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DEFB1_CAPHI
ID   DEFB1_CAPHI             Reviewed;          64 AA.
AC   O97946;
DT   15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1999, sequence version 1.
DT   25-MAY-2022, entry version 71.
DE   RecName: Full=Beta-defensin 1;
DE            Short=BD-1;
DE   AltName: Full=Defensin, beta 1;
DE   Flags: Precursor;
GN   Name=DEFB1;
OS   Capra hircus (Goat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Caprinae; Capra.
OX   NCBI_TaxID=9925;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Tongue;
RX   PubMed=10531296; DOI=10.1128/iai.67.11.6221-6224.1999;
RA   Zhao C., Nguyen T., Liu L., Shamova O., Brogden K., Lehrer R.I.;
RT   "Differential expression of caprine beta-defensins in digestive and
RT   respiratory tissues.";
RL   Infect. Immun. 67:6221-6224(1999).
CC   -!- FUNCTION: Has bactericidal activity. May act as a ligand for C-C
CC       chemokine receptor CCR6. Positively regulates the sperm motility and
CC       bactericidal activity in a CCR6-dependent manner. Binds to CCR6 and
CC       triggers Ca2+ mobilization in the sperm which is important for its
CC       motility. {ECO:0000250|UniProtKB:P60022}.
CC   -!- SUBUNIT: Monomer. Homodimer. {ECO:0000250|UniProtKB:P60022}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:P60022}. Membrane
CC       {ECO:0000250|UniProtKB:P60022}. Note=Associates with tumor cell
CC       membrane-derived microvesicles. {ECO:0000250|UniProtKB:P60022}.
CC   -!- SIMILARITY: Belongs to the beta-defensin family. {ECO:0000305}.
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DR   EMBL; Y17679; CAA76811.1; -; mRNA.
DR   AlphaFoldDB; O97946; -.
DR   SMR; O97946; -.
DR   STRING; 9925.ENSCHIP00000001150; -.
DR   Proteomes; UP000291000; Unassembled WGS sequence.
DR   GO; GO:0019898; C:extrinsic component of membrane; ISS:UniProtKB.
DR   GO; GO:1990742; C:microvesicle; ISS:UniProtKB.
DR   GO; GO:0097225; C:sperm midpiece; ISS:UniProtKB.
DR   GO; GO:0031731; F:CCR6 chemokine receptor binding; ISS:UniProtKB.
DR   GO; GO:0042802; F:identical protein binding; ISS:UniProtKB.
DR   GO; GO:0035584; P:calcium-mediated signaling using intracellular calcium source; ISS:UniProtKB.
DR   GO; GO:0019933; P:cAMP-mediated signaling; ISS:UniProtKB.
DR   GO; GO:0050829; P:defense response to Gram-negative bacterium; ISS:UniProtKB.
DR   GO; GO:0050830; P:defense response to Gram-positive bacterium; ISS:UniProtKB.
DR   GO; GO:0060474; P:positive regulation of flagellated sperm motility involved in capacitation; ISS:UniProtKB.
DR   InterPro; IPR001855; Defensin_beta-typ.
DR   InterPro; IPR006080; Defensin_beta/alpha.
DR   Pfam; PF00711; Defensin_beta; 1.
DR   SMART; SM00048; DEFSN; 1.
PE   3: Inferred from homology;
KW   Antibiotic; Antimicrobial; Defensin; Disulfide bond; Membrane;
KW   Reference proteome; Secreted; Signal.
FT   SIGNAL          1..20
FT                   /evidence="ECO:0000255"
FT   PROPEP          21..26
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000006888"
FT   PEPTIDE         27..64
FT                   /note="Beta-defensin 1"
FT                   /id="PRO_0000006889"
FT   DISULFID        31..60
FT                   /evidence="ECO:0000250"
FT   DISULFID        38..53
FT                   /evidence="ECO:0000250"
FT   DISULFID        43..61
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   64 AA;  7258 MW;  492B824C8F57B042 CRC64;
     MRLHHLLLVL FFLVLSAGSG FTQGIRSRRS CHRNKGVCAL TRCPRNMRQI GTCFGPPVKC
     CRKK
 
 
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