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Q9I930 (FUCL2_ANGJA) Reviewed, UniProtKB/Swiss-Prot

Last modified October 19, 2011. Version 46. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Fucolectin-2
OrganismAnguilla japonica (Japanese eel)
Taxonomic identifier7937 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiActinopterygiiNeopterygiiTeleosteiAnguilliformesAnguillidaeAnguilla

Protein attributes

Sequence length180 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

Acts as a defensive agent. Recognizes blood group fucosylated oligosaccharides including A, B, H and Lewis B-type antigens. Does not recognize Lewis A antigen and has low affinity for monovalent haptens. Ref.1

Subunit structure

Homotrimer By similarity. UniProtKB Q7SIC1

Subcellular location

Secretedextracellular space Ref.1.

Tissue specificity

Parenchymal hepatocytes. Ref.1

Miscellaneous

Binds 1 calcium ion per monomer By similarity.

Sequence similarities

Belongs to the fucolectin family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2222 Potential
Chain23 – 180158Fucolectin-2
PRO_0000223933

Regions

Region31 – 179149F5/8 type C-like
Region49 – 502Antigenic glycan By similarity UniProtKB Q7SIC1
Region104 – 1052Antigenic glycan By similarity UniProtKB Q7SIC1
Motif101 – 1033Cell attachment site

Sites

Metal binding581Calcium; via carbonyl oxygen By similarity UniProtKB Q7SIC1
Metal binding611Calcium By similarity UniProtKB Q7SIC1
Metal binding631Calcium; via carbonyl oxygen By similarity UniProtKB Q7SIC1
Metal binding721Calcium By similarity UniProtKB Q7SIC1
Metal binding1681Calcium; via carbonyl oxygen By similarity UniProtKB Q7SIC1
Metal binding1691Calcium By similarity UniProtKB Q7SIC1
Binding site691Antigenic glycan By similarity UniProtKB Q7SIC1
Binding site751Antigenic glycan By similarity UniProtKB Q7SIC1
Binding site1011Antigenic glycan By similarity UniProtKB Q7SIC1
Binding site1081Antigenic glycan By similarity UniProtKB Q7SIC1

Amino acid modifications

Disulfide bond73 ↔ 168 By similarity UniProtKB Q7SIC1
Disulfide bond104 ↔ 105 By similarity UniProtKB Q7SIC1
Disulfide bond130 ↔ 146 By similarity UniProtKB Q7SIC1

Sequences

Sequence LengthMass (Da)Tools
Q9I930 [UniParc].

Last modified October 1, 2000. Version 1.
Checksum: D572D09AED85C206

FASTA18019,776
        10         20         30         40         50         60 
MKVKMIMLLF QILAILTLKS DSADVPDGYI QENVALRGRA TQSAQLRGEH AGISHASNAI 

        70         80         90        100        110        120 
DGNRDSYFYH GSCSHTEGDN PLWRVDLLQV YTITSVTITN RGDCCGERIS GARILIGKHL 

       130        140        150        160        170        180 
ENNGINNPEC STINIMAAGE TRTFHCPQPM IGRYVTVYLP KTGTLHLCEV EVNVLFPAPC 

« Hide

References

[1]"Multiplicity, structures, and endocrine and exocrine natures of eel fucose-binding lectins."
Honda S., Kashiwagi M., Miyamoto K., Takei Y., Hirose S.
J. Biol. Chem. 275:33151-33157(2000) [PubMed: 10924498] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
Tissue: Liver.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AB037868 mRNA. Translation: BAB03524.1.

3D structure databases

ProteinModelPortalQ9I930.
SMRQ9I930. Positions 25-178.
ModBaseSearch...

Protein family/group databases

CAZyCBM47. Carbohydrate-Binding Module Family 47.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Phylogenomic databases

HOVERGENHBG066195.

Family and domain databases

InterProIPR000421. Coagulation_fac_5/8-C_type_dom.
IPR006585. FTP1.
IPR008979. Galactose-bd-like.
[Graphical view]
PfamPF00754. F5_F8_type_C. 1 hit.
[Graphical view]
SMARTSM00607. FTP. 1 hit.
[Graphical view]
SUPFAMSSF49785. Gal_bind_like. 1 hit.
ProtoNetSearch...

Entry information

Entry nameFUCL2_ANGJA
AccessionPrimary (citable) accession number: Q9I930
Entry history
Integrated into UniProtKB/Swiss-Prot: February 21, 2006
Last sequence update: October 1, 2000
Last modified: October 19, 2011
This is version 46 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families