ID   CLD16_BOVIN             Reviewed;         254 AA.
AC   Q9XT98;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1999, sequence version 1.
DT   03-AUG-2022, entry version 123.
DE   RecName: Full=Claudin-16;
DE            Short=CL-16;
GN   Name=CLDN16;
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], AND INVOLVEMENT IN CINF.
RX   PubMed=10810088; DOI=10.1101/gr.10.5.659;
RA   Hirano T., Kobayashi N., Itoh T., Takasuga A., Nakamaru T., Hirotsune S.,
RA   Sugimoto Y.;
RT   "Null mutation of PCLN-1/claudin-16 results in bovine chronic interstitial
RT   nephritis.";
RL   Genome Res. 10:659-663(2000).
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   -!- TISSUE SPECIFICITY: Expressed preferentially in kidney.
CC   -!- DISEASE: Note=Defects in CLDN16 are a cause of an autosomal recessive
CC       chronic interstitial nephritis with diffuse zonal fibrosis (CINF). CINF
CC       is characterized by increased blood urea nitrogen, creatinine, and
CC       urinary proteins, leads to lethality before puberty, usually within the
CC       first 6 months or year of life.
CC   -!- SIMILARITY: Belongs to the claudin family. {ECO:0000305}.
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DR   EMBL; AB030082; BAA82553.1; -; mRNA.
DR   RefSeq; NP_776944.1; NM_174519.2.
DR   AlphaFoldDB; Q9XT98; -.
DR   SMR; Q9XT98; -.
DR   STRING; 9913.ENSBTAP00000008509; -.
DR   PaxDb; Q9XT98; -.
DR   Ensembl; ENSBTAT00000008509; ENSBTAP00000008509; ENSBTAG00000006494.
DR   GeneID; 282184; -.
DR   KEGG; bta:282184; -.
DR   CTD; 10686; -.
DR   VEuPathDB; HostDB:ENSBTAG00000006494; -.
DR   VGNC; VGNC:27406; CLDN16.
DR   eggNOG; ENOG502QRY9; Eukaryota.
DR   GeneTree; ENSGT00730000111162; -.
DR   HOGENOM; CLU_079378_0_0_1; -.
DR   InParanoid; Q9XT98; -.
DR   OMA; GLHCVKF; -.
DR   OrthoDB; 1169036at2759; -.
DR   TreeFam; TF331936; -.
DR   Proteomes; UP000009136; Chromosome 1.
DR   Bgee; ENSBTAG00000006494; Expressed in adult mammalian kidney and 17 other tissues.
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: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   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..254
FT                   /note="Claudin-16"
FT                   /id="PRO_0000144773"
FT   TOPO_DOM        1..22
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        23..43
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        44..98
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        99..119
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        120..134
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        135..155
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        156..188
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        189..209
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        210..254
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   254 AA;  27992 MW;  38B00835FF894ECC CRC64;
     MGPGLAASHV SFPDSLLAKM RDLLQYVACF FAFFSAGFLV VATWTDCWMV NADDSLEVST
     KCRGLWWECV TNAFDGIRTC DEYDSILAEH SLKLVVTRAL MITADILAGF GFITLLLGLD
     CVKFLPDEPY IKVRISFVAG TTLLIAGAPG IIGSVWYAVD VYVERSSLVL HNIFLGIQYK
     FGWSCWLGMA GSLGCFLAGA ILTCCLYLFK DVGPERSYPY STRKAYSTTA VSMPRSHAIP
     RTQTAKMYAV DTRV