P51798 (CLCN7_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
H(+)/Cl(-) exchange transporter 7

Alternative name(s):
Chloride channel protein 7
Short name=ClC-7

Gene names

Name:

CLCN7

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	805 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Mediates the exchange of chloride ions against protons. Functions as antiporter and contributes to the acidification of the lysosome lumen. Ref.10
Subcellular location	Lysosome membrane; Multi-pass membrane protein Ref.9 Ref.10.
Tissue specificity	Brain, testis, muscle and kidney.
Involvement in disease	Defects in CLCN7 are the cause of osteopetrosis autosomal recessive type 4 (OPTB4) [MIM:611490]; also known as infantile malignant osteopetrosis type 2. Osteopetrosis is a rare genetic disease characterized by abnormally dense bone, due to defective resorption of immature bone. The disorder occurs in two forms: a severe autosomal recessive form occurring in utero, infancy, or childhood, and a benign autosomal dominant form occurring in adolescence or adulthood. Ref.11 Ref.12 Ref.13 Ref.14 Ref.15 Defects in CLCN7 are the cause of osteopetrosis autosomal dominant type 2 (OPTA2) [MIM:166600]; also known as autosomal dominant Albers-Schonberg disease or marble disease autosomal dominant. Osteopetrosis is a rare genetic disease characterized by abnormally dense bone, due to defective resorption of immature bone. The disorder occurs in two forms: a severe autosomal recessive form occurring in utero, infancy, or childhood, and a benign autosomal dominant form occurring in adolescence or adulthood. OPTA2 is the most common form of osteopetrosis, occurring in adolescence or adulthood. It is characterized by sclerosis, predominantly involving the spine, the pelvis and the skull base.
Miscellaneous	The CLC channel family contains both chloride channels and proton-coupled anion transporters that exchange chloride or another anion for protons. The presence of conserved gating glutamate residues is typical for family members that function as antiporters By similarity.
Sequence similarities	Belongs to the chloride channel (TC 2.A.49) family. ClC-7/CLCN7 subfamily. [View classification] Contains 2 CBS domains.

Ontologies

Keywords
Biological process	Antiport Ion transport Transport
Cellular component	Lysosome Membrane
Coding sequence diversity	Polymorphism
Disease	Disease mutation Osteopetrosis
Domain	CBS domain Repeat Transmembrane Transmembrane helix
Ligand	ATP-binding Chloride Nucleotide-binding
PTM	Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Cellular component	integral to membrane Inferred from electronic annotation. Source: UniProtKB-KW lysosomal membrane Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW antiporter activity Inferred from electronic annotation. Source: UniProtKB-KW voltage-gated chloride channel activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 805	805	H(+)/Cl(-) exchange transporter 7		PRO_0000094452
Regions
	Topological domain	1 – 126	126	Cytoplasmic By similarity
	Transmembrane	127 – 159	33	Helical; By similarity
	Transmembrane	174 – 197	24	Helical; By similarity
	Intramembrane	206 – 213	8	Helical; By similarity
	Transmembrane	223 – 241	19	Helical; By similarity
	Transmembrane	247 – 264	18	Helical; By similarity
	Intramembrane	288 – 300	13	Helical; By similarity
	Intramembrane	304 – 312	9	Helical; By similarity
	Transmembrane	322 – 341	20	Helical; By similarity
	Transmembrane	375 – 405	31	Helical; By similarity
	Transmembrane	410 – 432	23	Helical; By similarity
	Transmembrane	487 – 507	21	Helical; By similarity
	Transmembrane	512 – 535	24	Helical; By similarity
	Intramembrane	545 – 559	15	Helical; By similarity
	Intramembrane	560 – 562	3	Note=Loop between two helices; By similarity
	Intramembrane	563 – 574	12	Helical; By similarity
	Intramembrane	575 – 578	4	Note=Loop between two helices; By similarity
	Transmembrane	579 – 597	19	Helical; By similarity
	Topological domain	598 – 805	208	Cytoplasmic By similarity
	Domain	631 – 695	65	CBS 1
	Domain	741 – 799	59	CBS 2
	Nucleotide binding	658 – 660	3	ATP By similarity
	Nucleotide binding	783 – 786	4	ATP By similarity
	Motif	203 – 207	5	Selectivity filter part_1 By similarity
	Motif	245 – 249	5	Selectivity filter part_2 By similarity
	Motif	512 – 516	5	Selectivity filter part_3 By similarity
Sites
	Binding site	204	1	Chloride By similarity
	Binding site	514	1	Chloride; via amide nitrogen By similarity
	Binding site	602	1	Chloride By similarity
	Site	247	1	Mediates proton transfer from the outer aqueous phase to the interior of the protein; involved in linking H(+) and Cl(-) transport By similarity
	Site	314	1	Mediates proton transfer from the protein to the inner aqueous phase By similarity
Amino acid modifications
	Modified residue	9	1	Phosphoserine Ref.8
	Modified residue	60	1	Phosphoserine Ref.8
	Modified residue	61	1	Phosphoserine Ref.8
Natural variations
	Natural variant	132	1	L → P in OPTB4. Ref.15		VAR_064637
	Natural variant	214	1	N → S in OPTB4. Ref.15		VAR_064638
	Natural variant	215	1	G → R in OPTA2. Ref.13 Ref.15		VAR_020997
	Natural variant	227	1	Missing in OPTB4.		VAR_064639
	Natural variant	240	1	G → R in OPTB4. Ref.13 Ref.15		VAR_020998
	Natural variant	249	1	P → R in OPTB4. Ref.13		VAR_020999
	Natural variant	261	1	I → F in OPTB4. Ref.14		VAR_037427
	Natural variant	286	1	R → Q in OPTA2. Ref.13 Ref.15		VAR_021000
	Natural variant	318	1	F → L in OPTA2. Ref.15		VAR_064640
	Natural variant	332	1	M → V in OPTB4. Ref.13		VAR_021001
	Natural variant	403	1	R → Q in OPTB4. Ref.15		VAR_064641
	Natural variant	418	1	V → M. Ref.13 Corresponds to variant rs12926089 [ dbSNP | Ensembl ].		VAR_021002
	Natural variant	490	1	L → F in OPTA2. Ref.13		VAR_021003
	Natural variant	521	1	G → R in OPTB4. Ref.15		VAR_064642
	Natural variant	526	1	R → Q in OPTB4. Ref.15		VAR_064643
	Natural variant	526	1	R → W in OPTB4. Ref.13 Ref.15		VAR_021004
	Natural variant	549	1	L → P in OPTB4. Ref.15		VAR_064644
	Natural variant	614	1	L → P in OPTB4. Ref.13		VAR_021005
	Natural variant	651	1	L → P in OPTB4. Ref.15		VAR_064645
	Natural variant	677	1	G → V in OPTA2. Ref.13		VAR_021006
	Natural variant	744	1	S → F in OPTB4. Ref.13		VAR_021007
	Natural variant	758	1	F → L in OPTA2. Ref.15		VAR_064646
	Natural variant	762	1	R → Q in OPTA2 and OPTB4; not detected in the fibroblasts from the patient. Ref.11 Ref.15		VAR_017838
	Natural variant	762	1	R → W in OPTB4. Ref.15		VAR_064647
	Natural variant	766	1	L → P in OPTB4. Ref.12		VAR_017839
	Natural variant	767	1	R → P in OPTB4. Ref.15		VAR_064648
	Natural variant	767	1	R → Q in OPTB4. Ref.13		VAR_021008
	Natural variant	767	1	R → W in OPTA2 and OPTB4. Ref.12 Ref.13 Ref.15		VAR_017840
Experimental info
	Sequence conflict	267	1	T → S in CAA91556. Ref.5
	Sequence conflict	279	1	F → L in CAA91556. Ref.5
	Sequence conflict	279	1	F → L in CAA05083. Ref.6

Sequences

	Sequence		Length	Mass (Da)
	P51798 [UniParc]. Last modified January 11, 2001. Version 2. Checksum: E56BC0B4ADE1C695	FASTA	805	88,679
	10 20 30 40 50 60 MANVSKKVSW SGRDRDDEEA APLLRRTARP GGGTPLLNGA GPGAARQSPR SALFRVGHMS 70 80 90 100 110 120 SVELDDELLD PDMDPPHPFP KEIPHNEKLL SLKYESLDYD NSENQLFLEE ERRINHTAFR 130 140 150 160 170 180 TVEIKRWVIC ALIGILTGLV ACFIDIVVEN LAGLKYRVIK GNIDKFTEKG GLSFSLLLWA 190 200 210 220 230 240 TLNAAFVLVG SVIVAFIEPV AAGSGIPQIK CFLNGVKIPH VVRLKTLVIK VSGVILSVVG 250 260 270 280 290 300 GLAVGKEGPM IHSGSVIAAG ISQGRSTSLK RDFKIFEYFR RDTEKRDFVS AGAAAGVSAA 310 320 330 340 350 360 FGAPVGGVLF SLEEGASFWN QFLTWRIFFA SMISTFTLNF VLSIYHGNMW DLSSPGLINF 370 380 390 400 410 420 GRFDSEKMAY TIHEIPVFIA MGVVGGVLGA VFNALNYWLT MFRIRYIHRP CLQVIEAVLV 430 440 450 460 470 480 AAVTATVAFV LIYSSRDCQP LQGGSMSYPL QLFCADGEYN SMAAAFFNTP EKSVVSLFHD 490 500 510 520 530 540 PPGSYNPLTL GLFTLVYFFL ACWTYGLTVS AGVFIPSLLI GAAWGRLFGI SLSYLTGAAI 550 560 570 580 590 600 WADPGKYALM GAAAQLGGIV RMTLSLTVIM MEATSNVTYG FPIMLVLMTA KIVGDVFIEG 610 620 630 640 650 660 LYDMHIQLQS VPFLHWEAPV TSHSLTAREV MSTPVTCLRR REKVGVIVDV LSDTASNHNG 670 680 690 700 710 720 FPVVEHADDT QPARLQGLIL RSQLIVLLKH KVFVERSNLG LVQRRLRLKD FRDAYPRFPP 730 740 750 760 770 780 IQSIHVSQDE RECTMDLSEF MNPSPYTVPQ EASLPRVFKL FRALGLRHLV VVDNRNQVVG 790 800 LVTRKDLARY RLGKRGLEEL SLAQT

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Ion channels in lens epithelia." Rae J.L. Submitted (JAN-2000) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Lens epithelium.
[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: 14702039] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Brain.
[3]	"The sequence and analysis of duplication-rich human chromosome 16." Martin J., Han C., Gordon L.A., Terry A., Prabhakar S., She X., Xie G., Hellsten U., Chan Y.M., Altherr M., Couronne O., Aerts A., Bajorek E., Black S., Blumer H., Branscomb E., Brown N.C., Bruno W.J. , Buckingham J.M., Callen D.F., Campbell C.S., Campbell M.L., Campbell E.W., Caoile C., Challacombe J.F., Chasteen L.A., Chertkov O., Chi H.C., Christensen M., Clark L.M., Cohn J.D., Denys M., Detter J.C., Dickson M., Dimitrijevic-Bussod M., Escobar J., Fawcett J.J., Flowers D., Fotopulos D., Glavina T., Gomez M., Gonzales E., Goodstein D., Goodwin L.A., Grady D.L., Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Hildebrand C.E., Huang W., Israni S., Jett J., Jewett P.B., Kadner K., Kimball H., Kobayashi A., Krawczyk M.-C., Leyba T., Longmire J.L., Lopez F., Lou Y., Lowry S., Ludeman T., Manohar C.F., Mark G.A., McMurray K.L., Meincke L.J., Morgan J., Moyzis R.K., Mundt M.O., Munk A.C., Nandkeshwar R.D., Pitluck S., Pollard M., Predki P., Parson-Quintana B., Ramirez L., Rash S., Retterer J., Ricke D.O., Robinson D.L., Rodriguez A., Salamov A., Saunders E.H., Scott D., Shough T., Stallings R.L., Stalvey M., Sutherland R.D., Tapia R., Tesmer J.G., Thayer N., Thompson L.S., Tice H., Torney D.C., Tran-Gyamfi M., Tsai M., Ulanovsky L.E., Ustaszewska A., Vo N., White P.S., Williams A.L., Wills P.L., Wu J.-R., Wu K., Yang J., DeJong P., Bruce D., Doggett N.A., Deaven L., Schmutz J., Grimwood J., Richardson P., Rokhsar D.S., Eichler E.E., Gilna P., Lucas S.M., Myers R.M., Rubin E.M., Pennacchio L.A. Nature 432:988-994(2004) [PubMed: 15616553] [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: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Skin.
[5]	"ClC-6 and ClC-7 are two novel broadly expressed members of the CLC chloride channel family." Brandt S., Jentsch T.J. FEBS Lett. 377:15-20(1995) [PubMed: 8543009] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 17-805. Tissue: Brain.
[6]	"The exon-intron architecture of human chloride channel genes is not conserved." Eggermont J. Biochim. Biophys. Acta 1397:156-160(1998) [PubMed: 9565675] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 275-432.
[7]	Schutte B.C., Malik M.I., Fingert J., Stone E., Lamb F.S. Submitted (MAR-1997) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 744-805. Tissue: Mammary gland.
[8]	"Global, in vivo, and site-specific phosphorylation dynamics in signaling networks." Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M. Cell 127:635-648(2006) [PubMed: 17081983] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-9; SER-60 AND SER-61, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[9]	"Integral and associated lysosomal membrane proteins." Schroeder B., Wrocklage C., Pan C., Jaeger R., Koesters B., Schaefer H., Elsaesser H.-P., Mann M., Hasilik A. Traffic 8:1676-1686(2007) [PubMed: 17897319] [Abstract] Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS], MASS SPECTROMETRY. Tissue: Placenta.
[10]	"The Cl-/H+ antiporter ClC-7 is the primary chloride permeation pathway in lysosomes." Graves A.R., Curran P.K., Smith C.L., Mindell J.A. Nature 453:788-792(2008) [PubMed: 18449189] [Abstract] Cited for: FUNCTION, SUBCELLULAR LOCATION.
[11]	"Loss of the ClC-7 chloride channel leads to osteopetrosis in mice and man." Kornak U., Kasper D., Boesl M.R., Kaiser E., Schweizer M., Schulz A., Friedrich W., Delling G., Jentsch T.J. Cell 104:205-215(2001) [PubMed: 11207362] [Abstract] Cited for: VARIANT OPTB4 GLN-762.
[12]	"Albers-Schonberg disease (autosomal dominant osteopetrosis, type II) results from mutations in the ClCN7 chloride channel gene." Cleiren E., Benichou O., Van Hul E., Gram J., Bollerslav J., Singer F.R., Beaverson K., Aledo A., Whyte M.P., Yoneyama T., de Vernejoul M.-C., Van Hul W. Hum. Mol. Genet. 10:2861-2867(2001) [PubMed: 11741829] [Abstract] Cited for: VARIANT OPTB4 PRO-766, VARIANT OPTA2 TRP-767.
[13]	"Chloride channel ClCN7 mutations are responsible for severe recessive, dominant, and intermediate osteopetrosis." Frattini A., Pangrazio A., Susani L., Sobacchi C., Mirolo M., Abinun M., Andolina M., Flanagan A., Horwitz E.M., Mihci E., Notarangelo L.D., Ramenghi U., Teti A., Van Hove J., Vujic D., Young T., Albertini A., Orchard P.J., Vezzoni P., Villa A. J. Bone Miner. Res. 18:1740-1747(2003) [PubMed: 14584882] [Abstract] Cited for: VARIANTS OPTB4 ARG-240; ARG-249; VAL-332; TRP-526; PRO-614; PHE-744; GLN-767 AND TRP-767, VARIANTS OPTA2 ARG-215; GLN-286; PHE-490 AND VAL-677, VARIANT MET-418.
[14]	"DNA-based diagnosis of malignant osteopetrosis by whole-genome scan using a single-nucleotide polymorphism microarray: standardization of molecular investigations of genetic diseases due to consanguinity." Lam C.-W., Tong S.-F., Wong K., Luo Y.F., Tang H.-Y., Ha S.-Y., Chan M.H.-M. J. Hum. Genet. 52:98-101(2007) [PubMed: 17033731] [Abstract] Cited for: VARIANT OPTB4 PHE-261.
[15]	"Molecular and clinical heterogeneity in CLCN7-dependent osteopetrosis: report of 20 novel mutations." Pangrazio A., Pusch M., Caldana E., Frattini A., Lanino E., Tamhankar P.M., Phadke S., Lopez A.G., Orchard P., Mihci E., Abinun M., Wright M., Vettenranta K., Bariae I., Melis D., Tezcan I., Baumann C., Locatelli F. , Zecca M., Horwitz E., Mansour L.S., Van Roij M., Vezzoni P., Villa A., Sobacchi C. Hum. Mutat. 31:E1071-E1080(2010) [PubMed: 19953639] [Abstract] Cited for: VARIANTS OPTB4 PRO-132; SER-214; LEU-227 DEL; ARG-240; GLN-403; ARG-521; GLN-526; TRP-526; PRO-549; PRO-651; TRP-762 AND PRO-767, VARIANTS OPTA2 ARG-215; GLN-286; LEU-318; LEU-758; GLN-762 AND TRP-767.
+	Additional computationally mapped references.

Web resources

GeneReviews

Cross-references

Sequence databases
EMBL GenBank DDBJ	AF224741 mRNA. Translation: AAF34711.1. AK291404 mRNA. Translation: BAF84093.1. AL031705 Genomic DNA. No translation available. BC012737 mRNA. Translation: AAH12737.1. Z67743 mRNA. Translation: CAA91556.1. AJ001910 Genomic DNA. Translation: CAA05083.1. U88844 mRNA. Translation: AAB48530.1.
IPI	IPI00020524.
PIR	S68427.
RefSeq	NP_001107803.1. NM_001114331.1. NP_001278.1. NM_001287.4.
UniGene	Hs.459649.
3D structure databases
ProteinModelPortal	P51798.
SMR	P51798. Positions 624-796.
ModBase	Search...
Protein-protein interaction databases
STRING	P51798.
Protein family/group databases
TCDB	2.A.49.3.3. chloride carrier/channel (ClC) family.
PTM databases
PhosphoSite	P51798.
Polymorphism databases
DMDM	12644301.
Proteomic databases
PRIDE	P51798.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000428756; ENSP00000404772; ENSG00000103249.
GeneID	1186.
KEGG	hsa:1186.
UCSC	uc002clv.2. human.
Organism-specific databases
CTD	1186.
GeneCards	GC16M001494.
H-InvDB	HIX0012684.
HGNC	HGNC:2025. CLCN7.
HPA	HPA043019. HPA043586.
MIM	166600. phenotype. 602727. gene. 611490. phenotype.
neXtProt	NX_P51798.
Orphanet	53. Albers-Schoenberg osteopetrosis. 667. Autosomal recessive malignant osteopetrosis. 210110. Intermediate osteopetrosis.
GenAtlas	Search...
Phylogenomic databases
eggNOG	prNOG14647.
HOVERGEN	HBG050985.
PhylomeDB	P51798.
Gene expression databases
ArrayExpress	P51798.
Bgee	P51798.
CleanEx	HS_CLCN7.
Genevestigator	P51798.
GermOnline	ENSG00000103249. Homo sapiens.
Family and domain databases
InterPro	IPR014743. Cl-channel_core. IPR001807. Cl-channel_volt-gated. IPR002249. Cl_channel-7. IPR000644. Cysta_beta_synth_core. [Graphical view]
Gene3D	G3DSA:1.10.3080.10. Cl-channel_core. 2 hits.
KO	K05016.
PANTHER	PTHR11689. Cl-channel_volt. 1 hit.
Pfam	PF00571. CBS. 2 hits. PF00654. Voltage_CLC. 1 hit. [Graphical view]
PRINTS	PR00762. CLCHANNEL. PR01118. CLCHANNEL7.
SMART	SM00116. CBS. 2 hits. [Graphical view]
SUPFAM	SSF81340. Cl-channel_core. 1 hit.
PROSITE	PS51371. CBS. 2 hits. [Graphical view]
ProtoNet	Search...
Other
NextBio	4908.
SOURCE	Search...

Entry information

Entry name

CLCN7_HUMAN

Accession

Primary (citable) accession number: P51798
Secondary accession number(s): A6NEJ7, A8K5T9, Q9NYX5

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1996
Last sequence update:	January 11, 2001
Last modified:	January 25, 2012
This is version 126 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.