Full text data of LGALS7
LGALS7
(PIG1)
[Confidence: low (only semi-automatic identification from reviews)]
Galectin-7; Gal-7 (HKL-14; PI7; p53-induced gene 1 protein)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
Galectin-7; Gal-7 (HKL-14; PI7; p53-induced gene 1 protein)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
UniProt
P47929
ID LEG7_HUMAN Reviewed; 136 AA.
AC P47929; Q6IB87;
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
read moreDT 23-JAN-2007, sequence version 2.
DT 22-JAN-2014, entry version 139.
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;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND PROTEIN SEQUENCE OF 8-20; 76-83;
RP 112-118 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.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA 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
RT project: 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.,
RA Zuraw B.L., Hsu D.K., Liu F.T.;
RT "Galectin-7 (PIG1) exhibits pro-apoptotic function through JNK
RT activation 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.,
RA 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
CC protein that functions intracellularly upstream of JNK activation
CC and cytochrome c release.
CC -!- SUBUNIT: Monomer.
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Secreted (Potential).
CC Note=May be secreted by a non-classical secretory pathway.
CC -!- TISSUE SPECIFICITY: Mainly expressed in stratified squamous
CC epithelium.
CC -!- INDUCTION: By p53/TP53.
CC -!- SIMILARITY: Contains 1 galectin domain.
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";
CC -----------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution-NoDerivs License
CC -----------------------------------------------------------------------
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 PIR; I55469; I55469.
DR RefSeq; NP_001035972.1; NM_001042507.3.
DR RefSeq; NP_002298.1; NM_002307.3.
DR UniGene; Hs.558355; -.
DR UniGene; Hs.702546; -.
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; 5GAL; X-ray; 2.00 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; 5GAL; -.
DR ProteinModelPortal; P47929; -.
DR SMR; P47929; 4-136.
DR IntAct; P47929; 8.
DR MINT; MINT-1154298; -.
DR STRING; 9606.ENSP00000313571; -.
DR BindingDB; P47929; -.
DR ChEMBL; CHEMBL5008; -.
DR PhosphoSite; P47929; -.
DR PaxDb; P47929; -.
DR PeptideAtlas; P47929; -.
DR PRIDE; P47929; -.
DR Ensembl; ENST00000314980; ENSP00000313571; ENSG00000178934.
DR Ensembl; ENST00000378626; ENSP00000367891; ENSG00000205076.
DR GeneID; 3963; -.
DR GeneID; 653499; -.
DR KEGG; hsa:3963; -.
DR KEGG; hsa:653499; -.
DR UCSC; uc002oje.3; human.
DR CTD; 3963; -.
DR CTD; 653499; -.
DR GeneCards; GC19M039261; -.
DR GeneCards; GC19P039279; -.
DR HGNC; HGNC:6568; LGALS7.
DR HGNC; HGNC:34447; LGALS7B.
DR HPA; CAB025100; -.
DR HPA; CAB032606; -.
DR HPA; HPA001549; -.
DR MIM; 600615; gene.
DR neXtProt; NX_P47929; -.
DR PharmGKB; PA162393892; -.
DR eggNOG; NOG301549; -.
DR HOGENOM; HOG000293279; -.
DR HOVERGEN; HBG006255; -.
DR InParanoid; P47929; -.
DR KO; K10092; -.
DR OMA; RHRMPLA; -.
DR OrthoDB; EOG7S7SFG; -.
DR PhylomeDB; P47929; -.
DR EvolutionaryTrace; P47929; -.
DR GeneWiki; LGALS7; -.
DR NextBio; 15548; -.
DR PRO; PR:P47929; -.
DR ArrayExpress; P47929; -.
DR Bgee; P47929; -.
DR CleanEx; HS_LGALS7; -.
DR Genevestigator; P47929; -.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
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; TAS:ProtInc.
DR GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
DR GO; GO:0007157; P:heterophilic cell-cell adhesion; TAS:ProtInc.
DR Gene3D; 2.60.120.200; -; 1.
DR InterPro; IPR008985; ConA-like_lec_gl_sf.
DR InterPro; IPR013320; ConA-like_subgrp.
DR InterPro; IPR001079; Galectin_CRD.
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; Complete proteome; Cytoplasm;
KW Direct protein sequencing; Lectin; Nucleus; Reference proteome;
KW Secreted.
FT CHAIN 1 136 Galectin-7.
FT /FTId=PRO_0000076940.
FT DOMAIN 6 136 Galectin.
FT REGION 70 76 Beta-galactoside binding (Potential).
FT STRAND 6 9
FT STRAND 16 26
FT STRAND 32 42
FT STRAND 47 54
FT TURN 55 58
FT STRAND 59 66
FT STRAND 85 93
FT STRAND 95 102
FT STRAND 105 111
FT HELIX 116 118
FT STRAND 121 127
FT STRAND 129 135
SQ SEQUENCE 136 AA; 15075 MW; F613D3540331C13F CRC64;
MSNVPHKSSL PEGIRPGTVL RIRGLVPPNA SRFHVNLLCG EEQGSDAALH FNPRLDTSEV
VFNSKEQGSW GREERGPGVP FQRGQPFEVL IIASDDGFKA VVGDAQYHHF RHRLPLARVR
LVEVGGDVQL DSVRIF
//
ID LEG7_HUMAN Reviewed; 136 AA.
AC P47929; Q6IB87;
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
read moreDT 23-JAN-2007, sequence version 2.
DT 22-JAN-2014, entry version 139.
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;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND PROTEIN SEQUENCE OF 8-20; 76-83;
RP 112-118 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.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA 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
RT project: 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.,
RA Zuraw B.L., Hsu D.K., Liu F.T.;
RT "Galectin-7 (PIG1) exhibits pro-apoptotic function through JNK
RT activation 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.,
RA 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
CC protein that functions intracellularly upstream of JNK activation
CC and cytochrome c release.
CC -!- SUBUNIT: Monomer.
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Secreted (Potential).
CC Note=May be secreted by a non-classical secretory pathway.
CC -!- TISSUE SPECIFICITY: Mainly expressed in stratified squamous
CC epithelium.
CC -!- INDUCTION: By p53/TP53.
CC -!- SIMILARITY: Contains 1 galectin domain.
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";
CC -----------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution-NoDerivs License
CC -----------------------------------------------------------------------
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 PIR; I55469; I55469.
DR RefSeq; NP_001035972.1; NM_001042507.3.
DR RefSeq; NP_002298.1; NM_002307.3.
DR UniGene; Hs.558355; -.
DR UniGene; Hs.702546; -.
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; 5GAL; X-ray; 2.00 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; 5GAL; -.
DR ProteinModelPortal; P47929; -.
DR SMR; P47929; 4-136.
DR IntAct; P47929; 8.
DR MINT; MINT-1154298; -.
DR STRING; 9606.ENSP00000313571; -.
DR BindingDB; P47929; -.
DR ChEMBL; CHEMBL5008; -.
DR PhosphoSite; P47929; -.
DR PaxDb; P47929; -.
DR PeptideAtlas; P47929; -.
DR PRIDE; P47929; -.
DR Ensembl; ENST00000314980; ENSP00000313571; ENSG00000178934.
DR Ensembl; ENST00000378626; ENSP00000367891; ENSG00000205076.
DR GeneID; 3963; -.
DR GeneID; 653499; -.
DR KEGG; hsa:3963; -.
DR KEGG; hsa:653499; -.
DR UCSC; uc002oje.3; human.
DR CTD; 3963; -.
DR CTD; 653499; -.
DR GeneCards; GC19M039261; -.
DR GeneCards; GC19P039279; -.
DR HGNC; HGNC:6568; LGALS7.
DR HGNC; HGNC:34447; LGALS7B.
DR HPA; CAB025100; -.
DR HPA; CAB032606; -.
DR HPA; HPA001549; -.
DR MIM; 600615; gene.
DR neXtProt; NX_P47929; -.
DR PharmGKB; PA162393892; -.
DR eggNOG; NOG301549; -.
DR HOGENOM; HOG000293279; -.
DR HOVERGEN; HBG006255; -.
DR InParanoid; P47929; -.
DR KO; K10092; -.
DR OMA; RHRMPLA; -.
DR OrthoDB; EOG7S7SFG; -.
DR PhylomeDB; P47929; -.
DR EvolutionaryTrace; P47929; -.
DR GeneWiki; LGALS7; -.
DR NextBio; 15548; -.
DR PRO; PR:P47929; -.
DR ArrayExpress; P47929; -.
DR Bgee; P47929; -.
DR CleanEx; HS_LGALS7; -.
DR Genevestigator; P47929; -.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
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; TAS:ProtInc.
DR GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
DR GO; GO:0007157; P:heterophilic cell-cell adhesion; TAS:ProtInc.
DR Gene3D; 2.60.120.200; -; 1.
DR InterPro; IPR008985; ConA-like_lec_gl_sf.
DR InterPro; IPR013320; ConA-like_subgrp.
DR InterPro; IPR001079; Galectin_CRD.
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; Complete proteome; Cytoplasm;
KW Direct protein sequencing; Lectin; Nucleus; Reference proteome;
KW Secreted.
FT CHAIN 1 136 Galectin-7.
FT /FTId=PRO_0000076940.
FT DOMAIN 6 136 Galectin.
FT REGION 70 76 Beta-galactoside binding (Potential).
FT STRAND 6 9
FT STRAND 16 26
FT STRAND 32 42
FT STRAND 47 54
FT TURN 55 58
FT STRAND 59 66
FT STRAND 85 93
FT STRAND 95 102
FT STRAND 105 111
FT HELIX 116 118
FT STRAND 121 127
FT STRAND 129 135
SQ SEQUENCE 136 AA; 15075 MW; F613D3540331C13F CRC64;
MSNVPHKSSL PEGIRPGTVL RIRGLVPPNA SRFHVNLLCG EEQGSDAALH FNPRLDTSEV
VFNSKEQGSW GREERGPGVP FQRGQPFEVL IIASDDGFKA VVGDAQYHHF RHRLPLARVR
LVEVGGDVQL DSVRIF
//
MIM
600615
*RECORD*
*FIELD* NO
600615
*FIELD* TI
*600615 LECTIN, GALACTOSIDE-BINDING, SOLUBLE, 7; LGALS7
;;GALECTIN 7; GAL7
*FIELD* TX
read more
DESCRIPTION
Galectins belong to a family of related beta-galactoside-binding
lectins, also referred to as S-type or S-Lac lectins. Members of this
family have been implicated in a variety of functions, including growth
regulation, cell adhesion, migration, neoplastic transformation, and
immune responses. In addition to galectin-7, the family includes
galectin-1 (LGALS1; 150570), also known as galaptin, a homodimer with
subunit molecular mass of 14,500, which is abundant in smooth and
skeletal muscle, although it is also found in many other cell types;
galectin-2 (LGALS2; 150571), a homodimer with a subunit molecular mass
of 14,650 originally described in a hepatoma; galectin-3 (LGALS3;
153619), also known as MAC2, that is abundant in activated macrophages
and epithelial cells; and galectin-4 (LGALS4; 602518), a monomer with a
molecular mass of 36,300 containing 2 carboxyhydrate-binding domains
within a single polypeptide chain.
CLONING
In the course of a systematic search for keratinocyte proteins whose
levels are differentially regulated in transformed cells and which may
play a role in the maintenance of the normal phenotype, Madsen et al.
(1995) cloned a novel member of the galectin family, designated
galectin-7. This is an abundant keratinocyte protein whose expression is
abrogated in SV40 transformed keratinocytes. It is a monomeric
beta-galactoside-binding protein with a very narrow tissue distribution.
The galectin-7 corresponds to IEF (isoelectric focusing) 17 as
determined by 2-dimensional gel electrophoresis analysis of proteins
expressed by transiently transfected COS-1 cells. The protein was found
mainly in stratified squamous epithelium. The antigen localized to basal
keratinocytes, although it was also found, albeit at lower levels, in
the suprabasal layers where it concentrated to areas of cell-to-cell
contact. The cellular localization and its striking down-regulation in
cultured keratinocytes imply a role in cell-cell and/or cell-matrix
interactions necessary for normal growth control.
GENE FUNCTION
Cao et al. (2003) reported the role of the carbohydrate-binding protein,
galectin-7, in reepithelialization of corneal wounds. They found that
expression of galectin-7 was markedly upregulated in corneal epithelium
after injury and that exogenous galectin-7 stimulated
reepithelialization of corneal wounds. The stimulatory effect of
galectin-7 on corneal epithelial wound closure was specifically
inhibited by beta-lactose, a competing sugar, but unaffected by sucrose,
an irrelevant disaccharide.
MAPPING
By Southern blotting of human/rodent cell hybrids, Madsen et al. (1995)
mapped the galectin-7 gene to chromosome 19.
ANIMAL MODEL
Using models of corneal wound healing, Cao et al. (2002) found that
reepithelialization of wounds was significantly slower in Gal3-null mice
compared with wildtype mice, and the difference was not due to a reduced
epithelial cell proliferation rate. Gene expression analysis using cDNA
microarrays revealed that healing corneas of Gal3-null mice had reduced
levels of Gal7. Exogenous application of Gal7, but not Gal3, accelerated
reepithelialization of wounds in Gal3-null mice. Both Gal3 and Gal7
accelerated corneal wound healing in wildtype mice. Cao et al. (2002)
concluded that both GAL3 and GAL7 play a role in reepithelialization of
corneal wounds.
*FIELD* RF
1. Cao, Z.; Said, N.; Amin, S.; Wu, H. K.; Bruce, A.; Garate, M.;
Hsu, D. K.; Kuwabara, I.; Liu, F.-T.; Panjwani, N.: Galectin-3 and
-7, but not galectin-1, play a role in re-epithelialization of wounds. J.
Biol. Chem. 277: 42299-42305, 2002.
2. Cao, Z.; Said, N.; Wu, H. K.; Kuwabara, I.; Liu, F.-T.; Panjwani,
N.: Galectin-7 as a potential mediator of corneal epithelial cell
migration. Arch. Ophthal. 121: 82-86, 2003.
3. Madsen, P.; Rasmussen, H. H.; Flint, T.; Gromov, P.; Kruse, T.
A.; Honore, B.; Vorum, H.; Celis, J. E.: Cloning, expression, and
chromosome mapping of human galectin-7. J. Biol. Chem. 270: 5823-5829,
1995.
*FIELD* CN
Jane Kelly - updated: 3/4/2003
Patricia A. Hartz - updated: 12/17/2002
*FIELD* CD
Victor A. McKusick: 6/16/1995
*FIELD* ED
terry: 04/04/2005
cwells: 3/4/2003
mgross: 1/3/2003
terry: 12/17/2002
dkim: 7/21/1998
mark: 6/16/1995
*RECORD*
*FIELD* NO
600615
*FIELD* TI
*600615 LECTIN, GALACTOSIDE-BINDING, SOLUBLE, 7; LGALS7
;;GALECTIN 7; GAL7
*FIELD* TX
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DESCRIPTION
Galectins belong to a family of related beta-galactoside-binding
lectins, also referred to as S-type or S-Lac lectins. Members of this
family have been implicated in a variety of functions, including growth
regulation, cell adhesion, migration, neoplastic transformation, and
immune responses. In addition to galectin-7, the family includes
galectin-1 (LGALS1; 150570), also known as galaptin, a homodimer with
subunit molecular mass of 14,500, which is abundant in smooth and
skeletal muscle, although it is also found in many other cell types;
galectin-2 (LGALS2; 150571), a homodimer with a subunit molecular mass
of 14,650 originally described in a hepatoma; galectin-3 (LGALS3;
153619), also known as MAC2, that is abundant in activated macrophages
and epithelial cells; and galectin-4 (LGALS4; 602518), a monomer with a
molecular mass of 36,300 containing 2 carboxyhydrate-binding domains
within a single polypeptide chain.
CLONING
In the course of a systematic search for keratinocyte proteins whose
levels are differentially regulated in transformed cells and which may
play a role in the maintenance of the normal phenotype, Madsen et al.
(1995) cloned a novel member of the galectin family, designated
galectin-7. This is an abundant keratinocyte protein whose expression is
abrogated in SV40 transformed keratinocytes. It is a monomeric
beta-galactoside-binding protein with a very narrow tissue distribution.
The galectin-7 corresponds to IEF (isoelectric focusing) 17 as
determined by 2-dimensional gel electrophoresis analysis of proteins
expressed by transiently transfected COS-1 cells. The protein was found
mainly in stratified squamous epithelium. The antigen localized to basal
keratinocytes, although it was also found, albeit at lower levels, in
the suprabasal layers where it concentrated to areas of cell-to-cell
contact. The cellular localization and its striking down-regulation in
cultured keratinocytes imply a role in cell-cell and/or cell-matrix
interactions necessary for normal growth control.
GENE FUNCTION
Cao et al. (2003) reported the role of the carbohydrate-binding protein,
galectin-7, in reepithelialization of corneal wounds. They found that
expression of galectin-7 was markedly upregulated in corneal epithelium
after injury and that exogenous galectin-7 stimulated
reepithelialization of corneal wounds. The stimulatory effect of
galectin-7 on corneal epithelial wound closure was specifically
inhibited by beta-lactose, a competing sugar, but unaffected by sucrose,
an irrelevant disaccharide.
MAPPING
By Southern blotting of human/rodent cell hybrids, Madsen et al. (1995)
mapped the galectin-7 gene to chromosome 19.
ANIMAL MODEL
Using models of corneal wound healing, Cao et al. (2002) found that
reepithelialization of wounds was significantly slower in Gal3-null mice
compared with wildtype mice, and the difference was not due to a reduced
epithelial cell proliferation rate. Gene expression analysis using cDNA
microarrays revealed that healing corneas of Gal3-null mice had reduced
levels of Gal7. Exogenous application of Gal7, but not Gal3, accelerated
reepithelialization of wounds in Gal3-null mice. Both Gal3 and Gal7
accelerated corneal wound healing in wildtype mice. Cao et al. (2002)
concluded that both GAL3 and GAL7 play a role in reepithelialization of
corneal wounds.
*FIELD* RF
1. Cao, Z.; Said, N.; Amin, S.; Wu, H. K.; Bruce, A.; Garate, M.;
Hsu, D. K.; Kuwabara, I.; Liu, F.-T.; Panjwani, N.: Galectin-3 and
-7, but not galectin-1, play a role in re-epithelialization of wounds. J.
Biol. Chem. 277: 42299-42305, 2002.
2. Cao, Z.; Said, N.; Wu, H. K.; Kuwabara, I.; Liu, F.-T.; Panjwani,
N.: Galectin-7 as a potential mediator of corneal epithelial cell
migration. Arch. Ophthal. 121: 82-86, 2003.
3. Madsen, P.; Rasmussen, H. H.; Flint, T.; Gromov, P.; Kruse, T.
A.; Honore, B.; Vorum, H.; Celis, J. E.: Cloning, expression, and
chromosome mapping of human galectin-7. J. Biol. Chem. 270: 5823-5829,
1995.
*FIELD* CN
Jane Kelly - updated: 3/4/2003
Patricia A. Hartz - updated: 12/17/2002
*FIELD* CD
Victor A. McKusick: 6/16/1995
*FIELD* ED
terry: 04/04/2005
cwells: 3/4/2003
mgross: 1/3/2003
terry: 12/17/2002
dkim: 7/21/1998
mark: 6/16/1995