ID   LEG1_PIG                Reviewed;         135 AA.
AC   Q49I35;
DT   04-APR-2006, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   03-AUG-2022, entry version 80.
DE   RecName: Full=Galectin-1;
DE            Short=Gal-1;
DE   AltName: Full=Lectin galactoside-binding soluble 1;
GN   Name=LGALS1;
OS   Sus scrofa (Pig).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX   NCBI_TaxID=9823;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RA   Niu B.Y., Li F.E., Xiong Y.Z.;
RT   "Isolation and sequence analysis of galectin 1.";
RL   Submitted (JAN-2005) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Lectin that binds beta-galactoside and a wide array of
CC       complex carbohydrates. Plays a role in regulating apoptosis, cell
CC       proliferation and cell differentiation. Inhibits CD45 protein
CC       phosphatase activity and therefore the dephosphorylation of Lyn kinase.
CC       Strong inducer of T-cell apoptosis. {ECO:0000250|UniProtKB:P09382}.
CC   -!- SUBUNIT: Homodimer. Binds LGALS3BP. Interacts with CD2, CD3, CD4, CD6,
CC       CD7, CD43, ALCAM and CD45. Interacts with laminin (via poly-N-
CC       acetyllactosamine). Interacts with SUSD2. Interacts with cargo receptor
CC       TMED10; the interaction mediates the translocation from the cytoplasm
CC       into the ERGIC (endoplasmic reticulum-Golgi intermediate compartment)
CC       and thereby secretion. {ECO:0000250|UniProtKB:P09382}.
CC   -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
CC       matrix {ECO:0000250|UniProtKB:P09382}. Cytoplasm
CC       {ECO:0000250|UniProtKB:P09382}. Secreted
CC       {ECO:0000250|UniProtKB:P09382}. Note=Can be secreted; the secretion is
CC       dependent on protein unfolding and facilitated by the cargo receptor
CC       TMED10; it results in protein translocation from the cytoplasm into the
CC       ERGIC (endoplasmic reticulum-Golgi intermediate compartment) followed
CC       by vesicle entry and secretion. {ECO:0000250|UniProtKB:P09382}.
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DR   EMBL; AY885253; AAX85355.1; -; mRNA.
DR   AlphaFoldDB; Q49I35; -.
DR   SMR; Q49I35; -.
DR   IntAct; Q49I35; 1.
DR   STRING; 9823.ENSSSCP00000000129; -.
DR   PaxDb; Q49I35; -.
DR   PeptideAtlas; Q49I35; -.
DR   PRIDE; Q49I35; -.
DR   eggNOG; KOG3587; Eukaryota.
DR   InParanoid; Q49I35; -.
DR   ChiTaRS; LGALS1; pig.
DR   Proteomes; UP000008227; Unplaced.
DR   Proteomes; UP000314985; Unplaced.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
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   GO; GO:0006915; P:apoptotic process; 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   2: Evidence at transcript level;
KW   Acetylation; Apoptosis; Cytoplasm; Extracellular matrix; Lectin;
KW   Phosphoprotein; Reference proteome; Secreted.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000250|UniProtKB:P09382"
FT   CHAIN           2..135
FT                   /note="Galectin-1"
FT                   /id="PRO_0000231038"
FT   DOMAIN          4..135
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                   /evidence="ECO:0000250"
FT   BINDING         53
FT                   /ligand="a beta-D-galactoside"
FT                   /ligand_id="ChEBI:CHEBI:28034"
FT                   /evidence="ECO:0000250"
FT   BINDING         62
FT                   /ligand="a beta-D-galactoside"
FT                   /ligand_id="ChEBI:CHEBI:28034"
FT                   /evidence="ECO:0000250"
FT   BINDING         69..72
FT                   /ligand="a beta-D-galactoside"
FT                   /ligand_id="ChEBI:CHEBI:28034"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         2
FT                   /note="N-acetylalanine"
FT                   /evidence="ECO:0000250|UniProtKB:P09382"
FT   MOD_RES         13
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:P16045"
FT   MOD_RES         19
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:P16045"
FT   MOD_RES         29
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:P09382"
FT   MOD_RES         30
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P09382"
FT   MOD_RES         128
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:P16045"
SQ   SEQUENCE   135 AA;  14694 MW;  38877BF21BC67AFB CRC64;
     MACGLVASNL NLKPGECLKV RGEVAPDAKS FVLNLGKDSN NLCLHFNPRF DMHGDINTIV
     CNSKDGGAWG AEQRESAFPF QPGSVVEVCI SFGQTDLTIK LPDGYEFSFP NRLNLEAIEH
     LAADGDFKIK CVAFE