LEG7_HUMAN
ID LEG7_HUMAN Reviewed; 136 AA.
AC P47929; Q6IB87;
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 201.
DE RecName: Full=Galectin-7;
DE Short=Gal-7;
DE AltName: Full=HKL-14;
DE AltName: Full=PI7;
DE AltName: Full=p53-induced gene 1 protein;
GN Name=LGALS7; Synonyms=PIG1;
GN and
GN Name=LGALS7B;
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 [MRNA], AND PROTEIN SEQUENCE OF 8-20; 76-83; 112-118
RP AND 121-133.
RC TISSUE=Epidermis;
RX PubMed=7534301; DOI=10.1074/jbc.270.11.5823;
RA Madsen P., Rasmussen H.H., Flint T., Gromov P., Kruse T.A., Honore B.,
RA Vorum H., Celis J.E.;
RT "Cloning, expression, and chromosome mapping of human galectin-7.";
RL J. Biol. Chem. 270:5823-5829(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Epidermis;
RX PubMed=7729568; DOI=10.1006/dbio.1995.1078;
RA Magnaldo T., Bernerd F., Darmon M.;
RT "Galectin-7, a human 14-kDa S-lectin, specifically expressed in
RT keratinocytes and sensitive to retinoic acid.";
RL Dev. Biol. 168:259-271(1995).
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].
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain, and PNS;
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 [6]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=11706006; DOI=10.1074/jbc.m109360200;
RA Kuwabara I., Kuwabara Y., Yang R.Y., Schuler M., Green D.R., Zuraw B.L.,
RA Hsu D.K., Liu F.T.;
RT "Galectin-7 (PIG1) exhibits pro-apoptotic function through JNK activation
RT and mitochondrial cytochrome c release.";
RL J. Biol. Chem. 277:3487-3497(2002).
RN [7]
RP X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS).
RX PubMed=9760227; DOI=10.1021/bi981056x;
RA Leonidas D.D., Vatzaki E.H., Vorum H., Celis J.E., Madsen P., Acharya K.R.;
RT "Structural basis for the recognition of carbohydrates by human galectin-
RT 7.";
RL Biochemistry 37:13930-13940(1998).
CC -!- FUNCTION: Could be involved in cell-cell and/or cell-matrix
CC interactions necessary for normal growth control. Pro-apoptotic protein
CC that functions intracellularly upstream of JNK activation and
CC cytochrome c release. {ECO:0000269|PubMed:11706006}.
CC -!- SUBUNIT: Monomer.
CC -!- INTERACTION:
CC P47929; Q96D03: DDIT4L; NbExp=3; IntAct=EBI-357504, EBI-742054;
CC P47929; P17066: HSPA6; NbExp=3; IntAct=EBI-357504, EBI-355106;
CC P47929; Q9Y333: LSM2; NbExp=3; IntAct=EBI-357504, EBI-347416;
CC P47929; Q04837: SSBP1; NbExp=6; IntAct=EBI-357504, EBI-353460;
CC P47929; Q15750: TAB1; NbExp=3; IntAct=EBI-357504, EBI-358643;
CC P47929; O43548: TGM5; NbExp=3; IntAct=EBI-357504, EBI-12027348;
CC P47929; Q8IY57-5: YAF2; NbExp=3; IntAct=EBI-357504, EBI-12111538;
CC P47929; P0DTC2: S; Xeno; NbExp=2; IntAct=EBI-357504, EBI-25474821;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:11706006}. Nucleus
CC {ECO:0000269|PubMed:11706006}. Secreted {ECO:0000305}. Note=May be
CC secreted by a non-classical secretory pathway.
CC -!- TISSUE SPECIFICITY: Mainly expressed in stratified squamous epithelium.
CC -!- INDUCTION: By p53/TP53.
CC -!- WEB RESOURCE: Name=Functional Glycomics Gateway - Glycan Binding;
CC Note=Galectin-7;
CC URL="http://www.functionalglycomics.org/glycomics/GBPServlet?&operationType=view&cbpId=cbp_hum_Stlect_00143";
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DR EMBL; L07769; AAA67899.1; -; mRNA.
DR EMBL; U06643; AAA86820.1; -; mRNA.
DR EMBL; CR456917; CAG33198.1; -; mRNA.
DR EMBL; CH471126; EAW56817.1; -; Genomic_DNA.
DR EMBL; CH471126; EAW56818.1; -; Genomic_DNA.
DR EMBL; BC042911; AAH42911.2; -; mRNA.
DR EMBL; BC061588; AAH61588.1; -; mRNA.
DR EMBL; BC073743; AAH73743.1; -; mRNA.
DR CCDS; CCDS42565.1; -.
DR PIR; I55469; I55469.
DR RefSeq; NP_001035972.1; NM_001042507.3.
DR RefSeq; NP_002298.1; NM_002307.3.
DR PDB; 1BKZ; X-ray; 1.90 A; A/B=2-136.
DR PDB; 2GAL; X-ray; 2.00 A; A/B=2-136.
DR PDB; 3GAL; X-ray; 1.90 A; A/B=2-136.
DR PDB; 3ZXE; X-ray; 1.67 A; A/B=4-136.
DR PDB; 3ZXF; X-ray; 1.38 A; A/B=1-136.
DR PDB; 4GAL; X-ray; 1.95 A; A/B=2-136.
DR PDB; 4UW3; X-ray; 1.48 A; A/B=1-136.
DR PDB; 4UW4; X-ray; 1.77 A; A/B=1-136.
DR PDB; 4UW5; X-ray; 2.04 A; A/B/C/D/E/F=1-136.
DR PDB; 4UW6; X-ray; 1.79 A; A/B=1-136.
DR PDB; 4XBQ; X-ray; 2.23 A; A/B=1-136.
DR PDB; 4Y26; X-ray; 2.61 A; A/B=4-136.
DR PDB; 5GAL; X-ray; 2.00 A; A/B=2-136.
DR PDB; 5H9Q; X-ray; 1.93 A; A/B=1-136.
DR PDB; 5H9S; X-ray; 1.82 A; A/B=1-136.
DR PDB; 6VTO; X-ray; 1.69 A; A/B=2-136.
DR PDB; 6VTP; X-ray; 2.30 A; A/B=2-136.
DR PDB; 6VTQ; X-ray; 1.95 A; A/B=2-136.
DR PDB; 6VTR; X-ray; 2.30 A; A/B=2-136.
DR PDB; 6VTS; X-ray; 1.90 A; A/B=2-136.
DR PDBsum; 1BKZ; -.
DR PDBsum; 2GAL; -.
DR PDBsum; 3GAL; -.
DR PDBsum; 3ZXE; -.
DR PDBsum; 3ZXF; -.
DR PDBsum; 4GAL; -.
DR PDBsum; 4UW3; -.
DR PDBsum; 4UW4; -.
DR PDBsum; 4UW5; -.
DR PDBsum; 4UW6; -.
DR PDBsum; 4XBQ; -.
DR PDBsum; 4Y26; -.
DR PDBsum; 5GAL; -.
DR PDBsum; 5H9Q; -.
DR PDBsum; 5H9S; -.
DR PDBsum; 6VTO; -.
DR PDBsum; 6VTP; -.
DR PDBsum; 6VTQ; -.
DR PDBsum; 6VTR; -.
DR PDBsum; 6VTS; -.
DR AlphaFoldDB; P47929; -.
DR BMRB; P47929; -.
DR SMR; P47929; -.
DR BioGRID; 110154; 121.
DR BioGRID; 575831; 104.
DR IntAct; P47929; 71.
DR MINT; P47929; -.
DR STRING; 9606.ENSP00000313571; -.
DR BindingDB; P47929; -.
DR ChEMBL; CHEMBL5008; -.
DR DrugBank; DB02678; beta-D-Galactosamine.
DR DrugBank; DB02379; Beta-D-Glucose.
DR UniLectin; P47929; -.
DR GlyGen; P47929; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; P47929; -.
DR PhosphoSitePlus; P47929; -.
DR SwissPalm; P47929; -.
DR BioMuta; LGALS7B; -.
DR DMDM; 1346431; -.
DR EPD; P47929; -.
DR jPOST; P47929; -.
DR MassIVE; P47929; -.
DR MaxQB; P47929; -.
DR PaxDb; P47929; -.
DR PeptideAtlas; P47929; -.
DR PRIDE; P47929; -.
DR ProteomicsDB; 55824; -.
DR Antibodypedia; 16627; 309 antibodies from 20 providers.
DR Antibodypedia; 652; 171 antibodies from 26 providers.
DR DNASU; 653499; -.
DR Ensembl; ENST00000314980.5; ENSP00000313571.3; ENSG00000178934.5.
DR Ensembl; ENST00000378626.5; ENSP00000367891.3; ENSG00000205076.5.
DR Ensembl; ENST00000634448.2; ENSP00000489395.1; ENSG00000282902.2.
DR Ensembl; ENST00000634800.1; ENSP00000489582.1; ENSG00000283082.1.
DR GeneID; 3963; -.
DR GeneID; 653499; -.
DR KEGG; hsa:3963; -.
DR KEGG; hsa:653499; -.
DR MANE-Select; ENST00000314980.5; ENSP00000313571.3; NM_001042507.4; NP_001035972.1.
DR MANE-Select; ENST00000378626.5; ENSP00000367891.3; NM_002307.4; NP_002298.1.
DR UCSC; uc002oje.4; human.
DR CTD; 3963; -.
DR CTD; 653499; -.
DR DisGeNET; 3963; -.
DR DisGeNET; 653499; -.
DR GeneCards; LGALS7; -.
DR GeneCards; LGALS7B; -.
DR HGNC; HGNC:6568; LGALS7.
DR HGNC; HGNC:34447; LGALS7B.
DR HPA; ENSG00000178934; Tissue enriched (skin).
DR HPA; ENSG00000205076; Tissue enhanced (esophagus, skin).
DR MIM; 600615; gene.
DR MIM; 617139; gene.
DR neXtProt; NX_P47929; -.
DR OpenTargets; ENSG00000178934; -.
DR OpenTargets; ENSG00000205076; -.
DR PharmGKB; PA162393892; -.
DR VEuPathDB; HostDB:ENSG00000178934; -.
DR VEuPathDB; HostDB:ENSG00000205076; -.
DR eggNOG; KOG3587; Eukaryota.
DR GeneTree; ENSGT00940000155398; -.
DR HOGENOM; CLU_037794_3_3_1; -.
DR InParanoid; P47929; -.
DR OMA; SIEAFNI; -.
DR OrthoDB; 1486238at2759; -.
DR PhylomeDB; P47929; -.
DR TreeFam; TF315551; -.
DR PathwayCommons; P47929; -.
DR SignaLink; P47929; -.
DR BioGRID-ORCS; 3963; 10 hits in 994 CRISPR screens.
DR BioGRID-ORCS; 653499; 27 hits in 984 CRISPR screens.
DR EvolutionaryTrace; P47929; -.
DR GeneWiki; LGALS7; -.
DR Pharos; P47929; Tbio.
DR PRO; PR:P47929; -.
DR Proteomes; UP000005640; Chromosome 19.
DR RNAct; P47929; protein.
DR Bgee; ENSG00000178934; Expressed in skin of abdomen and 73 other tissues.
DR ExpressionAtlas; P47929; baseline and differential.
DR Genevisible; P47929; HS.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0005615; C:extracellular space; TAS:ProtInc.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0030246; F:carbohydrate binding; IBA:GO_Central.
DR GO; GO:0016936; F:galactoside binding; IBA:GO_Central.
DR GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
DR GO; GO:0007157; P:heterophilic cell-cell adhesion via plasma membrane cell adhesion molecules; TAS:ProtInc.
DR GO; GO:2000562; P:negative regulation of CD4-positive, alpha-beta T cell proliferation; IBA:GO_Central.
DR GO; GO:0032689; P:negative regulation of interferon-gamma production; IBA:GO_Central.
DR GO; GO:0010628; P:positive regulation of gene expression; IBA:GO_Central.
DR CDD; cd00070; GLECT; 1.
DR InterPro; IPR013320; ConA-like_dom_sf.
DR InterPro; IPR044156; Galectin-like.
DR InterPro; IPR030640; Galectin_7.
DR InterPro; IPR001079; Galectin_CRD.
DR PANTHER; PTHR11346; PTHR11346; 1.
DR PANTHER; PTHR11346:SF107; PTHR11346:SF107; 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; Apoptosis; Cytoplasm; Direct protein sequencing; Lectin;
KW Nucleus; Reference proteome; Secreted.
FT CHAIN 1..136
FT /note="Galectin-7"
FT /id="PRO_0000076940"
FT DOMAIN 6..136
FT /note="Galectin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00639"
FT BINDING 70..76
FT /ligand="a beta-D-galactoside"
FT /ligand_id="ChEBI:CHEBI:28034"
FT /evidence="ECO:0000255"
FT STRAND 6..9
FT /evidence="ECO:0007829|PDB:3ZXF"
FT STRAND 16..26
FT /evidence="ECO:0007829|PDB:3ZXF"
FT STRAND 32..42
FT /evidence="ECO:0007829|PDB:3ZXF"
FT STRAND 47..54
FT /evidence="ECO:0007829|PDB:3ZXF"
FT TURN 55..58
FT /evidence="ECO:0007829|PDB:3ZXF"
FT STRAND 59..66
FT /evidence="ECO:0007829|PDB:3ZXF"
FT STRAND 85..93
FT /evidence="ECO:0007829|PDB:3ZXF"
FT STRAND 95..102
FT /evidence="ECO:0007829|PDB:3ZXF"
FT STRAND 105..111
FT /evidence="ECO:0007829|PDB:3ZXF"
FT HELIX 116..118
FT /evidence="ECO:0007829|PDB:3ZXF"
FT STRAND 121..127
FT /evidence="ECO:0007829|PDB:3ZXF"
FT STRAND 129..135
FT /evidence="ECO:0007829|PDB:3ZXF"
SQ SEQUENCE 136 AA; 15075 MW; F613D3540331C13F CRC64;
MSNVPHKSSL PEGIRPGTVL RIRGLVPPNA SRFHVNLLCG EEQGSDAALH FNPRLDTSEV
VFNSKEQGSW GREERGPGVP FQRGQPFEVL IIASDDGFKA VVGDAQYHHF RHRLPLARVR
LVEVGGDVQL DSVRIF