CLD16_RAT
ID CLD16_RAT Reviewed; 235 AA.
AC Q91Y55;
DT 10-MAY-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 25-MAY-2022, entry version 92.
DE RecName: Full=Claudin-16;
DE AltName: Full=Paracellin-1;
GN Name=Cldn16;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Sprague-Dawley; TISSUE=Kidney;
RX PubMed=11729235; DOI=10.1681/asn.v12122664;
RA Weber S., Schlingmann K.P., Peters M., Nejsum L.N., Nielsen S., Engel H.,
RA Grzeschik K.H., Seyberth H.W., Grone H.J., Nusing R., Konrad M.;
RT "Primary gene structure and expression studies of rodent paracellin-1.";
RL J. Am. Soc. Nephrol. 12:2664-2672(2001).
CC -!- FUNCTION: Plays a major role in tight junction-specific obliteration of
CC the intercellular space, through calcium-independent cell-adhesion
CC activity. Involved in paracellular magnesium reabsorption. Required for
CC a selective paracellular conductance. May form, alone or in partnership
CC with other constituents, an intercellular pore permitting paracellular
CC passage of magnesium and calcium ions down their electrochemical
CC gradients. Alternatively, it could be a sensor of magnesium
CC concentration that could alter paracellular permeability mediated by
CC other factors (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cell junction, tight junction. Cell membrane;
CC Multi-pass membrane protein.
CC -!- SIMILARITY: Belongs to the claudin family. {ECO:0000305}.
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DR EMBL; AF333099; AAK52459.1; -; mRNA.
DR AlphaFoldDB; Q91Y55; -.
DR SMR; Q91Y55; -.
DR BioGRID; 250891; 1.
DR STRING; 10116.ENSRNOP00000044832; -.
DR iPTMnet; Q91Y55; -.
DR PhosphoSitePlus; Q91Y55; -.
DR PaxDb; Q91Y55; -.
DR UCSC; RGD:620322; rat.
DR RGD; 620322; Cldn16.
DR eggNOG; ENOG502QRY9; Eukaryota.
DR InParanoid; Q91Y55; -.
DR PhylomeDB; Q91Y55; -.
DR PRO; PR:Q91Y55; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0005923; C:bicellular tight junction; IDA:RGD.
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:0042802; F:identical protein binding; ISS:UniProtKB.
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: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:0006811; P:ion transport; IEA:UniProtKB-KW.
DR GO; GO:0051928; P:positive regulation of calcium ion transport; IDA:RGD.
DR GO; GO:0070633; P:transepithelial transport; IDA:RGD.
DR InterPro; IPR006187; Claudin.
DR InterPro; IPR003927; Claudin16.
DR InterPro; IPR017974; Claudin_CS.
DR InterPro; IPR004031; PMP22/EMP/MP20/Claudin.
DR PANTHER; PTHR12002; PTHR12002; 1.
DR PANTHER; PTHR12002:SF56; PTHR12002:SF56; 1.
DR Pfam; PF00822; PMP22_Claudin; 1.
DR PRINTS; PR01447; CLAUDIN16.
DR PROSITE; PS01346; CLAUDIN; 1.
PE 2: Evidence at transcript level;
KW Cell junction; Cell membrane; Ion transport; Magnesium; Membrane;
KW Reference proteome; Tight junction; Transmembrane; Transmembrane helix;
KW Transport.
FT CHAIN 1..235
FT /note="Claudin-16"
FT /id="PRO_0000144776"
FT TOPO_DOM 1..3
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 4..24
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 25..79
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 80..100
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 101..115
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 116..136
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 137..169
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 170..190
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 191..235
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
SQ SEQUENCE 235 AA; 26091 MW; 357E658C317050C2 CRC64;
MKDLLQYAAC FLAIFSTGFL IVATRTDCWM VNADDSLEVS TKCRGLWWEC VTNAFDGIRT
CDEYDSIYAE HPLKLVVTRA LMITADILAG FGFITLLLGL DCVKFLPDEP HIKVRLCFVA
GTVLLIAGTP GIIGSVWYAV DVYVERSSLV LHNIFLGIQY KFGWSCWLGM AGSLGCFLAG
ALLTCCLYLF KDVGPERNYP YAMRKPYSTA GVSMAKSYKA PRTETAKMYA VDTRV