CLDN4
entrez
1364
canonical
uniprot
O14493
canonical
ensembl
ENSG00000189143
resolver
ensp
ENSP00000342445
resolver
ensp
ENSP00000388639
resolver
ensp
ENSP00000409544
resolver
enst
ENST00000340958
resolver
enst
ENST00000431918
resolver
enst
ENST00000435050
resolver
genesymbol
CLDN4
resolver
genesymbol_syn
CPER
resolver
genesymbol_syn
CPETR1
resolver
genesymbol_syn
WBSCR8
resolver
hgnc
HGNC:2046
resolver
uniprot
Q75L80
resolver
uniprot_entry
CLD4_HUMAN
resolver
uniprot_entry
Q75L80_HUMAN
resolver
amino_acid_sequence
MASMGLQVMGIALAVLGWLAVMLCCALPMWRVTAFIGSNIVTSQTIWEGLWMNCVVQSTGQMQCKVYDSLLALPQDLQAARALVIISIIVAALGVLLSVVGGKCTNCLEDESAKAKTMIVAGVVFLLAGLMVIVPVSWTAHNIIQDFYNPLVASGQKREMGASLYVGWAASGLLLLGGGLLCCNCPPRTDKPYSAKYSAARSAAASNYV
uniprot
proteins
disease_involvement
DISEASE: Note=CLDN4 is located in the Williams-Beuren syndrome (WBS) critical region. WBS results from a hemizygous deletion of several genes on chromosome 7q11.23, thought to arise as a consequence of unequal crossing over between highly homologous low-copy repeat sequences flanking the deleted region.
uniprot
proteins
function
FUNCTION: Can associate with other claudins to regulate tight junction structural and functional strand dynamics (PubMed:35773259, PubMed:36008380). May coassemble with CLDN8 into tight junction strands containing anion-selective channels that convey paracellular chloride permeability in renal collecting ducts (By similarity) (PubMed:36008380). May integrate into CLDN3 strands to modulate localized tight junction barrier properties (PubMed:35773259, PubMed:36008380). May disrupt strand assembly of channel-forming CLDN2 and CLDN15 and inhibit cation conductance (PubMed:35773259, PubMed:36008380). Cannot form tight junction strands on its own (PubMed:35773259, PubMed:36008380). {ECO:0000250|UniProtKB:O35054, ECO:0000269|PubMed:35773259, ECO:0000269|PubMed:36008380}.
uniprot
proteins
mass_dalton
22077
uniprot
proteins
mutagenesis
MUTAGEN 35; /note="F->A: Decreases interaction with Clostridium perfringens CPE."; /evidence="ECO:0000269|PubMed:27647526"; MUTAGEN 35; /note="F->D: Abolishes interaction with Clostridium perfringens CPE."; /evidence="ECO:0000269|PubMed:27647526"; MUTAGEN 40; /note="I->A: No effect on interaction with Clostridium perfringens CPE."; /evidence="ECO:0000269|PubMed:27647526"; MUTAGEN 40; /note="I->D: Strongly decreases interaction with Clostridium perfringens CPE."; /evidence="ECO:0000269|PubMed:27647526"; MUTAGEN 53; /note="N->A,D: Decreases interaction with Clostridium perfringens CPE."; /evidence="ECO:0000269|PubMed:27647526"; MUTAGEN 208; /note="Y->F: Loss of phosphorylation by EPHA2."; /evidence="ECO:0000269|PubMed:16236711
uniprot
proteins
post_translational_modification
PTM: Phosphorylated. Phosphorylation by EPHA2 is stimulated by EFNA1 and alters interaction with TJP1. {ECO:0000269|PubMed:16236711}.
uniprot
proteins
protein_family
Claudin family
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
16236711
uniprot
proteins
pubmed
20375010
uniprot
proteins
pubmed
21269460
uniprot
proteins
pubmed
24787463
uniprot
proteins
pubmed
27647526
uniprot
proteins
pubmed
30734065
uniprot
proteins
pubmed
35773259
uniprot
proteins
pubmed
36008380
uniprot
proteins
pubmed
9334247
uniprot
proteins
sequence_length
209
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cell junction, tight junction {ECO:0000269|PubMed:30734065}. Cell membrane {ECO:0000269|PubMed:20375010}; Multi-pass membrane protein {ECO:0000255}.
uniprot
proteins
transmembrane_region
TRANSMEM 8..28; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 82..102; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 118..138; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 161..181; /note="Helical"; /evidence="ECO:0000255
uniprot
proteins