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   02-OCT-2024, entry version 213.
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
RT   galectin-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   PDB; 7N4O; X-ray; 2.05 A; A/B=2-136.
DR   PDB; 7N57; X-ray; 1.83 A; A/B=2-136.
DR   PDB; 7N6C; X-ray; 2.10 A; A/B=2-136.
DR   PDB; 7N8D; X-ray; 2.49 A; A/B=2-136.
DR   PDB; 7N8G; X-ray; 1.95 A; A/B=2-136.
DR   PDB; 7N96; X-ray; 2.38 A; A/B=2-136.
DR   PDB; 7RDG; X-ray; 3.00 A; A/B/C/D=2-136.
DR   PDB; 7TKW; X-ray; 1.85 A; A/B=2-136.
DR   PDB; 7TKX; X-ray; 1.83 A; A/B=2-136.
DR   PDB; 7TKY; X-ray; 2.53 A; A/B=2-136.
DR   PDB; 7TKZ; X-ray; 1.83 A; A/B=2-136.
DR   PDB; 7TRN; X-ray; 1.95 A; A/B/C/D=2-136.
DR   PDB; 7TRO; X-ray; 1.80 A; A/B=2-136.
DR   PDB; 7XAC; X-ray; 1.80 A; A/B=1-136.
DR   PDB; 7XBL; X-ray; 2.00 A; A/B=1-136.
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   PDBsum; 7N4O; -.
DR   PDBsum; 7N57; -.
DR   PDBsum; 7N6C; -.
DR   PDBsum; 7N8D; -.
DR   PDBsum; 7N8G; -.
DR   PDBsum; 7N96; -.
DR   PDBsum; 7RDG; -.
DR   PDBsum; 7TKW; -.
DR   PDBsum; 7TKX; -.
DR   PDBsum; 7TKY; -.
DR   PDBsum; 7TKZ; -.
DR   PDBsum; 7TRN; -.
DR   PDBsum; 7TRO; -.
DR   PDBsum; 7XAC; -.
DR   PDBsum; 7XBL; -.
DR   AlphaFoldDB; P47929; -.
DR   BMRB; P47929; -.
DR   SMR; P47929; -.
DR   BioGRID; 110154; 135.
DR   BioGRID; 575831; 105.
DR   IntAct; P47929; 122.
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   jPOST; P47929; -.
DR   MassIVE; P47929; -.
DR   PaxDb; 9606-ENSP00000313571; -.
DR   PeptideAtlas; P47929; -.
DR   PRIDE; P47929; -.
DR   ProteomicsDB; 55824; -.
DR   ABCD; P47929; 12 sequenced antibodies.
DR   Antibodypedia; 16627; 309 antibodies from 20 providers.
DR   Antibodypedia; 652; 221 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   AGR; HGNC:34447; -.
DR   AGR; HGNC:6568; -.
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; Group enriched (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; GNHFADF; -.
DR   OrthoDB; 4576960at2759; -.
DR   PhylomeDB; P47929; -.
DR   TreeFam; TF315551; -.
DR   PathwayCommons; P47929; -.
DR   Reactome; R-HSA-9725554; Differentiation of keratinocytes in interfollicular epidermis in mammalian skin.
DR   SignaLink; P47929; -.
DR   BioGRID-ORCS; 3963; 10 hits in 1047 CRISPR screens.
DR   BioGRID-ORCS; 653499; 27 hits in 1037 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 74 other cell types or tissues.
DR   ExpressionAtlas; P47929; baseline and differential.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR   GO; GO:0005615; C:extracellular space; TAS:ProtInc.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0030246; F:carbohydrate 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   CDD; cd00070; GLECT; 1.
DR   Gene3D; 2.60.120.200; -; 1.
DR   InterPro; IPR013320; ConA-like_dom_sf.
DR   InterPro; IPR044156; Galectin-like.
DR   InterPro; IPR001079; Galectin_CRD.
DR   PANTHER; PTHR11346; GALECTIN; 1.
DR   PANTHER; PTHR11346:SF107; GALECTIN-7; 1.
DR   Pfam; PF00337; Gal-bind_lectin; 1.
DR   SMART; SM00908; Gal-bind_lectin; 1.
DR   SMART; SM00276; GLECT; 1.
DR   SUPFAM; SSF49899; Concanavalin A-like lectins/glucanases; 1.
DR   PROSITE; PS51304; GALECTIN; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Apoptosis; Cytoplasm; Direct protein sequencing; Lectin;
KW   Nucleus; Proteomics identification; 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
//