LEG4_MOUSE
ID LEG4_MOUSE Reviewed; 326 AA.
AC Q8K419; O88353; Q91X74;
DT 02-FEB-2004, integrated into UniProtKB/Swiss-Prot.
DT 02-FEB-2004, sequence version 2.
DT 03-AUG-2022, entry version 145.
DE RecName: Full=Galectin-4;
DE Short=Gal-4;
DE AltName: Full=Lactose-binding lectin 4;
GN Name=Lgals4;
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].
RC STRAIN=BALB/cJ; TISSUE=Liver;
RA Maly P., Jenikova G., Cummings R.D.;
RT "Molecular cloning and tissue distribution of mouse galectin-4.";
RL Submitted (JUL-2001) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=C57BL/6J; TISSUE=Colon;
RA Hokama A., Tanaka Y., Mizoguchi A.;
RL Submitted (MAY-2002) to the EMBL/GenBank/DDBJ databases.
RN [3]
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 [4]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 22-321, AND TISSUE SPECIFICITY.
RC STRAIN=129/Sv; TISSUE=Colon;
RX PubMed=9446608; DOI=10.1074/jbc.273.5.2954;
RA Gitt M.A., Colnot C., Poirier F., Nani K.J., Barondes S.H., Leffler H.;
RT "Galectin-4 and galectin-6 are two closely related lectins expressed in
RT mouse gastrointestinal tract.";
RL J. Biol. Chem. 273:2954-2960(1998).
RN [5]
RP X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 8-159.
RG RIKEN structural genomics initiative (RSGI);
RT "Crystal structure of the N-terminal domain of mouse galectin-4.";
RL Submitted (OCT-2007) to the PDB data bank.
CC -!- FUNCTION: Galectin that binds lactose and a related range of sugars.
CC {ECO:0000250}.
CC -!- SUBUNIT: Monomer. {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Epithelial cells of the embryonic and adult
CC gastrointestinal tract. Expressed at about equal levels in colon and
CC small intestine but much less in stomach. {ECO:0000269|PubMed:9446608}.
CC -!- DOMAIN: Contains two homologous but distinct carbohydrate-binding
CC domains.
CC -!- WEB RESOURCE: Name=Functional Glycomics Gateway - Glycan Binding;
CC Note=Galectin-4;
CC URL="http://www.functionalglycomics.org/glycomics/GBPServlet?&operationType=view&cbpId=cbp_mou_Stlect_200";
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DR EMBL; AY044870; AAK97790.1; -; mRNA.
DR EMBL; AF510729; AAM44060.1; -; mRNA.
DR EMBL; BC011236; AAH11236.1; -; mRNA.
DR EMBL; BC021632; AAH21632.1; -; mRNA.
DR EMBL; BC030297; AAH30297.1; -; mRNA.
DR EMBL; AF026795; AAC27245.1; -; mRNA.
DR CCDS; CCDS21058.1; -.
DR RefSeq; NP_034836.1; NM_010706.2.
DR PDB; 2DYC; X-ray; 2.40 A; A=9-159.
DR PDB; 3I8T; X-ray; 2.10 A; A=2-152.
DR PDBsum; 2DYC; -.
DR PDBsum; 3I8T; -.
DR AlphaFoldDB; Q8K419; -.
DR SMR; Q8K419; -.
DR BioGRID; 201144; 1.
DR IntAct; Q8K419; 3.
DR STRING; 10090.ENSMUSP00000066461; -.
DR UniLectin; Q8K419; -.
DR iPTMnet; Q8K419; -.
DR PhosphoSitePlus; Q8K419; -.
DR jPOST; Q8K419; -.
DR MaxQB; Q8K419; -.
DR PaxDb; Q8K419; -.
DR PRIDE; Q8K419; -.
DR ProteomicsDB; 291936; -.
DR Antibodypedia; 30166; 380 antibodies from 35 providers.
DR DNASU; 16855; -.
DR Ensembl; ENSMUST00000066723; ENSMUSP00000066461; ENSMUSG00000053964.
DR GeneID; 16855; -.
DR KEGG; mmu:16855; -.
DR UCSC; uc009gac.2; mouse.
DR CTD; 3960; -.
DR MGI; MGI:107536; Lgals4.
DR VEuPathDB; HostDB:ENSMUSG00000053964; -.
DR eggNOG; KOG3587; Eukaryota.
DR GeneTree; ENSGT00940000160378; -.
DR HOGENOM; CLU_037794_1_0_1; -.
DR InParanoid; Q8K419; -.
DR OMA; HWGGRFY; -.
DR OrthoDB; 829777at2759; -.
DR PhylomeDB; Q8K419; -.
DR TreeFam; TF315551; -.
DR BioGRID-ORCS; 16855; 0 hits in 71 CRISPR screens.
DR ChiTaRS; Lgals4; mouse.
DR EvolutionaryTrace; Q8K419; -.
DR PRO; PR:Q8K419; -.
DR Proteomes; UP000000589; Chromosome 7.
DR RNAct; Q8K419; protein.
DR Bgee; ENSMUSG00000053964; Expressed in right colon and 164 other tissues.
DR ExpressionAtlas; Q8K419; baseline and differential.
DR Genevisible; Q8K419; MM.
DR GO; GO:0062023; C:collagen-containing extracellular matrix; HDA:BHF-UCL.
DR GO; GO:0005615; C:extracellular space; IDA:MGI.
DR GO; GO:0030246; F:carbohydrate binding; IEA:UniProtKB-KW.
DR GO; GO:0016936; F:galactoside binding; IDA:MGI.
DR GO; GO:0002780; P:antibacterial peptide biosynthetic process; IDA:MGI.
DR GO; GO:0042742; P:defense response to bacterium; IDA:MGI.
DR CDD; cd00070; GLECT; 2.
DR DisProt; DP02811; -.
DR InterPro; IPR013320; ConA-like_dom_sf.
DR InterPro; IPR044156; Galectin-like.
DR InterPro; IPR015533; Galectin4/6.
DR InterPro; IPR001079; Galectin_CRD.
DR PANTHER; PTHR11346; PTHR11346; 1.
DR PANTHER; PTHR11346:SF32; PTHR11346:SF32; 1.
DR Pfam; PF00337; Gal-bind_lectin; 2.
DR SMART; SM00908; Gal-bind_lectin; 2.
DR SMART; SM00276; GLECT; 2.
DR SUPFAM; SSF49899; SSF49899; 2.
DR PROSITE; PS51304; GALECTIN; 2.
PE 1: Evidence at protein level;
KW 3D-structure; Lectin; Reference proteome; Repeat.
FT CHAIN 1..326
FT /note="Galectin-4"
FT /id="PRO_0000076935"
FT DOMAIN 19..150
FT /note="Galectin 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00639"
FT DOMAIN 198..326
FT /note="Galectin 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00639"
FT BINDING 259..265
FT /ligand="a beta-D-galactoside"
FT /ligand_id="ChEBI:CHEBI:28034"
FT /evidence="ECO:0000250"
FT CONFLICT 77
FT /note="N -> K (in Ref. 2 and 4)"
FT /evidence="ECO:0000305"
FT CONFLICT 160
FT /note="P -> A (in Ref. 4; AAC27245)"
FT /evidence="ECO:0000305"
FT CONFLICT 208..209
FT /note="VR -> LP (in Ref. 4; AAC27245)"
FT /evidence="ECO:0000305"
FT STRAND 17..22
FT /evidence="ECO:0007829|PDB:3I8T"
FT STRAND 32..39
FT /evidence="ECO:0007829|PDB:3I8T"
FT STRAND 45..55
FT /evidence="ECO:0007829|PDB:3I8T"
FT STRAND 60..67
FT /evidence="ECO:0007829|PDB:3I8T"
FT STRAND 69..71
FT /evidence="ECO:0007829|PDB:3I8T"
FT STRAND 73..80
FT /evidence="ECO:0007829|PDB:3I8T"
FT STRAND 88..91
FT /evidence="ECO:0007829|PDB:3I8T"
FT STRAND 100..107
FT /evidence="ECO:0007829|PDB:3I8T"
FT STRAND 109..116
FT /evidence="ECO:0007829|PDB:3I8T"
FT STRAND 119..125
FT /evidence="ECO:0007829|PDB:3I8T"
FT HELIX 130..132
FT /evidence="ECO:0007829|PDB:3I8T"
FT STRAND 135..150
FT /evidence="ECO:0007829|PDB:3I8T"
SQ SEQUENCE 326 AA; 36372 MW; 7F3DD89862A853B5 CRC64;
MAYVPAPGYQ PTYNPTLPYK RPIPGGLSVG MSVYIQGMAK ENMRRFHVNF AVGQDDGADV
AFHFNPRFDG WDKVVFNTMQ SGQWGKEEKK KSMPFQKGKH FELVFMVMPE HYKVVVNGNS
FYEYGHRLPV QMVTHLQVDG DLELQSINFL GGQPAAAPYP GAMTIPAYPA GSPGYNPPQM
NTLPVMTGPP VFNPRVPYVG ALQGGLTVRR TIIIKGYVLP TARNFVINFK VGSSGDIALH
LNPRIGDSVV RNSFMNGSWG AEERKVAYNP FGPGQFFDLS IRCGMDRFKV FANGQHLFDF
SHRFQAFQMV DTLEINGDIT LSYVQI
