DEFB5_BOVIN
ID DEFB5_BOVIN Reviewed; 64 AA.
AC P46163; O97533;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2000, sequence version 4.
DT 03-AUG-2022, entry version 126.
DE RecName: Full=Beta-defensin 5;
DE AltName: Full=BNBD-5;
DE AltName: Full=BNDB-5;
DE Flags: Precursor;
GN Name=DEFB5; Synonyms=BNBD5;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Kurts B., Pitra C., Schwerin M., Seyfert H.-M.;
RT "Beta defensin-encoding genes are selected for divergent sequences of the
RT mature anti-bacterial peptide.";
RL Submitted (AUG-2000) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1-54, AND TISSUE SPECIFICITY.
RC TISSUE=Alveolar macrophage;
RX PubMed=9453661; DOI=10.1128/iai.66.2.878-881.1998;
RA Ryan L.K., Rhodes J., Bhat M., Diamond G.;
RT "Expression of beta-defensin genes in bovine alveolar macrophages.";
RL Infect. Immun. 66:878-881(1998).
RN [3]
RP PROTEIN SEQUENCE OF 23-64, PYROGLUTAMATE FORMATION AT GLN-23, FUNCTION, AND
RP TISSUE SPECIFICITY.
RC STRAIN=Hereford; TISSUE=Neutrophil;
RX PubMed=8454635; DOI=10.1016/s0021-9258(18)53298-1;
RA Selsted M.E., Tang Y.-Q., Morris W.L., McGuire P.A., Novotny M.J.,
RA Smith W., Henschen A.H., Cullor J.S.;
RT "Purification, primary structures, and antibacterial activities of beta-
RT defensins, a new family of antimicrobial peptides from bovine
RT neutrophils.";
RL J. Biol. Chem. 268:6641-6648(1993).
RN [4]
RP SEQUENCE REVISION TO C-TERMINUS.
RA Selsted M.E.;
RL Submitted (MAY-1996) to UniProtKB.
CC -!- FUNCTION: Has bactericidal activity. Active against E.coli ML35 but not
CC against S.aureus 502A. {ECO:0000269|PubMed:8454635}.
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- TISSUE SPECIFICITY: Neutrophilic granules. Alveolar macrophages.
CC {ECO:0000269|PubMed:8454635, ECO:0000269|PubMed:9453661}.
CC -!- SIMILARITY: Belongs to the beta-defensin family. {ECO:0000305}.
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DR EMBL; AJ278799; CAC15400.1; -; Genomic_DNA.
DR EMBL; AF014108; AAD01523.1; -; mRNA.
DR PIR; E45495; E45495.
DR RefSeq; NP_001124233.1; NM_001130761.1.
DR AlphaFoldDB; P46163; -.
DR SMR; P46163; -.
DR PaxDb; P46163; -.
DR PRIDE; P46163; -.
DR GeneID; 783935; -.
DR CTD; 81007; -.
DR HOGENOM; CLU_189296_4_1_1; -.
DR InParanoid; P46163; -.
DR Proteomes; UP000009136; Unplaced.
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; IBA:GO_Central.
DR InterPro; IPR001855; Defensin_beta-typ.
DR InterPro; IPR006080; Defensin_beta/alpha.
DR Pfam; PF00711; Defensin_beta; 1.
DR SMART; SM00048; DEFSN; 1.
PE 1: Evidence at protein level;
KW Antibiotic; Antimicrobial; Defensin; Direct protein sequencing;
KW Disulfide bond; Pyrrolidone carboxylic acid; Reference proteome; Secreted;
KW Signal.
FT SIGNAL 1..22
FT /evidence="ECO:0000269|PubMed:8454635"
FT PEPTIDE 23..64
FT /note="Beta-defensin 5"
FT /id="PRO_0000006883"
FT MOD_RES 23
FT /note="Pyrrolidone carboxylic acid"
FT /evidence="ECO:0000269|PubMed:8454635"
FT DISULFID 31..60
FT /evidence="ECO:0000250"
FT DISULFID 38..53
FT /evidence="ECO:0000250"
FT DISULFID 43..61
FT /evidence="ECO:0000250"
FT CONFLICT 54
FT /note="F -> S (in Ref. 2; AAD01523)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 64 AA; 7228 MW; 125A5278709131FC CRC64;
MRLHHLLLVL LFLVLSAGSG FTQVVRNPQS CRWNMGVCIP ISCPGNMRQI GTCFGPRVPC
CRRW
