UniProt Accession

 LEG1_RAT; P11762 

Genbank Protein ID

 M19036; BC058476 

Genbank Nucleotide ID

 AAA40822.1; AAH58476.1 

Protein Name

 Galectin-1 

Protein Synonyms/Alias

 Gal-1; 14 kDa lectin; Beta-galactoside-binding lectin L-14-I; Galaptin; Lactose-binding lectin 1; Lectin galactoside-binding soluble 1; RL 14.5; S-Lac lectin 1 

Gene Name

 Lgals1 

Gene Synonyms/Alias

  

Created Date

 July 27, 2013 

Organism

 Rattus norvegicus (Rat) 

NCBI Taxa ID

 10116 

Lysine Modification

Position	Peptide	Type	References
19	LKPGECLKVRGELAP	acetylation	[1]
29	GELAPDAKSFVLNLG	acetylation	[1]
108	LPDGHEFKFPNRLNM	acetylation	[1]
128	MAADGDFKIKCVAFE	acetylation	[1]

Reference

 [1] Proteomic analysis of lysine acetylation sites in rat tissues reveals organ specificity and subcellular patterns.
 Lundby A, Lage K, Weinert BT, Bekker-Jensen DB, Secher A, Skovgaard T, Kelstrup CD, Dmytriyev A, Choudhary C, Lundby C, Olsen JV.
 Cell Rep. 2012 Aug 30;2(2):419-31. [PMID: 22902405] 

Functional Description

 May regulate apoptosis, cell proliferation and cell differentiation. Binds beta-galactoside and a wide array of complex carbohydrates (By similarity). 

Sequence Annotation

 DOMAIN 4 135 Galectin.
 REGION 45 49 Beta-galactoside binding (By similarity).
 REGION 69 72 Beta-galactoside binding (By similarity).
 BINDING 53 53 Beta-galactoside (By similarity).
 BINDING 62 62 Beta-galactoside (By similarity).
 MOD_RES 2 2 N-acetylalanine (By similarity).
 MOD_RES 29 29 N6-acetyllysine (By similarity).  

Keyword

 3D-structure; Acetylation; Complete proteome; Direct protein sequencing; Extracellular matrix; Lectin; Reference proteome; Secreted. 

Sequence Source

 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 

Protein Length

 135 AA 

Protein Sequence

Gene Ontology

 GO:0009986; C:cell surface; IDA:RGD.
 GO:0005737; C:cytoplasm; IDA:RGD.
 GO:0005615; C:extracellular space; IEA:Compara.
 GO:0005634; C:nucleus; IDA:RGD.
 GO:0005578; C:proteinaceous extracellular matrix; IEA:UniProtKB-SubCell.
 GO:0016936; F:galactoside binding; IEA:InterPro.
 GO:0030395; F:lactose binding; IDA:RGD.
 GO:0043236; F:laminin binding; IDA:RGD.
 GO:0042803; F:protein homodimerization activity; IDA:RGD.
 GO:0004871; F:signal transducer activity; IEA:Compara.
 GO:0071333; P:cellular response to glucose stimulus; IEP:RGD.
 GO:0071407; P:cellular response to organic cyclic compound; IEP:RGD.
 GO:0033555; P:multicellular organismal response to stress; IEP:RGD.
 GO:0045445; P:myoblast differentiation; IEA:Compara.
 GO:0010812; P:negative regulation of cell-substrate adhesion; IDA:RGD.
 GO:0010977; P:negative regulation of neuron projection development; IMP:RGD.
 GO:0002317; P:plasma cell differentiation; IEA:Compara.
 GO:0034120; P:positive regulation of erythrocyte aggregation; IDA:RGD.
 GO:0043123; P:positive regulation of I-kappaB kinase/NF-kappaB cascade; IEA:Compara.
 GO:0048678; P:response to axon injury; IEP:RGD.
 GO:0042493; P:response to drug; IEP:RGD.
 GO:0031295; P:T cell costimulation; IEA:Compara. 

Interpro

 IPR008985; ConA-like_lec_gl_sf.
 IPR013320; ConA-like_subgrp.
 IPR015535; Galectin_1.
 IPR001079; Galectin_CRD. 

Pfam

 PF00337; Gal-bind_lectin 

SMART

 SM00908; Gal-bind_lectin
 SM00276; GLECT 

PROSITE

 PS51304; GALECTIN 

PRINTS