LEG1_MOUSE
ID LEG1_MOUSE Reviewed; 135 AA.
AC P16045; P05163; P11946; P17601; Q4FZH4; Q99M27; Q9D0X0;
DT 13-AUG-1987, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 204.
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; Synonyms=Gbp;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND FUNCTION.
RC STRAIN=C3H/HeJ; TISSUE=Skeletal muscle;
RX PubMed=2803247; DOI=10.1042/bj2610847;
RA Wilson T.J.G., Firth M.N., Powell J.T., Harrison F.L.;
RT "The sequence of the mouse 14 kDa beta-galactoside-binding lectin and
RT evidence for its synthesis on free cytoplasmic ribosomes.";
RL Biochem. J. 261:847-852(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=BALB/cJ; TISSUE=Liver;
RX PubMed=2025648; DOI=10.1016/0167-4781(91)90084-y;
RA Chiariotti L., Wells V., Bruni C.B., Mallucci L.;
RT "Structure and expression of the negative growth factor mouse beta-
RT galactoside binding protein gene.";
RL Biochim. Biophys. Acta 1089:54-60(1991).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=1986871; DOI=10.1016/0092-8674(91)90211-g;
RA Wells V., Mallucci L.;
RT "Identification of an autocrine negative growth factor: mouse beta-
RT galactoside-binding protein is a cytostatic factor and cell growth
RT regulator.";
RL Cell 64:91-97(1991).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=1638977; DOI=10.1242/dev.115.1.143;
RA Poirier F., Timmons P.M., Chan C.T., Guenet J.-L., Rigby P.W.;
RT "Expression of the L14 lectin during mouse embryogenesis suggests multiple
RT roles during pre- and post-implantation development.";
RL Development 115:143-155(1992).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Embryo;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Czech II, and NIH Black Swiss; TISSUE=Mammary gland, and Thyroid;
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 [7]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1-107.
RC TISSUE=Skeletal muscle;
RX PubMed=2335567; DOI=10.1083/jcb.110.5.1681;
RA Cooper D.N.W., Barondes S.H.;
RT "Evidence for export of a muscle lectin from cytosol to extracellular
RT matrix and for a novel secretory mechanism.";
RL J. Cell Biol. 110:1681-1691(1990).
RN [8]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1-105.
RX PubMed=3335026;
RA Raz A., Carmi P., Pazerni G.;
RT "Expression of two different endogenous galactoside-binding lectins sharing
RT sequence homology.";
RL Cancer Res. 48:645-649(1988).
RN [9]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 68-134.
RX PubMed=3020551; DOI=10.1073/pnas.83.20.7603;
RA Gitt M.A., Barondes S.H.;
RT "Evidence that a human soluble beta-galactoside-binding lectin is encoded
RT by a family of genes.";
RL Proc. Natl. Acad. Sci. U.S.A. 83:7603-7607(1986).
RN [10]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [11]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-13; LYS-19; LYS-29; LYS-108 AND
RP LYS-128, SUCCINYLATION [LARGE SCALE ANALYSIS] AT LYS-108, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic fibroblast;
RX PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001;
RA Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y.,
RA Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.;
RT "SIRT5-mediated lysine desuccinylation impacts diverse metabolic
RT pathways.";
RL Mol. Cell 50:919-930(2013).
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 ECO:0000269|PubMed:1986871}.
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 -!- CAUTION: Was originally thought to originate from human.
CC {ECO:0000305|PubMed:3020551}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA37313.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=AK004298; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; X15986; CAA34117.1; -; mRNA.
DR EMBL; X53067; CAA37242.1; -; mRNA.
DR EMBL; X51577; CAA35930.1; -; Genomic_DNA.
DR EMBL; X51578; CAA35930.1; JOINED; Genomic_DNA.
DR EMBL; X51579; CAA35930.1; JOINED; Genomic_DNA.
DR EMBL; M57470; AAA37667.1; -; mRNA.
DR EMBL; X66532; CAA47143.1; -; mRNA.
DR EMBL; AK004298; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; BC002063; AAH02063.1; -; mRNA.
DR EMBL; BC099479; AAH99479.1; -; mRNA.
DR EMBL; X51903; CAA36183.1; -; mRNA.
DR EMBL; M33214; AAA37313.1; ALT_FRAME; mRNA.
DR EMBL; M14087; AAA36172.1; -; mRNA.
DR CCDS; CCDS27628.1; -.
DR PIR; B26495; B26495.
DR PIR; S07162; S07162.
DR PIR; S11718; LNMSGB.
DR RefSeq; NP_032521.1; NM_008495.2.
DR PDB; 4LBQ; X-ray; 2.40 A; A/B/C/D=1-135.
DR PDBsum; 4LBQ; -.
DR AlphaFoldDB; P16045; -.
DR SMR; P16045; -.
DR BioGRID; 201142; 20.
DR ComplexPortal; CPX-94; Galectin-1 complex.
DR IntAct; P16045; 7.
DR MINT; P16045; -.
DR STRING; 10090.ENSMUSP00000086795; -.
DR ChEMBL; CHEMBL4105904; -.
DR UniLectin; P16045; -.
DR iPTMnet; P16045; -.
DR PhosphoSitePlus; P16045; -.
DR SwissPalm; P16045; -.
DR REPRODUCTION-2DPAGE; IPI00229517; -.
DR REPRODUCTION-2DPAGE; P16045; -.
DR SWISS-2DPAGE; P16045; -.
DR UCD-2DPAGE; P16045; -.
DR CPTAC; non-CPTAC-3587; -.
DR EPD; P16045; -.
DR jPOST; P16045; -.
DR MaxQB; P16045; -.
DR PaxDb; P16045; -.
DR PeptideAtlas; P16045; -.
DR PRIDE; P16045; -.
DR ProteomicsDB; 264932; -.
DR TopDownProteomics; P16045; -.
DR ABCD; P16045; 2 sequenced antibodies.
DR Antibodypedia; 269; 1008 antibodies from 46 providers.
DR DNASU; 16852; -.
DR Ensembl; ENSMUST00000089377; ENSMUSP00000086795; ENSMUSG00000068220.
DR GeneID; 16852; -.
DR KEGG; mmu:16852; -.
DR UCSC; uc007wrv.1; mouse.
DR CTD; 3956; -.
DR MGI; MGI:96777; Lgals1.
DR VEuPathDB; HostDB:ENSMUSG00000068220; -.
DR eggNOG; KOG3587; Eukaryota.
DR GeneTree; ENSGT00940000155534; -.
DR HOGENOM; CLU_037794_5_0_1; -.
DR InParanoid; P16045; -.
DR OMA; CNSKKME; -.
DR OrthoDB; 1429018at2759; -.
DR PhylomeDB; P16045; -.
DR TreeFam; TF315551; -.
DR Reactome; R-MMU-381426; Regulation of Insulin-like Growth Factor (IGF) transport and uptake by Insulin-like Growth Factor Binding Proteins (IGFBPs).
DR Reactome; R-MMU-8957275; Post-translational protein phosphorylation.
DR BioGRID-ORCS; 16852; 4 hits in 71 CRISPR screens.
DR ChiTaRS; Lgals1; mouse.
DR PRO; PR:P16045; -.
DR Proteomes; UP000000589; Chromosome 15.
DR RNAct; P16045; protein.
DR Bgee; ENSMUSG00000068220; Expressed in endothelial cell of lymphatic vessel and 285 other tissues.
DR ExpressionAtlas; P16045; baseline and differential.
DR Genevisible; P16045; MM.
DR GO; GO:0009986; C:cell surface; ISO:MGI.
DR GO; GO:0062023; C:collagen-containing extracellular matrix; HDA:BHF-UCL.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0005576; C:extracellular region; TAS:Reactome.
DR GO; GO:0005615; C:extracellular space; IDA:MGI.
DR GO; GO:1990724; C:galectin complex; ISO:MGI.
DR GO; GO:0005634; C:nucleus; ISO:MGI.
DR GO; GO:0030246; F:carbohydrate binding; IDA:MGI.
DR GO; GO:0005534; F:galactose binding; NAS:UniProtKB.
DR GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR GO; GO:0030395; F:lactose binding; ISO:MGI.
DR GO; GO:0043236; F:laminin binding; ISO:MGI.
DR GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
DR GO; GO:0098609; P:cell-cell adhesion; ISO:MGI.
DR GO; GO:0007157; P:heterophilic cell-cell adhesion via plasma membrane cell adhesion molecules; NAS:UniProtKB.
DR GO; GO:0045445; P:myoblast differentiation; IDA:MGI.
DR GO; GO:0010812; P:negative regulation of cell-substrate adhesion; ISO:MGI.
DR GO; GO:0010977; P:negative regulation of neuron projection development; ISO:MGI.
DR GO; GO:0002317; P:plasma cell differentiation; IDA:MGI.
DR GO; GO:0043065; P:positive regulation of apoptotic process; ISO:MGI.
DR GO; GO:0034120; P:positive regulation of erythrocyte aggregation; ISO:MGI.
DR GO; GO:0050729; P:positive regulation of inflammatory response; ISO:MGI.
DR GO; GO:0046598; P:positive regulation of viral entry into host cell; ISO:MGI.
DR GO; GO:0031295; P:T cell costimulation; IDA:MGI.
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; Extracellular matrix;
KW 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_0000076918"
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:0007744|PubMed:23806337"
FT MOD_RES 19
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 29
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:23806337"
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:0007744|PubMed:23806337"
FT MOD_RES 108
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 128
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:23806337"
FT CONFLICT 78
FT /note="F -> S (in Ref. 3; AAA37667)"
FT /evidence="ECO:0000305"
FT CONFLICT 86
FT /note="T -> I (in Ref. 6; AAH02063)"
FT /evidence="ECO:0000305"
FT CONFLICT 131..134
FT /note="CVAF -> VRGL (in Ref. 9; AAA36172)"
FT /evidence="ECO:0000305"
FT STRAND 6..8
FT /evidence="ECO:0007829|PDB:4LBQ"
FT STRAND 17..24
FT /evidence="ECO:0007829|PDB:4LBQ"
FT STRAND 33..38
FT /evidence="ECO:0007829|PDB:4LBQ"
FT STRAND 41..49
FT /evidence="ECO:0007829|PDB:4LBQ"
FT STRAND 58..65
FT /evidence="ECO:0007829|PDB:4LBQ"
FT STRAND 73..75
FT /evidence="ECO:0007829|PDB:4LBQ"
FT STRAND 84..92
FT /evidence="ECO:0007829|PDB:4LBQ"
FT STRAND 94..100
FT /evidence="ECO:0007829|PDB:4LBQ"
FT STRAND 106..110
FT /evidence="ECO:0007829|PDB:4LBQ"
FT STRAND 120..123
FT /evidence="ECO:0007829|PDB:4LBQ"
FT STRAND 127..135
FT /evidence="ECO:0007829|PDB:4LBQ"
SQ SEQUENCE 135 AA; 14866 MW; FD6967C1F4117122 CRC64;
MACGLVASNL NLKPGECLKV RGEVASDAKS FVLNLGKDSN NLCLHFNPRF NAHGDANTIV
CNTKEDGTWG TEHREPAFPF QPGSITEVCI TFDQADLTIK LPDGHEFKFP NRLNMEAINY
MAADGDFKIK CVAFE
