DEFB8_MOUSE
ID DEFB8_MOUSE Reviewed; 60 AA.
AC Q91V82; Q8R556;
DT 27-SEP-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 25-MAY-2022, entry version 115.
DE RecName: Full=Beta-defensin 8;
DE Short=BD-8;
DE Short=mBD-8;
DE AltName: Full=Defensin, beta 8;
DE AltName: Full=Defensin-related peptide;
DE AltName: Full=Defr1;
DE Flags: Precursor;
GN Name=Defb8;
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].
RC STRAIN=C57BL/6J;
RX PubMed=12226710; DOI=10.1007/s00335-002-3014-5;
RA Morrison G.M., Rolfe M., Kilanowski F.M., Cross S.H., Dorin J.R.;
RT "Identification and characterisation a novel murine beta defensin related
RT gene.";
RL Mamm. Genome 13:445-451(2002).
RN [2]
RP ERRATUM OF PUBMED:12226710.
RX DOI=10.1007/s00335-002-0016-2;
RA Morrison G.M., Rolfe M., Kilanowski F.M., Cross S.H., Dorin J.R.;
RL Mamm. Genome 13:603-603(2002).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
RC TISSUE=Lung;
RA Conejo-Garcia J.-R., Nehls M.C., Wattler S., Bals R., Heitland A.,
RA Kluever E., Liepke C., Adermann K., Forssmann W.-G.;
RT "Cloning and characterization of mBD-7 and mBD-8, two novel mouse beta-
RT defensins.";
RL Submitted (JUL-2001) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP STRUCTURE BY NMR OF 26-60, AND DISULFIDE BONDS.
RX PubMed=11714914; DOI=10.1110/ps.24401;
RA Bauer F., Schweimer K., Kluever E., Conejo-Garcia J.-R., Forssmann W.-G.,
RA Roesch P., Adermann K., Sticht H.;
RT "Structure determination of human and murine beta-defensins reveals
RT structural conservation in the absence of significant sequence
RT similarity.";
RL Protein Sci. 10:2470-2479(2001).
CC -!- FUNCTION: A synthetic peptide displays antimicrobial activities against
CC S.aureus, P.aeruginosa, E.coli and B.cepacia. The antimicrobial
CC activity against S.aureus, E.coli and B.cepacia is reduced in raised
CC concentration of NaCl, but its action against P.aeruginosa is
CC independent of NaCl concentration.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Most highly expressed in testis and heart.
CC -!- SIMILARITY: Belongs to the beta-defensin family. {ECO:0000305}.
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DR EMBL; AJ344114; CAC86998.1; -; Genomic_DNA.
DR EMBL; AJ300674; CAC44635.1; -; mRNA.
DR EMBL; AJ300673; CAC44634.1; -; Genomic_DNA.
DR RefSeq; NP_694748.3; NM_153108.4.
DR PDB; 1E4R; NMR; -; A=26-60.
DR PDBsum; 1E4R; -.
DR AlphaFoldDB; Q91V82; -.
DR SMR; Q91V82; -.
DR STRING; 10090.ENSMUSP00000033854; -.
DR PaxDb; Q91V82; -.
DR PRIDE; Q91V82; -.
DR ProteomicsDB; 279337; -.
DR DNASU; 244334; -.
DR GeneID; 244334; -.
DR KEGG; mmu:244334; -.
DR CTD; 244334; -.
DR MGI; MGI:2654206; Defb8.
DR eggNOG; ENOG502SYUI; Eukaryota.
DR InParanoid; Q91V82; -.
DR OrthoDB; 1916627at2759; -.
DR BioGRID-ORCS; 244334; 1 hit in 70 CRISPR screens.
DR EvolutionaryTrace; Q91V82; -.
DR PRO; PR:Q91V82; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; Q91V82; protein.
DR GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR GO; GO:0031731; F:CCR6 chemokine receptor binding; IBA:GO_Central.
DR GO; GO:0042056; F:chemoattractant activity; IBA:GO_Central.
DR GO; GO:0060326; P:cell chemotaxis; 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; IMP:UniProtKB.
DR GO; GO:0050830; P:defense response to Gram-positive bacterium; IMP:UniProtKB.
DR GO; GO:0045087; P:innate immune response; IMP:UniProtKB.
DR InterPro; IPR001855; Defensin_beta-typ.
DR Pfam; PF00711; Defensin_beta; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Antibiotic; Antimicrobial; Defensin; Disulfide bond;
KW Reference proteome; Secreted; Signal.
FT SIGNAL 1..22
FT /evidence="ECO:0000255"
FT PROPEP 23..25
FT /id="PRO_0000006935"
FT PEPTIDE 26..60
FT /note="Beta-defensin 8"
FT /id="PRO_0000006936"
FT DISULFID 31..58
FT /evidence="ECO:0000269|PubMed:11714914"
FT DISULFID 38..52
FT /evidence="ECO:0000269|PubMed:11714914"
FT DISULFID 42..59
FT /evidence="ECO:0000269|PubMed:11714914"
FT CONFLICT 27
FT /note="E -> D (in Ref. 1; CAC86998)"
FT /evidence="ECO:0000305"
FT CONFLICT 30..31
FT /note="SC -> TY (in Ref. 1; CAC86998)"
FT /evidence="ECO:0000305"
FT HELIX 31..34
FT /evidence="ECO:0007829|PDB:1E4R"
FT STRAND 37..40
FT /evidence="ECO:0007829|PDB:1E4R"
FT STRAND 46..50
FT /evidence="ECO:0007829|PDB:1E4R"
FT STRAND 54..60
FT /evidence="ECO:0007829|PDB:1E4R"
SQ SEQUENCE 60 AA; 6760 MW; 7213024CF909A59B CRC64;
MRIHYLLFTF LLVLLSPLAA FSQKINEPVS CIRNGGICQY RCIGLRHKIG TCGSPFKCCK
