DEFA1_HORSE
ID DEFA1_HORSE Reviewed; 98 AA.
AC A6YB85;
DT 30-NOV-2016, integrated into UniProtKB/Swiss-Prot.
DT 21-AUG-2007, sequence version 1.
DT 03-AUG-2022, entry version 45.
DE RecName: Full=Alpha-defensin 1 {ECO:0000303|PubMed:17620056, ECO:0000312|EMBL:ABP96800.1};
DE Flags: Precursor;
GN Name=DEFA1 {ECO:0000303|PubMed:17620056, ECO:0000312|EMBL:ABP96800.1};
OS Equus caballus (Horse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Perissodactyla; Equidae; Equus.
OX NCBI_TaxID=9796 {ECO:0000312|EMBL:ABP96800.1};
RN [1] {ECO:0000312|EMBL:ABP96800.1}
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TISSUE SPECIFICITY, AND CIRCULAR
RP DICHROISM ANALYSIS.
RC TISSUE=Small intestine {ECO:0000303|PubMed:17620056};
RX PubMed=17620056; DOI=10.1042/bj20070747;
RA Bruhn O., Regenhard P., Michalek M., Paul S., Gelhaus C., Jung S.,
RA Thaller G., Podschun R., Leippe M., Grotzinger J., Kalm E.;
RT "A novel horse alpha-defensin: gene transcription, recombinant expression
RT and characterization of the structure and function.";
RL Biochem. J. 407:267-276(2007).
RN [2]
RP FUNCTION.
RX PubMed=19211153; DOI=10.1016/j.vetimm.2009.01.005;
RA Bruhn O., Cauchard J., Schlusselhuber M., Gelhaus C., Podschun R.,
RA Thaller G., Laugier C., Leippe M., Groetzinger J.;
RT "Antimicrobial properties of the equine alpha-defensin DEFA1 against
RT bacterial horse pathogens.";
RL Vet. Immunol. Immunopathol. 130:102-106(2009).
RN [3]
RP FUNCTION, AND CIRCULAR DICHROISM ANALYSIS.
RX PubMed=22232283; DOI=10.1128/aac.05797-11;
RA Schlusselhuber M., Jung S., Bruhn O., Goux D., Leippe M., Leclercq R.,
RA Laugier C., Groetzinger J., Cauchard J.;
RT "In vitro potential of equine DEFA1 and eCATH1 as alternative antimicrobial
RT drugs in rhodococcosis treatment.";
RL Antimicrob. Agents Chemother. 56:1749-1755(2012).
RN [4] {ECO:0007744|PDB:2MXQ}
RP STRUCTURE BY NMR OF 65-98, FUNCTION, AND DISULFIDE BONDS.
RX PubMed=25769951; DOI=10.1016/j.bbrc.2015.02.168;
RA Michalek M., Jung S., Shomali M.R., Cauchard S., Sonnichsen F.D.,
RA Grotzinger J.;
RT "Solution structure and functional studies of the highly potent equine
RT antimicrobial peptide DEFA1.";
RL Biochem. Biophys. Res. Commun. 459:668-672(2015).
CC -!- FUNCTION: Has broad-spectrum antimicrobial properties (PubMed:17620056,
CC PubMed:19211153). The antimicrobial activity decreases in the present
CC of salt in vitro (PubMed:19211153). Binds anionic phospholipids, which
CC leads to the aggregation of liposomes in vitro (PubMed:25769951).
CC Membrane permeabilization of the target cells is an essential part of
CC the peptide's mode of antimicrobial activity (PubMed:17620056,
CC PubMed:22232283). No hemolytic activity against sheep or horse
CC erythrocytes (PubMed:22232283). Has antibacterial activity against the
CC bacterial horse pathogens Gram-positive R.equi ATCC 33701 P(-) (minimum
CC bactericidal concentration or MBC=5 ug/ml) and R.equi ATCC 33701 P(+)
CC (MBC=5 ug/ml), which are resistant against beta-lactam antibiotics.
CC Also has antibacterial activity against highly infectious wild-type
CC strain R.equi 85F P(+) (MBC=5 ug/ml), S.equi subsp. equi (MBC=5 ug/ml),
CC S.equi subsp. zooepidemicus (MBC=5 ug/ml), S.dysgalactiae subsp.
CC equisimilis (MBC=10 ug/ml), S.choleraesuis subsp. choleraesuis serovar
CC Typhimurium (MBC=10 ug/ml), and P.multocida subsp. multocida (MBC=>10
CC ug/ml) (PubMed:19211153). Probably contributes to the antimicrobial
CC barrier function of the small bowel mucosa (Probable).
CC {ECO:0000269|PubMed:17620056, ECO:0000269|PubMed:19211153,
CC ECO:0000269|PubMed:22232283, ECO:0000269|PubMed:25769951}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:Q01523}.
CC -!- TISSUE SPECIFICITY: Paneth cells of the small bowel.
CC {ECO:0000269|PubMed:17620056}.
CC -!- SIMILARITY: Belongs to the alpha-defensin family. {ECO:0000255,
CC 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; EF379126; ABP96800.1; -; mRNA.
DR PDB; 2MXQ; NMR; -; A=65-98.
DR PDBsum; 2MXQ; -.
DR AlphaFoldDB; A6YB85; -.
DR SMR; A6YB85; -.
DR STRING; 9796.ENSECAP00000009578; -.
DR PeptideAtlas; A6YB85; -.
DR Ensembl; ENSECAT00000012154; ENSECAP00000009578; ENSECAG00000011787.
DR GeneTree; ENSGT00940000153268; -.
DR Proteomes; UP000002281; Chromosome 27.
DR Bgee; ENSECAG00000011787; Expressed in testis.
DR GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR GO; GO:0005543; F:phospholipid binding; IDA:UniProtKB.
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:0042742; P:defense response to bacterium; IDA:UniProtKB.
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.
PE 1: Evidence at protein level;
KW 3D-structure; Antibiotic; Antimicrobial; Defensin; Disulfide bond;
KW Reference proteome; Secreted; Signal.
FT SIGNAL 1..19
FT /evidence="ECO:0000250|UniProtKB:P59665"
FT PROPEP 20..63
FT /evidence="ECO:0000250|UniProtKB:Q62716"
FT /id="PRO_0000438588"
FT PEPTIDE 64..98
FT /note="Alpha-defensin 1"
FT /id="PRO_5002705446"
FT DISULFID 66..96
FT /evidence="ECO:0000269|PubMed:25769951,
FT ECO:0007744|PDB:2MXQ"
FT DISULFID 68..84
FT /evidence="ECO:0000269|PubMed:25769951,
FT ECO:0007744|PDB:2MXQ"
FT DISULFID 74..95
FT /evidence="ECO:0000269|PubMed:25769951,
FT ECO:0007744|PDB:2MXQ"
FT STRAND 71..73
FT /evidence="ECO:0007829|PDB:2MXQ"
FT STRAND 75..77
FT /evidence="ECO:0007829|PDB:2MXQ"
FT TURN 85..88
FT /evidence="ECO:0007829|PDB:2MXQ"
SQ SEQUENCE 98 AA; 10843 MW; C840F202F5526268 CRC64;
MRTLTLLTAL LLLALQVQTQ SLEETADQVP AQDQPGAEAQ DITISFAGDE RSAREASKSL
IGTASCTCRR AWICRWGERH SGKCIDQKGS TYRLCCRR
