CLD3_BOVIN
ID CLD3_BOVIN Reviewed; 219 AA.
AC Q765N9; Q3T0H1;
DT 29-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 110.
DE RecName: Full=Claudin-3;
GN Name=CLDN3;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Duodenum;
RA Ohta H., Takiguchi M., Inaba M.;
RT "Localization of claudin proteins in bovine duodenum.";
RL Submitted (JUL-2003) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Crossbred X Angus; TISSUE=Ileum;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases.
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; AB115781; BAD01113.1; -; mRNA.
DR EMBL; BC102398; AAI02399.1; -; mRNA.
DR RefSeq; NP_991370.1; NM_205801.2.
DR AlphaFoldDB; Q765N9; -.
DR SMR; Q765N9; -.
DR STRING; 9913.ENSBTAP00000001810; -.
DR PaxDb; Q765N9; -.
DR Ensembl; ENSBTAT00000001810; ENSBTAP00000001810; ENSBTAG00000040432.
DR GeneID; 404153; -.
DR KEGG; bta:404153; -.
DR CTD; 1365; -.
DR VEuPathDB; HostDB:ENSBTAG00000040432; -.
DR VGNC; VGNC:27414; CLDN3.
DR eggNOG; ENOG502QRZ8; Eukaryota.
DR GeneTree; ENSGT00940000162095; -.
DR HOGENOM; CLU_076370_1_2_1; -.
DR InParanoid; Q765N9; -.
DR OMA; LCSIICC; -.
DR OrthoDB; 1231389at2759; -.
DR TreeFam; TF331936; -.
DR Proteomes; UP000009136; Chromosome 25.
DR Bgee; ENSBTAG00000040432; Expressed in saliva-secreting gland and 86 other tissues.
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; IEA:Ensembl.
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; IEA:Ensembl.
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..219
FT /note="Claudin-3"
FT /id="PRO_0000144736"
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..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:0000250|UniProtKB:Q9Z0G9"
FT MOD_RES 198
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q63400"
FT MOD_RES 208
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O15551"
SQ SEQUENCE 219 AA; 23382 MW; 887D970A83AD19E0 CRC64;
MSMGLEIAGT SLAVLGWLCT IVCCALPMWR VTAFIGSSII TAQITWEGLW MNCVVQSTGQ
MQCKVYDSLL ALPQDLQAAR ALIVIAILLA VFGLLVALVG AQCTNCVQDD TAKAKITIVA
GVLFLLAALL TLVPVSWSAN TIIRDFYNPL VPEAQKREMG AALYVGWAAS ALQLLGGALL
CCSCPPRDNY ARTKIVYSAP RSTGPVTSTG TAYDRKDYV
