ID   LEG6_CHICK              Reviewed;         134 AA.
AC   P23668; Q53YM0;
DT   01-NOV-1991, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1991, sequence version 1.
DT   03-AUG-2022, entry version 145.
DE   RecName: Full=16 kDa beta-galactoside-binding lectin;
DE   AltName: Full=C-16;
DE   AltName: Full=Galectin CG-16;
OS   Gallus gallus (Chicken).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC   Phasianinae; Gallus.
OX   NCBI_TaxID=9031;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Kidney;
RA   Kaltner H., Gabius H.-J.;
RT   "Chicken galectin CG-16 (16 kDa beta-galactoside-binding lectin), full
RT   length cDNA from embryonic kidney.";
RL   Submitted (FEB-2004) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 1-117, PROTEIN SEQUENCE OF 1-60; 65-98 AND
RP   101-134, AND ACETYLATION AT MET-1.
RC   TISSUE=Liver;
RX   PubMed=2254315; DOI=10.1016/s0021-9258(18)45779-1;
RA   Sakakura Y., Hirabayashi J., Oda Y., Ohyama Y., Kasai K.;
RT   "Structure of chicken 16-kDa beta-galactoside-binding lectin. Complete
RT   amino acid sequence, cloning of cDNA, and production of recombinant
RT   lectin.";
RL   J. Biol. Chem. 265:21573-21579(1990).
RN   [3]
RP   X-RAY CRYSTALLOGRAPHY (2.15 ANGSTROMS).
RC   TISSUE=Liver;
RX   PubMed=10610778; DOI=10.1006/jmbi.1999.3273;
RA   Varela P.F., Solis D., Diaz-Maurino T., Kaltner H., Gabius H.-J.,
RA   Romero A.;
RT   "The 2.15 A crystal structure of CG-16, the developmentally regulated
RT   homodimeric chicken galectin.";
RL   J. Mol. Biol. 294:537-549(1999).
CC   -!- FUNCTION: This protein binds beta-galactoside. Its physiological
CC       function is not yet known. It may be involved in the regulation of
CC       differentiation.
CC   -!- SUBUNIT: Homodimer.
CC   -!- TISSUE SPECIFICITY: Mainly in the liver (adult), mainly in the muscle
CC       (embryo).
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AY553270; AAS59560.1; -; mRNA.
DR   EMBL; M57240; AAA48626.1; -; mRNA.
DR   PIR; A36496; LNCH16.
DR   RefSeq; NP_996788.1; NM_206905.1.
DR   PDB; 1QMJ; X-ray; 2.15 A; A/B=3-134.
DR   PDBsum; 1QMJ; -.
DR   AlphaFoldDB; P23668; -.
DR   SMR; P23668; -.
DR   STRING; 9031.ENSGALP00000041067; -.
DR   UniLectin; P23668; -.
DR   iPTMnet; P23668; -.
DR   PaxDb; P23668; -.
DR   GeneID; 404269; -.
DR   KEGG; gga:404269; -.
DR   CTD; 404269; -.
DR   VEuPathDB; HostDB:geneid_404269; -.
DR   eggNOG; KOG3587; Eukaryota.
DR   HOGENOM; CLU_037794_5_0_1; -.
DR   OrthoDB; 1429018at2759; -.
DR   PhylomeDB; P23668; -.
DR   EvolutionaryTrace; P23668; -.
DR   PRO; PR:P23668; -.
DR   Proteomes; UP000000539; Unplaced.
DR   GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR   GO; GO:0030246; F:carbohydrate binding; IBA:GO_Central.
DR   GO; GO:0043236; F:laminin binding; IBA:GO_Central.
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;
KW   Reference proteome.
FT   CHAIN           1..134
FT                   /note="16 kDa beta-galactoside-binding lectin"
FT                   /id="PRO_0000076952"
FT   DOMAIN          4..134
FT                   /note="Galectin"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00639"
FT   BINDING         69..75
FT                   /ligand="a beta-D-galactoside"
FT                   /ligand_id="ChEBI:CHEBI:28034"
FT                   /evidence="ECO:0000255"
FT   MOD_RES         1
FT                   /note="N-acetylmethionine"
FT                   /evidence="ECO:0000269|PubMed:2254315"
FT   STRAND          6..9
FT                   /evidence="ECO:0007829|PDB:1QMJ"
FT   STRAND          18..24
FT                   /evidence="ECO:0007829|PDB:1QMJ"
FT   STRAND          29..38
FT                   /evidence="ECO:0007829|PDB:1QMJ"
FT   STRAND          41..52
FT                   /evidence="ECO:0007829|PDB:1QMJ"
FT   STRAND          55..61
FT                   /evidence="ECO:0007829|PDB:1QMJ"
FT   STRAND          73..76
FT                   /evidence="ECO:0007829|PDB:1QMJ"
FT   STRAND          85..92
FT                   /evidence="ECO:0007829|PDB:1QMJ"
FT   STRAND          94..100
FT                   /evidence="ECO:0007829|PDB:1QMJ"
FT   STRAND          105..109
FT                   /evidence="ECO:0007829|PDB:1QMJ"
FT   STRAND          119..133
FT                   /evidence="ECO:0007829|PDB:1QMJ"
SQ   SEQUENCE   134 AA;  14934 MW;  7E698A458EA444BA CRC64;
     MEQGLVVTQL DVQPGECVKV KGKILSDAKG FSVNVGKDSS TLMLHFNPRF DCHGDVNTVV
     CNSKEDGTWG EEDRKADFPF QQGDKVEICI SFDAAEVKVK VPEVEFEFPN RLGMEKIQYL
     AVEGDFKVKA IKFS