DEFA4_MOUSE
ID DEFA4_MOUSE Reviewed; 92 AA.
AC P28311; A3KPC1; Q9QZL4;
DT 01-DEC-1992, integrated into UniProtKB/Swiss-Prot.
DT 20-JUN-2002, sequence version 4.
DT 03-AUG-2022, entry version 133.
DE RecName: Full=Defensin alpha 4 {ECO:0000312|MGI:MGI:99584};
DE AltName: Full=Defensin-related cryptdin-4 {ECO:0000303|PubMed:10569786};
DE Flags: Precursor;
GN Name=Defa4 {ECO:0000312|MGI:MGI:99584};
GN Synonyms=Defcr4 {ECO:0000303|PubMed:10569786};
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], SUBCELLULAR LOCATION, AND TISSUE
RP SPECIFICITY.
RC STRAIN=129/SvJ;
RX PubMed=10569786; DOI=10.1128/iai.67.12.6643-6651.1999;
RA Ouellette A.J., Darmoul D., Tran D., Huttner K.M., Yuan J., Selsted M.E.;
RT "Peptide localization and gene structure of cryptdin 4, a differentially
RT expressed mouse Paneth cell alpha-defensin.";
RL Infect. Immun. 67:6643-6651(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE OF 4-92, AND FUNCTION.
RC STRAIN=C3H/HeJ, and Swiss Webster; TISSUE=Intestinal crypt;
RX PubMed=7927786; DOI=10.1128/iai.62.11.5040-5047.1994;
RA Ouellette A.J., Hsieh M.M., Nosek M.T., Cano-Gauci D.F., Huttner K.M.,
RA Buick R.N., Selsted M.E.;
RT "Mouse Paneth cell defensins: primary structures and antibacterial
RT activities of numerous cryptdin isoforms.";
RL Infect. Immun. 62:5040-5047(1994).
RN [4]
RP NUCLEOTIDE SEQUENCE OF 59-92.
RC STRAIN=129/SvJ, and C3H/HeJ; TISSUE=Small intestine;
RX PubMed=8188287; DOI=10.1006/geno.1994.1093;
RA Huttner K.M., Selsted M.E., Ouellette A.J.;
RT "Structure and diversity of the murine cryptdin gene family.";
RL Genomics 19:448-453(1994).
RN [5]
RP PROTEIN SEQUENCE OF 61-92.
RC STRAIN=CD-1; TISSUE=Ileum, and Jejunum;
RX PubMed=1500431; DOI=10.1083/jcb.118.4.929;
RA Selsted M.E., Miller S.I., Henschen A.H., Ouellette A.J.;
RT "Enteric defensins: antibiotic peptide components of intestinal host
RT defense.";
RL J. Cell Biol. 118:929-936(1992).
RN [6]
RP STRUCTURE BY NMR OF 61-92, AND DISULFIDE BONDS.
RX PubMed=15595831; DOI=10.1021/bi048645p;
RA Jing W., Hunter H.N., Tanabe H., Ouellette A.J., Vogel H.J.;
RT "Solution structure of cryptdin-4, a mouse paneth cell alpha-defensin.";
RL Biochemistry 43:15759-15766(2004).
CC -!- FUNCTION: Host-defense peptide that has antimicrobial activity
CC (PubMed:7927786). Exhibits activity against Gram-negative E.coli (in
CC vitro) (PubMed:7927786). Probably contributes to the antimicrobial
CC barrier function of the small bowel mucosa (PubMed:7927786).
CC {ECO:0000269|PubMed:7927786, ECO:0000303|PubMed:7927786}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:Q01523}.
CC Cytoplasmic vesicle, secretory vesicle {ECO:0000269|PubMed:10569786}.
CC -!- TISSUE SPECIFICITY: Paneth cells of the small bowel.
CC {ECO:0000269|PubMed:10569786}.
CC -!- SIMILARITY: Belongs to the alpha-defensin family. {ECO:0000305}.
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DR EMBL; AF178040; AAD51759.1; -; Genomic_DNA.
DR EMBL; BC134360; AAI34361.1; -; mRNA.
DR EMBL; U03032; AAA57172.1; -; mRNA.
DR PIR; I48887; I48887.
DR RefSeq; NP_034169.2; NM_010039.2.
DR PDB; 1TV0; NMR; -; A=61-92.
DR PDB; 2GW9; NMR; -; A=61-92.
DR PDB; 2GWP; NMR; -; A=61-92.
DR PDB; 2LEW; NMR; -; A=61-92.
DR PDB; 2LEY; NMR; -; A=61-92.
DR PDB; 7RC7; NMR; -; A=61-92.
DR PDB; 7RC8; NMR; -; A=61-92.
DR PDBsum; 1TV0; -.
DR PDBsum; 2GW9; -.
DR PDBsum; 2GWP; -.
DR PDBsum; 2LEW; -.
DR PDBsum; 2LEY; -.
DR PDBsum; 7RC7; -.
DR PDBsum; 7RC8; -.
DR AlphaFoldDB; P28311; -.
DR SMR; P28311; -.
DR TCDB; 1.C.19.1.5; the defensin (defensin) family.
DR PeptideAtlas; P28311; -.
DR PRIDE; P28311; -.
DR DNASU; 13238; -.
DR GeneID; 13238; -.
DR KEGG; mmu:13238; -.
DR UCSC; uc029wro.1; mouse.
DR CTD; 1669; -.
DR MGI; MGI:99584; Defa4.
DR InParanoid; P28311; -.
DR PhylomeDB; P28311; -.
DR BioGRID-ORCS; 13238; 1 hit in 17 CRISPR screens.
DR EvolutionaryTrace; P28311; -.
DR PRO; PR:P28311; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; P28311; protein.
DR GO; GO:0042582; C:azurophil granule; ISO:MGI.
DR GO; GO:0005615; C:extracellular space; IDA:MGI.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; ISO:MGI.
DR GO; GO:0030496; C:midbody; ISO:MGI.
DR GO; GO:0030141; C:secretory granule; ISO:MGI.
DR GO; GO:0030133; C:transport vesicle; IEA:UniProtKB-SubCell.
DR GO; GO:0005543; F:phospholipid binding; IDA:MGI.
DR GO; GO:0042803; F:protein homodimerization activity; ISO:MGI.
DR GO; GO:0019731; P:antibacterial humoral response; IDA:MGI.
DR GO; GO:0061844; P:antimicrobial humoral immune response mediated by antimicrobial peptide; ISO:MGI.
DR GO; GO:0071222; P:cellular response to lipopolysaccharide; IBA:GO_Central.
DR GO; GO:0042742; P:defense response to bacterium; IDA:MGI.
DR GO; GO:0050829; P:defense response to Gram-negative bacterium; ISO:MGI.
DR GO; GO:0050830; P:defense response to Gram-positive bacterium; ISO:MGI.
DR GO; GO:0045087; P:innate immune response; ISO:MGI.
DR GO; GO:0002227; P:innate immune response in mucosa; IBA:GO_Central.
DR GO; GO:0051873; P:killing by host of symbiont cells; ISO:MGI.
DR GO; GO:0031640; P:killing of cells of another organism; IMP:CAFA.
DR GO; GO:0051673; P:membrane disruption in another organism; IDA:MGI.
DR GO; GO:0032757; P:positive regulation of interleukin-8 production; ISO:MGI.
DR GO; GO:1905710; P:positive regulation of membrane permeability; ISO:MGI.
DR GO; GO:0051289; P:protein homotetramerization; ISO:MGI.
DR InterPro; IPR016327; Alpha-defensin.
DR InterPro; IPR002366; Alpha-defensin_propep.
DR InterPro; IPR006080; Defensin_beta/alpha.
DR PANTHER; PTHR11876; PTHR11876; 1.
DR Pfam; PF00879; Defensin_propep; 1.
DR PIRSF; PIRSF001875; Alpha-defensin; 1.
DR SMART; SM00048; DEFSN; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Antibiotic; Antimicrobial; Cytoplasmic vesicle; Defensin;
KW Direct protein sequencing; Disulfide bond; Reference proteome; Secreted;
KW Signal.
FT SIGNAL 1..19
FT /evidence="ECO:0000255"
FT PROPEP 20..58
FT /id="PRO_0000006823"
FT PEPTIDE 59..92
FT /note="Defensin alpha 4"
FT /id="PRO_0000006824"
FT REGION 23..42
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 64..89
FT /evidence="ECO:0000269|PubMed:15595831"
FT DISULFID 66..81
FT /evidence="ECO:0000269|PubMed:15595831"
FT DISULFID 71..88
FT /evidence="ECO:0000269|PubMed:15595831"
FT CONFLICT 30
FT /note="K -> N (in Ref. 2; AAI34361)"
FT /evidence="ECO:0000305"
FT STRAND 65..69
FT /evidence="ECO:0007829|PDB:1TV0"
FT STRAND 77..80
FT /evidence="ECO:0007829|PDB:2LEW"
FT STRAND 81..88
FT /evidence="ECO:0007829|PDB:1TV0"
SQ SEQUENCE 92 AA; 10272 MW; BF632838D52AFCE2 CRC64;
MKTLVLLSAL VLLAFQVQAD PIQNTDEETK TEEQPGEEDQ AVSISFGGQE GSALHEKSLR
GLLCYCRKGH CKRGERVRGT CGIRFLYCCP RR
