRYGTCF YLGRVWAFCC