ID   FUCL2_ANGJA             Reviewed;         180 AA.
AC   Q9I930;
DT   21-FEB-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   03-AUG-2022, entry version 64.
DE   RecName: Full=Fucolectin-2;
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:BAB03524.1}
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, AND TISSUE
RP   SPECIFICITY.
RC   TISSUE=Liver {ECO:0000312|EMBL:BAB03524.1};
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, extracellular space
CC       {ECO:0000269|PubMed:10924498}.
CC   -!- TISSUE SPECIFICITY: Parenchymal hepatocytes.
CC       {ECO:0000269|PubMed:10924498}.
CC   -!- MISCELLANEOUS: Binds 1 calcium ion per monomer. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the fucolectin family. {ECO:0000305}.
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DR   EMBL; AB037868; BAB03524.1; -; mRNA.
DR   AlphaFoldDB; Q9I930; -.
DR   SMR; Q9I930; -.
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..22
FT                   /evidence="ECO:0000255"
FT   CHAIN           23..180
FT                   /note="Fucolectin-2"
FT                   /evidence="ECO:0000305"
FT                   /id="PRO_0000223933"
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   180 AA;  19776 MW;  D572D09AED85C206 CRC64;
     MKVKMIMLLF QILAILTLKS DSADVPDGYI QENVALRGRA TQSAQLRGEH AGISHASNAI
     DGNRDSYFYH GSCSHTEGDN PLWRVDLLQV YTITSVTITN RGDCCGERIS GARILIGKHL
     ENNGINNPEC STINIMAAGE TRTFHCPQPM IGRYVTVYLP KTGTLHLCEV EVNVLFPAPC