LEG2_HUMAN
ID LEG2_HUMAN Reviewed; 132 AA.
AC P05162; Q6FGY4;
DT 13-AUG-1987, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1994, sequence version 3.
DT 03-AUG-2022, entry version 197.
DE RecName: Full=Galectin-2;
DE Short=Gal-2;
DE AltName: Full=Beta-galactoside-binding lectin L-14-II;
DE AltName: Full=HL14;
DE AltName: Full=Lactose-binding lectin 2;
DE AltName: Full=S-Lac lectin 2;
GN Name=LGALS2;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
RX PubMed=1375225; DOI=10.1016/s0021-9258(19)50059-x;
RA Gitt M.A., Massa S.M., Leffler H., Barondes S.H.;
RT "Isolation and expression of a gene encoding L-14-II, a new human soluble
RT lactose-binding lectin.";
RL J. Biol. Chem. 267:10601-10606(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=15461802; DOI=10.1186/gb-2004-5-10-r84;
RA Collins J.E., Wright C.L., Edwards C.A., Davis M.P., Grinham J.A.,
RA Cole C.G., Goward M.E., Aguado B., Mallya M., Mokrab Y., Huckle E.J.,
RA Beare D.M., Dunham I.;
RT "A genome annotation-driven approach to cloning the human ORFeome.";
RL Genome Biol. 5:R84.1-R84.11(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
RT "Cloning of human full open reading frames in Gateway(TM) system entry
RT vector (pDONR201).";
RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=10591208; DOI=10.1038/990031;
RA Dunham I., Hunt A.R., Collins J.E., Bruskiewich R., Beare D.M., Clamp M.,
RA Smink L.J., Ainscough R., Almeida J.P., Babbage A.K., Bagguley C.,
RA Bailey J., Barlow K.F., Bates K.N., Beasley O.P., Bird C.P., Blakey S.E.,
RA Bridgeman A.M., Buck D., Burgess J., Burrill W.D., Burton J., Carder C.,
RA Carter N.P., Chen Y., Clark G., Clegg S.M., Cobley V.E., Cole C.G.,
RA Collier R.E., Connor R., Conroy D., Corby N.R., Coville G.J., Cox A.V.,
RA Davis J., Dawson E., Dhami P.D., Dockree C., Dodsworth S.J., Durbin R.M.,
RA Ellington A.G., Evans K.L., Fey J.M., Fleming K., French L., Garner A.A.,
RA Gilbert J.G.R., Goward M.E., Grafham D.V., Griffiths M.N.D., Hall C.,
RA Hall R.E., Hall-Tamlyn G., Heathcott R.W., Ho S., Holmes S., Hunt S.E.,
RA Jones M.C., Kershaw J., Kimberley A.M., King A., Laird G.K., Langford C.F.,
RA Leversha M.A., Lloyd C., Lloyd D.M., Martyn I.D., Mashreghi-Mohammadi M.,
RA Matthews L.H., Mccann O.T., Mcclay J., Mclaren S., McMurray A.A.,
RA Milne S.A., Mortimore B.J., Odell C.N., Pavitt R., Pearce A.V., Pearson D.,
RA Phillimore B.J.C.T., Phillips S.H., Plumb R.W., Ramsay H., Ramsey Y.,
RA Rogers L., Ross M.T., Scott C.E., Sehra H.K., Skuce C.D., Smalley S.,
RA Smith M.L., Soderlund C., Spragon L., Steward C.A., Sulston J.E.,
RA Swann R.M., Vaudin M., Wall M., Wallis J.M., Whiteley M.N., Willey D.L.,
RA Williams L., Williams S.A., Williamson H., Wilmer T.E., Wilming L.,
RA Wright C.L., Hubbard T., Bentley D.R., Beck S., Rogers J., Shimizu N.,
RA Minoshima S., Kawasaki K., Sasaki T., Asakawa S., Kudoh J., Shintani A.,
RA Shibuya K., Yoshizaki Y., Aoki N., Mitsuyama S., Roe B.A., Chen F., Chu L.,
RA Crabtree J., Deschamps S., Do A., Do T., Dorman A., Fang F., Fu Y., Hu P.,
RA Hua A., Kenton S., Lai H., Lao H.I., Lewis J., Lewis S., Lin S.-P., Loh P.,
RA Malaj E., Nguyen T., Pan H., Phan S., Qi S., Qian Y., Ray L., Ren Q.,
RA Shaull S., Sloan D., Song L., Wang Q., Wang Y., Wang Z., White J.,
RA Willingham D., Wu H., Yao Z., Zhan M., Zhang G., Chissoe S., Murray J.,
RA Miller N., Minx P., Fulton R., Johnson D., Bemis G., Bentley D.,
RA Bradshaw H., Bourne S., Cordes M., Du Z., Fulton L., Goela D., Graves T.,
RA Hawkins J., Hinds K., Kemp K., Latreille P., Layman D., Ozersky P.,
RA Rohlfing T., Scheet P., Walker C., Wamsley A., Wohldmann P., Pepin K.,
RA Nelson J., Korf I., Bedell J.A., Hillier L.W., Mardis E., Waterston R.,
RA Wilson R., Emanuel B.S., Shaikh T., Kurahashi H., Saitta S., Budarf M.L.,
RA McDermid H.E., Johnson A., Wong A.C.C., Morrow B.E., Edelmann L., Kim U.J.,
RA Shizuya H., Simon M.I., Dumanski J.P., Peyrard M., Kedra D., Seroussi E.,
RA Fransson I., Tapia I., Bruder C.E., O'Brien K.P., Wilkinson P.,
RA Bodenteich A., Hartman K., Hu X., Khan A.S., Lane L., Tilahun Y.,
RA Wright H.;
RT "The DNA sequence of human chromosome 22.";
RL Nature 402:489-495(1999).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Colon;
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 OF 4-132.
RX PubMed=1988031; DOI=10.1021/bi00215a013;
RA Gitt M.A., Barondes S.H.;
RT "Genomic sequence and organization of two members of a human lectin gene
RT family.";
RL Biochemistry 30:82-89(1991).
RN [8]
RP PRELIMINARY NUCLEOTIDE SEQUENCE [MRNA] OF 6-132, AND VARIANT ILE-119.
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 [9]
RP X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS).
RX PubMed=8262940; DOI=10.2210/pdb1hlc/pdb;
RA Lobsanov Y.D., Gitt M.A., Leffler H., Barondes S.H., Rini J.M.;
RT "X-ray crystal structure of the human dimeric S-Lac lectin, L-14-II, in
RT complex with lactose at 2.9-A resolution.";
RL J. Biol. Chem. 268:27034-27038(1993).
RN [10]
RP VARIANT [LARGE SCALE ANALYSIS] GLN-132.
RX PubMed=16959974; DOI=10.1126/science.1133427;
RA Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D.,
RA Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P.,
RA Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V.,
RA Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H.,
RA Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W.,
RA Velculescu V.E.;
RT "The consensus coding sequences of human breast and colorectal cancers.";
RL Science 314:268-274(2006).
CC -!- FUNCTION: This protein binds beta-galactoside. Its physiological
CC function is not yet known.
CC -!- SUBUNIT: Homodimer.
CC -!- INTERACTION:
CC P05162; Q96HA8: NTAQ1; NbExp=3; IntAct=EBI-7181544, EBI-741158;
CC P05162; O00560: SDCBP; NbExp=9; IntAct=EBI-7181544, EBI-727004;
CC P05162; Q9H190: SDCBP2; NbExp=7; IntAct=EBI-7181544, EBI-742426;
CC -!- WEB RESOURCE: Name=Functional Glycomics Gateway - Glycan Binding;
CC Note=Galectin-2;
CC URL="http://www.functionalglycomics.org/glycomics/GBPServlet?&operationType=view&cbpId=cbp_hum_Stlect_280";
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DR EMBL; M87860; AAA59512.1; -; Genomic_DNA.
DR EMBL; M87857; AAA59512.1; JOINED; Genomic_DNA.
DR EMBL; M87858; AAA59512.1; JOINED; Genomic_DNA.
DR EMBL; M87859; AAA59512.1; JOINED; Genomic_DNA.
DR EMBL; M87842; AAA59513.1; -; mRNA.
DR EMBL; CR456512; CAG30398.1; -; mRNA.
DR EMBL; CR541972; CAG46770.1; -; mRNA.
DR EMBL; CR542000; CAG46797.1; -; mRNA.
DR EMBL; AL022315; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471095; EAW60167.1; -; Genomic_DNA.
DR EMBL; BC059782; AAH59782.1; -; mRNA.
DR EMBL; M14079; AAA36171.1; -; mRNA.
DR CCDS; CCDS13950.1; -.
DR PIR; A38140; A38140.
DR RefSeq; NP_006489.1; NM_006498.2.
DR PDB; 1HLC; X-ray; 2.90 A; A/B=4-132.
DR PDB; 5DG1; X-ray; 3.20 A; A/B/C/D/H/I=1-132.
DR PDB; 5DG2; X-ray; 1.61 A; A/B=1-132.
DR PDB; 5EWS; X-ray; 2.00 A; A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P=1-131.
DR PDBsum; 1HLC; -.
DR PDBsum; 5DG1; -.
DR PDBsum; 5DG2; -.
DR PDBsum; 5EWS; -.
DR AlphaFoldDB; P05162; -.
DR SMR; P05162; -.
DR BioGRID; 110148; 10.
DR ComplexPortal; CPX-95; Galectin-2 complex.
DR IntAct; P05162; 4.
DR MINT; P05162; -.
DR STRING; 9606.ENSP00000215886; -.
DR BindingDB; P05162; -.
DR ChEMBL; CHEMBL5977; -.
DR DrugBank; DB02379; Beta-D-Glucose.
DR UniLectin; P05162; -.
DR iPTMnet; P05162; -.
DR PhosphoSitePlus; P05162; -.
DR BioMuta; LGALS2; -.
DR DMDM; 585388; -.
DR jPOST; P05162; -.
DR MassIVE; P05162; -.
DR MaxQB; P05162; -.
DR PaxDb; P05162; -.
DR PeptideAtlas; P05162; -.
DR PRIDE; P05162; -.
DR ProteomicsDB; 51810; -.
DR Antibodypedia; 286; 317 antibodies from 31 providers.
DR DNASU; 3957; -.
DR Ensembl; ENST00000215886.6; ENSP00000215886.4; ENSG00000100079.7.
DR GeneID; 3957; -.
DR KEGG; hsa:3957; -.
DR MANE-Select; ENST00000215886.6; ENSP00000215886.4; NM_006498.3; NP_006489.1.
DR UCSC; uc003ata.4; human.
DR CTD; 3957; -.
DR DisGeNET; 3957; -.
DR GeneCards; LGALS2; -.
DR HGNC; HGNC:6562; LGALS2.
DR HPA; ENSG00000100079; Tissue enhanced (gallbladder, intestine, kidney, pancreas).
DR MalaCards; LGALS2; -.
DR MIM; 150571; gene.
DR neXtProt; NX_P05162; -.
DR OpenTargets; ENSG00000100079; -.
DR PharmGKB; PA164741896; -.
DR VEuPathDB; HostDB:ENSG00000100079; -.
DR eggNOG; KOG3587; Eukaryota.
DR GeneTree; ENSGT00940000155025; -.
DR HOGENOM; CLU_037794_5_0_1; -.
DR InParanoid; P05162; -.
DR OMA; GSMMNFP; -.
DR OrthoDB; 1429018at2759; -.
DR PhylomeDB; P05162; -.
DR TreeFam; TF315551; -.
DR PathwayCommons; P05162; -.
DR SignaLink; P05162; -.
DR BioGRID-ORCS; 3957; 14 hits in 1072 CRISPR screens.
DR ChiTaRS; LGALS2; human.
DR EvolutionaryTrace; P05162; -.
DR GeneWiki; LGALS2; -.
DR GenomeRNAi; 3957; -.
DR Pharos; P05162; Tbio.
DR PRO; PR:P05162; -.
DR Proteomes; UP000005640; Chromosome 22.
DR RNAct; P05162; protein.
DR Bgee; ENSG00000100079; Expressed in gall bladder and 131 other tissues.
DR ExpressionAtlas; P05162; baseline and differential.
DR Genevisible; P05162; HS.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:1990724; C:galectin complex; IPI:ComplexPortal.
DR GO; GO:0030246; F:carbohydrate binding; IEA:UniProtKB-KW.
DR GO; GO:0016936; F:galactoside binding; IBA:GO_Central.
DR GO; GO:0098609; P:cell-cell adhesion; IDA:ComplexPortal.
DR GO; GO:0043065; P:positive regulation of apoptotic process; IDA:ComplexPortal.
DR GO; GO:0050729; P:positive regulation of inflammatory response; IEA:Ensembl.
DR GO; GO:0043029; P:T cell homeostasis; IDA:ComplexPortal.
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; Lectin; Reference proteome.
FT CHAIN 1..132
FT /note="Galectin-2"
FT /id="PRO_0000076924"
FT DOMAIN 4..131
FT /note="Galectin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00639"
FT BINDING 65..71
FT /ligand="a beta-D-galactoside"
FT /ligand_id="ChEBI:CHEBI:28034"
FT /evidence="ECO:0000255"
FT VARIANT 119
FT /note="V -> I (in dbSNP:rs2235339)"
FT /evidence="ECO:0000269|PubMed:3020551"
FT /id="VAR_049767"
FT VARIANT 132
FT /note="E -> Q (in a breast cancer sample; somatic mutation;
FT dbSNP:rs1434020843)"
FT /evidence="ECO:0000269|PubMed:16959974"
FT /id="VAR_036570"
FT STRAND 6..9
FT /evidence="ECO:0007829|PDB:5DG2"
FT STRAND 17..24
FT /evidence="ECO:0007829|PDB:5DG2"
FT STRAND 29..38
FT /evidence="ECO:0007829|PDB:5DG2"
FT STRAND 41..49
FT /evidence="ECO:0007829|PDB:5DG2"
FT TURN 50..53
FT /evidence="ECO:0007829|PDB:5DG2"
FT STRAND 54..61
FT /evidence="ECO:0007829|PDB:5DG2"
FT STRAND 69..71
FT /evidence="ECO:0007829|PDB:5DG2"
FT STRAND 81..88
FT /evidence="ECO:0007829|PDB:5DG2"
FT STRAND 90..96
FT /evidence="ECO:0007829|PDB:5DG2"
FT STRAND 98..100
FT /evidence="ECO:0007829|PDB:5DG1"
FT STRAND 102..106
FT /evidence="ECO:0007829|PDB:5DG2"
FT STRAND 116..131
FT /evidence="ECO:0007829|PDB:5DG2"
SQ SEQUENCE 132 AA; 14644 MW; E30B8768630A2ACB CRC64;
MTGELEVKNM DMKPGSTLKI TGSIADGTDG FVINLGQGTD KLNLHFNPRF SESTIVCNSL
DGSNWGQEQR EDHLCFSPGS EVKFTVTFES DKFKVKLPDG HELTFPNRLG HSHLSYLSVR
GGFNMSSFKL KE
