ID   AJL1_ANGJA              Reviewed;         142 AA.
AC   Q801X7;
DT   07-DEC-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   03-AUG-2022, entry version 60.
DE   RecName: Full=Galactose-binding lectin l-1;
DE            Short=Galectin;
DE   AltName: Full=Ajl-1;
GN   Name=l-1 {ECO:0000303|PubMed:14698218};
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:BAC67210.1}
RP   NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 8-13; 64-73 AND 109-141,
RP   FUNCTION, SUBUNIT, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RC   TISSUE=Skin mucus {ECO:0000269|PubMed:14698218};
RX   PubMed=14698218; DOI=10.1016/j.dci.2003.08.006;
RA   Tasumi S., Yang W.-J., Usami T., Tsutsui S., Ohira T., Kawazoe I.,
RA   Wilder M.N., Aida K., Suzuki Y.;
RT   "Characteristics and primary structure of a galectin in the skin mucus of
RT   the Japanese eel, Anguilla japonica.";
RL   Dev. Comp. Immunol. 28:325-335(2004).
RN   [2] {ECO:0000305}
RP   SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND MASS SPECTROMETRY.
RC   TISSUE=Skin mucus {ECO:0000269|PubMed:11959866};
RX   PubMed=11959866; DOI=10.1074/jbc.m202648200;
RA   Tasumi S., Ohira T., Kawazoe I., Suetake H., Suzuki Y., Aida K.;
RT   "Primary structure and characteristics of a lectin from skin mucus of the
RT   Japanese eel Anguilla japonica.";
RL   J. Biol. Chem. 277:27305-27311(2002).
CC   -!- FUNCTION: Involved in host defense at the body surface. Causes
CC       agglutination of the Gram-positive bacterium S.difficile. Possesses
CC       calcium-independent hemagglutinating activity.
CC       {ECO:0000269|PubMed:14698218}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:14698218}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:11959866,
CC       ECO:0000269|PubMed:14698218}.
CC   -!- TISSUE SPECIFICITY: Skin; highest expression in that of individuals
CC       showing resistance to infectious disease. {ECO:0000269|PubMed:11959866,
CC       ECO:0000269|PubMed:14698218}.
CC   -!- PTM: The N-terminus is blocked. {ECO:0000269|PubMed:11959866,
CC       ECO:0000269|PubMed:14698218}.
CC   -!- MASS SPECTROMETRY: Mass=16091; Method=MALDI;
CC       Evidence={ECO:0000269|PubMed:11959866};
CC   -!- MISCELLANEOUS: Binds beta-galactoside inhibiting its haemagglutinating
CC       activity. {ECO:0000269|PubMed:14698218}.
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DR   EMBL; AB098064; BAC67210.1; -; mRNA.
DR   AlphaFoldDB; Q801X7; -.
DR   SMR; Q801X7; -.
DR   GO; GO:0005576; C:extracellular region; IDA:UniProtKB.
DR   GO; GO:0030246; F:carbohydrate binding; IDA:UniProtKB.
DR   GO; GO:0050830; P:defense response to Gram-positive bacterium; IDA:UniProtKB.
DR   GO; GO:0043152; P:induction of bacterial agglutination; IDA:UniProtKB.
DR   CDD; cd00070; GLECT; 1.
DR   InterPro; IPR013320; ConA-like_dom_sf.
DR   InterPro; IPR044156; Galectin-like.
DR   InterPro; IPR001079; Galectin_CRD.
DR   PANTHER; PTHR11346; PTHR11346; 1.
DR   Pfam; PF00337; Gal-bind_lectin; 1.
DR   SMART; SM00908; Gal-bind_lectin; 1.
DR   SMART; SM00276; GLECT; 1.
DR   SUPFAM; SSF49899; SSF49899; 1.
DR   PROSITE; PS51304; GALECTIN; 1.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; Glycoprotein; Hemagglutinin; Lectin; Secreted.
FT   CHAIN           1..142
FT                   /note="Galactose-binding lectin l-1"
FT                   /id="PRO_0000076953"
FT   DOMAIN          3..134
FT                   /note="Galectin"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00639"
FT   BINDING         68..74
FT                   /ligand="a beta-D-galactoside"
FT                   /ligand_id="ChEBI:CHEBI:28034"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        130
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CONFLICT        72
FT                   /note="Q -> E (in Ref. 1; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        111
FT                   /note="H -> HN (in Ref. 1; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        116
FT                   /note="E -> EQ (in Ref. 1; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        134
FT                   /note="N -> L (in Ref. 1; AA sequence)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   142 AA;  16205 MW;  A437DBF509C9EE22 CRC64;
     MDFVEVKNLI MKSGMELKVN GVFNANPERF SINVGHSTEE IAVHVDVRFS YLSDKRQLII
     NHKTGDAWQE EQRDARFPFT AGQAFQVSVV FNFDTFDIYL PDGQVAHFTN HLGAQEYKYI
     FFVGDATVKN ISVNVADKPT KR