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Claudin-3 (Rat ventral prostate.1 protein) (RVP1)

 CLD3_RAT                Reviewed;         219 AA.
Q63400;
30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
30-MAY-2000, sequence version 2.
20-JUN-2018, entry version 104.
RecName: Full=Claudin-3;
AltName: Full=Rat ventral prostate.1 protein;
Short=RVP1;
Name=Cldn3;
Rattus norvegicus (Rat).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Rattus.
NCBI_TaxID=10116;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=1723140; DOI=10.1210/mend-5-10-1381;
Briehl M.M., Miesfeld R.L.;
"Isolation and characterization of transcripts induced by androgen
withdrawal and apoptotic cell death in the rat ventral prostate.";
Mol. Endocrinol. 5:1381-1388(1991).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Keen T.J., Inglehearn C.F.;
Submitted (SEP-1998) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Prostate;
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]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-197 AND SER-198, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22673903; DOI=10.1038/ncomms1871;
Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A.,
Lundby C., Olsen J.V.;
"Quantitative maps of protein phosphorylation sites across 14
different rat organs and tissues.";
Nat. Commun. 3:876-876(2012).
-!- FUNCTION: Plays a major role in tight junction-specific
obliteration of the intercellular space, through calcium-
independent cell-adhesion activity.
{ECO:0000250|UniProtKB:Q9Z0G9}.
-!- 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 (By similarity).
{ECO:0000250|UniProtKB:Q9Z0G9}.
-!- SUBCELLULAR LOCATION: Cell junction, tight junction
{ECO:0000250|UniProtKB:Q9Z0G9}. Cell membrane
{ECO:0000250|UniProtKB:Q9Z0G9}; Multi-pass membrane protein
{ECO:0000250|UniProtKB:Q9Z0G9}.
-!- SIMILARITY: Belongs to the claudin family. {ECO:0000305}.
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EMBL; M74067; AAA41760.1; -; mRNA.
EMBL; AJ011656; CAA09727.1; -; Genomic_DNA.
EMBL; BC062411; AAH62411.1; -; mRNA.
PIR; A39484; A39484.
RefSeq; NP_113888.2; NM_031700.2.
UniGene; Rn.4513; -.
STRING; 10116.ENSRNOP00000064411; -.
iPTMnet; Q63400; -.
PhosphoSitePlus; Q63400; -.
PaxDb; Q63400; -.
PRIDE; Q63400; -.
Ensembl; ENSRNOT00000075280; ENSRNOP00000064411; ENSRNOG00000046007.
GeneID; 65130; -.
KEGG; rno:65130; -.
CTD; 1365; -.
RGD; 68425; Cldn3.
eggNOG; ENOG410IIJR; Eukaryota.
eggNOG; ENOG410YA61; LUCA.
GeneTree; ENSGT00760000118928; -.
HOVERGEN; HBG000643; -.
InParanoid; Q63400; -.
KO; K06087; -.
OMA; LCTIVCC; -.
OrthoDB; EOG091G0MMR; -.
PhylomeDB; Q63400; -.
PRO; PR:Q63400; -.
Proteomes; UP000002494; Chromosome 12.
Bgee; ENSRNOG00000046007; -.
Genevisible; Q63400; RN.
GO; GO:0016327; C:apicolateral plasma membrane; IEA:Ensembl.
GO; GO:0005923; C:bicellular tight junction; IDA:RGD.
GO; GO:0005737; C:cytoplasm; IDA:RGD.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0016328; C:lateral plasma membrane; IDA:RGD.
GO; GO:0042802; F:identical protein binding; ISS:UniProtKB.
GO; GO:0005198; F:structural molecule activity; IEA:InterPro.
GO; GO:0070830; P:bicellular tight junction assembly; IEA:Ensembl.
GO; GO:0016338; P:calcium-independent cell-cell adhesion via plasma membrane cell-adhesion molecules; ISS:UniProtKB.
GO; GO:0003382; P:epithelial cell morphogenesis; ISS:UniProtKB.
GO; GO:0051291; P:protein heterooligomerization; IEA:Ensembl.
GO; GO:0051260; P:protein homooligomerization; IEA:Ensembl.
GO; GO:0045471; P:response to ethanol; IEP:RGD.
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;
Cell junction; Cell membrane; Complete proteome; Membrane;
Phosphoprotein; Reference proteome; Tight junction; Transmembrane;
Transmembrane helix.
CHAIN 1 219 Claudin-3.
/FTId=PRO_0000144740.
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 137 161 Extracellular. {ECO:0000255}.
TRANSMEM 162 182 Helical. {ECO:0000255}.
TOPO_DOM 183 219 Cytoplasmic. {ECO:0000255}.
REGION 218 219 Interactions with TJP1, TJP2 and TJP3.
{ECO:0000250}.
MOD_RES 197 197 Phosphotyrosine.
{ECO:0000244|PubMed:22673903}.
MOD_RES 198 198 Phosphoserine.
{ECO:0000244|PubMed:22673903}.
CONFLICT 4 4 G -> S (in Ref. 1; AAA41760).
{ECO:0000305}.
CONFLICT 55 55 Missing (in Ref. 1; AAA41760).
{ECO:0000305}.
CONFLICT 217 219 DYV -> TTSERPGARTPHHHHYQPSMYPTRPACSLASETT
PPSRRLQTPRSLLARLEEDRQPGVPFSPVAT (in Ref.
1). {ECO:0000305}.
SEQUENCE 219 AA; 23315 MW; 820CC6BFC20D122D CRC64;
MSMGLEITGT SLAVLGWLCT IVCCALPMWR VSAFIGSSII TAQITWEGLW MNCVVQSTGQ
MQCKMYDSLL ALPQDLQAAR ALIVVSILLA AFGLLVALVG AQCTNCVQDE TAKAKITIVA
GVLFLLAAVL TLVPVSWSAN TIIRDFYNPL VPEAQKREMG TGLYVGWAAA ALQLLGGALL
CCSCPPREKY APTKILYSAP RSTGPGTGTG TAYDRKDYV


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