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P51795

- CLCN5_HUMAN

UniProt

P51795 - CLCN5_HUMAN

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Protein

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

Gene
CLCN5, CLCK2
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

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 – 1681Chloride By similarity
Sitei211 – 2111Mediates proton transfer from the outer aqueous phase to the interior of the protein; involved in linking H(+) and Cl(-) transport By similarity
Sitei268 – 2681Mediates proton transfer from the protein to the inner aqueous phase By similarity
Binding sitei455 – 4551Chloride; via amide nitrogen By similarity
Binding sitei558 – 5581Chloride By 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
Complete GO annotation...

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

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 5454Cytoplasmic By similarityAdd
BLAST
Transmembranei55 – 9238Helical; By similarityAdd
BLAST
Transmembranei138 – 16124Helical; By similarityAdd
BLAST
Intramembranei170 – 1778Helical; By similarity
Transmembranei186 – 20520Helical; By similarityAdd
BLAST
Transmembranei211 – 23020Helical; By similarityAdd
BLAST
Intramembranei242 – 25413Helical; By similarityAdd
BLAST
Intramembranei258 – 2669Helical; By similarity
Transmembranei278 – 29619Helical; By similarityAdd
BLAST
Transmembranei319 – 34527Helical; By similarityAdd
BLAST
Transmembranei352 – 37221Helical; By similarityAdd
BLAST
Transmembranei428 – 44821Helical; By similarityAdd
BLAST
Transmembranei453 – 47220Helical; By similarityAdd
BLAST
Intramembranei500 – 51415Helical; By similarityAdd
BLAST
Intramembranei515 – 5173Note=Loop between two helices; By similarity
Intramembranei518 – 52912Helical; By similarityAdd
BLAST
Intramembranei530 – 5345Note=Loop between two helices; By similarity
Transmembranei535 – 55218Helical; By similarityAdd
BLAST
Topological domaini553 – 746194Cytoplasmic By similarityAdd
BLAST

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
Complete GO annotation...

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.
Note: The disease is caused by mutations affecting the gene represented in this entry.2 Publications
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. 6 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.
Note: The disease is caused by mutations affecting the gene represented in this entry.13 Publications
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. 3 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. 2 Publications
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. 2 Publications
VAR_065594
Natural varianti221 – 2211C → R in NPHL2; retained in the endoplasmic reticulum; improperly N-glycosylated and non-functional. 2 Publications
VAR_065595
Natural varianti225 – 2251L → P in NPHL2; retained in the endoplasmic reticulum; improperly N-glycosylated and non-functional. 1 Publication
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. 4 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. 2 Publications
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. 2 Publications
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. 2 Publications
VAR_065604
Natural varianti340 – 3401N → K in NPHL2; retained in the endoplasmic reticulum; improperly N-glycosylated and non-functional. 2 Publications
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. 1 Publication
VAR_065608
Natural varianti513 – 5131G → R in NPHL2. 2 Publications
VAR_065609
Natural varianti516 – 5161R → W in NPHL2; causes retention in the endoplasmic reticulum and alters protein stability; total loss of function. 2 Publications
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. 2 Publications
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. 2 Publications
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. 2 Publications
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.
Note: The disease is caused by mutations affecting the gene represented in this entry.1 Publication
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.
Note: The disease is caused by mutations affecting the gene represented in this entry.3 Publications
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti280 – 2801R → P in LMWPHN; 70% reduction in chloride transport activity and alters targeting to endosomes. 2 Publications
VAR_001619
Natural varianti524 – 5241I → K in LMWPHN; causes retention in the endoplasmic reticulum and alters protein stability; total loss of function. 2 Publications
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.

Miscellaneous databases

EvolutionaryTraceiP51795.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini586 – 65065CBS 1Add
BLAST
Domaini682 – 74261CBS 2Add
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi167 – 1715Selectivity filter part_1 By similarity
Motifi209 – 2135Selectivity filter part_2 By similarity
Motifi453 – 4575Selectivity filter part_3 By similarity

Sequence similaritiesi

Contains 2 CBS domains.

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

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. 3 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. 2 Publications
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. 2 Publications
VAR_065594
Natural varianti221 – 2211C → R in NPHL2; retained in the endoplasmic reticulum; improperly N-glycosylated and non-functional. 2 Publications
VAR_065595
Natural varianti225 – 2251L → P in NPHL2; retained in the endoplasmic reticulum; improperly N-glycosylated and non-functional. 1 Publication
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. 6 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. 4 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. 2 Publications
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. 2 Publications
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. 2 Publications
VAR_065604
Natural varianti280 – 2801R → P in LMWPHN; 70% reduction in chloride transport activity and alters targeting to endosomes. 2 Publications
VAR_001619
Natural varianti340 – 3401N → K in NPHL2; retained in the endoplasmic reticulum; improperly N-glycosylated and non-functional. 2 Publications
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. 1 Publication
VAR_065608
Natural varianti513 – 5131G → R in NPHL2. 2 Publications
VAR_065609
Natural varianti516 – 5161R → W in NPHL2; causes retention in the endoplasmic reticulum and alters protein stability; total loss of function. 2 Publications
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. 2 Publications
VAR_065611
Natural varianti527 – 5271E → D in NPHL2; abolishes the chloride currents; total loss of function. 2 Publications
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. 2 Publications
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. 2 Publications
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. VSP_042046

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti732 – 7321I → V in BAG51748. 1 Publication

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]
ENST00000594930; ENSP00000470026; ENSG00000269240. [P51795-2]
ENST00000598870; ENSP00000469532; ENSG00000269240. [P51795-1]
ENST00000600725; ENSP00000470125; ENSG00000269240. [P51795-2]
ENST00000601418; ENSP00000471330; ENSG00000269240. [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 ]
ENST00000594930 ; ENSP00000470026 ; ENSG00000269240 . [P51795-2 ]
ENST00000598870 ; ENSP00000469532 ; ENSG00000269240 . [P51795-1 ]
ENST00000600725 ; ENSP00000470125 ; ENSG00000269240 . [P51795-2 ]
ENST00000601418 ; ENSP00000471330 ; ENSG00000269240 . [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

« Hide 'large scale' publications
  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: September 3, 2014
This is version 143 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

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