ID   CLD16_MOUSE             Reviewed;         235 AA.
AC   Q925N4; Q542L7;
DT   10-MAY-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2001, sequence version 1.
DT   03-AUG-2022, entry version 136.
DE   RecName: Full=Claudin-16;
DE   AltName: Full=Paracellin-1;
GN   Name=Cldn16;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=BALB/cJ;
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).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Kidney;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA   Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA   Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA   Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA   Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA   Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA   Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA   Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA   Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA   Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA   Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA   Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA   Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA   Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA   Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA   Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA   Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA   Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA   Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA   Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA   van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA   Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA   Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA   Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA   Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA   Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA   Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA   Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA   Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
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; AF323748; AAK49518.1; -; mRNA.
DR   EMBL; AK085268; BAC39406.1; -; mRNA.
DR   EMBL; AK085333; BAC39425.1; -; mRNA.
DR   CCDS; CCDS28088.1; -.
DR   RefSeq; NP_444471.1; NM_053241.5.
DR   AlphaFoldDB; Q925N4; -.
DR   SMR; Q925N4; -.
DR   STRING; 10090.ENSMUSP00000124528; -.
DR   PhosphoSitePlus; Q925N4; -.
DR   PaxDb; Q925N4; -.
DR   PRIDE; Q925N4; -.
DR   ProteomicsDB; 285481; -.
DR   Antibodypedia; 19357; 201 antibodies from 25 providers.
DR   DNASU; 114141; -.
DR   Ensembl; ENSMUST00000115302; ENSMUSP00000110957; ENSMUSG00000038148.
DR   Ensembl; ENSMUST00000161053; ENSMUSP00000124528; ENSMUSG00000038148.
DR   GeneID; 114141; -.
DR   KEGG; mmu:114141; -.
DR   UCSC; uc007yva.2; mouse.
DR   CTD; 10686; -.
DR   MGI; MGI:2148742; Cldn16.
DR   VEuPathDB; HostDB:ENSMUSG00000038148; -.
DR   eggNOG; ENOG502QRY9; Eukaryota.
DR   GeneTree; ENSGT00730000111162; -.
DR   HOGENOM; CLU_079378_1_0_1; -.
DR   InParanoid; Q925N4; -.
DR   OMA; GLHCVKF; -.
DR   OrthoDB; 1169036at2759; -.
DR   PhylomeDB; Q925N4; -.
DR   TreeFam; TF331936; -.
DR   BioGRID-ORCS; 114141; 2 hits in 74 CRISPR screens.
DR   PRO; PR:Q925N4; -.
DR   Proteomes; UP000000589; Chromosome 16.
DR   RNAct; Q925N4; protein.
DR   Bgee; ENSMUSG00000038148; Expressed in right kidney and 6 other tissues.
DR   ExpressionAtlas; Q925N4; baseline and differential.
DR   Genevisible; Q925N4; MM.
DR   GO; GO:0005923; C:bicellular tight junction; IDA:MGI.
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; ISO:MGI.
DR   GO; GO:0070633; P:transepithelial transport; ISO:MGI.
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_0000144775"
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;  26100 MW;  C0601A64D87891FF CRC64;
     MKDLLQYAAC FLAIFSTGFL IVATWTDCWM VNADDSLEVS TKCRGLWWEC VTNAFDGIRT
     CDEYDSIYAE HPLKLVVTRA LMITADILAG FGFITLLLGL DCVKFLPDDP QIKVRLCFVA
     GTTLLIAGTP GIIGSVWYAV DVYVERSSLV LHNIFLGIQY KFGWSCWLGM AGSLGCFLAG
     ALLTCCLYLF KDVGPERNYP YAMRKPYSTA GVSMAKSYKA PRTETAKMYA VDTRV