FUCL4_ANGJA
ID FUCL4_ANGJA Reviewed; 179 AA.
AC Q9I928;
DT 21-FEB-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 61.
DE RecName: Full=Fucolectin-4;
DE Flags: Precursor;
OS Anguilla japonica (Japanese eel).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Anguilliformes; Anguillidae;
OC Anguilla.
OX NCBI_TaxID=7937;
RN [1] {ECO:0000305, ECO:0000312|EMBL:BAB03526.1}
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, AND TISSUE
RP SPECIFICITY.
RC TISSUE=Gill {ECO:0000312|EMBL:BAB03526.1};
RX PubMed=10924498; DOI=10.1074/jbc.m002337200;
RA Honda S., Kashiwagi M., Miyamoto K., Takei Y., Hirose S.;
RT "Multiplicity, structures, and endocrine and exocrine natures of eel
RT fucose-binding lectins.";
RL J. Biol. Chem. 275:33151-33157(2000).
CC -!- FUNCTION: Acts as a defensive agent. Recognizes blood group fucosylated
CC oligosaccharides including A, B, H and Lewis B-type antigens. Does not
CC recognize Lewis A antigen and has low affinity for monovalent haptens.
CC {ECO:0000269|PubMed:10924498}.
CC -!- SUBUNIT: Homotrimer. {ECO:0000250|UniProtKB:Q7SIC1}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:10924498}.
CC -!- TISSUE SPECIFICITY: Gill mucous cells. {ECO:0000269|PubMed:10924498}.
CC -!- MISCELLANEOUS: Binds 1 calcium ion per monomer. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the fucolectin family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AB037870; BAB03526.1; -; mRNA.
DR AlphaFoldDB; Q9I928; -.
DR SMR; Q9I928; -.
DR CAZy; CBM47; Carbohydrate-Binding Module Family 47.
DR GO; GO:0005615; C:extracellular space; IDA:UniProtKB.
DR GO; GO:0005509; F:calcium ion binding; ISS:UniProtKB.
DR GO; GO:0030246; F:carbohydrate binding; IDA:UniProtKB.
DR GO; GO:0042806; F:fucose binding; IDA:UniProtKB.
DR GO; GO:0010185; P:regulation of cellular defense response; TAS:UniProtKB.
DR GO; GO:0001868; P:regulation of complement activation, lectin pathway; TAS:UniProtKB.
DR GO; GO:0045088; P:regulation of innate immune response; TAS:UniProtKB.
DR InterPro; IPR000421; FA58C.
DR InterPro; IPR006585; FTP1.
DR InterPro; IPR008979; Galactose-bd-like_sf.
DR Pfam; PF00754; F5_F8_type_C; 1.
DR SMART; SM00607; FTP; 1.
DR SUPFAM; SSF49785; SSF49785; 1.
PE 2: Evidence at transcript level;
KW Calcium; Disulfide bond; Lectin; Metal-binding; Secreted; Signal.
FT SIGNAL 1..23
FT /evidence="ECO:0000255"
FT CHAIN 24..179
FT /note="Fucolectin-4"
FT /evidence="ECO:0000305"
FT /id="PRO_0000223935"
FT REGION 31..179
FT /note="F5/8 type C-like"
FT MOTIF 101..103
FT /note="Cell attachment site"
FT /evidence="ECO:0000255"
FT BINDING 58
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 61
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:Q7SIC1"
FT BINDING 63
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 72
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:Q7SIC1"
FT BINDING 75
FT /ligand="alpha-L-fucose"
FT /ligand_id="ChEBI:CHEBI:42548"
FT /evidence="ECO:0000250|UniProtKB:Q7SIC1"
FT BINDING 101
FT /ligand="alpha-L-fucose"
FT /ligand_id="ChEBI:CHEBI:42548"
FT /evidence="ECO:0000250|UniProtKB:Q7SIC1"
FT BINDING 108
FT /ligand="alpha-L-fucose"
FT /ligand_id="ChEBI:CHEBI:42548"
FT /evidence="ECO:0000250|UniProtKB:Q7SIC1"
FT BINDING 168
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 169
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:Q7SIC1"
FT DISULFID 73..168
FT /evidence="ECO:0000250|UniProtKB:Q7SIC1"
FT DISULFID 104..105
FT /evidence="ECO:0000250|UniProtKB:Q7SIC1"
FT DISULFID 130..146
FT /evidence="ECO:0000250|UniProtKB:Q7SIC1"
SQ SEQUENCE 179 AA; 19467 MW; 84D82EA004BED41A CRC64;
MEVKTIMLLF QILAISTLKQ GSAHVPDGYV EENVALRGRA TQSAQLRGEH AALAHASNAI
DGNRDSNYHH GSCTHTEGAN PWWRVDLLQV YTIASVTITN RGDCCGERIS GARILIGNSL
ENNGINNPQC SVIGSLATGE TRTFHCPQPM IGRYVTVYLP KIESLQLCEV EVNALLPVN