CLD3_RAT
ID CLD3_RAT Reviewed; 219 AA.
AC Q63400;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 30-MAY-2000, sequence version 2.
DT 03-AUG-2022, entry version 119.
DE RecName: Full=Claudin-3;
DE AltName: Full=Rat ventral prostate.1 protein;
DE Short=RVP1;
GN Name=Cldn3;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=1723140; DOI=10.1210/mend-5-10-1381;
RA Briehl M.M., Miesfeld R.L.;
RT "Isolation and characterization of transcripts induced by androgen
RT withdrawal and apoptotic cell death in the rat ventral prostate.";
RL Mol. Endocrinol. 5:1381-1388(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Keen T.J., Inglehearn C.F.;
RL Submitted (SEP-1998) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Prostate;
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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-197 AND SER-198, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
CC -!- FUNCTION: Plays a major role in tight junction-specific obliteration of
CC the intercellular space, through calcium-independent cell-adhesion
CC activity. {ECO:0000250|UniProtKB:Q9Z0G9}.
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 (By similarity).
CC {ECO:0000250|UniProtKB:Q9Z0G9}.
CC -!- SUBCELLULAR LOCATION: Cell junction, tight junction
CC {ECO:0000250|UniProtKB:Q9Z0G9}. Cell membrane
CC {ECO:0000250|UniProtKB:Q9Z0G9}; Multi-pass membrane protein
CC {ECO:0000250|UniProtKB:Q9Z0G9}.
CC -!- SIMILARITY: Belongs to the claudin family. {ECO:0000305}.
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DR EMBL; M74067; AAA41760.1; -; mRNA.
DR EMBL; AJ011656; CAA09727.1; -; Genomic_DNA.
DR EMBL; BC062411; AAH62411.1; -; mRNA.
DR PIR; A39484; A39484.
DR RefSeq; NP_113888.2; NM_031700.2.
DR AlphaFoldDB; Q63400; -.
DR SMR; Q63400; -.
DR STRING; 10116.ENSRNOP00000064411; -.
DR iPTMnet; Q63400; -.
DR PhosphoSitePlus; Q63400; -.
DR PaxDb; Q63400; -.
DR Ensembl; ENSRNOT00000075280; ENSRNOP00000064411; ENSRNOG00000046007.
DR GeneID; 65130; -.
DR KEGG; rno:65130; -.
DR CTD; 1365; -.
DR RGD; 68425; Cldn3.
DR eggNOG; ENOG502QRZ8; Eukaryota.
DR GeneTree; ENSGT00940000162095; -.
DR HOGENOM; CLU_076370_1_2_1; -.
DR InParanoid; Q63400; -.
DR OMA; LCSIICC; -.
DR OrthoDB; 1231389at2759; -.
DR PhylomeDB; Q63400; -.
DR PRO; PR:Q63400; -.
DR Proteomes; UP000002494; Chromosome 12.
DR Bgee; ENSRNOG00000046007; Expressed in jejunum and 14 other tissues.
DR Genevisible; Q63400; RN.
DR GO; GO:0043296; C:apical junction complex; ISO:RGD.
DR GO; GO:0016327; C:apicolateral plasma membrane; ISO:RGD.
DR GO; GO:0005923; C:bicellular tight junction; IDA:RGD.
DR GO; GO:0005911; C:cell-cell junction; ISO:RGD.
DR GO; GO:0005737; C:cytoplasm; IDA:RGD.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0016328; C:lateral plasma membrane; IDA:RGD.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0032991; C:protein-containing complex; ISO:RGD.
DR GO; GO:0070160; C:tight junction; ISO:RGD.
DR GO; GO:0042802; F:identical protein binding; ISS:UniProtKB.
DR GO; GO:0005198; F:structural molecule activity; IEA:InterPro.
DR GO; GO:0031532; P:actin cytoskeleton reorganization; ISO:RGD.
DR GO; GO:0070830; P:bicellular tight junction assembly; ISO:RGD.
DR GO; GO:0016338; P:calcium-independent cell-cell adhesion via plasma membrane cell-adhesion molecules; ISS:UniProtKB.
DR GO; GO:0007155; P:cell adhesion; IBA:GO_Central.
DR GO; GO:0034331; P:cell junction maintenance; ISO:RGD.
DR GO; GO:0003382; P:epithelial cell morphogenesis; ISS:UniProtKB.
DR GO; GO:0014045; P:establishment of endothelial blood-brain barrier; ISO:RGD.
DR GO; GO:0030336; P:negative regulation of cell migration; ISO:RGD.
DR GO; GO:0008285; P:negative regulation of cell population proliferation; ISO:RGD.
DR GO; GO:0010629; P:negative regulation of gene expression; ISO:RGD.
DR GO; GO:0061045; P:negative regulation of wound healing; ISO:RGD.
DR GO; GO:1903348; P:positive regulation of bicellular tight junction assembly; ISO:RGD.
DR GO; GO:1901890; P:positive regulation of cell junction assembly; ISO:RGD.
DR GO; GO:0030335; P:positive regulation of cell migration; ISO:RGD.
DR GO; GO:0010628; P:positive regulation of gene expression; ISO:RGD.
DR GO; GO:1905050; P:positive regulation of metallopeptidase activity; ISO:RGD.
DR GO; GO:0001934; P:positive regulation of protein phosphorylation; ISO:RGD.
DR GO; GO:0090303; P:positive regulation of wound healing; ISO:RGD.
DR GO; GO:0022604; P:regulation of cell morphogenesis; ISO:RGD.
DR GO; GO:0090559; P:regulation of membrane permeability; ISO:RGD.
DR GO; GO:0150111; P:regulation of transepithelial transport; ISO:RGD.
DR GO; GO:0045471; P:response to ethanol; IEP:RGD.
DR GO; GO:0140459; P:response to Gram-positive bacterium; IEP:RGD.
DR GO; GO:0001666; P:response to hypoxia; ISO:RGD.
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 Cell junction; Cell membrane; Membrane; Phosphoprotein; Reference proteome;
KW Tight junction; Transmembrane; Transmembrane helix.
FT CHAIN 1..219
FT /note="Claudin-3"
FT /id="PRO_0000144740"
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..161
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 162..182
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 183..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:22673903"
FT MOD_RES 198
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT CONFLICT 4
FT /note="G -> S (in Ref. 1; AAA41760)"
FT /evidence="ECO:0000305"
FT CONFLICT 55
FT /note="Missing (in Ref. 1; AAA41760)"
FT /evidence="ECO:0000305"
FT CONFLICT 217..219
FT /note="DYV -> TTSERPGARTPHHHHYQPSMYPTRPACSLASETTPPSRRLQTPRS
FT LLARLEEDRQPGVPFSPVAT (in Ref. 1)"
FT /evidence="ECO:0000305"
SQ 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
