ID   LEG1_RHIAE              Reviewed;         134 AA.
AC   P56217;
DT   15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT   15-DEC-1998, sequence version 2.
DT   03-AUG-2022, entry version 101.
DE   RecName: Full=Galectin-1;
DE            Short=Gal-1;
OS   Rhinella arenarum (Argentine common toad) (Bufo arenarum).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Neobatrachia; Hyloidea; Bufonidae; Rhinella.
OX   NCBI_TaxID=38577;
RN   [1]
RP   PROTEIN SEQUENCE, ACETYLATION AT ALA-1, AND CHARACTERIZATION.
RC   TISSUE=Ovary;
RX   PubMed=8955156; DOI=10.1074/jbc.271.51.33083;
RA   Ahmed H., Pohl J., Fink N.E., Strobel F., Vasta G.R.;
RT   "The primary structure and carbohydrate specificity of a beta-galactosyl-
RT   binding lectin from toad (Bufo arenarum Hensel) ovary reveal closer
RT   similarities to the mammalian galectin-1 than to the galectin from the
RT   clawed frog Xenopus laevis.";
RL   J. Biol. Chem. 271:33083-33094(1996).
RN   [2]
RP   X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) IN COMPLEX WITH CARBOHYDRATE.
RC   TISSUE=Ovary;
RX   PubMed=10861929;
RX   DOI=10.1002/1097-0134(20000815)40:3<378::aid-prot40>3.0.co;2-7;
RA   Bianchet M.A., Ahmed H., Vasta G.R., Amzel L.M.;
RT   "Soluble beta-galactosyl-binding lectin (galectin) from toad ovary:
RT   crystallographic studies of two protein-sugar complexes.";
RL   Proteins 40:378-388(2000).
CC   -!- FUNCTION: May regulate cell apoptosis and cell differentiation. Binds
CC       beta-galactoside and a wide array of complex carbohydrates (By
CC       similarity). {ECO:0000250}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:10861929}.
CC   -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
CC       matrix.
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DR   PDB; 1A78; X-ray; 2.00 A; A/B=1-134.
DR   PDB; 1GAN; X-ray; 2.23 A; A/B=1-134.
DR   PDBsum; 1A78; -.
DR   PDBsum; 1GAN; -.
DR   AlphaFoldDB; P56217; -.
DR   SMR; P56217; -.
DR   UniLectin; P56217; -.
DR   iPTMnet; P56217; -.
DR   EvolutionaryTrace; P56217; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
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; Extracellular matrix;
KW   Lectin; Secreted.
FT   CHAIN           1..134
FT                   /note="Galectin-1"
FT                   /id="PRO_0000076922"
FT   DOMAIN          4..134
FT                   /note="Galectin"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00639"
FT   BINDING         45..49
FT                   /ligand="a beta-D-galactoside"
FT                   /ligand_id="ChEBI:CHEBI:28034"
FT   BINDING         53
FT                   /ligand="a beta-D-galactoside"
FT                   /ligand_id="ChEBI:CHEBI:28034"
FT   BINDING         62
FT                   /ligand="a beta-D-galactoside"
FT                   /ligand_id="ChEBI:CHEBI:28034"
FT   BINDING         69..72
FT                   /ligand="a beta-D-galactoside"
FT                   /ligand_id="ChEBI:CHEBI:28034"
FT   MOD_RES         1
FT                   /note="N-acetylalanine"
FT                   /evidence="ECO:0000269|PubMed:8955156"
FT   STRAND          6..12
FT                   /evidence="ECO:0007829|PDB:1A78"
FT   STRAND          16..23
FT                   /evidence="ECO:0007829|PDB:1A78"
FT   STRAND          29..38
FT                   /evidence="ECO:0007829|PDB:1A78"
FT   STRAND          41..52
FT                   /evidence="ECO:0007829|PDB:1A78"
FT   STRAND          55..65
FT                   /evidence="ECO:0007829|PDB:1A78"
FT   STRAND          73..75
FT                   /evidence="ECO:0007829|PDB:1A78"
FT   STRAND          84..92
FT                   /evidence="ECO:0007829|PDB:1A78"
FT   STRAND          94..101
FT                   /evidence="ECO:0007829|PDB:1A78"
FT   STRAND          106..110
FT                   /evidence="ECO:0007829|PDB:1A78"
FT   STRAND          116..133
FT                   /evidence="ECO:0007829|PDB:1A78"
SQ   SEQUENCE   134 AA;  14711 MW;  A0C180443EBE7737 CRC64;
     ASAGVAVTNL NLKPGHCVEI KGSIPPDCKG FAVNLGEDAS NFLLHFNARF DLHGDVNKIV
     CNSKEADAWG SEQREEVFPF QQGAEVMVCF EYQTQKIIIK FSSGDQFSFP VRKVLPSIPF
     LSLEGLAFKS ITTE