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Chloride channel protein 1 (ClC-1) (Chloride channel protein, skeletal muscle)

 CLCN1_HUMAN             Reviewed;         988 AA.
P35523; A4D2H5; Q2M202;
01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
02-NOV-2010, sequence version 3.
18-JUL-2018, entry version 179.
RecName: Full=Chloride channel protein 1;
Short=ClC-1;
AltName: Full=Chloride channel protein, skeletal muscle;
Name=CLCN1; Synonyms=CLC1;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], VARIANT MCAD LEU-480,
VARIANT GLN-300, CHARACTERIZATION OF VARIANTS MCAD GLU-230 AND
LEU-480, CHARACTERIZATION OF VARIANT GLN-300, AND FUNCTION.
PubMed=8112288;
Steinmeyer K., Lorenz C., Pusch M., Koch M.C., Jentsch T.J.;
"Multimeric structure of ClC-1 chloride channel revealed by mutations
in dominant myotonia congenita (Thomsen).";
EMBO J. 13:737-743(1994).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=12690205; DOI=10.1126/science.1083423;
Scherer S.W., Cheung J., MacDonald J.R., Osborne L.R., Nakabayashi K.,
Herbrick J.-A., Carson A.R., Parker-Katiraee L., Skaug J., Khaja R.,
Zhang J., Hudek A.K., Li M., Haddad M., Duggan G.E., Fernandez B.A.,
Kanematsu E., Gentles S., Christopoulos C.C., Choufani S.,
Kwasnicka D., Zheng X.H., Lai Z., Nusskern D.R., Zhang Q., Gu Z.,
Lu F., Zeesman S., Nowaczyk M.J., Teshima I., Chitayat D., Shuman C.,
Weksberg R., Zackai E.H., Grebe T.A., Cox S.R., Kirkpatrick S.J.,
Rahman N., Friedman J.M., Heng H.H.Q., Pelicci P.G., Lo-Coco F.,
Belloni E., Shaffer L.G., Pober B., Morton C.C., Gusella J.F.,
Bruns G.A.P., Korf B.R., Quade B.J., Ligon A.H., Ferguson H.,
Higgins A.W., Leach N.T., Herrick S.R., Lemyre E., Farra C.G.,
Kim H.-G., Summers A.M., Gripp K.W., Roberts W., Szatmari P.,
Winsor E.J.T., Grzeschik K.-H., Teebi A., Minassian B.A., Kere J.,
Armengol L., Pujana M.A., Estivill X., Wilson M.D., Koop B.F.,
Tosi S., Moore G.E., Boright A.P., Zlotorynski E., Kerem B.,
Kroisel P.M., Petek E., Oscier D.G., Mould S.J., Doehner H.,
Doehner K., Rommens J.M., Vincent J.B., Venter J.C., Li P.W.,
Mural R.J., Adams M.D., Tsui L.-C.;
"Human chromosome 7: DNA sequence and biology.";
Science 300:767-772(2003).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT TRP-118.
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).
[4]
NUCLEOTIDE SEQUENCE [MRNA] OF 171-988, AND VARIANT MCAR CYS-413.
PubMed=1379744; DOI=10.1126/science.1379744;
Koch M.C., Steinmeyer K., Lorenz C., Ricker K., Wolf F., Otto M.,
Zoll B., Lehmann-Horn F., Grzeschik K.-H., Jentsch T.J.;
"The skeletal muscle chloride channel in dominant and recessive human
myotonia.";
Science 257:797-800(1992).
[5]
PARTIAL NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], AND VARIANT MCAD
GLU-230.
PubMed=7981750; DOI=10.1038/ng0493-305;
George A.L. Jr., Crackower M.A., Abdalla J.A., Hudson A.J.,
Ebers G.C.;
"Molecular basis of Thomsen's disease (autosomal dominant myotonia
congenita).";
Nat. Genet. 3:305-310(1993).
[6]
FUNCTION, AND CHARACTERIZATION OF VARIANT MCAD GLU-230.
PubMed=9122265; DOI=10.1073/pnas.94.6.2729;
Fahlke C., Beck C.L., George A.L. Jr.;
"A mutation in autosomal dominant myotonia congenita affects pore
properties of the muscle chloride channel.";
Proc. Natl. Acad. Sci. U.S.A. 94:2729-2734(1997).
[7]
FUNCTION, AND CHARACTERIZATION OF VARIANT MYOTONIA LEVIOR ARG-552.
PubMed=12456816; DOI=10.1113/jphysiol.2002.027037;
Ryan A., Ruedel R., Kuchenbecker M., Fahlke C.;
"A novel alteration of muscle chloride channel gating in myotonia
levior.";
J. Physiol. (Lond.) 545:345-354(2002).
[8]
VARIANT MCAR SER-496, CHARACTERIZATION OF VARIANT MCAR SER-496, AND
FUNCTION.
PubMed=7951242; DOI=10.1093/hmg/3.6.941;
Lorenz C., Meyer-Kleine C., Steinmeyer K., Koch M.C., Jentsch T.J.;
"Genomic organization of the human muscle chloride channel ClC-1 and
analysis of novel mutations leading to Becker-type myotonia.";
Hum. Mol. Genet. 3:941-946(1994).
[9]
VARIANT MCAR GLY-136.
PubMed=7981681; DOI=10.1093/hmg/3.7.1123;
Heine R., George A.L. Jr., Pika U., Deymeer F., Ruedel R.,
Lehmann-Horn F.;
"Proof of a non-functional muscle chloride channel in recessive
myotonia congenita (Becker) by detection of a 4 base pair deletion.";
Hum. Mol. Genet. 3:1123-1128(1994).
[10]
VARIANTS MCAR LEU-167 AND GLN-338, AND VARIANT GLN-300.
PubMed=7874130;
George A.L. Jr., Sloan-Brown K., Fenichel G.M., Mitchell G.A.,
Spiegel R., Pascuzzi R.M.;
"Nonsense and missense mutations of the muscle chloride channel gene
in patients with myotonia congenita.";
Hum. Mol. Genet. 3:2071-2072(1994).
[11]
VARIANTS MCAR AND MCAD.
PubMed=8533761;
Meyer-Kleine C., Steinmeyer K., Ricker K., Jentsch T.J., Koch M.C.;
"Spectrum of mutations in the major human skeletal muscle chloride
channel gene (CLCN1) leading to myotonia.";
Am. J. Hum. Genet. 57:1325-1334(1995).
[12]
VARIANT MCAD MET-290, VARIANT MYOTONIA LEVIOR ARG-552, AND VARIANT
TRP-118.
PubMed=7581380; DOI=10.1093/hmg/4.8.1397;
Lehmann-Horn F., Mailaender V., Heine R., George A.L. Jr.;
"Myotonia levior is a chloride channel disorder.";
Hum. Mol. Genet. 4:1397-1402(1995).
[13]
VARIANT MCAD MET-290, VARIANT MCAR LYS-291, CHARACTERIZATION OF
VARIANTS MCAD MET-290; GLN-317 AND LEU-480, CHARACTERIZATION OF
VARIANT MCAR LYS-291, CHARACTERIZATION OF VARIANT MYOTONIA LEVIOR
ARG-552, AND MUTAGENESIS OF ILE-290 AND GLU-291.
PubMed=8845168; DOI=10.1016/0896-6273(95)90023-3;
Pusch M., Steinmeyer K., Koch M.C., Jentsch T.J.;
"Mutations in dominant human myotonia congenita drastically alter the
voltage dependence of the CIC-1 chloride channel.";
Neuron 15:1455-1463(1995).
[14]
VARIANTS MCAR CYS-150; ARG-200; CYS-261 AND VAL-415.
PubMed=8571958;
Mailaender V., Heine R., Deymeer F., Lehmann-Horn F.;
"Novel muscle chloride channel mutations and their effects on
heterozygous carriers.";
Am. J. Hum. Genet. 58:317-324(1996).
[15]
VARIANTS MCAD/MCAR LEU-236; GLU-285; ALA-286; SER-307; VAL-485 AND
ASN-556, CHARACTERIZATION OF VARIANTS MCAD/MCAR LEU-236; GLU-285;
ALA-286; SER-307 AND ASN-556, AND FUNCTION.
PubMed=9736777; DOI=10.1093/hmg/7.11.1753;
Kubisch C., Schmidt-Rose T., Fontaine B., Bretag A.H., Jentsch T.J.;
"ClC-1 chloride channel mutations in myotonia congenita: variable
penetrance of mutations shifting the voltage dependence.";
Hum. Mol. Genet. 7:1753-1760(1998).
[16]
VARIANTS MCAR ILE-563 AND LEU-708.
PubMed=10215406;
DOI=10.1002/(SICI)1098-1004(1998)11:4<331::AID-HUMU13>3.3.CO;2-S;
Sangiuolo F., Botta A., Mesoraca A., Servidei S., Merlini L.,
Fratta G., Novelli G., Dallapiccola B.;
"Identification of five new mutations and three novel polymorphisms in
the muscle chloride channel gene (CLCN1) in 20 Italian patients with
dominant and recessive myotonia congenita.";
Hum. Mutat. 11:331-331(1998).
[17]
VARIANTS MCAD/MCAR VAL-161; THR-313 AND ASN-556.
PubMed=9566422; DOI=10.1212/WNL.50.4.1176;
Plassart-Schiess E., Gervais A., Eymard B., Lagueny A., Pouget J.,
Warter J.-M., Fardeau M., Jentsch T.J., Fontaine B.;
"Novel muscle chloride channel (CLCN1) mutations in myotonia congenita
with various modes of inheritance including incomplete dominance and
penetrance.";
Neurology 50:1176-1179(1998).
[18]
VARIANT MCAR ARG-499, CHARACTERIZATION OF VARIANT MCAR ARG-499, AND
MUTAGENESIS OF ARG-496; GLY-499 AND GLU-500.
PubMed=10644771; DOI=10.1074/jbc.275.4.2999;
Zhang J., Sanguinetti M.C., Kwiecinski H., Ptacek L.J.;
"Mechanism of inverted activation of ClC-1 channels caused by a novel
myotonia congenita mutation.";
J. Biol. Chem. 275:2999-3005(2000).
[19]
VARIANT MCAR LEU-932.
PubMed=11113225; DOI=10.1212/WNL.55.11.1697;
Nagamitsu S., Matsuura T., Khajavi M., Armstrong R., Gooch C.,
Harati Y., Ashizawa T.;
"A 'dystrophic' variant of autosomal recessive myotonia congenita
caused by novel mutations in the CLCN1 gene.";
Neurology 55:1697-1703(2000).
[20]
VARIANTS MCAD VAL-128; LYS-193; SER-307 AND LEU-480, VARIANT MCAR
GLU-285, AND VARIANTS THR-437 AND ASN-614.
PubMed=12661046; DOI=10.1002/mus.10347;
Colding-Joergensen E., DunOe M., Schwartz M., Vissing J.;
"Decrement of compound muscle action potential is related to mutation
type in myotonia congenita.";
Muscle Nerve 27:449-455(2003).
[21]
VARIANT [LARGE SCALE ANALYSIS] LYS-548.
PubMed=16959974; DOI=10.1126/science.1133427;
Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D.,
Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S.,
Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J.,
Dawson D., Willson J.K.V., Gazdar A.F., Hartigan J., Wu L., Liu C.,
Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N.,
Vogelstein B., Kinzler K.W., Velculescu V.E.;
"The consensus coding sequences of human breast and colorectal
cancers.";
Science 314:268-274(2006).
[22]
VARIANT MCAR SER-190.
PubMed=19697366; DOI=10.1002/mus.21525;
Shalata A., Furman H., Adir V., Adir N., Hujeirat Y., Shalev S.A.,
Borochowitz Z.U.;
"Myotonia congenita in a large consanguineous Arab family: insight
into the clinical spectrum of carriers and double heterozygotes of a
novel mutation in the chloride channel CLCN1 gene.";
Muscle Nerve 41:464-469(2010).
[23]
VARIANTS MCAR ARG-164; ARG-197; ILE-533; LEU-536; SER-845 AND GLU-947,
CHARACTERIZATION OF VARIANTS MCAR ARG-164; SER-190; ARG-197 AND
SER-845, AND FUNCTION.
PubMed=22521272; DOI=10.1016/j.jns.2012.03.024;
Ulzi G., Lecchi M., Sansone V., Redaelli E., Corti E., Saccomanno D.,
Pagliarani S., Corti S., Magri F., Raimondi M., D'Angelo G.,
Modoni A., Bresolin N., Meola G., Wanke E., Comi G.P., Lucchiari S.;
"Myotonia congenita: novel mutations in CLCN1 gene and functional
characterizations in Italian patients.";
J. Neurol. Sci. 318:65-71(2012).
[24]
VARIANTS MCAR LEU-167; ARG-277; TYR-277 AND THR-527, AND
CHARACTERIZATION OF VARIANTS MCAR ARG-277 AND TYR-277.
PubMed=22641783; DOI=10.1113/jphysiol.2012.232785;
Weinberger S., Wojciechowski D., Sternberg D., Lehmann-Horn F.,
Jurkat-Rott K., Becher T., Begemann B., Fahlke C., Fischer M.;
"Disease-causing mutations C277R and C277Y modify gating of human ClC-
1 chloride channels in myotonia congenita.";
J. Physiol. (Lond.) 590:3449-3464(2012).
[25]
VARIANTS MCAD PRO-198 AND LEU-484, CHARACTERIZATION OF VARIANTS MCAD
PRO-198 AND LEU-484, VARIANTS MCAR PRO-628 AND GLY-640, AND
CHARACTERIZATION OF VARIANTS MCAR PRO-628 AND GLY-640.
PubMed=26096614; DOI=10.1113/JP270358;
Imbrici P., Maggi L., Mangiatordi G.F., Dinardo M.M., Altamura C.,
Brugnoni R., Alberga D., Pinter G.L., Ricci G., Siciliano G.,
Micheli R., Annicchiarico G., Lattanzi G., Nicolotti O., Morandi L.,
Bernasconi P., Desaphy J.F., Mantegazza R., Camerino D.C.;
"ClC-1 mutations in myotonia congenita patients: insights into
molecular gating mechanisms and genotype-phenotype correlation.";
J. Physiol. (Lond.) 593:4181-4199(2015).
[26]
VARIANTS MCAR ALA-82; SER-190; VAL-270 AND TRP-453, CHARACTERIZATION
OF VARIANTS MCAR ALA-82; SER-190; VAL-270 AND TRP-453, AND FUNCTION.
PubMed=26007199; DOI=10.1007/s12017-015-8356-8;
Portaro S., Altamura C., Licata N., Camerino G.M., Imbrici P.,
Musumeci O., Rodolico C., Conte Camerino D., Toscano A., Desaphy J.F.;
"Clinical, molecular, and functional characterization of CLCN1
mutations in three families with recessive myotonia congenita.";
NeuroMolecular Med. 17:285-296(2015).
[27]
VARIANTS MCAR ARG-43; LEU-70; ASP-137; HIS-160; SER-496 AND GLU-855,
CHARACTERIZATION OF VARIANTS MCAR ARG-43; LEU-70; ASP-137 AND HIS-160,
FUNCTION, SUBCELLULAR LOCATION, AND SUBUNIT.
PubMed=26502825; DOI=10.1038/srep15382;
Ronstedt K., Sternberg D., Detro-Dassen S., Gramkow T., Begemann B.,
Becher T., Kilian P., Grieschat M., Machtens J.P., Schmalzing G.,
Fischer M., Fahlke C.;
"Impaired surface membrane insertion of homo- and heterodimeric human
muscle chloride channels carrying amino-terminal myotonia-causing
mutations.";
Sci. Rep. 5:15382-15382(2015).
[28]
VARIANTS MCAR CYS-105; LEU-167 AND PRO-412, VARIANT ARG-154,
CHARACTERIZATION OF VARIANTS MCAR CYS-105; LEU-167 AND PRO-412,
CHARACTERIZATION OF VARIANT ARG-154, AND FUNCTION.
PubMed=26510092; DOI=10.1002/humu.22916;
Vindas-Smith R., Fiore M., Vasquez M., Cuenca P., Del Valle G.,
Lagostena L., Gaitan-Penas H., Estevez R., Pusch M., Morales F.;
"Identification and functional characterization of CLCN1 mutations
found in nondystrophic myotonia patients.";
Hum. Mutat. 37:74-83(2016).
[29]
VARIANT MCAD LYS-950.
PubMed=27653901; DOI=10.1016/j.jns.2016.08.030;
Kato H., Kokunai Y., Dalle C., Kubota T., Madokoro Y., Yuasa H.,
Uchida Y., Ikeda T., Mochizuki H., Nicole S., Fontaine B.,
Takahashi M.P., Mitake S.;
"A case of non-dystrophic myotonia with concomitant mutations in the
SCN4A and CLCN1 genes.";
J. Neurol. Sci. 369:254-258(2016).
[30]
VARIANT MCAD HIS-480, AND CHARACTERIZATION OF VARIANT MCAD HIS-480.
PubMed=27666773; DOI=10.1016/j.nmd.2016.08.016;
Mori Y., Yamashita S., Kato M., Masuda T., Takamatsu K., Kumamoto T.,
Sasaki R., Ando Y.;
"Thomsen disease with ptosis and abnormal MR findings.";
Neuromuscul. Disord. 26:805-808(2016).
-!- FUNCTION: Voltage-gated chloride channel. Chloride channels have
several functions including the regulation of cell volume;
membrane potential stabilization, signal transduction and
transepithelial transport. {ECO:0000269|PubMed:12456816,
ECO:0000269|PubMed:22521272, ECO:0000269|PubMed:26007199,
ECO:0000269|PubMed:26502825, ECO:0000269|PubMed:26510092,
ECO:0000269|PubMed:7951242, ECO:0000269|PubMed:8112288,
ECO:0000269|PubMed:9122265, ECO:0000269|PubMed:9736777}.
-!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:26502825}.
-!- INTERACTION:
Q92624:APPBP2; NbExp=5; IntAct=EBI-10206780, EBI-743771;
Q8IZU0:FAM9B; NbExp=3; IntAct=EBI-10206780, EBI-10175124;
-!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:26502825};
Multi-pass membrane protein {ECO:0000255}.
-!- TISSUE SPECIFICITY: Predominantly expressed in skeletal muscles.
-!- DISEASE: Myotonia congenita, autosomal dominant (MCAD)
[MIM:160800]: A non-dystrophic skeletal muscle disorder
characterized by muscle stiffness and an inability of the muscle
to relax after voluntary contraction. Most patients have symptom
onset in the legs, which later progresses to the arms, neck, and
facial muscles. Many patients show marked hypertrophy of the lower
limb muscles. The autosomal dominant form (Thomsen disease) is
less common and less severe than the autosomal recessive one
(Becker disease). A milder form of autosomal dominant myotonia is
characterized by isolated myotonia without muscle weakness,
hypotrophy, or hypertrophy (myotonia levior).
{ECO:0000269|PubMed:12661046, ECO:0000269|PubMed:26096614,
ECO:0000269|PubMed:27653901, ECO:0000269|PubMed:27666773,
ECO:0000269|PubMed:7581380, ECO:0000269|PubMed:7981750,
ECO:0000269|PubMed:8112288, ECO:0000269|PubMed:8533761,
ECO:0000269|PubMed:8845168, ECO:0000269|PubMed:9122265,
ECO:0000269|PubMed:9566422, ECO:0000269|PubMed:9736777}. Note=The
disease is caused by mutations affecting the gene represented in
this entry.
-!- DISEASE: Myotonia congenita, autosomal recessive (MCAR)
[MIM:255700]: A non-dystrophic skeletal muscle disorder
characterized by muscle stiffness and an inability of the muscle
to relax after voluntary contraction. Most patients have symptom
onset in the legs, which later progresses to the arms, neck, and
facial muscles. Many patients show marked hypertrophy of the lower
limb muscles. The autosomal recessive form (Becker disease) is
more severe than the autosomal dominant one (Thomsen disease).
{ECO:0000269|PubMed:10215406, ECO:0000269|PubMed:10644771,
ECO:0000269|PubMed:11113225, ECO:0000269|PubMed:12661046,
ECO:0000269|PubMed:1379744, ECO:0000269|PubMed:19697366,
ECO:0000269|PubMed:22521272, ECO:0000269|PubMed:22641783,
ECO:0000269|PubMed:26007199, ECO:0000269|PubMed:26096614,
ECO:0000269|PubMed:26502825, ECO:0000269|PubMed:26510092,
ECO:0000269|PubMed:7874130, ECO:0000269|PubMed:7951242,
ECO:0000269|PubMed:7981681, ECO:0000269|PubMed:8533761,
ECO:0000269|PubMed:8571958, ECO:0000269|PubMed:8845168,
ECO:0000269|PubMed:9566422, ECO:0000269|PubMed:9736777}. 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-1/CLCN1 subfamily. {ECO:0000305}.
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EMBL; Z25587; CAA80996.1; -; Genomic_DNA.
EMBL; Z25884; CAA81103.1; -; mRNA.
EMBL; CH236959; EAL23786.1; -; Genomic_DNA.
EMBL; BC112156; AAI12157.1; -; mRNA.
EMBL; BC113495; AAI13496.1; -; mRNA.
EMBL; M97820; -; NOT_ANNOTATED_CDS; mRNA.
EMBL; L08261; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; L08262; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; L08263; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; L08264; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; L08265; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; Z25753; CAB56792.1; -; Genomic_DNA.
EMBL; Z25754; CAB56792.1; JOINED; Genomic_DNA.
EMBL; Z25755; CAB56792.1; JOINED; Genomic_DNA.
EMBL; Z25756; CAB56792.1; JOINED; Genomic_DNA.
EMBL; Z25757; CAB56792.1; JOINED; Genomic_DNA.
EMBL; Z25758; CAB56792.1; JOINED; Genomic_DNA.
EMBL; Z25759; CAB56792.1; JOINED; Genomic_DNA.
EMBL; Z25760; CAB56792.1; JOINED; Genomic_DNA.
EMBL; Z25761; CAB56792.1; JOINED; Genomic_DNA.
EMBL; Z25762; CAB56792.1; JOINED; Genomic_DNA.
EMBL; Z25763; CAB56792.1; JOINED; Genomic_DNA.
EMBL; Z25764; CAB56792.1; JOINED; Genomic_DNA.
EMBL; Z25765; CAB56792.1; JOINED; Genomic_DNA.
EMBL; Z25766; CAB56792.1; JOINED; Genomic_DNA.
EMBL; Z25767; CAB56792.1; JOINED; Genomic_DNA.
EMBL; Z25752; CAB56792.1; JOINED; Genomic_DNA.
EMBL; Z25768; CAB56814.1; -; Genomic_DNA.
EMBL; Z25872; CAB56814.1; JOINED; Genomic_DNA.
CCDS; CCDS5881.1; -.
PIR; S37078; S37078.
RefSeq; NP_000074.2; NM_000083.2.
UniGene; Hs.121483; -.
ProteinModelPortal; P35523; -.
BioGrid; 107594; 10.
IntAct; P35523; 4.
STRING; 9606.ENSP00000339867; -.
BindingDB; P35523; -.
TCDB; 2.A.49.2.1; the chloride carrier/channel (clc) family.
iPTMnet; P35523; -.
PhosphoSitePlus; P35523; -.
BioMuta; CLCN1; -.
DMDM; 311033468; -.
EPD; P35523; -.
PaxDb; P35523; -.
PeptideAtlas; P35523; -.
PRIDE; P35523; -.
ProteomicsDB; 55076; -.
DNASU; 1180; -.
Ensembl; ENST00000343257; ENSP00000339867; ENSG00000188037.
GeneID; 1180; -.
KEGG; hsa:1180; -.
UCSC; uc003wcr.2; human.
CTD; 1180; -.
DisGeNET; 1180; -.
EuPathDB; HostDB:ENSG00000188037.10; -.
GeneCards; CLCN1; -.
GeneReviews; CLCN1; -.
HGNC; HGNC:2019; CLCN1.
MalaCards; CLCN1; -.
MIM; 118425; gene.
MIM; 160800; phenotype.
MIM; 255700; phenotype.
neXtProt; NX_P35523; -.
OpenTargets; ENSG00000188037; -.
Orphanet; 614; Thomsen and Becker disease.
PharmGKB; PA26546; -.
eggNOG; KOG0476; Eukaryota.
eggNOG; COG0038; LUCA.
GeneTree; ENSGT00760000119109; -.
HOGENOM; HOG000231297; -.
HOVERGEN; HBG005332; -.
InParanoid; P35523; -.
KO; K05010; -.
OMA; SFTFPPG; -.
OrthoDB; EOG091G01RJ; -.
PhylomeDB; P35523; -.
TreeFam; TF352264; -.
Reactome; R-HSA-2672351; Stimuli-sensing channels.
ChiTaRS; CLCN1; human.
GeneWiki; CLCN1; -.
GenomeRNAi; 1180; -.
PRO; PR:P35523; -.
Proteomes; UP000005640; Chromosome 7.
Bgee; ENSG00000188037; -.
CleanEx; HS_CLCN1; -.
ExpressionAtlas; P35523; baseline and differential.
Genevisible; P35523; HS.
GO; GO:0034707; C:chloride channel complex; IEA:UniProtKB-KW.
GO; GO:0005887; C:integral component of plasma membrane; IDA:UniProtKB.
GO; GO:0005886; C:plasma membrane; TAS:Reactome.
GO; GO:0042383; C:sarcolemma; IEA:Ensembl.
GO; GO:0042803; F:protein homodimerization activity; IDA:UniProtKB.
GO; GO:0005247; F:voltage-gated chloride channel activity; IMP:UniProtKB.
GO; GO:1902476; P:chloride transmembrane transport; IMP:UniProtKB.
GO; GO:0034220; P:ion transmembrane transport; TAS:Reactome.
GO; GO:0006936; P:muscle contraction; IMP:UniProtKB.
GO; GO:0019227; P:neuronal action potential propagation; IEA:Ensembl.
GO; GO:0034765; P:regulation of ion transmembrane transport; IEA:UniProtKB-KW.
Gene3D; 1.10.3080.10; -; 1.
InterPro; IPR000644; CBS_dom.
InterPro; IPR014743; Cl-channel_core.
InterPro; IPR001807; Cl-channel_volt-gated.
InterPro; IPR002243; Cl_channel-1.
Pfam; PF00654; Voltage_CLC; 1.
PRINTS; PR00762; CLCHANNEL.
PRINTS; PR01112; CLCHANNEL1.
SUPFAM; SSF81340; SSF81340; 1.
PROSITE; PS51371; CBS; 2.
1: Evidence at protein level;
CBS domain; Cell membrane; Chloride; Chloride channel;
Complete proteome; Disease mutation; Ion channel; Ion transport;
Membrane; Phosphoprotein; Polymorphism; Reference proteome; Repeat;
Transmembrane; Transmembrane helix; Transport; Voltage-gated channel.
CHAIN 1 988 Chloride channel protein 1.
/FTId=PRO_0000094429.
TOPO_DOM 1 114 Cytoplasmic. {ECO:0000250}.
TRANSMEM 115 152 Helical. {ECO:0000250}.
TRANSMEM 159 182 Helical. {ECO:0000250}.
INTRAMEM 191 198 Helical. {ECO:0000250}.
TRANSMEM 207 225 Helical. {ECO:0000250}.
TRANSMEM 232 250 Helical. {ECO:0000250}.
INTRAMEM 266 278 Helical. {ECO:0000250}.
INTRAMEM 282 290 Helical. {ECO:0000250}.
TRANSMEM 302 321 Helical. {ECO:0000250}.
TRANSMEM 348 376 Helical. {ECO:0000250}.
TRANSMEM 385 404 Helical. {ECO:0000250}.
TRANSMEM 454 474 Helical. {ECO:0000250}.
TRANSMEM 482 505 Helical. {ECO:0000250}.
INTRAMEM 522 536 Helical. {ECO:0000250}.
INTRAMEM 537 538 Note=Loop between two helices.
{ECO:0000250}.
INTRAMEM 539 550 Helical. {ECO:0000250}.
INTRAMEM 551 555 Note=Loop between two helices.
{ECO:0000250}.
TRANSMEM 556 573 Helical. {ECO:0000250}.
TOPO_DOM 574 988 Cytoplasmic. {ECO:0000250}.
DOMAIN 609 668 CBS 1. {ECO:0000255|PROSITE-
ProRule:PRU00703}.
DOMAIN 821 876 CBS 2. {ECO:0000255|PROSITE-
ProRule:PRU00703}.
MOTIF 188 192 Selectivity filter part_1. {ECO:0000250}.
MOTIF 230 234 Selectivity filter part_2. {ECO:0000250}.
MOTIF 482 486 Selectivity filter part_3. {ECO:0000250}.
BINDING 189 189 Chloride. {ECO:0000250}.
BINDING 484 484 Chloride; via amide nitrogen.
{ECO:0000250}.
BINDING 578 578 Chloride. {ECO:0000250}.
MOD_RES 886 886 Phosphoserine.
{ECO:0000250|UniProtKB:Q64347}.
VARIANT 43 43 Q -> R (in MCAR; decreased chloride
transport; decreased localization to the
plasma membrane; dominant negative effect
on chloride transport and localization to
the plasma membrane; no significant
effect on chloride channel activity; no
effect on homodimerization).
{ECO:0000269|PubMed:26502825}.
/FTId=VAR_075588.
VARIANT 70 70 S -> L (in MCAR; unknown pathological
significance; no effect on chloride
transport; dbSNP:rs769312894).
{ECO:0000269|PubMed:26502825}.
/FTId=VAR_075589.
VARIANT 82 82 T -> A (in MCAR; unknown pathological
significance; no effect on chloride
transport; dbSNP:rs772100356).
{ECO:0000269|PubMed:26007199}.
/FTId=VAR_075590.
VARIANT 105 105 R -> C (in MCAR; no effect on chloride
transport; dbSNP:rs201509501).
{ECO:0000269|PubMed:26510092}.
/FTId=VAR_001582.
VARIANT 118 118 G -> W (in dbSNP:rs10282312).
{ECO:0000269|PubMed:15489334,
ECO:0000269|PubMed:7581380}.
/FTId=VAR_001583.
VARIANT 128 128 M -> V (in MCAD; dbSNP:rs80356699).
{ECO:0000269|PubMed:12661046}.
/FTId=VAR_075591.
VARIANT 136 136 D -> G (in MCAR).
{ECO:0000269|PubMed:7981681}.
/FTId=VAR_001584.
VARIANT 137 137 Y -> D (in MCAR; reduced chloride
transport; decreased localization to the
plasma membrane; no significant effect on
chloride channel activity;
dbSNP:rs748639603).
{ECO:0000269|PubMed:26502825}.
/FTId=VAR_075592.
VARIANT 150 150 Y -> C (in MCAR).
{ECO:0000269|PubMed:8571958}.
/FTId=VAR_001585.
VARIANT 154 154 Q -> R (polymorphism; no effect on
chloride transport; dbSNP:rs111482384).
{ECO:0000269|PubMed:26510092}.
/FTId=VAR_075593.
VARIANT 160 160 Q -> H (in MCAR; reduced chloride
transport; decreased localization to the
plasma membrane; no significant effect on
chloride channel activity;
dbSNP:rs771532474).
{ECO:0000269|PubMed:26502825}.
/FTId=VAR_075594.
VARIANT 161 161 F -> V (in MCAD and MCAR).
{ECO:0000269|PubMed:9566422}.
/FTId=VAR_001586.
VARIANT 164 164 W -> R (in MCAR; altered chloride channel
activity). {ECO:0000269|PubMed:22521272}.
/FTId=VAR_075595.
VARIANT 165 165 V -> G (in MCAR).
/FTId=VAR_001587.
VARIANT 167 167 F -> L (in MCAR; no effect on chloride
transport; dbSNP:rs149729531).
{ECO:0000269|PubMed:22641783,
ECO:0000269|PubMed:26510092,
ECO:0000269|PubMed:7874130}.
/FTId=VAR_001588.
VARIANT 190 190 G -> S (in MCAR; loss of chloride channel
activity; dbSNP:rs797045032).
{ECO:0000269|PubMed:19697366,
ECO:0000269|PubMed:22521272,
ECO:0000269|PubMed:26007199}.
/FTId=VAR_075596.
VARIANT 193 193 E -> K (in MCAD; dbSNP:rs80356686).
{ECO:0000269|PubMed:12661046}.
/FTId=VAR_075597.
VARIANT 197 197 I -> R (in MCAR; changed chloride channel
activity). {ECO:0000269|PubMed:22521272}.
/FTId=VAR_075598.
VARIANT 198 198 L -> P (in MCAD; reduced chloride
transport; changed calcium channel
activity; changed gating of the channel).
{ECO:0000269|PubMed:26096614}.
/FTId=VAR_075599.
VARIANT 200 200 G -> R (in MCAD and MCAR).
{ECO:0000269|PubMed:8571958}.
/FTId=VAR_001589.
VARIANT 230 230 G -> E (in MCAD and MCAR; changed ion
selectivity; loss of chloride transport;
mild dominant effect; dbSNP:rs80356700).
{ECO:0000269|PubMed:7981750,
ECO:0000269|PubMed:8112288,
ECO:0000269|PubMed:9122265}.
/FTId=VAR_001590.
VARIANT 236 236 V -> L (in MCAR; loss of chloride
transport; changed calcium channel
activity; changed gating of the channel).
{ECO:0000269|PubMed:9736777}.
/FTId=VAR_001591.
VARIANT 261 261 Y -> C (in MCAR; dbSNP:rs200621976).
{ECO:0000269|PubMed:8571958}.
/FTId=VAR_001592.
VARIANT 270 270 G -> V (in MCAR; decreased chloride
channel activity).
{ECO:0000269|PubMed:26007199}.
/FTId=VAR_075600.
VARIANT 277 277 C -> R (in MCAR; reduced chloride
transport; no effect on protein
abundance; dbSNP:rs757109632).
{ECO:0000269|PubMed:22641783}.
/FTId=VAR_075601.
VARIANT 277 277 C -> Y (in MCAR; reduced chloride
transport; changed calcium channel
activity; changed gating of the channel;
no effect on protein abundance).
{ECO:0000269|PubMed:22641783}.
/FTId=VAR_075602.
VARIANT 285 285 G -> E (in MCAR; loss of chloride channel
activity; dbSNP:rs150885084).
{ECO:0000269|PubMed:12661046,
ECO:0000269|PubMed:9736777}.
/FTId=VAR_001593.
VARIANT 286 286 V -> A (in MCAD; reduced chloride
transport; changed calcium channel
activity; changed gating of the channel;
dominant negative effect;
dbSNP:rs80356689).
{ECO:0000269|PubMed:9736777}.
/FTId=VAR_001594.
VARIANT 290 290 I -> M (in MCAD; reduced chloride
transport; changed chloride channel
activity; changed gating of the channel;
dominant negative effect;
dbSNP:rs80356690).
{ECO:0000269|PubMed:7581380,
ECO:0000269|PubMed:8845168}.
/FTId=VAR_001595.
VARIANT 291 291 E -> K (in MCAR; loss of calcium channel
activity; no dominant negative effect;
dbSNP:rs121912805).
{ECO:0000269|PubMed:8533761,
ECO:0000269|PubMed:8845168}.
/FTId=VAR_001596.
VARIANT 300 300 R -> Q (polymorphism; no effect on
chloride transport; dbSNP:rs118066140).
{ECO:0000269|PubMed:7874130,
ECO:0000269|PubMed:8112288}.
/FTId=VAR_001597.
VARIANT 307 307 F -> S (in MCAD; reduced chloride
transport; changed chloride channel
activity; changed gating of the channel;
dominant negative effect;
dbSNP:rs80356701).
{ECO:0000269|PubMed:12661046,
ECO:0000269|PubMed:9736777}.
/FTId=VAR_001598.
VARIANT 313 313 A -> T (in MCAD and MCAR;
dbSNP:rs80356692).
{ECO:0000269|PubMed:9566422}.
/FTId=VAR_001599.
VARIANT 317 317 R -> Q (in MCAD; reduced chloride
transport; changed chloride channel
activity; changed gating of the channel;
dbSNP:rs80356702).
{ECO:0000269|PubMed:8533761,
ECO:0000269|PubMed:8845168}.
/FTId=VAR_001600.
VARIANT 327 327 V -> I (in MCAR; dbSNP:rs774396430).
/FTId=VAR_001601.
VARIANT 329 329 I -> T (in MCAR).
/FTId=VAR_001602.
VARIANT 338 338 R -> Q (in MCAD and MCAR;
dbSNP:rs80356703).
{ECO:0000269|PubMed:7874130}.
/FTId=VAR_001603.
VARIANT 412 412 Q -> P (in MCAR; loss of chloride
transport; decreased localization to the
plasma membrane; loss of
homodimerization; might be degraded).
{ECO:0000269|PubMed:26510092}.
/FTId=VAR_075603.
VARIANT 413 413 F -> C (in MCAR; dbSNP:rs121912799).
{ECO:0000269|PubMed:1379744}.
/FTId=VAR_001604.
VARIANT 415 415 A -> V (in MCAR).
{ECO:0000269|PubMed:8571958}.
/FTId=VAR_001605.
VARIANT 437 437 A -> T (polymorphism; dbSNP:rs41276054).
{ECO:0000269|PubMed:12661046}.
/FTId=VAR_001606.
VARIANT 453 453 R -> W (in MCAR; unknown pathological
significance; no effect on chloride
channel activity; dbSNP:rs376026619).
{ECO:0000269|PubMed:26007199}.
/FTId=VAR_075604.
VARIANT 480 480 P -> H (in MCAD; decreased protein
abundance).
{ECO:0000269|PubMed:27666773}.
/FTId=VAR_077244.
VARIANT 480 480 P -> L (in MCAD; loss of chloride
transport; changed chloride channel
activity; changed gating of the channel;
dominant effect; dbSNP:rs80356694).
{ECO:0000269|PubMed:12661046,
ECO:0000269|PubMed:8112288,
ECO:0000269|PubMed:8845168}.
/FTId=VAR_001607.
VARIANT 482 482 G -> R (in MCAR; dbSNP:rs746125212).
/FTId=VAR_001608.
VARIANT 484 484 F -> L (in MCAD; reduced chloride
transport; changed calcium channel
activity; changed channel gating; no
dominant negative effect).
{ECO:0000269|PubMed:26096614}.
/FTId=VAR_075605.
VARIANT 485 485 M -> V (in MCAR; dbSNP:rs146457619).
{ECO:0000269|PubMed:9736777}.
/FTId=VAR_001609.
VARIANT 496 496 R -> S (in MCAR; loss of chloride channel
activity; recessive; dbSNP:rs121912801).
{ECO:0000269|PubMed:26502825,
ECO:0000269|PubMed:7951242}.
/FTId=VAR_001610.
VARIANT 499 499 G -> R (in MCAR; reduced chloride
transport; changed calcium channel
activity; changed channel gating;
dbSNP:rs121912807).
{ECO:0000269|PubMed:10644771}.
/FTId=VAR_075606.
VARIANT 527 527 I -> T (in MCAR; unknown pathological
significance).
{ECO:0000269|PubMed:22641783}.
/FTId=VAR_075607.
VARIANT 533 533 T -> I (in MCAR; unknown pathological
significance).
{ECO:0000269|PubMed:22521272}.
/FTId=VAR_075608.
VARIANT 536 536 V -> L (in MCAR; unknown pathological
significance).
{ECO:0000269|PubMed:22521272}.
/FTId=VAR_075609.
VARIANT 548 548 E -> K (in a breast cancer sample;
somatic mutation; dbSNP:rs546411827).
{ECO:0000269|PubMed:16959974}.
/FTId=VAR_036300.
VARIANT 552 552 Q -> R (in MCAD and MCAR; also found in
myotonia levior; reduced chloride
transport; changed calcium channel
activity; changed channel gating; weak
dominant negative effect;
dbSNP:rs80356696).
{ECO:0000269|PubMed:12456816,
ECO:0000269|PubMed:7581380,
ECO:0000269|PubMed:8845168}.
/FTId=VAR_001611.
VARIANT 556 556 I -> N (in MCAD and MCAR; mild form;
reduced chloride transport; changed
chloride channel activity; changed gating
of the channel; partial dominant negative
effect; dbSNP:rs80356697).
{ECO:0000269|PubMed:9566422,
ECO:0000269|PubMed:9736777}.
/FTId=VAR_001612.
VARIANT 563 563 V -> I (in MCAR).
{ECO:0000269|PubMed:10215406}.
/FTId=VAR_001613.
VARIANT 614 614 K -> N (polymorphism; dbSNP:rs140205115).
{ECO:0000269|PubMed:12661046}.
/FTId=VAR_075610.
VARIANT 628 628 L -> P (in MCAR; unknown pathological
significance; no effect on calcium
channel activity).
{ECO:0000269|PubMed:26096614}.
/FTId=VAR_075611.
VARIANT 640 640 V -> G (in MCAR; reduced calcium channel
activity). {ECO:0000269|PubMed:26096614}.
/FTId=VAR_075612.
VARIANT 708 708 F -> L (in MCAR).
{ECO:0000269|PubMed:10215406}.
/FTId=VAR_001614.
VARIANT 727 727 P -> L (in dbSNP:rs13438232).
/FTId=VAR_047779.
VARIANT 845 845 G -> S (in MCAR; unknown pathological
significance; no effect on chloride
channel activity; dbSNP:rs755433272).
{ECO:0000269|PubMed:22521272}.
/FTId=VAR_075613.
VARIANT 855 855 G -> E (in MCAR; unknown pathological
significance).
{ECO:0000269|PubMed:26502825}.
/FTId=VAR_075614.
VARIANT 932 932 P -> L (in MCAR; unknown pathological
significance; dbSNP:rs80356706).
{ECO:0000269|PubMed:11113225}.
/FTId=VAR_075615.
VARIANT 947 947 V -> E (in MCAR; unknown pathological
significance).
{ECO:0000269|PubMed:22521272}.
/FTId=VAR_075616.
VARIANT 950 950 E -> K (in MCAD; unknown pathological
significance; dbSNP:rs201506176).
{ECO:0000269|PubMed:27653901}.
/FTId=VAR_079520.
MUTAGEN 290 290 I->C,E,F,G,K,L,Q,T,V,Y: Changed chloride
channel activity; changed gating of the
channel. {ECO:0000269|PubMed:8845168}.
MUTAGEN 291 291 E->D: No effect on calcium channel
activity. {ECO:0000269|PubMed:8845168}.
MUTAGEN 291 291 E->L: Loss of calcium channel activity.
{ECO:0000269|PubMed:8845168}.
MUTAGEN 496 496 R->K: Changed gating of the channel.
{ECO:0000269|PubMed:10644771}.
MUTAGEN 499 499 G->K,E: Changed gating of the channel.
{ECO:0000269|PubMed:10644771}.
MUTAGEN 499 499 G->Q: No effect on gating of the channel.
{ECO:0000269|PubMed:10644771}.
MUTAGEN 500 500 E->Q: No effect on channel function.
{ECO:0000269|PubMed:10644771}.
CONFLICT 697 697 L -> P (in Ref. 1; CAA80996/CAA81103).
{ECO:0000305}.
SEQUENCE 988 AA; 108626 MW; CA838BCD2AF3CA68 CRC64;
MEQSRSQQRG GEQSWWGSDP QYQYMPFEHC TSYGLPSENG GLQHRLRKDA GPRHNVHPTQ
IYGHHKEQFS DREQDIGMPK KTGSSSTVDS KDEDHYSKCQ DCIHRLGQVV RRKLGEDGIF
LVLLGLLMAL VSWSMDYVSA KSLQAYKWSY AQMQPSLPLQ FLVWVTFPLV LILFSALFCH
LISPQAVGSG IPEMKTILRG VVLKEYLTMK AFVAKVVALT AGLGSGIPVG KEGPFVHIAS
ICAAVLSKFM SVFCGVYEQP YYYSDILTVG CAVGVGCCFG TPLGGVLFSI EVTSTYFAVR
NYWRGFFAAT FSAFVFRVLA VWNKDAVTIT ALFRTNFRMD FPFDLKELPA FAAIGICCGL
LGAVFVYLHR QVMLGVRKHK ALSQFLAKHR LLYPGIVTFV IASFTFPPGM GQFMAGELMP
REAISTLFDN NTWVKHAGDP ESLGQSAVWI HPRVNVVIII FLFFVMKFWM SIVATTMPIP
CGGFMPVFVL GAAFGRLVGE IMAMLFPDGI LFDDIIYKIL PGGYAVIGAA ALTGAVSHTV
STAVICFELT GQIAHILPMM VAVILANMVA QSLQPSLYDS IIQVKKLPYL PDLGWNQLSK
YTIFVEDIMV RDVKFVSASY TYGELRTLLQ TTTVKTLPLV DSKDSMILLG SVERSELQAL
LQRHLCPERR LRAAQEMARK LSELPYDGKA RLAGEGLPGA PPGRPESFAF VDEDEDEDLS
GKSELPPSLA LHPSTTAPLS PEEPNGPLPG HKQQPEAPEP AGQRPSIFQS LLHCLLGRAR
PTKKKTTQDS TDLVDNMSPE EIEAWEQEQL SQPVCFDSCC IDQSPFQLVE QTTLHKTHTL
FSLLGLHLAY VTSMGKLRGV LALEELQKAI EGHTKSGVQL RPPLASFRNT TSTRKSTGAP
PSSAENWNLP EDRPGATGTG DVIAASPETP VPSPSPEPPL SLAPGKVEGE LEELELVESP
GLEEELADIL QGPSLRSTDE EDEDELIL


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