DFAR2_MOUSE
ID DFAR2_MOUSE Reviewed; 91 AA.
AC P17534; Q64111;
DT 01-AUG-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 2.
DT 03-AUG-2022, entry version 101.
DE RecName: Full=Alpha-defensin-related sequence 2;
DE AltName: Full=CRS4C1;
DE AltName: Full=Cryptdin-related protein 4C-1;
DE AltName: Full=Defensin-related cryptdin-related sequence 2;
DE Flags: Precursor;
GN Name=Defa-rs2; Synonyms=Defcr-rs2;
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 [MRNA].
RC STRAIN=CD-1; TISSUE=Small intestine;
RX PubMed=2351676; DOI=10.1016/s0021-9258(19)38746-0;
RA Ouellette A.J., Lauldi J.C.;
RT "A novel mouse gene family coding for cationic, cysteine-rich peptides.
RT Regulation in small intestine and cells of myeloid origin.";
RL J. Biol. Chem. 265:9831-9837(1990).
RN [2]
RP ERRATUM OF PUBMED:2351676, AND SEQUENCE REVISION.
RX PubMed=8034619; DOI=10.1016/s0021-9258(17)32367-0;
RA Ouellette A.J., Lauldi J.C.;
RL J. Biol. Chem. 269:18702-18702(1994).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=129/SvJ; TISSUE=Small intestine;
RX PubMed=7896294; DOI=10.1006/geno.1994.1586;
RA Huttner K.M., Ouellette A.J.;
RT "A family of defensin-like genes codes for diverse cysteine-rich peptides
RT in mouse Paneth cells.";
RL Genomics 24:99-109(1994).
CC -!- FUNCTION: Apparent precursor of a secreted, cationic, proline- and
CC cysteine-rich peptide that contains Cys-Pro-Xaa repeats. Unlike
CC cryptdin, the proposed mature peptide region lacks the structural motif
CC characteristic of defensins. It may have microbicidal activities.
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- TISSUE SPECIFICITY: Small bowel, spleen, colon, kidney, liver, stomach
CC and femur marrow.
CC -!- DEVELOPMENTAL STAGE: Accumulates to high levels in intestinal crypt
CC epithelium during postnatal development.
CC -!- SIMILARITY: Belongs to the alpha-defensin family. {ECO:0000305}.
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DR EMBL; M33227; AAA18210.1; ALT_SEQ; mRNA.
DR EMBL; S77668; AAB33829.1; -; mRNA.
DR PIR; A59002; A59002.
DR RefSeq; NP_031873.1; NM_007847.1.
DR AlphaFoldDB; P17534; -.
DR PRIDE; P17534; -.
DR GeneID; 13222; -.
DR KEGG; mmu:13222; -.
DR CTD; 13222; -.
DR MGI; MGI:99592; Defa-rs2.
DR InParanoid; P17534; -.
DR PhylomeDB; P17534; -.
DR PRO; PR:P17534; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; P17534; protein.
DR GO; GO:0005615; C:extracellular space; ISO: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; IDA:MGI.
DR GO; GO:0042803; F:protein homodimerization activity; ISO:MGI.
DR GO; GO:0019731; P:antibacterial humoral response; IBA:GO_Central.
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; ISO:MGI.
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 PANTHER; PTHR11876; PTHR11876; 1.
DR Pfam; PF00879; Defensin_propep; 1.
DR PIRSF; PIRSF001875; Alpha-defensin; 1.
PE 2: Evidence at transcript level;
KW Antimicrobial; Defensin; Reference proteome; Repeat; Secreted; Signal.
FT SIGNAL 1..19
FT /evidence="ECO:0000255"
FT PROPEP 20..58
FT /evidence="ECO:0000255"
FT /id="PRO_0000006851"
FT PEPTIDE 59..91
FT /note="Alpha-defensin-related sequence 2"
FT /id="PRO_0000006852"
FT REPEAT 65..67
FT /note="1"
FT REPEAT 68..70
FT /note="2"
FT REPEAT 71..73
FT /note="3"
FT REPEAT 74..76
FT /note="4"
FT REPEAT 77..79
FT /note="5"
FT REPEAT 80..82
FT /note="6"
FT REPEAT 83..85
FT /note="7"
FT REGION 22..48
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 65..85
FT /note="7 X 3 AA tandem repeats of C-P-X"
SQ SEQUENCE 91 AA; 9980 MW; DF6E5B4316BA65CB CRC64;
MKKLVLLFAL VLLAFQVQAD SIQNTDEETK TEEQPGEKDQ AVSVSFGDPQ GSALQDAALG
WGRRCPQCPR CPSCPSCPRC PRCPRCKCNP K
