FUCL_ANGAN
ID FUCL_ANGAN Reviewed; 158 AA.
AC Q7SIC1;
DT 21-FEB-2006, integrated into UniProtKB/Swiss-Prot.
DT 15-DEC-2003, sequence version 1.
DT 03-AUG-2022, entry version 70.
DE RecName: Full=Fucolectin;
OS Anguilla anguilla (European freshwater eel) (Muraena anguilla).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Anguilliformes; Anguillidae;
OC Anguilla.
OX NCBI_TaxID=7936;
RN [1]
RP FUNCTION.
RX PubMed=15207656; DOI=10.1016/j.lfs.2004.02.016;
RA Wu A.M., Wu J.H., Singh T., Liu J.-H., Herp A.;
RT "Lectinochemical studies on the affinity of Anguilla anguilla agglutinin
RT for mammalian glycotopes.";
RL Life Sci. 75:1085-1103(2004).
RN [2] {ECO:0007744|PDB:1K12}
RP X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) IN COMPLEX WITH ALPHA-L-FUCOSE AND
RP CALCIUM, FUNCTION, AND SUBUNIT.
RX PubMed=12091873; DOI=10.1038/nsb817;
RA Bianchet M.A., Odom E.W., Vasta G.R., Amzel L.M.;
RT "A novel fucose recognition fold involved in innate immunity.";
RL Nat. Struct. Biol. 9:628-634(2002).
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:12091873, ECO:0000269|PubMed:15207656}.
CC -!- SUBUNIT: Homotrimer. {ECO:0000269|PubMed:12091873}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
CC -!- MISCELLANEOUS: Binds 1 calcium ion per monomer.
CC -!- SIMILARITY: Belongs to the fucolectin family. {ECO:0000305}.
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DR PDB; 1K12; X-ray; 1.90 A; A=1-158.
DR PDBsum; 1K12; -.
DR AlphaFoldDB; Q7SIC1; -.
DR SMR; Q7SIC1; -.
DR CAZy; CBM47; Carbohydrate-Binding Module Family 47.
DR UniLectin; Q7SIC1; -.
DR EvolutionaryTrace; Q7SIC1; -.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0005509; F:calcium ion binding; IDA: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 1: Evidence at protein level;
KW 3D-structure; Calcium; Disulfide bond; Lectin; Metal-binding; Secreted.
FT CHAIN 1..158
FT /note="Fucolectin"
FT /evidence="ECO:0000305"
FT /id="PRO_0000223931"
FT REGION 16..148
FT /note="F5/8 type C-like"
FT MOTIF 79..81
FT /note="Cell attachment site"
FT /evidence="ECO:0000255"
FT BINDING 35
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000269|PubMed:12091873,
FT ECO:0007744|PDB:1K12"
FT BINDING 38
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000269|PubMed:12091873,
FT ECO:0007744|PDB:1K12"
FT BINDING 40
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000269|PubMed:12091873,
FT ECO:0007744|PDB:1K12"
FT BINDING 49
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000269|PubMed:12091873,
FT ECO:0007744|PDB:1K12"
FT BINDING 52
FT /ligand="alpha-L-fucose"
FT /ligand_id="ChEBI:CHEBI:42548"
FT /evidence="ECO:0000269|PubMed:12091873,
FT ECO:0007744|PDB:1K12"
FT BINDING 79
FT /ligand="alpha-L-fucose"
FT /ligand_id="ChEBI:CHEBI:42548"
FT /evidence="ECO:0000269|PubMed:12091873,
FT ECO:0007744|PDB:1K12"
FT BINDING 86
FT /ligand="alpha-L-fucose"
FT /ligand_id="ChEBI:CHEBI:42548"
FT /evidence="ECO:0000269|PubMed:12091873,
FT ECO:0007744|PDB:1K12"
FT BINDING 146
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000269|PubMed:12091873,
FT ECO:0007744|PDB:1K12"
FT BINDING 147
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000269|PubMed:12091873,
FT ECO:0007744|PDB:1K12"
FT DISULFID 50..146
FT /evidence="ECO:0000269|PubMed:12091873"
FT DISULFID 82..83
FT /evidence="ECO:0000269|PubMed:12091873"
FT DISULFID 108..124
FT /evidence="ECO:0000269|PubMed:12091873"
FT STRAND 6..10
FT /evidence="ECO:0007829|PDB:1K12"
FT HELIX 11..14
FT /evidence="ECO:0007829|PDB:1K12"
FT STRAND 15..20
FT /evidence="ECO:0007829|PDB:1K12"
FT HELIX 28..30
FT /evidence="ECO:0007829|PDB:1K12"
FT HELIX 33..37
FT /evidence="ECO:0007829|PDB:1K12"
FT HELIX 45..47
FT /evidence="ECO:0007829|PDB:1K12"
FT STRAND 60..78
FT /evidence="ECO:0007829|PDB:1K12"
FT STRAND 80..82
FT /evidence="ECO:0007829|PDB:1K12"
FT TURN 84..89
FT /evidence="ECO:0007829|PDB:1K12"
FT STRAND 91..97
FT /evidence="ECO:0007829|PDB:1K12"
FT TURN 99..104
FT /evidence="ECO:0007829|PDB:1K12"
FT STRAND 107..110
FT /evidence="ECO:0007829|PDB:1K12"
FT STRAND 119..136
FT /evidence="ECO:0007829|PDB:1K12"
FT STRAND 139..141
FT /evidence="ECO:0007829|PDB:1K12"
FT STRAND 145..155
FT /evidence="ECO:0007829|PDB:1K12"
SQ SEQUENCE 158 AA; 16893 MW; 80DCA6BB1E5AD701 CRC64;
VIPEGYTQEN VAVRGKATQS AQLRGEHAAN SEASNAIDGN RDSNFYHGSC THSSGQANPW
WRVDLLQVYT ITSVTITNRG DCCGERISGA EINIGQHLAS NGVNNPECSV IGSMATGETK
TFHCPAPMIG RYVVTYLPTS ESLHLCEVEV NVDKPAAA
