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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
 
 
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