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P51795

- CLCN5_HUMAN

UniProt

P51795 - CLCN5_HUMAN

Protein

H(+)/Cl(-) exchange transporter 5

Gene

CLCN5

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 144 (01 Oct 2014)
      Sequence version 1 (01 Oct 1996)
      Previous versions | rss
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    Functioni

    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.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei168 – 1681ChlorideBy similarity
    Sitei211 – 2111Mediates proton transfer from the outer aqueous phase to the interior of the protein; involved in linking H(+) and Cl(-) transportBy similarity
    Sitei268 – 2681Mediates proton transfer from the protein to the inner aqueous phaseBy similarity
    Binding sitei455 – 4551Chloride; via amide nitrogenBy similarity
    Binding sitei558 – 5581ChlorideBy similarity
    Binding sitei596 – 5961ATP; via amide nitrogen and carbonyl oxygen

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi617 – 6193ATP
    Nucleotide bindingi724 – 7274ATP

    GO - Molecular functioni

    1. antiporter activity Source: UniProtKB-KW
    2. ATP binding Source: UniProtKB-KW
    3. chloride channel activity Source: ProtInc
    4. voltage-gated chloride channel activity Source: Ensembl

    GO - Biological processi

    1. chloride transmembrane transport Source: GOC
    2. endocytosis Source: Ensembl
    3. excretion Source: ProtInc
    4. ion transmembrane transport Source: Reactome
    5. transmembrane transport Source: Reactome
    6. transport Source: ProtInc

    Keywords - Biological processi

    Antiport, Ion transport, Transport

    Keywords - Ligandi

    ATP-binding, Chloride, Nucleotide-binding

    Enzyme and pathway databases

    ReactomeiREACT_160189. Stimuli-sensing channels.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    H(+)/Cl(-) exchange transporter 5
    Alternative name(s):
    Chloride channel protein 5
    Short name:
    ClC-5
    Chloride transporter ClC-5
    Gene namesi
    Name:CLCN5
    Synonyms:CLCK2
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome X

    Organism-specific databases

    HGNCiHGNC:2023. CLCN5.

    Subcellular locationi

    Golgi apparatus membrane 1 Publication; Multi-pass membrane protein 1 Publication. Endosome membrane 1 Publication; Multi-pass membrane protein 1 Publication. Cell membrane 1 Publication; Multi-pass membrane protein 1 Publication

    GO - Cellular componenti

    1. apical part of cell Source: UniProtKB
    2. endosome membrane Source: Reactome
    3. Golgi membrane Source: UniProtKB-SubCell
    4. integral component of plasma membrane Source: ProtInc
    5. lysosomal membrane Source: UniProtKB
    6. membrane Source: UniProtKB

    Keywords - Cellular componenti

    Cell membrane, Endosome, Golgi apparatus, Membrane

    Pathology & Biotechi

    Involvement in diseasei

    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.1 Publication
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti244 – 2441S → 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. 5 Publications
    VAR_001618
    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.11 Publications
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti30 – 301R → RH in NPHL2. 1 Publication
    VAR_001615
    Natural varianti57 – 571G → V in NPHL2; alters targeting to endosomes. 2 Publications
    VAR_001616
    Natural varianti179 – 1791G → D in NPHL2; retained in the endoplasmic reticulum; improperly N-glycosylated and non-functional. 1 Publication
    VAR_065591
    Natural varianti200 – 2001L → R in NPHL2; retained in the endoplasmic reticulum; improperly N-glycosylated and non-functional. 1 Publication
    VAR_001617
    Natural varianti203 – 2031S → L in NPHL2; retained in the endoplasmic reticulum; improperly N-glycosylated and non-functional. 1 Publication
    VAR_065592
    Natural varianti212 – 2121G → 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. 1 Publication
    VAR_065593
    Natural varianti219 – 2191C → R in NPHL2; retained in the endoplasmic reticulum; improperly N-glycosylated and non-functional. 1 Publication
    VAR_065594
    Natural varianti221 – 2211C → R in NPHL2; retained in the endoplasmic reticulum; improperly N-glycosylated and non-functional. 1 Publication
    VAR_065595
    Natural varianti225 – 2251L → P in NPHL2; retained in the endoplasmic reticulum; improperly N-glycosylated and non-functional.
    VAR_065596
    Natural varianti260 – 2601G → 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. 3 Publications
    VAR_065597
    Natural varianti267 – 2671E → A in NPHL2. 1 Publication
    VAR_065598
    Natural varianti267 – 2671Missing in NPHL2. 1 Publication
    VAR_065599
    Natural varianti270 – 2701S → G in NPHL2. 1 Publication
    VAR_065600
    Natural varianti270 – 2701S → R in NPHL2; retained in the endoplasmic reticulum; alters protein stability; associated with an abolition of chloride current. 1 Publication
    VAR_065601
    Natural varianti272 – 2721Y → 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. 1 Publication
    VAR_065602
    Natural varianti273 – 2731F → L in NPHL2. 1 Publication
    VAR_065603
    Natural varianti278 – 2781L → 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. 1 Publication
    VAR_065604
    Natural varianti340 – 3401N → K in NPHL2; retained in the endoplasmic reticulum; improperly N-glycosylated and non-functional. 1 Publication
    VAR_065605
    Natural varianti462 – 4621G → D in NPHL2. 1 Publication
    VAR_065606
    Natural varianti469 – 4691L → P in NPHL2; retained in the endoplasmic reticulum; improperly N-glycosylated and non-functional. 1 Publication
    VAR_065607
    Natural varianti512 – 5121G → R in NPHL2; abolishes the chloride currents. 1 Publication
    VAR_001621
    Natural varianti513 – 5131G → E in NPHL2; causes retention in the endoplasmic reticulum and alters protein stability; total loss of function.
    VAR_065608
    Natural varianti513 – 5131G → R in NPHL2. 1 Publication
    VAR_065609
    Natural varianti516 – 5161R → W in NPHL2; causes retention in the endoplasmic reticulum and alters protein stability; total loss of function. 1 Publication
    VAR_065610
    Natural varianti520 – 5201S → P in NPHL2. 1 Publication
    VAR_001622
    Natural varianti527 – 5271E → D in NPHL2; abolishes the chloride currents; total loss of function. 1 Publication
    VAR_001623
    Natural varianti545 – 5451S → N in NPHL2. 1 Publication
    VAR_065612
    Natural varianti546 – 5461K → 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. 1 Publication
    VAR_065613
    Natural varianti547 – 5471W → 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. 1 Publication
    VAR_065614
    Natural varianti657 – 6571T → S in NPHL2. 1 Publication
    Corresponds to variant rs144207967 [ dbSNP | Ensembl ].
    VAR_065615
    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.1 Publication
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti506 – 5061G → E in NPHL1. 1 Publication
    VAR_001620
    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.2 Publications
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti280 – 2801R → P in LMWPHN; 70% reduction in chloride transport activity and alters targeting to endosomes. 1 Publication
    VAR_001619
    Natural varianti524 – 5241I → K in LMWPHN; causes retention in the endoplasmic reticulum and alters protein stability; total loss of function. 1 Publication
    VAR_065611

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi211 – 2111E → A: Abolishes proton transport, but not chloride transport. 1 Publication
    Mutagenesisi617 – 6171Y → A: Strongly decreased affinity for ATP, but no effect on chloride transport. 1 Publication
    Mutagenesisi618 – 6181S → A: No effect ATP binding or chloride transport. 1 Publication
    Mutagenesisi672 – 6721Y → A: Abolishes interaction with NEDD4 and NEDD4L. 1 Publication
    Mutagenesisi727 – 7271D → A: Strongly decreased affinity for ATP, but no effect on chloride transport. 1 Publication

    Keywords - Diseasei

    Disease mutation

    Organism-specific databases

    MIMi300009. phenotype.
    300554. phenotype.
    308990. phenotype.
    310468. phenotype.
    Orphaneti93622. Dent disease type 1.
    PharmGKBiPA26550.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 746746H(+)/Cl(-) exchange transporter 5PRO_0000094446Add
    BLAST

    Post-translational modificationi

    Ubiquitinated by NEDD4L in the presence of albumin; which promotes endocytosis and proteasomal degradation.1 Publication

    Keywords - PTMi

    Ubl conjugation

    Proteomic databases

    MaxQBiP51795.
    PaxDbiP51795.
    PRIDEiP51795.

    Expressioni

    Tissue specificityi

    Kidney. Moderately expressed in aortic vascular smooth muscle and endothelial cells, and at a slightly higher level in the coronary vascular smooth muscle.1 Publication

    Gene expression databases

    BgeeiP51795.
    CleanExiHS_CLCN5.
    GenevestigatoriP51795.

    Organism-specific databases

    HPAiHPA000401.

    Interactioni

    Subunit structurei

    Interacts with NEDD4 and NEDD4L.1 Publication

    Protein-protein interaction databases

    BioGridi107598. 3 interactions.
    DIPiDIP-29263N.
    MINTiMINT-1524912.
    STRINGi9606.ENSP00000365256.

    Structurei

    Secondary structure

    1
    746
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi582 – 5854
    Beta strandi586 – 5883
    Beta strandi598 – 6014
    Helixi605 – 61410
    Beta strandi618 – 6247
    Turni626 – 6283
    Beta strandi630 – 6367
    Helixi637 – 64812
    Beta strandi659 – 6613
    Beta strandi663 – 6653
    Helixi680 – 6823
    Beta strandi683 – 6864
    Beta strandi689 – 6913
    Helixi696 – 70611
    Beta strandi709 – 7157
    Beta strandi718 – 7247
    Helixi725 – 73511

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2J9LX-ray2.30A/B/C/D/E/F571-746[»]
    2JA3X-ray3.05A/B/C/D/E/F571-746[»]
    ProteinModelPortaliP51795.
    SMRiP51795. Positions 124-737.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP51795.

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini1 – 5454CytoplasmicBy similarityAdd
    BLAST
    Topological domaini553 – 746194CytoplasmicBy similarityAdd
    BLAST

    Intramembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Intramembranei170 – 1778HelicalBy similarity
    Intramembranei242 – 25413HelicalBy similarityAdd
    BLAST
    Intramembranei258 – 2669HelicalBy similarity
    Intramembranei500 – 51415HelicalBy similarityAdd
    BLAST
    Intramembranei515 – 5173Note=Loop between two helicesBy similarity
    Intramembranei518 – 52912HelicalBy similarityAdd
    BLAST
    Intramembranei530 – 5345Note=Loop between two helicesBy similarity

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei55 – 9238HelicalBy similarityAdd
    BLAST
    Transmembranei138 – 16124HelicalBy similarityAdd
    BLAST
    Transmembranei186 – 20520HelicalBy similarityAdd
    BLAST
    Transmembranei211 – 23020HelicalBy similarityAdd
    BLAST
    Transmembranei278 – 29619HelicalBy similarityAdd
    BLAST
    Transmembranei319 – 34527HelicalBy similarityAdd
    BLAST
    Transmembranei352 – 37221HelicalBy similarityAdd
    BLAST
    Transmembranei428 – 44821HelicalBy similarityAdd
    BLAST
    Transmembranei453 – 47220HelicalBy similarityAdd
    BLAST
    Transmembranei535 – 55218HelicalBy similarityAdd
    BLAST

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini586 – 65065CBS 1PROSITE-ProRule annotationAdd
    BLAST
    Domaini682 – 74261CBS 2PROSITE-ProRule annotationAdd
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi167 – 1715Selectivity filter part_1By similarity
    Motifi209 – 2135Selectivity filter part_2By similarity
    Motifi453 – 4575Selectivity filter part_3By similarity

    Sequence similaritiesi

    Contains 2 CBS domains.PROSITE-ProRule annotation

    Keywords - Domaini

    CBS domain, Repeat, Transmembrane, Transmembrane helix

    Phylogenomic databases

    eggNOGiCOG0038.
    HOGENOMiHOG000164493.
    HOVERGENiHBG050984.
    InParanoidiP51795.
    KOiK05012.
    OMAiLMDIPGT.
    OrthoDBiEOG7MWGXT.
    PhylomeDBiP51795.
    TreeFamiTF313867.

    Family and domain databases

    Gene3Di1.10.3080.10. 3 hits.
    InterProiIPR000644. CBS_dom.
    IPR014743. Cl-channel_core.
    IPR001807. Cl-channel_volt-gated.
    IPR002247. Cl_channel-5.
    [Graphical view]
    PfamiPF00571. CBS. 2 hits.
    PF00654. Voltage_CLC. 1 hit.
    [Graphical view]
    PRINTSiPR00762. CLCHANNEL.
    PR01116. CLCHANNEL5.
    SMARTiSM00116. CBS. 2 hits.
    [Graphical view]
    SUPFAMiSSF81340. SSF81340. 3 hits.
    PROSITEiPS51371. CBS. 2 hits.
    [Graphical view]

    Sequences (2)i

    Sequence statusi: Complete.

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: P51795-1) [UniParc]FASTAAdd to Basket

    This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

    « Hide

    MDFLEEPIPG VGTYDDFNTI DWVREKSRDR DRHREITNKS KESTWALIHS    50
    VSDAFSGWLL MLLIGLLSGS LAGLIDISAH WMTDLKEGIC TGGFWFNHEH 100
    CCWNSEHVTF EERDKCPEWN SWSQLIISTD EGAFAYIVNY FMYVLWALLF 150
    AFLAVSLVKV FAPYACGSGI PEIKTILSGF IIRGYLGKWT LVIKTITLVL 200
    AVSSGLSLGK EGPLVHVACC CGNILCHCFN KYRKNEAKRR EVLSAAAAAG 250
    VSVAFGAPIG GVLFSLEEVS YYFPLKTLWR SFFAALVAAF TLRSINPFGN 300
    SRLVLFYVEF HTPWHLFELV PFILLGIFGG LWGALFIRTN IAWCRKRKTT 350
    QLGKYPVIEV LVVTAITAIL AFPNEYTRMS TSELISELFN DCGLLDSSKL 400
    CDYENRFNTS KGGELPDRPA GVGVYSAMWQ LALTLILKIV ITIFTFGMKI 450
    PSGLFIPSMA VGAIAGRLLG VGMEQLAYYH QEWTVFNSWC SQGADCITPG 500
    LYAMVGAAAC LGGVTRMTVS LVVIMFELTG GLEYIVPLMA AAMTSKWVAD 550
    ALGREGIYDA HIRLNGYPFL EAKEEFAHKT LAMDVMKPRR NDPLLTVLTQ 600
    DSMTVEDVET IISETTYSGF PVVVSRESQR LVGFVLRRDL IISIENARKK 650
    QDGVVSTSII YFTEHSPPLP PYTPPTLKLR NILDLSPFTV TDLTPMEIVV 700
    DIFRKLGLRQ CLVTHNGRLL GIITKKDVLK HIAQMANQDP DSILFN 746
    Length:746
    Mass (Da):83,147
    Last modified:October 1, 1996 - v1
    Checksum:iEF913C5BA40C85D8
    GO
    Isoform 2 (identifier: P51795-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-1: M → MAMWQGAMDNRGFQQGSFSSFQNSSSDEDLMDIPATAMDFSMRDDVPPLDREVGEDKSYNGGGIGSSNRIM

    Show »
    Length:816
    Mass (Da):90,785
    Checksum:iC9C63CC222959F35
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti732 – 7321I → V in BAG51748. (PubMed:14702039)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti30 – 301R → RH in NPHL2. 1 Publication
    VAR_001615
    Natural varianti57 – 571G → V in NPHL2; alters targeting to endosomes. 2 Publications
    VAR_001616
    Natural varianti142 – 1421M → I.
    Corresponds to variant rs34800648 [ dbSNP | Ensembl ].
    VAR_048694
    Natural varianti179 – 1791G → D in NPHL2; retained in the endoplasmic reticulum; improperly N-glycosylated and non-functional. 1 Publication
    VAR_065591
    Natural varianti200 – 2001L → R in NPHL2; retained in the endoplasmic reticulum; improperly N-glycosylated and non-functional. 1 Publication
    VAR_001617
    Natural varianti203 – 2031S → L in NPHL2; retained in the endoplasmic reticulum; improperly N-glycosylated and non-functional. 1 Publication
    VAR_065592
    Natural varianti212 – 2121G → 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. 1 Publication
    VAR_065593
    Natural varianti219 – 2191C → R in NPHL2; retained in the endoplasmic reticulum; improperly N-glycosylated and non-functional. 1 Publication
    VAR_065594
    Natural varianti221 – 2211C → R in NPHL2; retained in the endoplasmic reticulum; improperly N-glycosylated and non-functional. 1 Publication
    VAR_065595
    Natural varianti225 – 2251L → P in NPHL2; retained in the endoplasmic reticulum; improperly N-glycosylated and non-functional.
    VAR_065596
    Natural varianti244 – 2441S → 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. 5 Publications
    VAR_001618
    Natural varianti260 – 2601G → 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. 3 Publications
    VAR_065597
    Natural varianti267 – 2671E → A in NPHL2. 1 Publication
    VAR_065598
    Natural varianti267 – 2671Missing in NPHL2. 1 Publication
    VAR_065599
    Natural varianti270 – 2701S → G in NPHL2. 1 Publication
    VAR_065600
    Natural varianti270 – 2701S → R in NPHL2; retained in the endoplasmic reticulum; alters protein stability; associated with an abolition of chloride current. 1 Publication
    VAR_065601
    Natural varianti272 – 2721Y → 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. 1 Publication
    VAR_065602
    Natural varianti273 – 2731F → L in NPHL2. 1 Publication
    VAR_065603
    Natural varianti278 – 2781L → 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. 1 Publication
    VAR_065604
    Natural varianti280 – 2801R → P in LMWPHN; 70% reduction in chloride transport activity and alters targeting to endosomes. 1 Publication
    VAR_001619
    Natural varianti340 – 3401N → K in NPHL2; retained in the endoplasmic reticulum; improperly N-glycosylated and non-functional. 1 Publication
    VAR_065605
    Natural varianti462 – 4621G → D in NPHL2. 1 Publication
    VAR_065606
    Natural varianti469 – 4691L → P in NPHL2; retained in the endoplasmic reticulum; improperly N-glycosylated and non-functional. 1 Publication
    VAR_065607
    Natural varianti506 – 5061G → E in NPHL1. 1 Publication
    VAR_001620
    Natural varianti512 – 5121G → R in NPHL2; abolishes the chloride currents. 1 Publication
    VAR_001621
    Natural varianti513 – 5131G → E in NPHL2; causes retention in the endoplasmic reticulum and alters protein stability; total loss of function.
    VAR_065608
    Natural varianti513 – 5131G → R in NPHL2. 1 Publication
    VAR_065609
    Natural varianti516 – 5161R → W in NPHL2; causes retention in the endoplasmic reticulum and alters protein stability; total loss of function. 1 Publication
    VAR_065610
    Natural varianti520 – 5201S → P in NPHL2. 1 Publication
    VAR_001622
    Natural varianti524 – 5241I → K in LMWPHN; causes retention in the endoplasmic reticulum and alters protein stability; total loss of function. 1 Publication
    VAR_065611
    Natural varianti527 – 5271E → D in NPHL2; abolishes the chloride currents; total loss of function. 1 Publication
    VAR_001623
    Natural varianti545 – 5451S → N in NPHL2. 1 Publication
    VAR_065612
    Natural varianti546 – 5461K → 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. 1 Publication
    VAR_065613
    Natural varianti547 – 5471W → 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. 1 Publication
    VAR_065614
    Natural varianti657 – 6571T → S in NPHL2. 1 Publication
    Corresponds to variant rs144207967 [ dbSNP | Ensembl ].
    VAR_065615

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 11M → MAMWQGAMDNRGFQQGSFSS FQNSSSDEDLMDIPATAMDF SMRDDVPPLDREVGEDKSYN GGGIGSSNRIM in isoform 2. 1 PublicationVSP_042046

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X91906 mRNA. Translation: CAA63000.1.
    AK056560 mRNA. Translation: BAG51748.1.
    FO393402 Genomic DNA. No translation available.
    BC130429 mRNA. Translation: AAI30430.1.
    BC130431 mRNA. Translation: AAI30432.1.
    X81836 mRNA. Translation: CAA57430.1.
    BK000969 mRNA. Translation: DAA01544.1.
    CCDSiCCDS14328.1. [P51795-1]
    CCDS48115.1. [P51795-2]
    PIRiI37277.
    RefSeqiNP_000075.1. NM_000084.4. [P51795-1]
    NP_001121370.1. NM_001127898.3. [P51795-2]
    NP_001121371.1. NM_001127899.3. [P51795-2]
    NP_001269092.1. NM_001282163.1.
    UniGeneiHs.166486.
    Hs.745501.

    Genome annotation databases

    EnsembliENST00000307367; ENSP00000304257; ENSG00000171365. [P51795-1]
    ENST00000376088; ENSP00000365256; ENSG00000171365. [P51795-2]
    ENST00000376091; ENSP00000365259; ENSG00000171365. [P51795-2]
    ENST00000376108; ENSP00000365276; ENSG00000171365. [P51795-1]
    GeneIDi1184.
    KEGGihsa:1184.
    UCSCiuc004doq.1. human. [P51795-2]
    uc004dos.1. human. [P51795-1]

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X91906 mRNA. Translation: CAA63000.1 .
    AK056560 mRNA. Translation: BAG51748.1 .
    FO393402 Genomic DNA. No translation available.
    BC130429 mRNA. Translation: AAI30430.1 .
    BC130431 mRNA. Translation: AAI30432.1 .
    X81836 mRNA. Translation: CAA57430.1 .
    BK000969 mRNA. Translation: DAA01544.1 .
    CCDSi CCDS14328.1. [P51795-1 ]
    CCDS48115.1. [P51795-2 ]
    PIRi I37277.
    RefSeqi NP_000075.1. NM_000084.4. [P51795-1 ]
    NP_001121370.1. NM_001127898.3. [P51795-2 ]
    NP_001121371.1. NM_001127899.3. [P51795-2 ]
    NP_001269092.1. NM_001282163.1.
    UniGenei Hs.166486.
    Hs.745501.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2J9L X-ray 2.30 A/B/C/D/E/F 571-746 [» ]
    2JA3 X-ray 3.05 A/B/C/D/E/F 571-746 [» ]
    ProteinModelPortali P51795.
    SMRi P51795. Positions 124-737.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 107598. 3 interactions.
    DIPi DIP-29263N.
    MINTi MINT-1524912.
    STRINGi 9606.ENSP00000365256.

    Proteomic databases

    MaxQBi P51795.
    PaxDbi P51795.
    PRIDEi P51795.

    Protocols and materials databases

    DNASUi 1184.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000307367 ; ENSP00000304257 ; ENSG00000171365 . [P51795-1 ]
    ENST00000376088 ; ENSP00000365256 ; ENSG00000171365 . [P51795-2 ]
    ENST00000376091 ; ENSP00000365259 ; ENSG00000171365 . [P51795-2 ]
    ENST00000376108 ; ENSP00000365276 ; ENSG00000171365 . [P51795-1 ]
    GeneIDi 1184.
    KEGGi hsa:1184.
    UCSCi uc004doq.1. human. [P51795-2 ]
    uc004dos.1. human. [P51795-1 ]

    Organism-specific databases

    CTDi 1184.
    GeneCardsi GC0XP049687.
    GeneReviewsi CLCN5.
    HGNCi HGNC:2023. CLCN5.
    HPAi HPA000401.
    MIMi 300008. gene.
    300009. phenotype.
    300554. phenotype.
    308990. phenotype.
    310468. phenotype.
    neXtProti NX_P51795.
    Orphaneti 93622. Dent disease type 1.
    PharmGKBi PA26550.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG0038.
    HOGENOMi HOG000164493.
    HOVERGENi HBG050984.
    InParanoidi P51795.
    KOi K05012.
    OMAi LMDIPGT.
    OrthoDBi EOG7MWGXT.
    PhylomeDBi P51795.
    TreeFami TF313867.

    Enzyme and pathway databases

    Reactomei REACT_160189. Stimuli-sensing channels.

    Miscellaneous databases

    EvolutionaryTracei P51795.
    GeneWikii CLCN5.
    GenomeRNAii 1184.
    NextBioi 4894.
    PROi P51795.
    SOURCEi Search...

    Gene expression databases

    Bgeei P51795.
    CleanExi HS_CLCN5.
    Genevestigatori P51795.

    Family and domain databases

    Gene3Di 1.10.3080.10. 3 hits.
    InterProi IPR000644. CBS_dom.
    IPR014743. Cl-channel_core.
    IPR001807. Cl-channel_volt-gated.
    IPR002247. Cl_channel-5.
    [Graphical view ]
    Pfami PF00571. CBS. 2 hits.
    PF00654. Voltage_CLC. 1 hit.
    [Graphical view ]
    PRINTSi PR00762. CLCHANNEL.
    PR01116. CLCHANNEL5.
    SMARTi SM00116. CBS. 2 hits.
    [Graphical view ]
    SUPFAMi SSF81340. SSF81340. 3 hits.
    PROSITEi PS51371. CBS. 2 hits.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Cloning and characterization of CLCN5, the human kidney chloride channel gene implicated in Dent disease (an X-linked hereditary nephrolithiasis)."
      Fisher S.E., van Bakel I., Lloyd S.E., Pearce S.H.S., Thakker R.V., Craig I.W.
      Genomics 29:598-606(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
      Tissue: Kidney.
    2. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
      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.
      Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
    3. "The DNA sequence of the human X chromosome."
      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.
      Nature 434:325-337(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    4. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
      The MGC Project Team
      Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    5. "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)."
      Fisher S., Black G.C.M., Lloyd S.E., Hatchwell E., Wrong O., Thakker R.V., Craig I.W.
      Hum. Mol. Genet. 3:2053-2059(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 487-746.
      Tissue: Kidney.
    6. "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."
      Ludwig M., Waldegger S., Nuutinen M., Bokenkamp A., Reissinger A., Steckelbroeck S., Utsch B.
      Kidney Blood Press. Res. 26:176-184(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION (ISOFORM 2), ALTERNATIVE SPLICING.
    7. "Expression of CLCN voltage-gated chloride channel genes in human blood vessels."
      Lamb F.S., Clayton G.H., Liu B.-X., Smith R.L., Barna T.J., Schutte B.C.
      J. Mol. Cell. Cardiol. 31:657-666(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: TISSUE SPECIFICITY.
      Tissue: Aortic endothelium and Vascular smooth muscle.
    8. "Nedd4-2 functionally interacts with ClC-5: involvement in constitutive albumin endocytosis in proximal tubule cells."
      Hryciw D.H., Ekberg J., Lee A., Lensink I.L., Kumar S., Guggino W.B., Cook D.I., Pollock C.A., Poronnik P.
      J. Biol. Chem. 279:54996-55007(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH NEDD4 AND NEDD4L, UBIQUITINATION, MUTAGENESIS OF TYR-672.
    9. "Nucleotide recognition by the cytoplasmic domain of the human chloride transporter ClC-5."
      Meyer S., Savaresi S., Forster I.C., Dutzler R.
      Nat. Struct. Mol. Biol. 14:60-67(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 570-746 IN COMPLEXES WITH ATP AND ADP, MUTAGENESIS OF GLU-211; TYR-617; SER-618 AND ASP-727.
    10. Cited for: VARIANT XLRHR LEU-244, VARIANT NPHL1 GLU-506, VARIANTS NPHL2 ARG-200 AND PRO-520.
    11. "A second family with XLRH displays the mutation S244L in the CLCN5 gene."
      Oudet C., Martin-Coignard D., Pannetier S., Praud E., Champion G., Hanauer A.
      Hum. Genet. 99:781-784(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT NPHL2 LEU-244.
    12. "Characterisation of renal chloride channel, CLCN5, mutations in hypercalciuric nephrolithiasis (kidney stones) disorders."
      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.
      Hum. Mol. Genet. 6:1233-1239(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS NPHL2 HIS-30 INS; VAL-57; ARG-512 AND ASP-527.
    13. "Idiopathic low molecular weight proteinuria associated with hypercalciuric nephrocalcinosis in Japanese children is due to mutations of the renal chloride channel (CLCN5)."
      Lloyd S.E., Pearce S.H.S., Guenther W., Kawaguchi H., Igarashi T., Jentsch T.J., Thakker R.V.
      J. Clin. Invest. 99:967-974(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT LMWPHN PRO-280.
    14. "X-linked recessive nephrolithiasis: presentation and diagnosis in children."
      Schurman S.J., Norden A.G., Scheinman S.J.
      J. Pediatr. 132:859-862(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT NPHL2 VAL-57.
    15. "Functional characterization of renal chloride channel, CLCN5, mutations associated with Dent'sJapan disease."
      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.
      Kidney Int. 54:1850-1856(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS NPHL2 ARG-270 AND PHE-278, CHARACTERIZATION OF VARIANTS NPHL2 ARG-270 AND PHE-278.
    16. "Identification of two novel mutations in the CLCN5 gene in Japanese patients with familial idiopathic low molecular weight proteinuria (Japanese Dent's disease)."
      Takemura T., Hino S., Ikeda M., Okada M., Igarashi T., Inatomi J., Yoshioka K.
      Am. J. Kidney Dis. 37:138-143(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT LMWPHN LYS-524.
    17. Cited for: VARIANTS NPHL2 ARG-221; LEU-244; ALA-267; GLY-270; ASP-462; ARG-513; TRP-516; ASN-545; GLU-546 AND SER-657.
    18. Cited for: VARIANT NPHL2 VAL-260.
    19. Cited for: VARIANTS NPHL2 LEU-244; VAL-260; GLU-267 DEL; CYS-272 AND LYS-340.
    20. "Family history may be misleading in the diagnosis of Dent's disease."
      Anglani F., Bernich P., Tosetto E., Cara M., Lupo A., Nalesso F., D'Angelo A., Gambaro G.
      Urol. Res. 34:61-63(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS NPHL2 LEU-244 AND VAL-260.
    21. "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."
      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.
      J. Hum. Genet. 52:255-261(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS NPHL2 ARG-219; LEU-273 AND GLY-547.
    22. "Characterization of Dent's disease mutations of CLC-5 reveals a correlation between functional and cell biological consequences and protein structure."
      Smith A.J., Reed A.A., Loh N.Y., Thakker R.V., Lippiat J.D.
      Am. J. Physiol. 296:F390-F397(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: CHARACTERIZATION OF VARIANTS NPHL2 VAL-57; ARG-270; GLU-513; TRP-516 AND ASP-527, CHARACTERIZATION OF VARIANTS LMWPHN PRO-280 AND LYS-524, SUBCELLULAR LOCATION.
    23. "Novel CLCN5 mutations in patients with Dent's disease result in altered ion currents or impaired exchanger processing."
      Grand T., Mordasini D., L'Hoste S., Pennaforte T., Genete M., Biyeyeme M.J., Vargas-Poussou R., Blanchard A., Teulon J., Lourdel S.
      Kidney Int. 76:999-1005(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS NPHL2 ASP-179; LEU-203; ALA-212 AND PRO-469, CHARACTERIZATION OF VARIANTS NPHL2 ASP-179; ARG-200; LEU-203; ALA-212; ARG-219; ARG-221 AND PRO-469.
    24. Cited for: CHARACTERIZATION OF VARIANTS NPHL2 PRO-225; VAL-260; CYS-272; PHE-278; LYS-340; ARG-513; GLU-546 AND GLY-547, CHARACTERIZATION OF VARIANT XLRHR LEU-244.

    Entry informationi

    Entry nameiCLCN5_HUMAN
    AccessioniPrimary (citable) accession number: P51795
    Secondary accession number(s): A1L475
    , B3KPN6, Q5JQD5, Q7RTN8
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 1, 1996
    Last sequence update: October 1, 1996
    Last modified: October 1, 2014
    This is version 144 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program
    DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

    Miscellaneousi

    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.

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Human chromosome X
      Human chromosome X: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    6. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3