ID   LEG1_CONMY              Reviewed;         135 AA.
AC   P26788;
DT   01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1992, sequence version 1.
DT   03-AUG-2022, entry version 98.
DE   RecName: Full=Congerin-1;
DE   AltName: Full=Beta-galactoside-binding lectin 1;
DE   AltName: Full=Congerin I;
OS   Conger myriaster (Conger eel).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Anguilliformes; Congridae; Conger.
OX   NCBI_TaxID=7943;
RN   [1]
RP   PROTEIN SEQUENCE, AND ACETYLATION AT SER-1.
RC   TISSUE=Skin mucus;
RX   PubMed=1581341; DOI=10.1016/0304-4165(92)90109-8;
RA   Muramoto K., Kamiya H.;
RT   "The amino-acid sequence of a lectin from conger eel, Conger myriaster,
RT   skin mucus.";
RL   Biochim. Biophys. Acta 1116:129-136(1992).
RN   [2]
RP   X-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS).
RX   PubMed=10545323; DOI=10.1016/s0969-2126(00)80056-8;
RA   Shirai T., Mitsuyama C., Niwa Y., Matsui Y., Hotta H., Yamane T.,
RA   Kamiya H., Ishii C., Ogawa T., Muramoto K.;
RT   "High-resolution structure of the conger eel galectin, congerin I, in
RT   lactose-liganded and ligand-free forms: emergence of a new structure class
RT   by accelerated evolution.";
RL   Structure 7:1223-1233(1999).
CC   -!- FUNCTION: This protein binds beta-galactoside. Its physiological
CC       function is not yet known.
CC   -!- SUBUNIT: Homodimer.
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DR   PIR; S21102; S21102.
DR   PDB; 1C1F; X-ray; 1.60 A; A=1-135.
DR   PDB; 1C1L; X-ray; 1.50 A; A=1-135.
DR   PDBsum; 1C1F; -.
DR   PDBsum; 1C1L; -.
DR   AlphaFoldDB; P26788; -.
DR   SMR; P26788; -.
DR   UniLectin; P26788; -.
DR   iPTMnet; P26788; -.
DR   EvolutionaryTrace; P26788; -.
DR   GO; GO:0030246; F:carbohydrate binding; IEA:UniProtKB-KW.
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   3D-structure; Acetylation; Direct protein sequencing; Lectin.
FT   CHAIN           1..135
FT                   /note="Congerin-1"
FT                   /id="PRO_0000076954"
FT   DOMAIN          3..135
FT                   /note="Galectin"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00639"
FT   BINDING         70..76
FT                   /ligand="a beta-D-galactoside"
FT                   /ligand_id="ChEBI:CHEBI:28034"
FT                   /evidence="ECO:0000255"
FT   MOD_RES         1
FT                   /note="N-acetylserine"
FT                   /evidence="ECO:0000269|PubMed:1581341"
FT   STRAND          16..23
FT                   /evidence="ECO:0007829|PDB:1C1L"
FT   STRAND          29..37
FT                   /evidence="ECO:0007829|PDB:1C1L"
FT   STRAND          40..51
FT                   /evidence="ECO:0007829|PDB:1C1L"
FT   STRAND          54..65
FT                   /evidence="ECO:0007829|PDB:1C1L"
FT   HELIX           66..68
FT                   /evidence="ECO:0007829|PDB:1C1L"
FT   STRAND          74..76
FT                   /evidence="ECO:0007829|PDB:1C1L"
FT   STRAND          86..93
FT                   /evidence="ECO:0007829|PDB:1C1L"
FT   STRAND          95..102
FT                   /evidence="ECO:0007829|PDB:1C1L"
FT   STRAND          107..111
FT                   /evidence="ECO:0007829|PDB:1C1L"
FT   STRAND          121..134
FT                   /evidence="ECO:0007829|PDB:1C1L"
SQ   SEQUENCE   135 AA;  15204 MW;  3AEC767E39EBCE3B CRC64;
     SGGLQVKNFD FTVGKFLTVG GFINNSPQRF SVNVGESMNS LSLHLDHRFN YGADQNTIVM
     NSTLKGDNGW ETEQRSTNFT LSAGQYFEIT LSYDINKFYI DILDGPNLEF PNRYSKEFLP
     FLSLAGDARL TLVKE