ID   DEFA9_MOUSE             Reviewed;          93 AA.
AC   P50707;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1997, sequence version 2.
DT   03-AUG-2022, entry version 106.
DE   RecName: Full=Alpha-defensin 9;
DE   AltName: Full=Defensin-related cryptdin-9;
DE   Flags: Precursor;
GN   Name=Defa9; Synonyms=Defcr9;
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=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   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 59-93.
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).
CC   -!- FUNCTION: Probably contributes to the antimicrobial barrier function of
CC       the small bowel mucosa.
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- TISSUE SPECIFICITY: Paneth cells of the small bowel.
CC   -!- SIMILARITY: Belongs to the alpha-defensin family. {ECO:0000305}.
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DR   EMBL; U03037; AAA57177.1; -; mRNA.
DR   PIR; I48892; I48892.
DR   AlphaFoldDB; P50707; -.
DR   SMR; P50707; -.
DR   MaxQB; P50707; -.
DR   PeptideAtlas; P50707; -.
DR   PRIDE; P50707; -.
DR   MGI; MGI:99579; Defa9.
DR   InParanoid; P50707; -.
DR   PRO; PR:P50707; -.
DR   Proteomes; UP000000589; Unplaced.
DR   RNAct; P50707; 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; ISO: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: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; ISO: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; IPR006081; Alpha-defensin_C.
DR   InterPro; IPR002366; Alpha-defensin_propep.
DR   InterPro; IPR006080; Defensin_beta/alpha.
DR   PANTHER; PTHR11876; PTHR11876; 1.
DR   Pfam; PF00323; Defensin_1; 1.
DR   Pfam; PF00879; Defensin_propep; 1.
DR   PIRSF; PIRSF001875; Alpha-defensin; 1.
DR   SMART; SM00048; DEFSN; 1.
DR   PROSITE; PS00269; DEFENSIN; 1.
PE   2: Evidence at transcript level;
KW   Antibiotic; Antimicrobial; Defensin; Disulfide bond; Reference proteome;
KW   Secreted; Signal.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000255"
FT   PROPEP          20..58
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000006833"
FT   PEPTIDE         59..93
FT                   /note="Alpha-defensin 9"
FT                   /id="PRO_0000006834"
FT   REGION          23..56
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   DISULFID        64..92
FT                   /evidence="ECO:0000250"
FT   DISULFID        66..81
FT                   /evidence="ECO:0000250"
FT   DISULFID        71..91
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   93 AA;  10535 MW;  9A3DBAAED870E785 CRC64;
     MKTLVLLSAL VLLAFQVQAD PIQNTDEETK TEEQPGEEDQ AVSVSFGDPE GSSLQEESLR
     DLVCYCRKRG CKRREHMNGT CRKGHLLYML CCR