CLCN1_RAT
ID CLCN1_RAT Reviewed; 994 AA.
AC P35524;
DT 01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1994, sequence version 1.
DT 03-AUG-2022, entry version 137.
DE RecName: Full=Chloride channel protein 1;
DE Short=ClC-1;
DE AltName: Full=Chloride channel protein, skeletal muscle;
GN Name=Clcn1;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, AND TISSUE
RP SPECIFICITY.
RC TISSUE=Skeletal muscle;
RX PubMed=1659664; DOI=10.1038/354301a0;
RA Steinmeyer K., Ortland C., Jentsch T.J.;
RT "Primary structure and functional expression of a developmentally regulated
RT skeletal muscle chloride channel.";
RL Nature 354:301-304(1991).
RN [2]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-892, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
CC -!- FUNCTION: Voltage-gated chloride channel (PubMed:1659664). Plays an
CC important role in membrane repolarization in skeletal muscle cells
CC after muscle contraction (By similarity).
CC {ECO:0000250|UniProtKB:P35523, ECO:0000269|PubMed:1659664}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2 chloride(in) + H(+)(out) = 2 chloride(out) + H(+)(in);
CC Xref=Rhea:RHEA:29567, ChEBI:CHEBI:15378, ChEBI:CHEBI:17996;
CC Evidence={ECO:0000250|UniProtKB:P51798};
CC -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:P35523}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:1659664};
CC Multi-pass membrane protein {ECO:0000250|UniProtKB:P35523}.
CC -!- TISSUE SPECIFICITY: Predominantly expressed in skeletal muscles.
CC {ECO:0000269|PubMed:1659664}.
CC -!- MISCELLANEOUS: The CLC channel family contains both chloride channels
CC and proton-coupled anion transporters that exchange chloride or another
CC anion for protons. The absence of conserved gating glutamate residues
CC is typical for family members that function as channels (By
CC similarity). {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the chloride channel (TC 2.A.49) family. ClC-
CC 1/CLCN1 subfamily. {ECO:0000305}.
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DR EMBL; X62894; CAA44683.1; -; mRNA.
DR PIR; S19595; S19595.
DR RefSeq; NP_037279.1; NM_013147.1.
DR AlphaFoldDB; P35524; -.
DR SMR; P35524; -.
DR BioGRID; 247717; 3.
DR STRING; 10116.ENSRNOP00000043372; -.
DR BindingDB; P35524; -.
DR ChEMBL; CHEMBL4524038; -.
DR iPTMnet; P35524; -.
DR PhosphoSitePlus; P35524; -.
DR SwissPalm; P35524; -.
DR PaxDb; P35524; -.
DR GeneID; 25688; -.
DR KEGG; rno:25688; -.
DR UCSC; RGD:2360; rat.
DR CTD; 1180; -.
DR RGD; 2360; Clcn1.
DR eggNOG; KOG0476; Eukaryota.
DR InParanoid; P35524; -.
DR OrthoDB; 1131873at2759; -.
DR PhylomeDB; P35524; -.
DR Reactome; R-RNO-2672351; Stimuli-sensing channels.
DR PRO; PR:P35524; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0034707; C:chloride channel complex; IEA:UniProtKB-KW.
DR GO; GO:0005887; C:integral component of plasma membrane; ISS:UniProtKB.
DR GO; GO:0042383; C:sarcolemma; ISO:RGD.
DR GO; GO:0042803; F:protein homodimerization activity; ISS:UniProtKB.
DR GO; GO:0005247; F:voltage-gated chloride channel activity; IDA:RGD.
DR GO; GO:1902476; P:chloride transmembrane transport; ISO:RGD.
DR GO; GO:0006821; P:chloride transport; IDA:RGD.
DR GO; GO:0006936; P:muscle contraction; ISS:UniProtKB.
DR GO; GO:0019227; P:neuronal action potential propagation; ISO:RGD.
DR GO; GO:0034765; P:regulation of ion transmembrane transport; IEA:UniProtKB-KW.
DR Gene3D; 3.10.580.10; -; 2.
DR InterPro; IPR000644; CBS_dom.
DR InterPro; IPR046342; CBS_dom_sf.
DR InterPro; IPR014743; Cl-channel_core.
DR InterPro; IPR001807; Cl-channel_volt-gated.
DR InterPro; IPR002243; Cl_channel-1.
DR Pfam; PF00654; Voltage_CLC; 1.
DR PRINTS; PR00762; CLCHANNEL.
DR PRINTS; PR01112; CLCHANNEL1.
DR SUPFAM; SSF54631; SSF54631; 1.
DR SUPFAM; SSF81340; SSF81340; 1.
DR PROSITE; PS51371; CBS; 2.
PE 1: Evidence at protein level;
KW CBS domain; Cell membrane; Chloride; Chloride channel; Ion channel;
KW Ion transport; Membrane; Phosphoprotein; Reference proteome; Repeat;
KW Transmembrane; Transmembrane helix; Transport; Voltage-gated channel.
FT CHAIN 1..994
FT /note="Chloride channel protein 1"
FT /id="PRO_0000094431"
FT TOPO_DOM 1..118
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 119..150
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:P35523"
FT TOPO_DOM 151..158
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 159..179
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:P35523"
FT TOPO_DOM 180..183
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT INTRAMEM 184..195
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:P35523"
FT TOPO_DOM 196..208
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 209..228
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:P35523"
FT TRANSMEM 229..246
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:P35523"
FT TOPO_DOM 247..268
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT INTRAMEM 269..290
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:P35523"
FT TOPO_DOM 291..301
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 302..321
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:P35523"
FT TOPO_DOM 322..347
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 348..376
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:P35523"
FT TOPO_DOM 377..390
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 391..408
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:P35523"
FT TOPO_DOM 409..414
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT INTRAMEM 415..426
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:P35523"
FT TOPO_DOM 427..457
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 458..478
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:P35523"
FT TRANSMEM 479..498
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:P35523"
FT TOPO_DOM 499..521
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT INTRAMEM 522..554
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:P35523"
FT TOPO_DOM 555..557
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 558..578
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:P35523"
FT TOPO_DOM 579..994
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT DOMAIN 609..668
FT /note="CBS 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00703"
FT DOMAIN 827..882
FT /note="CBS 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00703"
FT REGION 37..61
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 710..769
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 880..923
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 965..994
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 188..192
FT /note="Selectivity filter part_1"
FT /evidence="ECO:0000250"
FT MOTIF 230..234
FT /note="Selectivity filter part_2"
FT /evidence="ECO:0000250"
FT MOTIF 482..486
FT /note="Selectivity filter part_3"
FT /evidence="ECO:0000250"
FT COMPBIAS 723..757
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 189
FT /ligand="chloride"
FT /ligand_id="ChEBI:CHEBI:17996"
FT /evidence="ECO:0000250|UniProtKB:P37019"
FT BINDING 484
FT /ligand="chloride"
FT /ligand_id="ChEBI:CHEBI:17996"
FT /evidence="ECO:0000250|UniProtKB:P37019"
FT BINDING 578
FT /ligand="chloride"
FT /ligand_id="ChEBI:CHEBI:17996"
FT /evidence="ECO:0000250|UniProtKB:P37019"
FT MOD_RES 892
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
SQ SEQUENCE 994 AA; 110073 MW; DCDDCD0D26E48FAE CRC64;
MERSQSQQHG GEQSWWGTAP QYQYMPFEHC TSYGLPSENG GLQHRPRKDL GPRHNAHPTQ
IYGHHKEQYS YQAQDRGIPK KTDSSSTVDS LDEDHYSKCQ DCVHRLGRVL RRKLGEDWIF
LVLLGLLMAL VSWCMDYVSA KSLQAYKWTY AQMQPSLPLQ YLAWVTFPLI LILFSALFCQ
LISPQAVGSG IPEMKTILRG VVLKEYLTLK AFVAKVVALT AGLGSGIPVG KEGPFVHIAS
ICAAVLSKFM SMFSGVYEQP YYYTDILTVG CAVGVGCCFG TPLGGVLFSI EVTSTYFAVR
NYWRGFFAAT FSAFVFRVLA VWNKDAVTIT ALFRTNFRMD FPFDLKELPA FAVIGICCGF
LGAVFVYLHR QVMLGVRKHK ALSQFLAKHR LLYPGIVTFV IASLTFPPGM GQFMAGELMP
REAISTLFDN NTWVKHIGDP KSLGQSAVWI HPQVNVVIII LLFFVMKFWM SIVATTMPIP
CGGFMPVFVL GAAFGRLVGE IMAMLFPEGI LFDDIIYKIL PGGYAVIGAA ALTGAVSHTV
STAVICFELT GQIAHILPMM VAVILANMVA QSLQPSLYDS IIQVKKLPYL PDLGWNQLSK
FTIFVEDIMV RDVKFVSASC TYGELRNLLQ TTTVKTLPLV DSKDSMILLG SVERSELQSL
LQRHLCAERR LKAAQDMARK LSELPYNGQA QLAGEWHPGG RPESFAFVDE DEDEDVSRKT
ELPQTPTPPP PPPPPLPPQF PIAPSYPEEP NGPLPSHKQP PEASDSADQR SSIFQRLLHC
LLGKAHSTKK KITQDSTDLV DNMSPEEIEA WEREQLSQPV CFDFCCIDQS PFQLVEQTTL
HKTHTLFSLL GLHLAYVTSM GKLRGVLALE ELQKAIKGHT KSGVQLRPPL ASFRNTTSIR
KTPGGPPPPA ESWNVPEGED GAPEREVMVP TMPETPVPPP SPEVPSCLAP ARVEGELEEL
EMVGNLGPEE DLADILHGPS LRSTDEEDED ELIL
