CLD3_CANLF
ID CLD3_CANLF Reviewed; 218 AA.
AC Q95KM5;
DT 23-JAN-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 110.
DE RecName: Full=Claudin-3;
GN Name=CLDN3;
OS Canis lupus familiaris (Dog) (Canis familiaris).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Canidae; Canis.
OX NCBI_TaxID=9615;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Liver;
RX PubMed=11309408; DOI=10.1083/jcb.153.2.263;
RA Furuse M., Furuse K., Sasaki H., Tsukita S.;
RT "Conversion of zonulae occludentes from tight to leaky strand type by
RT introducing claudin-2 into Madin-Darby canine kidney I cells.";
RL J. Cell Biol. 153:263-272(2001).
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; AF358908; AAK51434.1; -; mRNA.
DR RefSeq; NP_001003088.1; NM_001003088.1.
DR AlphaFoldDB; Q95KM5; -.
DR SMR; Q95KM5; -.
DR STRING; 9612.ENSCAFP00000018448; -.
DR PaxDb; Q95KM5; -.
DR Ensembl; ENSCAFT00000095044; ENSCAFP00000067609; ENSCAFG00000054920.
DR Ensembl; ENSCAFT00040019610; ENSCAFP00040017024; ENSCAFG00040010589.
DR Ensembl; ENSCAFT00845005651; ENSCAFP00845004483; ENSCAFG00845003145.
DR GeneID; 403648; -.
DR KEGG; cfa:403648; -.
DR CTD; 1365; -.
DR VEuPathDB; HostDB:ENSCAFG00845003145; -.
DR eggNOG; ENOG502QRZ8; Eukaryota.
DR GeneTree; ENSGT00940000162095; -.
DR HOGENOM; CLU_076370_1_2_1; -.
DR InParanoid; Q95KM5; -.
DR OMA; LCSIICC; -.
DR OrthoDB; 1231389at2759; -.
DR TreeFam; TF331936; -.
DR Proteomes; UP000002254; Chromosome 6.
DR GO; GO:0016327; C:apicolateral plasma membrane; IEA:Ensembl.
DR GO; GO:0005923; C:bicellular tight junction; ISS:UniProtKB.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0016328; C:lateral plasma membrane; IEA:Ensembl.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0032991; C:protein-containing complex; IEA:Ensembl.
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; IEA:Ensembl.
DR GO; GO:0070830; P:bicellular tight junction assembly; IBA:GO_Central.
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; IEA:Ensembl.
DR GO; GO:0003382; P:epithelial cell morphogenesis; ISS:UniProtKB.
DR GO; GO:0014045; P:establishment of endothelial blood-brain barrier; IEA:Ensembl.
DR GO; GO:0030336; P:negative regulation of cell migration; IEA:Ensembl.
DR GO; GO:0008285; P:negative regulation of cell population proliferation; IEA:Ensembl.
DR GO; GO:0010629; P:negative regulation of gene expression; IEA:Ensembl.
DR GO; GO:0061045; P:negative regulation of wound healing; IEA:Ensembl.
DR GO; GO:1903348; P:positive regulation of bicellular tight junction assembly; IEA:Ensembl.
DR GO; GO:0030335; P:positive regulation of cell migration; IEA:Ensembl.
DR GO; GO:0010628; P:positive regulation of gene expression; IEA:Ensembl.
DR GO; GO:1905050; P:positive regulation of metallopeptidase activity; IEA:Ensembl.
DR GO; GO:0001934; P:positive regulation of protein phosphorylation; IEA:Ensembl.
DR GO; GO:0090303; P:positive regulation of wound healing; IEA:Ensembl.
DR GO; GO:0022604; P:regulation of cell morphogenesis; IEA:Ensembl.
DR GO; GO:0090559; P:regulation of membrane permeability; IEA:Ensembl.
DR GO; GO:0150111; P:regulation of transepithelial transport; IEA:Ensembl.
DR GO; GO:0001666; P:response to hypoxia; IEA:Ensembl.
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 2: Evidence at transcript level;
KW Cell junction; Cell membrane; Membrane; Phosphoprotein; Reference proteome;
KW Tight junction; Transmembrane; Transmembrane helix.
FT CHAIN 1..218
FT /note="Claudin-3"
FT /id="PRO_0000144737"
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..218
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 217..218
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:0000250|UniProtKB:O15551"
SQ SEQUENCE 218 AA; 23148 MW; 907104E36F50DA70 CRC64;
MSMGLEIAGT SLAVLGWLST IVCCALPMWR VTAFIGSSII TAQITWEGLW MNCVVQSTGQ
MQCKVYDSLL ALPQDLQAAR ALIVVSILLA AFGLLVALVG AQCTNCVQDD TAKAKITIVA
GVLFLLAALL TLVPVSWSAN TIIRDFYNPL VPDAQKREMG AGLYVGWAAA ALQLLGGALL
CCSCPPRDKK YAPTKIVYSA PRSAGPGTST AYDRKDYV
