CLD3_MOUSE
ID CLD3_MOUSE Reviewed; 219 AA.
AC Q9Z0G9; Q91X40;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 03-AUG-2022, entry version 163.
DE RecName: Full=Claudin-3;
DE AltName: Full=Clostridium perfringens enterotoxin receptor 2;
DE Short=CPE-R 2;
DE Short=CPE-receptor 2;
GN Name=Cldn3; Synonyms=Cpetr2;
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] (ISOFORM 1).
RX PubMed=9878248; DOI=10.1006/geno.1998.5619;
RA Paperna T., Peoples R., Wang Y.K., Kaplan P., Francke U.;
RT "Genes for the CPE receptor (CPETR1) and the human homolog of RVP1 (CPETR2)
RT are localized within the Williams-Beuren syndrome deletion.";
RL Genomics 54:453-459(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), SUBCELLULAR LOCATION, AND TISSUE
RP SPECIFICITY.
RC TISSUE=Liver;
RX PubMed=9892664; DOI=10.1073/pnas.96.2.511;
RA Morita K., Furuse M., Fujimoto K., Tsukita S.;
RT "Claudin multigene family encoding four-transmembrane domain protein
RT components of tight junction strands.";
RL Proc. Natl. Acad. Sci. U.S.A. 96:511-516(1999).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
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 FUNCTION.
RX PubMed=10508613; DOI=10.1016/s0960-9822(99)80452-7;
RA Kubota K., Furuse M., Sasaki H., Sonoda N., Fujita K., Nagafuchi A.,
RA Tsukita S.;
RT "Ca(2+)-independent cell-adhesion activity of claudins, a family of
RT integral membrane proteins localized at tight junctions.";
RL Curr. Biol. 9:1035-1038(1999).
RN [5]
RP INTERACTION WITH CLDN1 AND CLDN2.
RX PubMed=10562289; DOI=10.1083/jcb.147.4.891;
RA Furuse M., Sasaki H., Tsukita S.;
RT "Manner of interaction of heterogeneous claudin species within and between
RT tight junction strands.";
RL J. Cell Biol. 147:891-903(1999).
RN [6]
RP INTERACTION WITH TJP1; TJP2 AND TJP3.
RX PubMed=10601346; DOI=10.1083/jcb.147.6.1351;
RA Itoh M., Furuse M., Morita K., Kubota K., Saitou M., Tsukita S.;
RT "Direct binding of three tight junction-associated MAGUKs, ZO-1, ZO-2, and
RT ZO-3, with the COOH termini of claudins.";
RL J. Cell Biol. 147:1351-1363(1999).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-197, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT "Large-scale phosphorylation analysis of mouse liver.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver, and Pancreas;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [9]
RP INTERACTION WITH CLOSTRIDIUM PERFRINGENS CPE.
RX PubMed=25678664; DOI=10.1126/science.1261833;
RA Saitoh Y., Suzuki H., Tani K., Nishikawa K., Irie K., Ogura Y., Tamura A.,
RA Tsukita S., Fujiyoshi Y.;
RT "Tight junctions. Structural insight into tight junction disassembly by
RT Clostridium perfringens enterotoxin.";
RL Science 347:775-778(2015).
CC -!- FUNCTION: Plays a major role in tight junction-specific obliteration of
CC the intercellular space, through calcium-independent cell-adhesion
CC activity. {ECO:0000269|PubMed:10508613}.
CC -!- SUBUNIT: Can form homo- and heteropolymers with other CLDN.
CC Homopolymers interact with CLDN1 and CLDN2 homopolymers. Directly
CC interacts with TJP1/ZO-1, TJP2/ZO-2 and TJP3/ZO-3.
CC {ECO:0000269|PubMed:10562289, ECO:0000269|PubMed:10601346}.
CC -!- SUBUNIT: (Microbial infection) Interacts with Clostridium perfringens
CC enterotoxin CPE; the interaction may disrupt claudin assembly in tight
CC junctions. {ECO:0000269|PubMed:25678664}.
CC -!- SUBCELLULAR LOCATION: Cell junction, tight junction
CC {ECO:0000269|PubMed:9892664}. Cell membrane
CC {ECO:0000269|PubMed:9892664}; Multi-pass membrane protein
CC {ECO:0000269|PubMed:9892664}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9Z0G9-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9Z0G9-2; Sequence=VSP_001101;
CC -!- TISSUE SPECIFICITY: Expressed at high levels in liver and lung and, at
CC lower levels, in kidney and testis. {ECO:0000269|PubMed:9892664}.
CC -!- SIMILARITY: Belongs to the claudin family. {ECO:0000305}.
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DR EMBL; AF095905; AAD14608.1; -; mRNA.
DR EMBL; AF087821; AAD09756.1; -; mRNA.
DR EMBL; BC012650; AAH12650.1; -; mRNA.
DR CCDS; CCDS19729.1; -. [Q9Z0G9-1]
DR RefSeq; NP_034032.1; NM_009902.4. [Q9Z0G9-1]
DR PDB; 6AKE; X-ray; 3.60 A; A/C=1-183.
DR PDB; 6AKF; X-ray; 3.90 A; A/C/E/G=1-183.
DR PDB; 6AKG; X-ray; 4.30 A; A/C=1-183.
DR PDBsum; 6AKE; -.
DR PDBsum; 6AKF; -.
DR PDBsum; 6AKG; -.
DR AlphaFoldDB; Q9Z0G9; -.
DR SMR; Q9Z0G9; -.
DR DIP; DIP-40779N; -.
DR IntAct; Q9Z0G9; 2.
DR MINT; Q9Z0G9; -.
DR STRING; 10090.ENSMUSP00000091799; -.
DR iPTMnet; Q9Z0G9; -.
DR PhosphoSitePlus; Q9Z0G9; -.
DR jPOST; Q9Z0G9; -.
DR MaxQB; Q9Z0G9; -.
DR PaxDb; Q9Z0G9; -.
DR PRIDE; Q9Z0G9; -.
DR ProteomicsDB; 283293; -. [Q9Z0G9-1]
DR ProteomicsDB; 283294; -. [Q9Z0G9-2]
DR Antibodypedia; 3638; 552 antibodies from 39 providers.
DR DNASU; 12739; -.
DR Ensembl; ENSMUST00000094245; ENSMUSP00000091799; ENSMUSG00000070473. [Q9Z0G9-1]
DR GeneID; 12739; -.
DR KEGG; mmu:12739; -.
DR UCSC; uc008zxe.2; mouse. [Q9Z0G9-1]
DR CTD; 1365; -.
DR MGI; MGI:1329044; Cldn3.
DR VEuPathDB; HostDB:ENSMUSG00000070473; -.
DR eggNOG; ENOG502QRZ8; Eukaryota.
DR GeneTree; ENSGT00940000162095; -.
DR HOGENOM; CLU_076370_1_2_1; -.
DR InParanoid; Q9Z0G9; -.
DR OMA; LCSIICC; -.
DR PhylomeDB; Q9Z0G9; -.
DR TreeFam; TF331936; -.
DR BioGRID-ORCS; 12739; 2 hits in 74 CRISPR screens.
DR ChiTaRS; Cldn3; mouse.
DR PRO; PR:Q9Z0G9; -.
DR Proteomes; UP000000589; Chromosome 5.
DR RNAct; Q9Z0G9; protein.
DR Bgee; ENSMUSG00000070473; Expressed in small intestine Peyer's patch and 147 other tissues.
DR ExpressionAtlas; Q9Z0G9; baseline and differential.
DR Genevisible; Q9Z0G9; MM.
DR GO; GO:0043296; C:apical junction complex; ISO:MGI.
DR GO; GO:0016327; C:apicolateral plasma membrane; IDA:UniProtKB.
DR GO; GO:0005923; C:bicellular tight junction; IDA:UniProtKB.
DR GO; GO:0005911; C:cell-cell junction; IDA:ARUK-UCL.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0016021; C:integral component of membrane; NAS:UniProtKB.
DR GO; GO:0016328; C:lateral plasma membrane; IDA:MGI.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0032991; C:protein-containing complex; ISO:MGI.
DR GO; GO:0070160; C:tight junction; ISO:MGI.
DR GO; GO:0042802; F:identical protein binding; IPI:UniProtKB.
DR GO; GO:0005198; F:structural molecule activity; IEA:InterPro.
DR GO; GO:0031532; P:actin cytoskeleton reorganization; ISO:MGI.
DR GO; GO:0070830; P:bicellular tight junction assembly; ISO:MGI.
DR GO; GO:0016338; P:calcium-independent cell-cell adhesion via plasma membrane cell-adhesion molecules; IDA:UniProtKB.
DR GO; GO:0007155; P:cell adhesion; IBA:GO_Central.
DR GO; GO:0034331; P:cell junction maintenance; IMP:ARUK-UCL.
DR GO; GO:0003382; P:epithelial cell morphogenesis; IDA:UniProtKB.
DR GO; GO:0014045; P:establishment of endothelial blood-brain barrier; IMP:ARUK-UCL.
DR GO; GO:0030336; P:negative regulation of cell migration; ISO:MGI.
DR GO; GO:0008285; P:negative regulation of cell population proliferation; ISO:MGI.
DR GO; GO:0010629; P:negative regulation of gene expression; ISO:MGI.
DR GO; GO:0061045; P:negative regulation of wound healing; ISO:MGI.
DR GO; GO:1903348; P:positive regulation of bicellular tight junction assembly; ISO:MGI.
DR GO; GO:1901890; P:positive regulation of cell junction assembly; ISO:MGI.
DR GO; GO:0030335; P:positive regulation of cell migration; ISO:MGI.
DR GO; GO:0010628; P:positive regulation of gene expression; ISO:MGI.
DR GO; GO:1905050; P:positive regulation of metallopeptidase activity; ISO:MGI.
DR GO; GO:0001934; P:positive regulation of protein phosphorylation; ISO:MGI.
DR GO; GO:0090303; P:positive regulation of wound healing; ISO:MGI.
DR GO; GO:0022604; P:regulation of cell morphogenesis; ISO:MGI.
DR GO; GO:0090559; P:regulation of membrane permeability; ISO:MGI.
DR GO; GO:0150111; P:regulation of transepithelial transport; ISO:MGI.
DR GO; GO:0045471; P:response to ethanol; IEA:Ensembl.
DR GO; GO:0140459; P:response to Gram-positive bacterium; IEA:Ensembl.
DR GO; GO:0001666; P:response to hypoxia; IEA:Ensembl.
DR InterPro; IPR006187; Claudin.
DR InterPro; IPR003549; Claudin3.
DR InterPro; IPR017974; Claudin_CS.
DR InterPro; IPR004031; PMP22/EMP/MP20/Claudin.
DR PANTHER; PTHR12002; PTHR12002; 1.
DR Pfam; PF00822; PMP22_Claudin; 1.
DR PRINTS; PR01378; CLAUDIN3.
DR PROSITE; PS01346; CLAUDIN; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Cell junction; Cell membrane; Membrane;
KW Phosphoprotein; Reference proteome; Tight junction; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..219
FT /note="Claudin-3"
FT /id="PRO_0000144739"
FT TOPO_DOM 1..8
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 9..29
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 30..80
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 81..101
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 102..115
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 116..136
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 137..159
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 160..180
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 181..219
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 218..219
FT /note="Interactions with TJP1, TJP2 and TJP3"
FT /evidence="ECO:0000250"
FT MOD_RES 197
FT /note="Phosphotyrosine"
FT /evidence="ECO:0007744|PubMed:17242355"
FT MOD_RES 198
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q63400"
FT VAR_SEQ 72..91
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_001101"
SQ SEQUENCE 219 AA; 23285 MW; 62F67810D9B9BD37 CRC64;
MSMGLEITGT SLAVLGWLCT IVCCALPMWR VSAFIGSSII TAQITWEGLW MNCVVQSTGQ
MQCKMYDSLL ALPQDLQAAR ALIVVSILLA AFGLLVALVG AQCTNCVQDE TAKAKITIVA
GVLFLLAALL TLVPVSWSAN TIIRDFYNPL VPEAQKREMG AGLYVGWAAA ALQLLGGALL
CCSCPPRDKY APTKILYSAP RSTGPGTGTG TAYDRKDYV
