LEG1_RAT
ID LEG1_RAT Reviewed; 135 AA.
AC P11762;
DT 01-OCT-1989, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 164.
DE RecName: Full=Galectin-1;
DE Short=Gal-1;
DE AltName: Full=14 kDa lectin;
DE AltName: Full=Beta-galactoside-binding lectin L-14-I;
DE AltName: Full=Galaptin;
DE AltName: Full=Lactose-binding lectin 1;
DE AltName: Full=Lectin galactoside-binding soluble 1;
DE AltName: Full=RL 14.5;
DE AltName: Full=S-Lac lectin 1;
GN Name=Lgals1;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=3349058; DOI=10.1021/bi00402a030;
RA Clerch L.B., Whitney P., Hass M., Brew K., Miller T., Werner R.,
RA Massaro D.;
RT "Sequence of a full-length cDNA for rat lung beta-galactoside-binding
RT protein: primary and secondary structure of the lectin.";
RL Biochemistry 27:692-699(1988).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Brain;
RX PubMed=2319298; DOI=10.1523/jneurosci.10-03-01004.1990;
RA Hynes M.A., Gitt M., Barondes S.H., Jessell T.M., Buck L.B.;
RT "Selective expression of an endogenous lactose-binding lectin gene in
RT subsets of central and peripheral neurons.";
RL J. Neurosci. 10:1004-1013(1990).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Pituitary;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4]
RP PROTEIN SEQUENCE OF 38-49, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC STRAIN=Sprague-Dawley; TISSUE=Spinal cord;
RA Lubec G., Afjehi-Sadat L.;
RL Submitted (NOV-2006) to UniProtKB.
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}.
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; M19036; AAA40822.1; -; mRNA.
DR EMBL; BC058476; AAH58476.1; -; mRNA.
DR PIR; A28703; LNRTGB.
DR RefSeq; NP_063969.1; NM_019904.1.
DR PDB; 3M2M; X-ray; 2.95 A; A/B/C/D/E/F/G/H=2-135.
DR PDB; 4GA9; X-ray; 1.88 A; A/B=2-135.
DR PDB; 4NO4; X-ray; 1.40 A; A/B/C/D/E/F=2-135.
DR PDBsum; 3M2M; -.
DR PDBsum; 4GA9; -.
DR PDBsum; 4NO4; -.
DR AlphaFoldDB; P11762; -.
DR SMR; P11762; -.
DR BioGRID; 248567; 1.
DR DIP; DIP-37188N; -.
DR IntAct; P11762; 2.
DR STRING; 10116.ENSRNOP00000013538; -.
DR BindingDB; P11762; -.
DR ChEMBL; CHEMBL4523183; -.
DR UniLectin; P11762; -.
DR iPTMnet; P11762; -.
DR PhosphoSitePlus; P11762; -.
DR jPOST; P11762; -.
DR PaxDb; P11762; -.
DR PRIDE; P11762; -.
DR Ensembl; ENSRNOT00000013538; ENSRNOP00000013538; ENSRNOG00000009884.
DR GeneID; 56646; -.
DR KEGG; rno:56646; -.
DR UCSC; RGD:69355; rat.
DR CTD; 3956; -.
DR RGD; 69355; Lgals1.
DR eggNOG; KOG3587; Eukaryota.
DR GeneTree; ENSGT00940000155534; -.
DR HOGENOM; CLU_037794_5_0_1; -.
DR InParanoid; P11762; -.
DR OMA; KIKCMAF; -.
DR OrthoDB; 1429018at2759; -.
DR PhylomeDB; P11762; -.
DR Reactome; R-RNO-381426; Regulation of Insulin-like Growth Factor (IGF) transport and uptake by Insulin-like Growth Factor Binding Proteins (IGFBPs).
DR Reactome; R-RNO-8957275; Post-translational protein phosphorylation.
DR EvolutionaryTrace; P11762; -.
DR PRO; PR:P11762; -.
DR Proteomes; UP000002494; Chromosome 7.
DR Bgee; ENSRNOG00000009884; Expressed in ovary and 20 other tissues.
DR Genevisible; P11762; RN.
DR GO; GO:0009986; C:cell surface; IDA:RGD.
DR GO; GO:0005737; C:cytoplasm; IDA:RGD.
DR GO; GO:0005829; C:cytosol; IDA:RGD.
DR GO; GO:0005615; C:extracellular space; ISO:RGD.
DR GO; GO:1990724; C:galectin complex; ISO:RGD.
DR GO; GO:0005634; C:nucleus; IDA:RGD.
DR GO; GO:0030246; F:carbohydrate binding; ISO:RGD.
DR GO; GO:0042802; F:identical protein binding; IPI:RGD.
DR GO; GO:0030395; F:lactose binding; IDA:RGD.
DR GO; GO:0043236; F:laminin binding; IDA:RGD.
DR GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
DR GO; GO:0098609; P:cell-cell adhesion; ISO:RGD.
DR GO; GO:0071333; P:cellular response to glucose stimulus; IEP:RGD.
DR GO; GO:0071407; P:cellular response to organic cyclic compound; IEP:RGD.
DR GO; GO:0045445; P:myoblast differentiation; ISO:RGD.
DR GO; GO:0010812; P:negative regulation of cell-substrate adhesion; IDA:RGD.
DR GO; GO:0010977; P:negative regulation of neuron projection development; IMP:RGD.
DR GO; GO:0002317; P:plasma cell differentiation; ISO:RGD.
DR GO; GO:0043065; P:positive regulation of apoptotic process; ISO:RGD.
DR GO; GO:0034120; P:positive regulation of erythrocyte aggregation; IDA:RGD.
DR GO; GO:0050729; P:positive regulation of inflammatory response; ISO:RGD.
DR GO; GO:0046598; P:positive regulation of viral entry into host cell; ISO:RGD.
DR GO; GO:0048678; P:response to axon injury; IEP:RGD.
DR GO; GO:0035900; P:response to isolation stress; IEP:RGD.
DR GO; GO:0009410; P:response to xenobiotic stimulus; IEP:RGD.
DR GO; GO:0031295; P:T cell costimulation; ISO:RGD.
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; Apoptosis; Cytoplasm; Direct protein sequencing;
KW Extracellular matrix; Lectin; 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_0000076920"
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 108
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P16045"
FT MOD_RES 108
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P16045"
FT MOD_RES 128
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P16045"
FT STRAND 4..7
FT /evidence="ECO:0007829|PDB:4NO4"
FT STRAND 17..24
FT /evidence="ECO:0007829|PDB:4NO4"
FT STRAND 30..38
FT /evidence="ECO:0007829|PDB:4NO4"
FT STRAND 41..52
FT /evidence="ECO:0007829|PDB:4NO4"
FT STRAND 55..65
FT /evidence="ECO:0007829|PDB:4NO4"
FT STRAND 73..75
FT /evidence="ECO:0007829|PDB:4NO4"
FT STRAND 84..92
FT /evidence="ECO:0007829|PDB:4NO4"
FT STRAND 94..100
FT /evidence="ECO:0007829|PDB:4NO4"
FT STRAND 106..110
FT /evidence="ECO:0007829|PDB:4NO4"
FT STRAND 120..135
FT /evidence="ECO:0007829|PDB:4NO4"
SQ SEQUENCE 135 AA; 14857 MW; A2C2DFB464FE81CF CRC64;
MACGLVASNL NLKPGECLKV RGELAPDAKS FVLNLGKDSN NLCLHFNPRF NAHGDANTIV
CNSKDDGTWG TEQRETAFPF QPGSITEVCI TFDQADLTIK LPDGHEFKFP NRLNMEAINY
MAADGDFKIK CVAFE
