CLD17_MOUSE
ID CLD17_MOUSE Reviewed; 224 AA.
AC Q8BXA6;
DT 24-MAY-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 114.
DE RecName: Full=Claudin-17;
GN Name=Cldn17;
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 [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Head;
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).
RN [2]
RP SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=22402829; DOI=10.1007/s00018-012-0949-x;
RA Krug S.M., Guenzel D., Conrad M.P., Rosenthal R., Fromm A., Amasheh S.,
RA Schulzke J.D., Fromm M.;
RT "Claudin-17 forms tight junction channels with distinct anion
RT selectivity.";
RL Cell. Mol. Life Sci. 69:2765-2778(2012).
CC -!- FUNCTION: Channel-forming tight junction protein with selectivity for
CC anions, including chloride and bicarbonate, and for solutes smaller
CC than 9 Angstrom in diameter. In the kidney proximal tubule, may be
CC involved in quantitative reabsorption of filtered anions. Does not
CC affect water permeability. {ECO:0000250|UniProtKB:P56750}.
CC -!- SUBUNIT: Interacts with OCLN. {ECO:0000250|UniProtKB:P56750}.
CC -!- SUBCELLULAR LOCATION: Cell junction, tight junction
CC {ECO:0000269|PubMed:22402829}. Cell membrane {ECO:0000305}; Multi-pass
CC membrane protein {ECO:0000255}.
CC -!- TISSUE SPECIFICITY: Expressed at high levels in the kidney and at
CC mucher lower levels in the brain. In the kidney, expression gradually
CC decreases from the proximal tubule downstream to the distal convoluted
CC tubule. Expressed in the thin ascending limb of Henle's loop, as well
CC as in the thick ascending limb of Henle's loop. In the distal
CC convoluted tubules, expressed only in a few tubules. Not detected in
CC the collecting duct. In the brain, expressed in blood vessels (at
CC protein level). {ECO:0000269|PubMed:22402829}.
CC -!- SIMILARITY: Belongs to the claudin family. {ECO:0000305}.
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DR EMBL; AK048287; BAC33296.1; -; mRNA.
DR CCDS; CCDS28295.1; -.
DR RefSeq; NP_852467.1; NM_181490.3.
DR AlphaFoldDB; Q8BXA6; -.
DR SMR; Q8BXA6; -.
DR STRING; 10090.ENSMUSP00000066427; -.
DR PhosphoSitePlus; Q8BXA6; -.
DR PaxDb; Q8BXA6; -.
DR PRIDE; Q8BXA6; -.
DR ProteomicsDB; 283291; -.
DR Antibodypedia; 6585; 127 antibodies from 24 providers.
DR DNASU; 239931; -.
DR Ensembl; ENSMUST00000069549; ENSMUSP00000066427; ENSMUSG00000055811.
DR GeneID; 239931; -.
DR KEGG; mmu:239931; -.
DR UCSC; uc007zuy.1; mouse.
DR CTD; 26285; -.
DR MGI; MGI:2652030; Cldn17.
DR VEuPathDB; HostDB:ENSMUSG00000055811; -.
DR eggNOG; ENOG502RTNJ; Eukaryota.
DR GeneTree; ENSGT00940000162550; -.
DR HOGENOM; CLU_076370_1_2_1; -.
DR InParanoid; Q8BXA6; -.
DR OMA; VCWTANI; -.
DR OrthoDB; 1314055at2759; -.
DR PhylomeDB; Q8BXA6; -.
DR TreeFam; TF331936; -.
DR BioGRID-ORCS; 239931; 3 hits in 71 CRISPR screens.
DR PRO; PR:Q8BXA6; -.
DR Proteomes; UP000000589; Chromosome 16.
DR RNAct; Q8BXA6; protein.
DR Bgee; ENSMUSG00000055811; Expressed in esophagus and 13 other tissues.
DR GO; GO:0005923; C:bicellular tight junction; ISS:UniProtKB.
DR GO; GO:0034707; C:chloride channel complex; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR GO; GO:0005254; F:chloride channel activity; IEA:UniProtKB-KW.
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 InterPro; IPR006187; Claudin.
DR InterPro; IPR017974; Claudin_CS.
DR InterPro; IPR004031; PMP22/EMP/MP20/Claudin.
DR PANTHER; PTHR12002; PTHR12002; 1.
DR Pfam; PF00822; PMP22_Claudin; 1.
DR PROSITE; PS01346; CLAUDIN; 1.
PE 1: Evidence at protein level;
KW Cell junction; Cell membrane; Chloride; Chloride channel; Ion channel;
KW Ion transport; Membrane; Reference proteome; Tight junction; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..224
FT /note="Claudin-17"
FT /id="PRO_0000144778"
FT TOPO_DOM 1..7
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 8..28
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 29..81
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 82..102
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 103..124
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 125..145
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 146..164
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 165..185
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 186..224
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
SQ SEQUENCE 224 AA; 24653 MW; 6E049CE63AB60A34 CRC64;
MAFYPLQIAG LVLGFFGLVG TIGTTLLPQW RVSAFIGSNI IIFERIWEGL WMNCIQQAMV
TLQCKFYNSI LALPPVLEAA RALMCVAVAL ALVALIIGIC GMKQLQCTGS SERVKAYLLG
TSGVLFILTG IFVLIPVSWT ANIIIRDFYD PTVHAGQKRE LGGALFLGWA TAAVLFIGGG
LLCGYCCCNR KERWHRYPVP AYRVPQKDNQ RNVTVPRKSS TSYV
