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Claudin-3 (Clostridium perfringens enterotoxin receptor 2) (CPE-R 2) (CPE-receptor 2)

 CLD3_MOUSE              Reviewed;         219 AA.
Q9Z0G9; Q91X40;
30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
01-MAY-1999, sequence version 1.
27-SEP-2017, entry version 136.
RecName: Full=Claudin-3;
AltName: Full=Clostridium perfringens enterotoxin receptor 2;
Short=CPE-R 2;
Short=CPE-receptor 2;
Name=Cldn3; Synonyms=Cpetr2;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
PubMed=9878248; DOI=10.1006/geno.1998.5619;
Paperna T., Peoples R., Wang Y.K., Kaplan P., Francke U.;
"Genes for the CPE receptor (CPETR1) and the human homolog of RVP1
(CPETR2) are localized within the Williams-Beuren syndrome deletion.";
Genomics 54:453-459(1998).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), SUBCELLULAR LOCATION, AND
TISSUE SPECIFICITY.
TISSUE=Liver;
PubMed=9892664; DOI=10.1073/pnas.96.2.511;
Morita K., Furuse M., Fujimoto K., Tsukita S.;
"Claudin multigene family encoding four-transmembrane domain protein
components of tight junction strands.";
Proc. Natl. Acad. Sci. U.S.A. 96:511-516(1999).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
TISSUE=Colon;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[4]
FUNCTION.
PubMed=10508613; DOI=10.1016/S0960-9822(99)80452-7;
Kubota K., Furuse M., Sasaki H., Sonoda N., Fujita K., Nagafuchi A.,
Tsukita S.;
"Ca(2+)-independent cell-adhesion activity of claudins, a family of
integral membrane proteins localized at tight junctions.";
Curr. Biol. 9:1035-1038(1999).
[5]
INTERACTION WITH CLDN1 AND CLDN2.
PubMed=10562289; DOI=10.1083/jcb.147.4.891;
Furuse M., Sasaki H., Tsukita S.;
"Manner of interaction of heterogeneous claudin species within and
between tight junction strands.";
J. Cell Biol. 147:891-903(1999).
[6]
INTERACTION WITH TJP1; TJP2 AND TJP3.
PubMed=10601346; DOI=10.1083/jcb.147.6.1351;
Itoh M., Furuse M., Morita K., Kubota K., Saitou M., Tsukita S.;
"Direct binding of three tight junction-associated MAGUKs, ZO-1, ZO-2,
and ZO-3, with the COOH termini of claudins.";
J. Cell Biol. 147:1351-1363(1999).
[7]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-197, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=17242355; DOI=10.1073/pnas.0609836104;
Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
"Large-scale phosphorylation analysis of mouse liver.";
Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
[8]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver, and Pancreas;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and
expression.";
Cell 143:1174-1189(2010).
-!- FUNCTION: Plays a major role in tight junction-specific
obliteration of the intercellular space, through calcium-
independent cell-adhesion activity. {ECO:0000269|PubMed:10508613}.
-!- SUBUNIT: Can form homo- and heteropolymers with other CLDN.
Homopolymers interact with CLDN1 and CLDN2 homopolymers. Directly
interacts with TJP1/ZO-1, TJP2/ZO-2 and TJP3/ZO-3.
{ECO:0000269|PubMed:10562289, ECO:0000269|PubMed:10601346}.
-!- SUBCELLULAR LOCATION: Cell junction, tight junction
{ECO:0000269|PubMed:9892664}. Cell membrane
{ECO:0000269|PubMed:9892664}; Multi-pass membrane protein
{ECO:0000269|PubMed:9892664}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=Q9Z0G9-1; Sequence=Displayed;
Name=2;
IsoId=Q9Z0G9-2; Sequence=VSP_001101;
Note=No experimental confirmation available.;
-!- TISSUE SPECIFICITY: Expressed at high levels in liver and lung
and, at lower levels, in kidney and testis.
{ECO:0000269|PubMed:9892664}.
-!- SIMILARITY: Belongs to the claudin family. {ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; AF095905; AAD14608.1; -; mRNA.
EMBL; AF087821; AAD09756.1; -; mRNA.
EMBL; BC012650; AAH12650.1; -; mRNA.
CCDS; CCDS19729.1; -. [Q9Z0G9-1]
RefSeq; NP_034032.1; NM_009902.4. [Q9Z0G9-1]
UniGene; Mm.158662; -.
ProteinModelPortal; Q9Z0G9; -.
DIP; DIP-40779N; -.
IntAct; Q9Z0G9; 2.
MINT; MINT-113483; -.
STRING; 10090.ENSMUSP00000091799; -.
iPTMnet; Q9Z0G9; -.
PhosphoSitePlus; Q9Z0G9; -.
PaxDb; Q9Z0G9; -.
PRIDE; Q9Z0G9; -.
Ensembl; ENSMUST00000094245; ENSMUSP00000091799; ENSMUSG00000070473. [Q9Z0G9-1]
GeneID; 12739; -.
KEGG; mmu:12739; -.
UCSC; uc008zxe.2; mouse. [Q9Z0G9-1]
CTD; 1365; -.
MGI; MGI:1329044; Cldn3.
eggNOG; ENOG410IIJR; Eukaryota.
eggNOG; ENOG410YA61; LUCA.
GeneTree; ENSGT00760000118928; -.
HOGENOM; HOG000220937; -.
HOVERGEN; HBG000643; -.
InParanoid; Q9Z0G9; -.
KO; K06087; -.
OMA; LCTIVCC; -.
OrthoDB; EOG091G0MMR; -.
PhylomeDB; Q9Z0G9; -.
TreeFam; TF331936; -.
PRO; PR:Q9Z0G9; -.
Proteomes; UP000000589; Chromosome 5.
Bgee; ENSMUSG00000070473; -.
CleanEx; MM_CLDN3; -.
ExpressionAtlas; Q9Z0G9; baseline and differential.
Genevisible; Q9Z0G9; MM.
GO; GO:0016327; C:apicolateral plasma membrane; IDA:UniProtKB.
GO; GO:0005923; C:bicellular tight junction; IDA:UniProtKB.
GO; GO:0005737; C:cytoplasm; IEA:Ensembl.
GO; GO:0070062; C:extracellular exosome; ISO:MGI.
GO; GO:0016021; C:integral component of membrane; NAS:UniProtKB.
GO; GO:0016328; C:lateral plasma membrane; IDA:MGI.
GO; GO:0042802; F:identical protein binding; IPI:UniProtKB.
GO; GO:0005198; F:structural molecule activity; IEA:InterPro.
GO; GO:0070830; P:bicellular tight junction assembly; ISO:MGI.
GO; GO:0016338; P:calcium-independent cell-cell adhesion via plasma membrane cell-adhesion molecules; IDA:UniProtKB.
GO; GO:0003382; P:epithelial cell morphogenesis; IDA:UniProtKB.
GO; GO:0051291; P:protein heterooligomerization; ISO:MGI.
GO; GO:0051260; P:protein homooligomerization; ISO:MGI.
GO; GO:0045471; P:response to ethanol; IEA:Ensembl.
GO; GO:0001666; P:response to hypoxia; IEA:Ensembl.
InterPro; IPR006187; Claudin.
InterPro; IPR003549; Claudin3.
InterPro; IPR017974; Claudin_CS.
InterPro; IPR004031; PMP22/EMP/MP20/Claudin.
PANTHER; PTHR12002; PTHR12002; 1.
Pfam; PF00822; PMP22_Claudin; 1.
PRINTS; PR01378; CLAUDIN3.
PROSITE; PS01346; CLAUDIN; 1.
1: Evidence at protein level;
Alternative splicing; Cell junction; Cell membrane; Complete proteome;
Membrane; Phosphoprotein; Reference proteome; Tight junction;
Transmembrane; Transmembrane helix.
CHAIN 1 219 Claudin-3.
/FTId=PRO_0000144739.
TOPO_DOM 1 8 Cytoplasmic. {ECO:0000255}.
TRANSMEM 9 29 Helical. {ECO:0000255}.
TOPO_DOM 30 80 Extracellular. {ECO:0000255}.
TRANSMEM 81 101 Helical. {ECO:0000255}.
TOPO_DOM 102 115 Cytoplasmic. {ECO:0000255}.
TRANSMEM 116 136 Helical. {ECO:0000255}.
TOPO_DOM 137 159 Extracellular. {ECO:0000255}.
TRANSMEM 160 180 Helical. {ECO:0000255}.
TOPO_DOM 181 219 Cytoplasmic. {ECO:0000255}.
REGION 218 219 Interactions with TJP1, TJP2 and TJP3.
{ECO:0000250}.
MOD_RES 197 197 Phosphotyrosine.
{ECO:0000244|PubMed:17242355}.
MOD_RES 198 198 Phosphoserine.
{ECO:0000250|UniProtKB:Q63400}.
VAR_SEQ 72 91 Missing (in isoform 2).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_001101.
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


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