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DFA31_MOUSE
ID   DFA31_MOUSE             Reviewed;          91 AA.
AC   P50715; Q64109; Q68VH1;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1997, sequence version 2.
DT   03-AUG-2022, entry version 100.
DE   RecName: Full=Alpha-defensin 31;
DE   AltName: Full=Alpha-defensin-related sequence 7;
DE   AltName: Full=Cryptdin-related protein 4C-2;
DE            Short=CRS4C2 {ECO:0000312|MGI:MGI:102509};
DE   AltName: Full=Defensin-related cryptdin-related sequence 7;
DE   Flags: Precursor;
GN   Name=Defa31 {ECO:0000312|MGI:MGI:102509};
GN   Synonyms=Defa-rs7 {ECO:0000312|MGI:MGI:102509},
GN   Defcr-rs7 {ECO:0000312|MGI:MGI:102509};
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], FUNCTION, AND TISSUE SPECIFICITY.
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).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND FUNCTION.
RC   STRAIN=C3H/HeN;
RX   PubMed=15235601; DOI=10.1038/ni1094;
RA   Hornef M.W., Putsep K., Karlsson J., Refai E., Andersson M.;
RT   "Increased diversity of intestinal antimicrobial peptides by covalent dimer
RT   formation.";
RL   Nat. Immunol. 5:836-843(2004).
CC   -!- FUNCTION: Apparent precursor of a secreted, cationic, proline- and
CC       cysteine-rich peptide that contains Cys-Pro-Xaa repeats
CC       (PubMed:7896294). Unlike cryptdin, the proposed mature peptide region
CC       lacks the structural motif characteristic of defensins
CC       (PubMed:7896294). It may have microbicidal activities
CC       (PubMed:15235601). {ECO:0000269|PubMed:15235601,
CC       ECO:0000269|PubMed:7896294}.
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- TISSUE SPECIFICITY: Paneth cells of the small bowel.
CC       {ECO:0000269|PubMed:7896294}.
CC   -!- SIMILARITY: Belongs to the alpha-defensin family. {ECO:0000305}.
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DR   EMBL; S77610; AAB33826.2; -; Genomic_DNA.
DR   EMBL; S77606; AAB33826.2; JOINED; Genomic_DNA.
DR   EMBL; U12564; AAA20977.1; -; Genomic_DNA.
DR   EMBL; AJ564870; CAD92332.1; -; mRNA.
DR   AlphaFoldDB; P50715; -.
DR   SMR; P50715; -.
DR   PRIDE; P50715; -.
DR   MGI; MGI:102509; Defa31.
DR   InParanoid; P50715; -.
DR   Reactome; R-MMU-1461973; Defensins.
DR   Reactome; R-MMU-1462054; Alpha-defensins.
DR   Reactome; R-MMU-6798695; Neutrophil degranulation.
DR   PRO; PR:P50715; -.
DR   Proteomes; UP000000589; Unplaced.
DR   RNAct; P50715; protein.
DR   GO; GO:0005615; C:extracellular space; ISO:MGI.
DR   GO; GO:0042802; F:identical protein binding; IPI: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; 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:MGI.
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; ISO:MGI.
DR   GO; GO:0051673; P:membrane disruption in another organism; IBA:GO_Central.
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..65
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000006853"
FT   PEPTIDE         66..91
FT                   /note="Alpha-defensin 31"
FT                   /id="PRO_0000006854"
FT   REPEAT          65..67
FT                   /note="1"
FT   REPEAT          68..70
FT                   /note="2"
FT   REPEAT          71..73
FT                   /note="3"
FT   REPEAT          77..79
FT                   /note="4"
FT   REPEAT          80..82
FT                   /note="5"
FT   REPEAT          83..85
FT                   /note="6"
FT   REGION          22..55
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          65..85
FT                   /note="6 X 3 AA tandem repeats of C-P-X"
FT   CONFLICT        56
FT                   /note="D -> DA (in Ref. 1; AAA20977)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   91 AA;  10055 MW;  B285679960C376D4 CRC64;
     MKKLVLLFAL VLLAFQVQAD SIQNTDEETK TEEQQGEEDQ AVSVSFGDPQ GSGLQDAALG
     WGRRCPRCPP CPRCSWCPRC PTCPRCNCNP K
 
 
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