CLD18_BOVIN
ID CLD18_BOVIN Reviewed; 261 AA.
AC Q0VCN0;
DT 23-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT 05-SEP-2006, sequence version 1.
DT 03-AUG-2022, entry version 91.
DE RecName: Full=Claudin-18;
GN Name=CLDN18;
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 [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Fetal lung;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (AUG-2006) 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}.
CC -!- SUBCELLULAR LOCATION: Cell junction, tight junction
CC {ECO:0000250|UniProtKB:P56857}. Cell membrane
CC {ECO:0000250|UniProtKB:P56857}; Multi-pass membrane protein
CC {ECO:0000255}. Note=Localizes to tight junctions in epithelial cells.
CC {ECO:0000250|UniProtKB:P56857}.
CC -!- SIMILARITY: Belongs to the claudin family. {ECO:0000305}.
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DR EMBL; BC120090; AAI20091.1; -; mRNA.
DR RefSeq; NP_001068984.1; NM_001075516.1.
DR AlphaFoldDB; Q0VCN0; -.
DR SMR; Q0VCN0; -.
DR STRING; 9913.ENSBTAP00000019421; -.
DR PaxDb; Q0VCN0; -.
DR Ensembl; ENSBTAT00000019421; ENSBTAP00000019421; ENSBTAG00000014589.
DR GeneID; 511460; -.
DR KEGG; bta:511460; -.
DR CTD; 51208; -.
DR VEuPathDB; HostDB:ENSBTAG00000014589; -.
DR VGNC; VGNC:27408; CLDN18.
DR eggNOG; ENOG502QTRB; Eukaryota.
DR GeneTree; ENSGT00940000158655; -.
DR HOGENOM; CLU_076370_2_1_1; -.
DR InParanoid; Q0VCN0; -.
DR OMA; TICQVMG; -.
DR OrthoDB; 1079889at2759; -.
DR TreeFam; TF331936; -.
DR Proteomes; UP000009136; Chromosome 1.
DR Bgee; ENSBTAG00000014589; Expressed in abomasum and 13 other tissues.
DR GO; GO:0005923; C:bicellular tight junction; IBA:GO_Central.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0005198; F:structural molecule activity; IEA:InterPro.
DR GO; GO:0070830; P:bicellular tight junction assembly; IBA:GO_Central.
DR GO; GO:0007155; P:cell adhesion; IBA:GO_Central.
DR GO; GO:0048565; P:digestive tract development; IEA:Ensembl.
DR GO; GO:0045779; P:negative regulation of bone resorption; IEA:Ensembl.
DR GO; GO:2001205; P:negative regulation of osteoclast development; IEA:Ensembl.
DR GO; GO:1900181; P:negative regulation of protein localization to nucleus; IEA:Ensembl.
DR GO; GO:0034504; P:protein localization to nucleus; IEA:Ensembl.
DR GO; GO:0071847; P:TNFSF11-mediated signaling pathway; IEA:Ensembl.
DR InterPro; IPR006187; Claudin.
DR InterPro; IPR003928; Claudin18.
DR InterPro; IPR017974; Claudin_CS.
DR InterPro; IPR004031; PMP22/EMP/MP20/Claudin.
DR PANTHER; PTHR12002; PTHR12002; 1.
DR PANTHER; PTHR12002:SF9; PTHR12002:SF9; 1.
DR Pfam; PF00822; PMP22_Claudin; 1.
DR PRINTS; PR01448; CLAUDIN18.
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..261
FT /note="Claudin-18"
FT /id="PRO_0000273422"
FT TOPO_DOM 1..6
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 7..27
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 28..80
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 81..101
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 102..122
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 123..143
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 144..174
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 175..195
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 196..261
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 228..261
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 214
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P56857"
SQ SEQUENCE 261 AA; 28033 MW; FA28474341093DAD CRC64;
MSTTRCQVVG FLLSILGLAG CIVATEMDMW STQDLYDNPV TAVFQYEGLW RSCVQQSSGF
TECRPYLTIL GLPAMLQAVR ALMIVGIVLS VIGLLVAIFA LKCIRMGNMD DSAKAKMTLT
SGIMFIIAGL CAIAGVSVFA NMLVTNFWMS TASMFTSMGG MVQTVQTRYT FGAALFVGWV
AGGLTLIGGV LMCIACRGLA PEETNYKAVS YHASGHNVAY RPGGFKASSG FESNTRNKKI
YDGGARTEDE GQSPPSKYDY V