ID   CLD3_HUMAN              Reviewed;         220 AA.
AC   O15551;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1998, sequence version 1.
DT   24-JAN-2024, entry version 182.
DE   RecName: Full=Claudin-3;
DE   AltName: Full=Clostridium perfringens enterotoxin receptor 2;
DE            Short=CPE-R 2;
DE            Short=CPE-receptor 2;
DE   AltName: Full=Rat ventral prostate.1 protein homolog;
DE            Short=hRVP1;
GN   Name=CLDN3; Synonyms=C7orf1, CPETR2;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=9441748; DOI=10.1006/geno.1997.5033;
RA   Peacock R.E., Keen T.J., Inglehearn C.F.;
RT   "Analysis of a human gene homologous to rat ventral prostate.1 protein.";
RL   Genomics 46:443-449(1997).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=9334247; DOI=10.1074/jbc.272.42.26652;
RA   Katahira J., Sugiyama H., Inoue N., Horiguchi Y., Matsuda M., Sugimoto N.;
RT   "Clostridium perfringens enterotoxin utilizes two structurally related
RT   membrane proteins as functional receptors in vivo.";
RL   J. Biol. Chem. 272:26652-26658(1997).
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   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-209, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Liver;
RX   PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA   Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA   Ye M., Zou H.;
RT   "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT   phosphoproteome.";
RL   J. Proteomics 96:253-262(2014).
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   -!- DISEASE: Note=CLDN3 is located in the Williams-Beuren syndrome (WBS)
CC       critical region. WBS results from a hemizygous deletion of several
CC       genes on chromosome 7q11.23, thought to arise as a consequence of
CC       unequal crossing over between highly homologous low-copy repeat
CC       sequences flanking the deleted region.
CC   -!- SIMILARITY: Belongs to the claudin family. {ECO:0000305}.
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DR   EMBL; AF007189; AAC78277.1; -; Genomic_DNA.
DR   EMBL; AB000714; BAA22986.1; -; mRNA.
DR   EMBL; BC016056; AAH16056.1; -; mRNA.
DR   CCDS; CCDS5559.1; -.
DR   RefSeq; NP_001297.1; NM_001306.3.
DR   AlphaFoldDB; O15551; -.
DR   SMR; O15551; -.
DR   BioGRID; 107757; 23.
DR   DIP; DIP-61079N; -.
DR   IntAct; O15551; 3.
DR   STRING; 9606.ENSP00000378577; -.
DR   TCDB; 1.H.1.1.15; the claudin tight junction (claudin1) family.
DR   iPTMnet; O15551; -.
DR   PhosphoSitePlus; O15551; -.
DR   SwissPalm; O15551; -.
DR   BioMuta; CLDN3; -.
DR   EPD; O15551; -.
DR   jPOST; O15551; -.
DR   MassIVE; O15551; -.
DR   PaxDb; 9606-ENSP00000378577; -.
DR   PeptideAtlas; O15551; -.
DR   ProteomicsDB; 48753; -.
DR   Pumba; O15551; -.
DR   ABCD; O15551; 6 sequenced antibodies.
DR   Antibodypedia; 3638; 662 antibodies from 39 providers.
DR   DNASU; 1365; -.
DR   Ensembl; ENST00000395145.3; ENSP00000378577.2; ENSG00000165215.6.
DR   GeneID; 1365; -.
DR   KEGG; hsa:1365; -.
DR   MANE-Select; ENST00000395145.3; ENSP00000378577.2; NM_001306.4; NP_001297.1.
DR   AGR; HGNC:2045; -.
DR   CTD; 1365; -.
DR   DisGeNET; 1365; -.
DR   GeneCards; CLDN3; -.
DR   HGNC; HGNC:2045; CLDN3.
DR   HPA; ENSG00000165215; Tissue enhanced (intestine, thyroid gland).
DR   MIM; 602910; gene.
DR   neXtProt; NX_O15551; -.
DR   OpenTargets; ENSG00000165215; -.
DR   PharmGKB; PA26571; -.
DR   VEuPathDB; HostDB:ENSG00000165215; -.
DR   eggNOG; ENOG502QRZ8; Eukaryota.
DR   GeneTree; ENSGT00940000162095; -.
DR   HOGENOM; CLU_076370_1_2_1; -.
DR   InParanoid; O15551; -.
DR   OMA; LCSIICC; -.
DR   OrthoDB; 4040914at2759; -.
DR   PhylomeDB; O15551; -.
DR   TreeFam; TF331936; -.
DR   PathwayCommons; O15551; -.
DR   Reactome; R-HSA-420029; Tight junction interactions.
DR   SignaLink; O15551; -.
DR   SIGNOR; O15551; -.
DR   BioGRID-ORCS; 1365; 15 hits in 1141 CRISPR screens.
DR   GeneWiki; CLDN3; -.
DR   GenomeRNAi; 1365; -.
DR   Pharos; O15551; Tbio.
DR   PRO; PR:O15551; -.
DR   Proteomes; UP000005640; Chromosome 7.
DR   RNAct; O15551; Protein.
DR   Bgee; ENSG00000165215; Expressed in mucosa of transverse colon and 135 other cell types or tissues.
DR   ExpressionAtlas; O15551; baseline and differential.
DR   GO; GO:0043296; C:apical junction complex; IMP:ARUK-UCL.
DR   GO; GO:0016327; C:apicolateral plasma membrane; IEA:Ensembl.
DR   GO; GO:0005923; C:bicellular tight junction; IDA:UniProtKB.
DR   GO; GO:0005911; C:cell-cell junction; IDA:ARUK-UCL.
DR   GO; GO:0016328; C:lateral plasma membrane; IEA:Ensembl.
DR   GO; GO:0016020; C:membrane; TAS:ProtInc.
DR   GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR   GO; GO:0032991; C:protein-containing complex; IDA:UniProtKB.
DR   GO; GO:0070160; C:tight junction; IDA:ARUK-UCL.
DR   GO; GO:0042802; F:identical protein binding; IPI:UniProtKB.
DR   GO; GO:0005198; F:structural molecule activity; IEA:InterPro.
DR   GO; GO:0004888; F:transmembrane signaling receptor activity; TAS:ProtInc.
DR   GO; GO:0030036; P:actin cytoskeleton organization; IMP:ARUK-UCL.
DR   GO; GO:0070830; P:bicellular tight junction assembly; IMP:UniProtKB.
DR   GO; GO:0016338; P:calcium-independent cell-cell adhesion via plasma membrane cell-adhesion molecules; IEA:Ensembl.
DR   GO; GO:0007155; P:cell adhesion; IBA:GO_Central.
DR   GO; GO:0034331; P:cell junction maintenance; ISS:ARUK-UCL.
DR   GO; GO:0003382; P:epithelial cell morphogenesis; ISS:UniProtKB.
DR   GO; GO:0014045; P:establishment of endothelial blood-brain barrier; ISS:ARUK-UCL.
DR   GO; GO:0035633; P:maintenance of blood-brain barrier; NAS:ARUK-UCL.
DR   GO; GO:0030336; P:negative regulation of cell migration; IMP:ARUK-UCL.
DR   GO; GO:0008285; P:negative regulation of cell population proliferation; IMP:ARUK-UCL.
DR   GO; GO:0010629; P:negative regulation of gene expression; IMP:ARUK-UCL.
DR   GO; GO:0061045; P:negative regulation of wound healing; IMP:ARUK-UCL.
DR   GO; GO:1903348; P:positive regulation of bicellular tight junction assembly; IMP:ARUK-UCL.
DR   GO; GO:1901890; P:positive regulation of cell junction assembly; IMP:ARUK-UCL.
DR   GO; GO:0030335; P:positive regulation of cell migration; IMP:ARUK-UCL.
DR   GO; GO:0010628; P:positive regulation of gene expression; IMP:ARUK-UCL.
DR   GO; GO:1905050; P:positive regulation of metallopeptidase activity; IMP:ARUK-UCL.
DR   GO; GO:0001934; P:positive regulation of protein phosphorylation; IMP:ARUK-UCL.
DR   GO; GO:0090303; P:positive regulation of wound healing; IMP:ARUK-UCL.
DR   GO; GO:0022604; P:regulation of cell morphogenesis; IMP:ARUK-UCL.
DR   GO; GO:0090559; P:regulation of membrane permeability; IMP:ARUK-UCL.
DR   GO; GO:0150111; P:regulation of transepithelial transport; IMP:ARUK-UCL.
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; IEP:UniProtKB.
DR   Gene3D; 1.20.140.150; -; 1.
DR   InterPro; IPR006187; Claudin.
DR   InterPro; IPR003549; Claudin3.
DR   InterPro; IPR017974; Claudin_CS.
DR   InterPro; IPR004031; PMP22/EMP/MP20/Claudin.
DR   PANTHER; PTHR12002; CLAUDIN; 1.
DR   PANTHER; PTHR12002:SF112; CLAUDIN-3; 1.
DR   Pfam; PF00822; PMP22_Claudin; 1.
DR   PRINTS; PR01077; CLAUDIN.
DR   PRINTS; PR01378; CLAUDIN3.
DR   PROSITE; PS01346; CLAUDIN; 1.
DR   Genevisible; O15551; HS.
PE   1: Evidence at protein level;
KW   Cell junction; Cell membrane; Membrane; Phosphoprotein; Reference proteome;
KW   Tight junction; Transmembrane; Transmembrane helix;
KW   Williams-Beuren syndrome.
FT   CHAIN           1..220
FT                   /note="Claudin-3"
FT                   /id="PRO_0000144738"
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..220
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   REGION          219..220
FT                   /note="Interactions with TJP1, TJP2 and TJP3"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         198
FT                   /note="Phosphotyrosine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9Z0G9"
FT   MOD_RES         199
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q63400"
FT   MOD_RES         209
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:24275569"
SQ   SEQUENCE   220 AA;  23319 MW;  1C826EFFF1563C56 CRC64;
     MSMGLEITGT ALAVLGWLGT IVCCALPMWR VSAFIGSNII TSQNIWEGLW MNCVVQSTGQ
     MQCKVYDSLL ALPQDLQAAR ALIVVAILLA AFGLLVALVG AQCTNCVQDD TAKAKITIVA
     GVLFLLAALL TLVPVSWSAN TIIRDFYNPV VPEAQKREMG AGLYVGWAAA ALQLLGGALL
     CCSCPPREKK YTATKVVYSA PRSTGPGASL GTGYDRKDYV
//