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H( )/Cl(-) exchange transporter 5 (Chloride channel protein 5) (ClC-5) (Chloride transporter ClC-5)

 CLCN5_HUMAN             Reviewed;         746 AA.
P51795; A1L475; B3KPN6; Q5JQD5; Q7RTN8;
01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
01-OCT-1996, sequence version 1.
25-OCT-2017, entry version 172.
RecName: Full=H(+)/Cl(-) exchange transporter 5;
AltName: Full=Chloride channel protein 5;
Short=ClC-5;
AltName: Full=Chloride transporter ClC-5;
Name=CLCN5; Synonyms=CLCK2;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
TISSUE=Kidney;
PubMed=8575751; DOI=10.1006/geno.1995.9960;
Fisher S.E., van Bakel I., Lloyd S.E., Pearce S.H.S., Thakker R.V.,
Craig I.W.;
"Cloning and characterization of CLCN5, the human kidney chloride
channel gene implicated in Dent disease (an X-linked hereditary
nephrolithiasis).";
Genomics 29:598-606(1995).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15772651; DOI=10.1038/nature03440;
Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D.,
Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A.,
Lovell F.L., Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G.,
Jones M.C., Hurles M.E., Andrews T.D., Scott C.E., Searle S.,
Ramser J., Whittaker A., Deadman R., Carter N.P., Hunt S.E., Chen R.,
Cree A., Gunaratne P., Havlak P., Hodgson A., Metzker M.L.,
Richards S., Scott G., Steffen D., Sodergren E., Wheeler D.A.,
Worley K.C., Ainscough R., Ambrose K.D., Ansari-Lari M.A., Aradhya S.,
Ashwell R.I., Babbage A.K., Bagguley C.L., Ballabio A., Banerjee R.,
Barker G.E., Barlow K.F., Barrett I.P., Bates K.N., Beare D.M.,
Beasley H., Beasley O., Beck A., Bethel G., Blechschmidt K., Brady N.,
Bray-Allen S., Bridgeman A.M., Brown A.J., Brown M.J., Bonnin D.,
Bruford E.A., Buhay C., Burch P., Burford D., Burgess J., Burrill W.,
Burton J., Bye J.M., Carder C., Carrel L., Chako J., Chapman J.C.,
Chavez D., Chen E., Chen G., Chen Y., Chen Z., Chinault C.,
Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S.,
Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S.,
Corby N., Connor R.E., David R., Davies J., Davis C., Davis J.,
Delgado O., Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S.,
Draper H., Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I.,
Eades T., Ellwood M., Emery-Cohen A., Errington H., Evans K.L.,
Faulkner L., Francis F., Frankland J., Fraser A.E., Galgoczy P.,
Gilbert J., Gill R., Gloeckner G., Gregory S.G., Gribble S.,
Griffiths C., Grocock R., Gu Y., Gwilliam R., Hamilton C., Hart E.A.,
Hawes A., Heath P.D., Heitmann K., Hennig S., Hernandez J.,
Hinzmann B., Ho S., Hoffs M., Howden P.J., Huckle E.J., Hume J.,
Hunt P.J., Hunt A.R., Isherwood J., Jacob L., Johnson D., Jones S.,
de Jong P.J., Joseph S.S., Keenan S., Kelly S., Kershaw J.K., Khan Z.,
Kioschis P., Klages S., Knights A.J., Kosiura A., Kovar-Smith C.,
Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L., Liu W.,
Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D.,
Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H.,
McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T.,
Milne S., Miner G., Mistry S.L., Morgan M., Morris S., Mueller I.,
Mullikin J.C., Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N.,
Okwuonu G., Palmer S., Pandian R., Parker D., Parrish J.,
Pasternak S., Patel D., Pearce A.V., Pearson D.M., Pelan S.E.,
Perez L., Porter K.M., Ramsey Y., Reichwald K., Rhodes S.,
Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K.,
Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D.,
Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R.,
Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T.,
Teague B., Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S.,
Tromans A.C., d'Urso M., Verduzco D., Villasana D., Waldron L.,
Wall M., Wang Q., Warren J., Warry G.L., Wei X., West A.,
Whitehead S.L., Whiteley M.N., Wilkinson J.E., Willey D.L.,
Williams G., Williams L., Williamson A., Williamson H., Wilming L.,
Woodmansey R.L., Wray P.W., Yen J., Zhang J., Zhou J., Zoghbi H.,
Zorilla S., Buck D., Reinhardt R., Poustka A., Rosenthal A.,
Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F.,
Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A.,
Nelson D.L., Weinstock G., Sulston J.E., Durbin R.M., Hubbard T.,
Gibbs R.A., Beck S., Rogers J., Bentley D.R.;
"The DNA sequence of the human X chromosome.";
Nature 434:325-337(2005).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[5]
NUCLEOTIDE SEQUENCE [MRNA] OF 487-746.
TISSUE=Kidney;
PubMed=7874126;
Fisher S., Black G.C.M., Lloyd S.E., Hatchwell E., Wrong O.,
Thakker R.V., Craig I.W.;
"Isolation and partial characterization of a chloride channel gene
which is expressed in kidney and is a candidate for Dent's disease (an
X-linked hereditary nephrolithiasis).";
Hum. Mol. Genet. 3:2053-2059(1994).
[6]
IDENTIFICATION (ISOFORM 2), AND ALTERNATIVE SPLICING.
PubMed=12886045; DOI=10.1159/000071883;
Ludwig M., Waldegger S., Nuutinen M., Bokenkamp A., Reissinger A.,
Steckelbroeck S., Utsch B.;
"Four additional CLCN5 exons encode a widely expressed novel long CLC-
5 isoform but fail to explain Dent's phenotype in patients without
mutations in the short variant.";
Kidney Blood Press. Res. 26:176-184(2003).
[7]
TISSUE SPECIFICITY.
TISSUE=Aortic endothelium, and Vascular smooth muscle;
PubMed=10198195; DOI=10.1006/jmcc.1998.0901;
Lamb F.S., Clayton G.H., Liu B.-X., Smith R.L., Barna T.J.,
Schutte B.C.;
"Expression of CLCN voltage-gated chloride channel genes in human
blood vessels.";
J. Mol. Cell. Cardiol. 31:657-666(1999).
[8]
INTERACTION WITH NEDD4 AND NEDD4L, UBIQUITINATION, AND MUTAGENESIS OF
TYR-672.
PubMed=15489223; DOI=10.1074/jbc.M411491200;
Hryciw D.H., Ekberg J., Lee A., Lensink I.L., Kumar S., Guggino W.B.,
Cook D.I., Pollock C.A., Poronnik P.;
"Nedd4-2 functionally interacts with ClC-5: involvement in
constitutive albumin endocytosis in proximal tubule cells.";
J. Biol. Chem. 279:54996-55007(2004).
[9]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=25944712; DOI=10.1002/pmic.201400617;
Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M.,
Ayoub D., Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
"N-terminome analysis of the human mitochondrial proteome.";
Proteomics 15:2519-2524(2015).
[10]
X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 570-746 IN COMPLEXES WITH ATP
AND ADP, AND MUTAGENESIS OF GLU-211; TYR-617; SER-618 AND ASP-727.
PubMed=17195847; DOI=10.1038/nsmb1188;
Meyer S., Savaresi S., Forster I.C., Dutzler R.;
"Nucleotide recognition by the cytoplasmic domain of the human
chloride transporter ClC-5.";
Nat. Struct. Mol. Biol. 14:60-67(2007).
[11]
VARIANT XLRHR LEU-244, VARIANT NPHL1 GLU-506, AND VARIANTS NPHL2
ARG-200 AND PRO-520.
PubMed=8559248; DOI=10.1038/379445a0;
Lloyd S.E., Pearce S.H.S., Fisher S.E., Steinmeyer K., Schwappach B.,
Schelnman S.J., Harding B., Bolino A., Devoto M., Goodyer P.,
Rigden S.P.A., Wrong O., Jentsch T.J., Craig I.W., Thakker R.V.;
"A common molecular basis for three inherited kidney stone diseases.";
Nature 379:445-449(1996).
[12]
VARIANT NPHL2 LEU-244.
PubMed=9187673; DOI=10.1007/s004390050448;
Oudet C., Martin-Coignard D., Pannetier S., Praud E., Champion G.,
Hanauer A.;
"A second family with XLRH displays the mutation S244L in the CLCN5
gene.";
Hum. Genet. 99:781-784(1997).
[13]
VARIANTS NPHL2 HIS-30 INS; VAL-57; ARG-512 AND ASP-527.
PubMed=9259268; DOI=10.1093/hmg/6.8.1233;
Lloyd S.E., Guenther W., Pearce S.H.S., Thomson A., Bianchi M.L.,
Bosio M., Craig I.W., Fisher S.E., Scheinman S.J., Wrong O.,
Jentsch T.J., Thakker R.V.;
"Characterisation of renal chloride channel, CLCN5, mutations in
hypercalciuric nephrolithiasis (kidney stones) disorders.";
Hum. Mol. Genet. 6:1233-1239(1997).
[14]
VARIANT LMWPHN PRO-280.
PubMed=9062355; DOI=10.1172/JCI119262;
Lloyd S.E., Pearce S.H.S., Guenther W., Kawaguchi H., Igarashi T.,
Jentsch T.J., Thakker R.V.;
"Idiopathic low molecular weight proteinuria associated with
hypercalciuric nephrocalcinosis in Japanese children is due to
mutations of the renal chloride channel (CLCN5).";
J. Clin. Invest. 99:967-974(1997).
[15]
VARIANT NPHL2 VAL-57.
PubMed=9602200; DOI=10.1016/S0022-3476(98)70318-X;
Schurman S.J., Norden A.G., Scheinman S.J.;
"X-linked recessive nephrolithiasis: presentation and diagnosis in
children.";
J. Pediatr. 132:859-862(1998).
[16]
VARIANTS NPHL2 ARG-270 AND PHE-278, AND CHARACTERIZATION OF VARIANTS
NPHL2 ARG-270 AND PHE-278.
PubMed=9853249; DOI=10.1046/j.1523-1755.1998.00203.x;
Igarashi T., Gunther W., Sekine T., Inatomi J., Shiraga H.,
Takahashi S., Suzuki J., Tsuru N., Yanagihara T., Shimazu M.,
Jentsch T.J., Thakker R.V.;
"Functional characterization of renal chloride channel, CLCN5,
mutations associated with Dent'sJapan disease.";
Kidney Int. 54:1850-1856(1998).
[17]
VARIANT LMWPHN LYS-524.
PubMed=11136179; DOI=10.1016/S0272-6386(01)80067-6;
Takemura T., Hino S., Ikeda M., Okada M., Igarashi T., Inatomi J.,
Yoshioka K.;
"Identification of two novel mutations in the CLCN5 gene in Japanese
patients with familial idiopathic low molecular weight proteinuria
(Japanese Dent's disease).";
Am. J. Kidney Dis. 37:138-143(2001).
[18]
VARIANTS NPHL2 ARG-221; LEU-244; ALA-267; GLY-270; ASP-462; ARG-513;
TRP-516; ASN-545; GLU-546 AND SER-657.
PubMed=15086899; DOI=10.1111/j.1523-1755.2004.00571.x;
Hoopes R.R. Jr., Raja K.M., Koich A., Hueber P., Reid R., Knohl S.J.,
Scheinman S.J.;
"Evidence for genetic heterogeneity in Dent's disease.";
Kidney Int. 65:1615-1620(2004).
[19]
VARIANT NPHL2 VAL-260.
PubMed=16247550; DOI=10.1007/s10038-005-0317-x;
Tosetto E., Graziotto R., Artifoni L., Nachtigal J., Cascone C.,
Conz P., Piva M., Dell'Aquila R., De Paoli Vitali E., Citron L.,
Nalesso F., Antonello A., Vertolli U., Zagatti R., Lupo A.,
D'Angelo A., Anglani F., Gambaro G.;
"Dent's disease and prevalence of renal stones in dialysis patients in
Northeastern Italy.";
J. Hum. Genet. 51:25-30(2006).
[20]
VARIANTS NPHL2 LEU-244; VAL-260; GLU-267 DEL; CYS-272 AND LYS-340.
PubMed=16822791; DOI=10.1093/ndt/gfl274;
Tosetto E., Ghiggeri G.M., Emma F., Barbano G., Carrea A., Vezzoli G.,
Torregrossa R., Cara M., Ripanti G., Ammenti A., Peruzzi L., Murer L.,
Ratsch I.M., Citron L., Gambaro G., D'angelo A., Anglani F.;
"Phenotypic and genetic heterogeneity in Dent's disease -- the results
of an Italian collaborative study.";
Nephrol. Dial. Transplant. 21:2452-2463(2006).
[21]
VARIANTS NPHL2 LEU-244 AND VAL-260.
PubMed=16416111; DOI=10.1007/s00240-005-0005-5;
Anglani F., Bernich P., Tosetto E., Cara M., Lupo A., Nalesso F.,
D'Angelo A., Gambaro G.;
"Family history may be misleading in the diagnosis of Dent's
disease.";
Urol. Res. 34:61-63(2006).
[22]
VARIANTS NPHL2 ARG-219; LEU-273 AND GLY-547.
PubMed=17262170; DOI=10.1007/s10038-007-0112-y;
Ramos-Trujillo E., Gonzalez-Acosta H., Flores C., Garcia-Nieto V.,
Guillen E., Gracia S., Vicente C., Espinosa L., Maseda M.A.,
Santos F., Camacho J.A., Claverie-Martin F.;
"A missense mutation in the chloride/proton ClC-5 antiporter gene
results in increased expression of an alternative mRNA form that lacks
exons 10 and 11. Identification of seven new CLCN5 mutations in
patients with Dent's disease.";
J. Hum. Genet. 52:255-261(2007).
[23]
VARIANT NPHL2 ARG-333.
PubMed=18025833; DOI=10.1159/000111253;
Tanuma A., Sato H., Takeda T., Hosojima M., Obayashi H., Hama H.,
Iino N., Hosaka K., Kaseda R., Imai N., Ueno M., Yamazaki M.,
Sakimura K., Gejyo F., Saito A.;
"Functional characterization of a novel missense CLCN5 mutation
causing alterations in proximal tubular endocytic machinery in Dent's
disease.";
Nephron Physiol. 107:87-97(2007).
[24]
CHARACTERIZATION OF VARIANTS NPHL2 VAL-57; ARG-270; GLU-513; TRP-516
AND ASP-527, CHARACTERIZATION OF VARIANTS LMWPHN PRO-280 AND LYS-524,
AND SUBCELLULAR LOCATION.
PubMed=19019917; DOI=10.1152/ajprenal.90526.2008;
Smith A.J., Reed A.A., Loh N.Y., Thakker R.V., Lippiat J.D.;
"Characterization of Dent's disease mutations of CLC-5 reveals a
correlation between functional and cell biological consequences and
protein structure.";
Am. J. Physiol. 296:F390-F397(2009).
[25]
VARIANTS NPHL2 ASP-179; LEU-203; ALA-212 AND PRO-469, AND
CHARACTERIZATION OF VARIANTS NPHL2 ASP-179; ARG-200; LEU-203; ALA-212;
ARG-219; ARG-221 AND PRO-469.
PubMed=19657328; DOI=10.1038/ki.2009.305;
Grand T., Mordasini D., L'Hoste S., Pennaforte T., Genete M.,
Biyeyeme M.J., Vargas-Poussou R., Blanchard A., Teulon J., Lourdel S.;
"Novel CLCN5 mutations in patients with Dent's disease result in
altered ion currents or impaired exchanger processing.";
Kidney Int. 76:999-1005(2009).
[26]
CHARACTERIZATION OF VARIANTS NPHL2 PRO-225; VAL-260; CYS-272; PHE-278;
LYS-340; ARG-513; GLU-546 AND GLY-547, AND CHARACTERIZATION OF VARIANT
XLRHR LEU-244.
PubMed=21305656; DOI=10.1002/humu.21467;
Grand T., L'Hoste S., Mordasini D., Defontaine N., Keck M.,
Pennaforte T., Genete M., Laghmani K., Teulon J., Lourdel S.;
"Heterogeneity in the processing of CLCN5 mutants related to Dent
disease.";
Hum. Mutat. 32:476-483(2011).
-!- FUNCTION: Proton-coupled chloride transporter. Functions as
antiport system and exchanges chloride ions against protons.
Important for normal acidification of the endosome lumen. May play
an important role in renal tubular function.
-!- SUBUNIT: Interacts with NEDD4 and NEDD4L.
{ECO:0000269|PubMed:15489223}.
-!- INTERACTION:
Self; NbExp=2; IntAct=EBI-13619183, EBI-13619183;
-!- SUBCELLULAR LOCATION: Golgi apparatus membrane
{ECO:0000269|PubMed:19019917}; Multi-pass membrane protein
{ECO:0000269|PubMed:19019917}. Endosome membrane
{ECO:0000269|PubMed:19019917}; Multi-pass membrane protein
{ECO:0000269|PubMed:19019917}. Cell membrane
{ECO:0000269|PubMed:19019917}; Multi-pass membrane protein
{ECO:0000269|PubMed:19019917}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=P51795-1; Sequence=Displayed;
Name=2;
IsoId=P51795-2; Sequence=VSP_042046;
-!- TISSUE SPECIFICITY: Kidney. Moderately expressed in aortic
vascular smooth muscle and endothelial cells, and at a slightly
higher level in the coronary vascular smooth muscle.
{ECO:0000269|PubMed:10198195}.
-!- PTM: Ubiquitinated by NEDD4L in the presence of albumin; which
promotes endocytosis and proteasomal degradation.
{ECO:0000269|PubMed:15489223}.
-!- DISEASE: Hypophosphatemic rickets, X-linked recessive (XLRHR)
[MIM:300554]: A renal disease belonging to the 'Dent disease
complex', a group of disorders characterized by proximal renal
tubular defect, hypercalciuria, nephrocalcinosis, and renal
insufficiency. The spectrum of phenotypic features is remarkably
similar in the various disorders, except for differences in the
severity of bone deformities and renal impairment. XLRH patients
present with rickets or osteomalacia, hypophosphatemia due to
decreased renal tubular phosphate reabsorption, hypercalciuria,
and low molecular weight proteinuria. Patients develop
nephrocalcinosis with progressive renal failure in adulthood.
Female carriers may have asymptomatic hypercalciuria or
hypophosphatemia only. {ECO:0000269|PubMed:21305656,
ECO:0000269|PubMed:8559248}. Note=The disease is caused by
mutations affecting the gene represented in this entry.
-!- DISEASE: Nephrolithiasis 2 (NPHL2) [MIM:300009]: An X-linked
recessive renal disease belonging to the 'Dent disease complex', a
group of disorders characterized by proximal renal tubular defect,
hypercalciuria, nephrocalcinosis, and renal insufficiency. The
spectrum of phenotypic features is remarkably similar in the
various disorders, except for differences in the severity of bone
deformities and renal impairment. Nephrolithiasis type 2 patients
manifest hypercalciuria, hypophosphatemia, aminoaciduria,
nephrocalcinosis and nephrolithiasis, renal insufficiency leading
to renal failure in adulthood, rickets (33% of patients) and
osteomalacia. {ECO:0000269|PubMed:15086899,
ECO:0000269|PubMed:16247550, ECO:0000269|PubMed:16416111,
ECO:0000269|PubMed:16822791, ECO:0000269|PubMed:17262170,
ECO:0000269|PubMed:18025833, ECO:0000269|PubMed:19019917,
ECO:0000269|PubMed:19657328, ECO:0000269|PubMed:21305656,
ECO:0000269|PubMed:8559248, ECO:0000269|PubMed:9187673,
ECO:0000269|PubMed:9259268, ECO:0000269|PubMed:9602200,
ECO:0000269|PubMed:9853249}. Note=The disease is caused by
mutations affecting the gene represented in this entry.
-!- DISEASE: Nephrolithiasis 1 (NPHL1) [MIM:310468]: An X-linked
recessive renal disease belonging to the 'Dent disease complex', a
group of disorders characterized by proximal renal tubular defect,
hypercalciuria, nephrocalcinosis and renal insufficiency. The
spectrum of phenotypic features is remarkably similar in the
various disorders, except for differences in the severity of bone
deformities and renal impairment. Nephrolithiasis type 1 presents
with hypercalciuria, nephrocalcinosis, renal stones and renal
insufficiency. Patients lack urinary acidification defects,
rickets, and osteomalacia. {ECO:0000269|PubMed:8559248}. Note=The
disease is caused by mutations affecting the gene represented in
this entry.
-!- DISEASE: Low molecular weight proteinuria with hypercalciuria and
nephrocalcinosis (LMWPHN) [MIM:308990]: An X-linked renal disease
belonging to the 'Dent disease complex', a group of disorders
characterized by proximal renal tubular defect, hypercalciuria,
nephrocalcinosis, and renal insufficiency. The spectrum of
phenotypic features is remarkably similar in the various
disorders, except for differences in the severity of bone
deformities and renal impairment. LMWPHN is a slowly progressive
disorder. Patients tend to have hypercalciuric nephrocalcinosis
without rickets or renal failure. {ECO:0000269|PubMed:11136179,
ECO:0000269|PubMed:19019917, ECO:0000269|PubMed:9062355}. Note=The
disease is caused by mutations affecting the gene represented in
this entry.
-!- MISCELLANEOUS: The CLC channel family contains both chloride
channels and proton-coupled anion transporters that exchange
chloride or another anion for protons. The absence of conserved
gating glutamate residues is typical for family members that
function as channels.
-!- SIMILARITY: Belongs to the chloride channel (TC 2.A.49) family.
ClC-5/CLCN5 subfamily. {ECO:0000305}.
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EMBL; X91906; CAA63000.1; -; mRNA.
EMBL; AK056560; BAG51748.1; -; mRNA.
EMBL; FO393402; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BC130429; AAI30430.1; -; mRNA.
EMBL; BC130431; AAI30432.1; -; mRNA.
EMBL; X81836; CAA57430.1; -; mRNA.
EMBL; BK000969; DAA01544.1; -; mRNA.
CCDS; CCDS14328.1; -. [P51795-1]
CCDS; CCDS48115.1; -. [P51795-2]
PIR; I37277; I37277.
RefSeq; NP_000075.1; NM_000084.4. [P51795-1]
RefSeq; NP_001121370.1; NM_001127898.3. [P51795-2]
RefSeq; NP_001121371.1; NM_001127899.3. [P51795-2]
RefSeq; NP_001269092.1; NM_001282163.1.
UniGene; Hs.166486; -.
UniGene; Hs.745501; -.
PDB; 2J9L; X-ray; 2.30 A; A/B/C/D/E/F=571-746.
PDB; 2JA3; X-ray; 3.05 A; A/B/C/D/E/F=571-746.
PDBsum; 2J9L; -.
PDBsum; 2JA3; -.
ProteinModelPortal; P51795; -.
SMR; P51795; -.
BioGrid; 107598; 9.
DIP; DIP-29263N; -.
IntAct; P51795; 1.
MINT; MINT-1524912; -.
STRING; 9606.ENSP00000365256; -.
iPTMnet; P51795; -.
PhosphoSitePlus; P51795; -.
MaxQB; P51795; -.
PaxDb; P51795; -.
PeptideAtlas; P51795; -.
PRIDE; P51795; -.
DNASU; 1184; -.
Ensembl; ENST00000307367; ENSP00000304257; ENSG00000171365. [P51795-1]
Ensembl; ENST00000376088; ENSP00000365256; ENSG00000171365. [P51795-2]
Ensembl; ENST00000376091; ENSP00000365259; ENSG00000171365. [P51795-2]
Ensembl; ENST00000376108; ENSP00000365276; ENSG00000171365. [P51795-1]
GeneID; 1184; -.
KEGG; hsa:1184; -.
UCSC; uc004doq.2; human. [P51795-1]
CTD; 1184; -.
DisGeNET; 1184; -.
EuPathDB; HostDB:ENSG00000171365.15; -.
GeneCards; CLCN5; -.
GeneReviews; CLCN5; -.
HGNC; HGNC:2023; CLCN5.
HPA; HPA000401; -.
HPA; HPA003213; -.
MalaCards; CLCN5; -.
MIM; 300008; gene.
MIM; 300009; phenotype.
MIM; 300554; phenotype.
MIM; 308990; phenotype.
MIM; 310468; phenotype.
neXtProt; NX_P51795; -.
OpenTargets; ENSG00000171365; -.
Orphanet; 93622; Dent disease type 1.
PharmGKB; PA26550; -.
eggNOG; KOG0475; Eukaryota.
eggNOG; COG0038; LUCA.
GeneTree; ENSGT00760000119109; -.
HOGENOM; HOG000164493; -.
HOVERGEN; HBG050984; -.
InParanoid; P51795; -.
KO; K05012; -.
OMA; WAIFNSW; -.
OrthoDB; EOG091G01YH; -.
PhylomeDB; P51795; -.
TreeFam; TF313867; -.
Reactome; R-HSA-2672351; Stimuli-sensing channels.
ChiTaRS; CLCN5; human.
EvolutionaryTrace; P51795; -.
GeneWiki; CLCN5; -.
GenomeRNAi; 1184; -.
PRO; PR:P51795; -.
Proteomes; UP000005640; Chromosome X.
Bgee; ENSG00000171365; -.
CleanEx; HS_CLCN5; -.
ExpressionAtlas; P51795; baseline and differential.
Genevisible; P51795; HS.
GO; GO:0045177; C:apical part of cell; IDA:UniProtKB.
GO; GO:0005829; C:cytosol; IDA:HPA.
GO; GO:0005768; C:endosome; IBA:GO_Central.
GO; GO:0010008; C:endosome membrane; TAS:Reactome.
GO; GO:0005794; C:Golgi apparatus; IDA:HPA.
GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
GO; GO:0005887; C:integral component of plasma membrane; TAS:ProtInc.
GO; GO:0005765; C:lysosomal membrane; IDA:UniProtKB.
GO; GO:0016020; C:membrane; IDA:UniProtKB.
GO; GO:0005886; C:plasma membrane; IDA:HPA.
GO; GO:0015297; F:antiporter activity; TAS:Reactome.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0005254; F:chloride channel activity; TAS:ProtInc.
GO; GO:0042802; F:identical protein binding; IPI:IntAct.
GO; GO:0005247; F:voltage-gated chloride channel activity; IBA:GO_Central.
GO; GO:0007588; P:excretion; TAS:ProtInc.
GO; GO:0034220; P:ion transmembrane transport; TAS:Reactome.
GO; GO:0006810; P:transport; TAS:ProtInc.
Gene3D; 1.10.3080.10; -; 1.
InterPro; IPR000644; CBS_dom.
InterPro; IPR014743; Cl-channel_core.
InterPro; IPR001807; Cl-channel_volt-gated.
InterPro; IPR002247; Cl_channel-5.
Pfam; PF00571; CBS; 2.
Pfam; PF00654; Voltage_CLC; 1.
PRINTS; PR00762; CLCHANNEL.
PRINTS; PR01116; CLCHANNEL5.
SMART; SM00116; CBS; 2.
SUPFAM; SSF81340; SSF81340; 3.
PROSITE; PS51371; CBS; 2.
1: Evidence at protein level;
3D-structure; Alternative splicing; Antiport; ATP-binding; CBS domain;
Cell membrane; Chloride; Complete proteome; Disease mutation;
Endosome; Golgi apparatus; Ion transport; Membrane;
Nucleotide-binding; Polymorphism; Reference proteome; Repeat;
Transmembrane; Transmembrane helix; Transport; Ubl conjugation.
CHAIN 1 746 H(+)/Cl(-) exchange transporter 5.
/FTId=PRO_0000094446.
TOPO_DOM 1 54 Cytoplasmic. {ECO:0000250}.
TRANSMEM 55 92 Helical. {ECO:0000250}.
TRANSMEM 138 161 Helical. {ECO:0000250}.
INTRAMEM 170 177 Helical. {ECO:0000250}.
TRANSMEM 186 205 Helical. {ECO:0000250}.
TRANSMEM 211 230 Helical. {ECO:0000250}.
INTRAMEM 242 254 Helical. {ECO:0000250}.
INTRAMEM 258 266 Helical. {ECO:0000250}.
TRANSMEM 278 296 Helical. {ECO:0000250}.
TRANSMEM 319 345 Helical. {ECO:0000250}.
TRANSMEM 352 372 Helical. {ECO:0000250}.
TRANSMEM 428 448 Helical. {ECO:0000250}.
TRANSMEM 453 472 Helical. {ECO:0000250}.
INTRAMEM 500 514 Helical. {ECO:0000250}.
INTRAMEM 515 517 Note=Loop between two helices.
{ECO:0000250}.
INTRAMEM 518 529 Helical. {ECO:0000250}.
INTRAMEM 530 534 Note=Loop between two helices.
{ECO:0000250}.
TRANSMEM 535 552 Helical. {ECO:0000250}.
TOPO_DOM 553 746 Cytoplasmic. {ECO:0000250}.
DOMAIN 586 650 CBS 1. {ECO:0000255|PROSITE-
ProRule:PRU00703}.
DOMAIN 682 742 CBS 2. {ECO:0000255|PROSITE-
ProRule:PRU00703}.
NP_BIND 617 619 ATP. {ECO:0000244|PDB:2J9L,
ECO:0000269|PubMed:17195847}.
NP_BIND 724 727 ATP. {ECO:0000244|PDB:2J9L,
ECO:0000269|PubMed:17195847}.
MOTIF 167 171 Selectivity filter part_1. {ECO:0000250}.
MOTIF 209 213 Selectivity filter part_2. {ECO:0000250}.
MOTIF 453 457 Selectivity filter part_3. {ECO:0000250}.
BINDING 168 168 Chloride. {ECO:0000250}.
BINDING 455 455 Chloride; via amide nitrogen.
{ECO:0000250}.
BINDING 558 558 Chloride. {ECO:0000250}.
BINDING 596 596 ATP; via amide nitrogen and carbonyl
oxygen. {ECO:0000244|PDB:2J9L,
ECO:0000269|PubMed:17195847}.
SITE 211 211 Mediates proton transfer from the outer
aqueous phase to the interior of the
protein; involved in linking H(+) and
Cl(-) transport. {ECO:0000250}.
SITE 268 268 Mediates proton transfer from the protein
to the inner aqueous phase.
{ECO:0000250}.
VAR_SEQ 1 1 M -> MAMWQGAMDNRGFQQGSFSSFQNSSSDEDLMDIPAT
AMDFSMRDDVPPLDREVGEDKSYNGGGIGSSNRIM (in
isoform 2).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_042046.
VARIANT 30 30 R -> RH (in NPHL2).
{ECO:0000269|PubMed:9259268}.
/FTId=VAR_001615.
VARIANT 57 57 G -> V (in NPHL2; alters targeting to
endosomes; dbSNP:rs151340629).
{ECO:0000269|PubMed:19019917,
ECO:0000269|PubMed:9259268,
ECO:0000269|PubMed:9602200}.
/FTId=VAR_001616.
VARIANT 142 142 M -> I (in dbSNP:rs34800648).
/FTId=VAR_048694.
VARIANT 179 179 G -> D (in NPHL2; retained in the
endoplasmic reticulum; improperly N-
glycosylated and non-functional).
{ECO:0000269|PubMed:19657328}.
/FTId=VAR_065591.
VARIANT 200 200 L -> R (in NPHL2; retained in the
endoplasmic reticulum; improperly N-
glycosylated and non-functional;
dbSNP:rs151340622).
{ECO:0000269|PubMed:19657328,
ECO:0000269|PubMed:8559248}.
/FTId=VAR_001617.
VARIANT 203 203 S -> L (in NPHL2; retained in the
endoplasmic reticulum; improperly N-
glycosylated and non-functional).
{ECO:0000269|PubMed:19657328}.
/FTId=VAR_065592.
VARIANT 212 212 G -> A (in NPHL2; trafficks normally to
the cell surface and to early endosomes;
endergoes complex glycosylation at the
cell surface like wild-type protein but
exhibits significant reductions in
outwardly rectifying ion currents).
{ECO:0000269|PubMed:19657328}.
/FTId=VAR_065593.
VARIANT 219 219 C -> R (in NPHL2; retained in the
endoplasmic reticulum; improperly N-
glycosylated and non-functional).
{ECO:0000269|PubMed:17262170,
ECO:0000269|PubMed:19657328}.
/FTId=VAR_065594.
VARIANT 221 221 C -> R (in NPHL2; retained in the
endoplasmic reticulum; improperly N-
glycosylated and non-functional).
{ECO:0000269|PubMed:15086899,
ECO:0000269|PubMed:19657328}.
/FTId=VAR_065595.
VARIANT 225 225 L -> P (in NPHL2; retained in the
endoplasmic reticulum; improperly N-
glycosylated and non-functional;
dbSNP:rs273585645).
{ECO:0000269|PubMed:21305656}.
/FTId=VAR_065596.
VARIANT 244 244 S -> L (in XLRHR; trafficks normally to
the cell surface and to early endosomes;
displays complex glycosylation at the
cell surface like wild-type protein;
exhibits reduced current;
dbSNP:rs151340626).
{ECO:0000269|PubMed:15086899,
ECO:0000269|PubMed:16416111,
ECO:0000269|PubMed:16822791,
ECO:0000269|PubMed:21305656,
ECO:0000269|PubMed:8559248,
ECO:0000269|PubMed:9187673}.
/FTId=VAR_001618.
VARIANT 260 260 G -> V (in NPHL2; delayed in processing
of the protein and decrease in the
stability of the mature complex
glycosylated form causing lower cell
surface expression; the early endosome
distribution is normal; shows abolished
current at the plasma membrane;
dbSNP:rs151340630).
{ECO:0000269|PubMed:16247550,
ECO:0000269|PubMed:16416111,
ECO:0000269|PubMed:16822791,
ECO:0000269|PubMed:21305656}.
/FTId=VAR_065597.
VARIANT 267 267 E -> A (in NPHL2).
{ECO:0000269|PubMed:15086899}.
/FTId=VAR_065598.
VARIANT 267 267 Missing (in NPHL2).
{ECO:0000269|PubMed:16822791}.
/FTId=VAR_065599.
VARIANT 270 270 S -> G (in NPHL2).
{ECO:0000269|PubMed:15086899}.
/FTId=VAR_065600.
VARIANT 270 270 S -> R (in NPHL2; retained in the
endoplasmic reticulum; alters protein
stability; associated with an abolition
of chloride current).
{ECO:0000269|PubMed:19019917,
ECO:0000269|PubMed:9853249}.
/FTId=VAR_065601.
VARIANT 272 272 Y -> C (in NPHL2; trafficks normally to
the cell surface and to early endosomes
and displays complex glycosylation at the
cell surface like wild-type protein;
exhibits no current; dbSNP:rs273585644).
{ECO:0000269|PubMed:16822791,
ECO:0000269|PubMed:21305656}.
/FTId=VAR_065602.
VARIANT 273 273 F -> L (in NPHL2).
{ECO:0000269|PubMed:17262170}.
/FTId=VAR_065603.
VARIANT 278 278 L -> F (in NPHL2; associated with a
marked reduction to about 30% of wild-
type chloride currents; no significant
differences between the expression of the
mutated and wild-type protein;
dbSNP:rs273585648).
{ECO:0000269|PubMed:21305656,
ECO:0000269|PubMed:9853249}.
/FTId=VAR_065604.
VARIANT 280 280 R -> P (in LMWPHN; 70% reduction in
chloride transport activity and alters
targeting to endosomes;
dbSNP:rs151340628).
{ECO:0000269|PubMed:19019917,
ECO:0000269|PubMed:9062355}.
/FTId=VAR_001619.
VARIANT 333 333 G -> R (in NPHL2; unknown pathological
significance).
{ECO:0000269|PubMed:18025833}.
/FTId=VAR_075519.
VARIANT 340 340 N -> K (in NPHL2; retained in the
endoplasmic reticulum; improperly N-
glycosylated and non-functional;
dbSNP:rs273585646).
{ECO:0000269|PubMed:16822791,
ECO:0000269|PubMed:21305656}.
/FTId=VAR_065605.
VARIANT 462 462 G -> D (in NPHL2).
{ECO:0000269|PubMed:15086899}.
/FTId=VAR_065606.
VARIANT 469 469 L -> P (in NPHL2; retained in the
endoplasmic reticulum; improperly N-
glycosylated and non-functional).
{ECO:0000269|PubMed:19657328}.
/FTId=VAR_065607.
VARIANT 506 506 G -> E (in NPHL1; dbSNP:rs151340625).
{ECO:0000269|PubMed:8559248}.
/FTId=VAR_001620.
VARIANT 512 512 G -> R (in NPHL2; abolishes the chloride
currents). {ECO:0000269|PubMed:9259268}.
/FTId=VAR_001621.
VARIANT 513 513 G -> E (in NPHL2; causes retention in the
endoplasmic reticulum and alters protein
stability; total loss of function).
{ECO:0000269|PubMed:19019917}.
/FTId=VAR_065608.
VARIANT 513 513 G -> R (in NPHL2; dbSNP:rs273585647).
{ECO:0000269|PubMed:15086899,
ECO:0000269|PubMed:21305656}.
/FTId=VAR_065609.
VARIANT 516 516 R -> W (in NPHL2; causes retention in the
endoplasmic reticulum and alters protein
stability; total loss of function;
dbSNP:rs797044812).
{ECO:0000269|PubMed:15086899,
ECO:0000269|PubMed:19019917}.
/FTId=VAR_065610.
VARIANT 520 520 S -> P (in NPHL2; dbSNP:rs151340623).
{ECO:0000269|PubMed:8559248}.
/FTId=VAR_001622.
VARIANT 524 524 I -> K (in LMWPHN; causes retention in
the endoplasmic reticulum and alters
protein stability; total loss of
function). {ECO:0000269|PubMed:11136179,
ECO:0000269|PubMed:19019917}.
/FTId=VAR_065611.
VARIANT 527 527 E -> D (in NPHL2; abolishes the chloride
currents; total loss of function).
{ECO:0000269|PubMed:19019917,
ECO:0000269|PubMed:9259268}.
/FTId=VAR_001623.
VARIANT 545 545 S -> N (in NPHL2).
{ECO:0000269|PubMed:15086899}.
/FTId=VAR_065612.
VARIANT 546 546 K -> E (in NPHL2; delayed in processing
of the protein and decrease in the
stability of the mature complex
glycosylated form causing lower cell
surface expression; the early endosome
distribution is normal; shows abolished
current at the plasma membrane).
{ECO:0000269|PubMed:15086899,
ECO:0000269|PubMed:21305656}.
/FTId=VAR_065613.
VARIANT 547 547 W -> G (in NPHL2; delayed in processing
of the protein and decrease in the
stability of the mature complex
glycosylated form causing lower cell
surface expression; the early endosome
distribution is normal; shows reduced
current at the plasma membrane;
dbSNP:rs273585650).
{ECO:0000269|PubMed:17262170,
ECO:0000269|PubMed:21305656}.
/FTId=VAR_065614.
VARIANT 657 657 T -> S (in NPHL2; dbSNP:rs144207967).
{ECO:0000269|PubMed:15086899}.
/FTId=VAR_065615.
MUTAGEN 211 211 E->A: Abolishes proton transport, but not
chloride transport.
{ECO:0000269|PubMed:17195847}.
MUTAGEN 617 617 Y->A: Strongly decreased affinity for
ATP, but no effect on chloride transport.
{ECO:0000269|PubMed:17195847}.
MUTAGEN 618 618 S->A: No effect ATP binding or chloride
transport. {ECO:0000269|PubMed:17195847}.
MUTAGEN 672 672 Y->A: Abolishes interaction with NEDD4
and NEDD4L.
{ECO:0000269|PubMed:15489223}.
MUTAGEN 727 727 D->A: Strongly decreased affinity for
ATP, but no effect on chloride transport.
{ECO:0000269|PubMed:17195847}.
CONFLICT 732 732 I -> V (in Ref. 2; BAG51748).
{ECO:0000305}.
HELIX 582 585 {ECO:0000244|PDB:2J9L}.
STRAND 586 588 {ECO:0000244|PDB:2J9L}.
STRAND 598 601 {ECO:0000244|PDB:2J9L}.
HELIX 605 614 {ECO:0000244|PDB:2J9L}.
STRAND 618 624 {ECO:0000244|PDB:2J9L}.
TURN 626 628 {ECO:0000244|PDB:2J9L}.
STRAND 630 636 {ECO:0000244|PDB:2J9L}.
HELIX 637 648 {ECO:0000244|PDB:2J9L}.
STRAND 659 661 {ECO:0000244|PDB:2J9L}.
STRAND 663 665 {ECO:0000244|PDB:2J9L}.
HELIX 680 682 {ECO:0000244|PDB:2J9L}.
STRAND 683 686 {ECO:0000244|PDB:2J9L}.
STRAND 689 691 {ECO:0000244|PDB:2J9L}.
HELIX 696 706 {ECO:0000244|PDB:2J9L}.
STRAND 709 715 {ECO:0000244|PDB:2J9L}.
STRAND 718 724 {ECO:0000244|PDB:2J9L}.
HELIX 725 735 {ECO:0000244|PDB:2J9L}.
SEQUENCE 746 AA; 83147 MW; EF913C5BA40C85D8 CRC64;
MDFLEEPIPG VGTYDDFNTI DWVREKSRDR DRHREITNKS KESTWALIHS VSDAFSGWLL
MLLIGLLSGS LAGLIDISAH WMTDLKEGIC TGGFWFNHEH CCWNSEHVTF EERDKCPEWN
SWSQLIISTD EGAFAYIVNY FMYVLWALLF AFLAVSLVKV FAPYACGSGI PEIKTILSGF
IIRGYLGKWT LVIKTITLVL AVSSGLSLGK EGPLVHVACC CGNILCHCFN KYRKNEAKRR
EVLSAAAAAG VSVAFGAPIG GVLFSLEEVS YYFPLKTLWR SFFAALVAAF TLRSINPFGN
SRLVLFYVEF HTPWHLFELV PFILLGIFGG LWGALFIRTN IAWCRKRKTT QLGKYPVIEV
LVVTAITAIL AFPNEYTRMS TSELISELFN DCGLLDSSKL CDYENRFNTS KGGELPDRPA
GVGVYSAMWQ LALTLILKIV ITIFTFGMKI PSGLFIPSMA VGAIAGRLLG VGMEQLAYYH
QEWTVFNSWC SQGADCITPG LYAMVGAAAC LGGVTRMTVS LVVIMFELTG GLEYIVPLMA
AAMTSKWVAD ALGREGIYDA HIRLNGYPFL EAKEEFAHKT LAMDVMKPRR NDPLLTVLTQ
DSMTVEDVET IISETTYSGF PVVVSRESQR LVGFVLRRDL IISIENARKK QDGVVSTSII
YFTEHSPPLP PYTPPTLKLR NILDLSPFTV TDLTPMEIVV DIFRKLGLRQ CLVTHNGRLL
GIITKKDVLK HIAQMANQDP DSILFN


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EIAAB37125 Gabt3,Gabt4,Gat3,GAT-3,Gat4,GAT-4,Gat-4,Mouse,Mus musculus,Slc6a11,Sodium- and chloride-dependent GABA transporter 3,Sodium- and chloride-dependent GABA transporter 4,Solute carrier family 6 member 11
EIAAB37153 Rat,Rattus norvegicus,Sit1,Slc6a20,Sodium- and chloride-dependent transporter XTRP3,Sodium_imino-acid transporter 1,Solute carrier family 6 member 20,Transporter rB21A,Xtrp3
EIAAB36601 Cation-chloride cotransporter 6,Cation-chloride cotransporter-interacting protein 1,CCC6,CCC-interacting protein 1,CIP1,hCCC6,hCIP1,Homo sapiens,Human,Potassium-chloride transporter 9,SLC12A9,Solute c


 

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