ID   LEG2_CONMY              Reviewed;         136 AA.
AC   Q9YIC2;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   03-AUG-2022, entry version 104.
DE   RecName: Full=Congerin-2;
DE   AltName: Full=Beta-galactoside-binding lectin 2;
DE   AltName: Full=Congerin II;
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   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=10478448; DOI=10.1271/bbb.63.1203;
RA   Ogawa T., Ishii C., Kagawa D., Muramoto K., Kamiya H.;
RT   "Accelerated evolution in the protein-coding region of galectin cDNAs,
RT   congerin I and congerin II, from skin mucus of conger eel (Conger
RT   myriaster).";
RL   Biosci. Biotechnol. Biochem. 63:1203-1208(1999).
RN   [2]
RP   PROTEIN SEQUENCE OF 2-136, AND ACETYLATION AT SER-2.
RC   TISSUE=Skin mucus;
RX   PubMed=10425711; DOI=10.1016/s0305-0491(99)00037-1;
RA   Muramoto K., Kagawa D., Sato T., Ogawa T., Nishida Y., Kamiya H.;
RT   "Functional and structural characterization of multiple galectins from the
RT   skin mucus of conger eel, Conger myriaster.";
RL   Comp. Biochem. Physiol. 123B:33-45(1999).
RN   [3]
RP   X-RAY CRYSTALLOGRAPHY (1.45 ANGSTROMS) IN COMPLEX WITH LACTOSE.
RX   PubMed=12206768; DOI=10.1016/s0022-2836(02)00700-3;
RA   Shirai T., Matsui Y., Shionyu-Mitsuyama C., Yamane T., Kamiya H., Ishii C.,
RA   Ogawa T., Muramoto K.;
RT   "Crystal structure of a conger eel galectin (congerin II) at 1.45A
RT   resolution: implication for the accelerated evolution of a new ligand-
RT   binding site following gene duplication.";
RL   J. Mol. Biol. 321:879-889(2002).
CC   -!- FUNCTION: This protein binds beta-galactoside. Its physiological
CC       function is not yet known.
CC   -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:12206768}.
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DR   EMBL; AB010277; BAA36386.1; -; mRNA.
DR   PDB; 1IS3; X-ray; 1.45 A; A=2-136.
DR   PDB; 1IS4; X-ray; 1.90 A; A=2-136.
DR   PDB; 1IS5; X-ray; 2.00 A; A=2-136.
DR   PDB; 1IS6; X-ray; 1.70 A; A=2-136.
DR   PDB; 1WLC; X-ray; 2.00 A; A=2-136.
DR   PDB; 1WLD; X-ray; 1.60 A; A=2-136.
DR   PDB; 1WLW; X-ray; 1.80 A; A=2-136.
DR   PDBsum; 1IS3; -.
DR   PDBsum; 1IS4; -.
DR   PDBsum; 1IS5; -.
DR   PDBsum; 1IS6; -.
DR   PDBsum; 1WLC; -.
DR   PDBsum; 1WLD; -.
DR   PDBsum; 1WLW; -.
DR   AlphaFoldDB; Q9YIC2; -.
DR   SMR; Q9YIC2; -.
DR   UniLectin; Q9YIC2; -.
DR   iPTMnet; Q9YIC2; -.
DR   EvolutionaryTrace; Q9YIC2; -.
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   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000269|PubMed:10425711"
FT   CHAIN           2..136
FT                   /note="Congerin-2"
FT                   /id="PRO_0000076955"
FT   DOMAIN          4..136
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         2
FT                   /note="N-acetylserine"
FT                   /evidence="ECO:0000269|PubMed:10425711"
FT   STRAND          5..13
FT                   /evidence="ECO:0007829|PDB:1IS3"
FT   STRAND          18..24
FT                   /evidence="ECO:0007829|PDB:1IS3"
FT   STRAND          30..38
FT                   /evidence="ECO:0007829|PDB:1IS3"
FT   STRAND          41..52
FT                   /evidence="ECO:0007829|PDB:1IS3"
FT   STRAND          57..65
FT                   /evidence="ECO:0007829|PDB:1IS3"
FT   TURN            66..68
FT                   /evidence="ECO:0007829|PDB:1IS3"
FT   STRAND          74..76
FT                   /evidence="ECO:0007829|PDB:1IS3"
FT   STRAND          85..93
FT                   /evidence="ECO:0007829|PDB:1IS3"
FT   STRAND          95..101
FT                   /evidence="ECO:0007829|PDB:1IS3"
FT   STRAND          107..111
FT                   /evidence="ECO:0007829|PDB:1IS3"
FT   STRAND          117..135
FT                   /evidence="ECO:0007829|PDB:1IS3"
SQ   SEQUENCE   136 AA;  15467 MW;  AABB02B9BEBA6A1A CRC64;
     MSDRAEVRNI PFKLGMYLTV GGVVNSNATR FSINVGESTD SIAMHMDHRF SYGADQNVLV
     LNSLVHNVGW QQEERSKKFP FTKGDHFQTT ITFDTHTFYI QLSNGETVEF PNRNKDAAFN
     LIYLAGDARL TFVRLE