LEG1_CRIGR
ID LEG1_CRIGR Reviewed; 135 AA.
AC P48538;
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 115.
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=S-Lac lectin 1;
GN Name=LGALS1;
OS Cricetulus griseus (Chinese hamster) (Cricetulus barabensis griseus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea;
OC Cricetidae; Cricetinae; Cricetulus.
OX NCBI_TaxID=10029;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, AND SUBUNIT.
RC TISSUE=Ovary;
RX PubMed=7890630; DOI=10.1074/jbc.270.10.5198;
RA Cho M., Cummings R.D.;
RT "Galectin-1, a beta-galactoside-binding lectin in Chinese hamster ovary
RT cells. I. Physical and chemical characterization.";
RL J. Biol. Chem. 270:5198-5206(1995).
CC -!- FUNCTION: Lectin that binds beta-galactoside and a wide array of
CC complex carbohydrates (PubMed:7890630). Plays a role in regulating
CC apoptosis, cell proliferation and cell differentiation. Inhibits CD45
CC protein phosphatase activity and therefore the dephosphorylation of Lyn
CC kinase. Strong inducer of T-cell apoptosis.
CC {ECO:0000250|UniProtKB:P09382, ECO:0000269|PubMed:7890630}.
CC -!- SUBUNIT: Binds LGALS3BP. Interacts with CD2, CD3, CD4, CD6, CD7, CD43,
CC ALCAM and CD45. Interacts with laminin. Interacts with SUSD2 (By
CC similarity). Exists in a reversible and active monomer-homodimer
CC equilibrium, the mononomer/dimer state is regulated by lectin
CC concentration. Interacts with cargo receptor TMED10; the interaction
CC mediates the translocation from the cytoplasm into the ERGIC
CC (endoplasmic reticulum-Golgi intermediate compartment) and thereby
CC secretion (By similarity). {ECO:0000250|UniProtKB:P09382,
CC ECO:0000269|PubMed:7890630}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:7890630}. Secreted,
CC extracellular space, extracellular matrix {ECO:0000269|PubMed:7890630}.
CC Secreted {ECO:0000250|UniProtKB:P09382}. Note=Can be secreted; the
CC secretion is dependent on protein unfolding and facilitated by the
CC cargo receptor TMED10; it results in protein translocation from the
CC cytoplasm into the ERGIC (endoplasmic reticulum-Golgi intermediate
CC compartment) followed by vesicle entry and secretion.
CC {ECO:0000250|UniProtKB:P09382}.
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DR EMBL; M96676; AAA36995.1; -; mRNA.
DR PIR; A55935; A55935.
DR RefSeq; XP_003510318.1; XM_003510270.3.
DR RefSeq; XP_007622829.1; XM_007624639.2.
DR AlphaFoldDB; P48538; -.
DR SMR; P48538; -.
DR STRING; 10029.XP_007622829.1; -.
DR Ensembl; ENSCGRT00001020755; ENSCGRP00001016511; ENSCGRG00001016814.
DR GeneID; 100751963; -.
DR KEGG; cge:100751963; -.
DR CTD; 3956; -.
DR eggNOG; KOG3587; Eukaryota.
DR GeneTree; ENSGT00940000155534; -.
DR OrthoDB; 1429018at2759; -.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005615; C:extracellular space; IEA:Ensembl.
DR GO; GO:1990724; C:galectin complex; IEA:Ensembl.
DR GO; GO:0030246; F:carbohydrate binding; IEA:UniProtKB-KW.
DR GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
DR GO; GO:0098609; P:cell-cell adhesion; IEA:Ensembl.
DR GO; GO:0045445; P:myoblast differentiation; IEA:Ensembl.
DR GO; GO:0002317; P:plasma cell differentiation; IEA:Ensembl.
DR GO; GO:0043065; P:positive regulation of apoptotic process; IEA:Ensembl.
DR GO; GO:0050729; P:positive regulation of inflammatory response; IEA:Ensembl.
DR GO; GO:0046598; P:positive regulation of viral entry into host cell; IEA:Ensembl.
DR GO; GO:0031295; P:T cell costimulation; IEA:Ensembl.
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 Acetylation; Apoptosis; Cytoplasm; Extracellular matrix; Lectin;
KW Phosphoprotein; 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_0000076916"
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"
SQ SEQUENCE 135 AA; 14803 MW; DC71757762BE4223 CRC64;
MACGLVASNL NLKPGECLKV RGEVAPDAKS FVLNLGKDSN NLCLHFNPRF NAHGDANTIV
CNSKDNGAWG TEHREPAFPF QPGSTVEVCI TFDQADLTIK LPDGHEFKFP NRLNMEAINY
MAADGDFKIK CVAFE
