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Protein

Volume-regulated anion channel subunit LRRC8D

Gene

LRRC8D

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

Functioni

Non-essential component of the volume-regulated anion channel (VRAC, also named VSOAC channel), an anion channel required to maintain a constant cell volume in response to extracellular or intracellular osmotic changes. The VRAC channel conducts iodide better than chloride and may also conduct organic osmolytes like taurine. Channel activity requires LRRC8A plus at least one other family member (LRRC8B, LRRC8C, LRRC8D or LRRC8E); channel characteristics depend on the precise subunit composition (PubMed:24790029, PubMed:26824658). LRRC8A and LRRC8D are required for the uptake of the drug cisplatin (PubMed:26530471). Mediates the import of the antibiotic blasticidin-S into the cell (PubMed:24782309).4 Publications

GO - Molecular functioni

  • volume-sensitive anion channel activity Source: UniProtKB

GO - Biological processi

  • anion transmembrane transport Source: UniProtKB
  • regulation of anion transport Source: GOC
Complete GO annotation...

Keywords - Molecular functioni

Ion channel

Keywords - Biological processi

Ion transport, Transport

Protein family/group databases

TCDBi1.A.25.3.1. the gap junction-forming innexin (innexin) family.

Names & Taxonomyi

Protein namesi
Recommended name:
Volume-regulated anion channel subunit LRRC8D
Alternative name(s):
Leucine-rich repeat-containing protein 5
Leucine-rich repeat-containing protein 8D
Gene namesi
Name:LRRC8D
Synonyms:LRRC5
ORF Names:UNQ213/PRO239
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 1

Organism-specific databases

HGNCiHGNC:16992. LRRC8D.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 2222CytoplasmicSequence analysisAdd
BLAST
Transmembranei23 – 4321HelicalSequence analysisAdd
BLAST
Topological domaini44 – 163120ExtracellularSequence analysisAdd
BLAST
Transmembranei164 – 18421HelicalSequence analysisAdd
BLAST
Topological domaini185 – 318134CytoplasmicSequence analysisAdd
BLAST
Transmembranei319 – 33921HelicalSequence analysisAdd
BLAST
Topological domaini340 – 36425ExtracellularSequence analysisAdd
BLAST
Transmembranei365 – 38521HelicalSequence analysisAdd
BLAST
Topological domaini386 – 858473CytoplasmicSequence analysisAdd
BLAST

GO - Cellular componenti

  • cytoplasm Source: UniProtKB
  • endoplasmic reticulum membrane Source: UniProtKB-SubCell
  • integral component of plasma membrane Source: UniProtKB
  • membrane Source: UniProtKB
  • plasma membrane Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Endoplasmic reticulum, Membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi44 – 441T → C: Alters channel anion selectivity. 1 Publication

Organism-specific databases

PharmGKBiPA30464.

Polymorphism and mutation databases

BioMutaiLRRC8D.
DMDMi51701663.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 858858Volume-regulated anion channel subunit LRRC8DPRO_0000084493Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei241 – 2411PhosphoserineCombined sources
Modified residuei242 – 2421PhosphoserineCombined sources
Modified residuei246 – 2461PhosphoserineCombined sources

Keywords - PTMi

Phosphoprotein

Proteomic databases

EPDiQ7L1W4.
MaxQBiQ7L1W4.
PaxDbiQ7L1W4.
PRIDEiQ7L1W4.
TopDownProteomicsiQ7L1W4.

PTM databases

iPTMnetiQ7L1W4.
PhosphoSiteiQ7L1W4.

Expressioni

Gene expression databases

BgeeiQ7L1W4.
CleanExiHS_LRRC8D.
ExpressionAtlasiQ7L1W4. baseline and differential.
GenevisibleiQ7L1W4. HS.

Organism-specific databases

HPAiHPA014745.

Interactioni

Subunit structurei

Heterooligomer; heterooligomerizes with other LRRC8 proteins (LRRC8A, LRRC8B, LRRC8C and/or LRRC8E), possibly to form a heterohexamer (PubMed:24790029, PubMed:26824658). In vivo, the subunit composition may depend primarily on expression levels, and heterooligomeric channels containing various proportions of the different LRRC8 proteins may coexist (Probable).Curated2 Publications

Protein-protein interaction databases

BioGridi120447. 5 interactions.
DIPiDIP-31280N.
IntActiQ7L1W4. 1 interaction.
MINTiMINT-4995188.
STRINGi9606.ENSP00000338887.

Structurei

3D structure databases

ProteinModelPortaliQ7L1W4.
SMRiQ7L1W4. Positions 469-847.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati514 – 53421LRR 1Add
BLAST
Repeati538 – 55922LRR 2Add
BLAST
Repeati561 – 58222LRR 3Add
BLAST
Repeati589 – 60921LRR 4Add
BLAST
Repeati612 – 63221LRR 5Add
BLAST
Repeati636 – 65722LRR 6Add
BLAST
Repeati659 – 68022LRR 7Add
BLAST
Repeati684 – 70522LRR 8Add
BLAST
Repeati707 – 72822LRR 9Add
BLAST
Repeati730 – 75122LRR 10Add
BLAST
Repeati753 – 77422LRR 11Add
BLAST
Repeati776 – 79722LRR 12Add
BLAST
Repeati799 – 82022LRR 13Add
BLAST

Sequence similaritiesi

Belongs to the LRRC8 family.Curated
Contains 13 LRR (leucine-rich) repeats.Curated

Keywords - Domaini

Leucine-rich repeat, Repeat, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiKOG0619. Eukaryota.
COG4886. LUCA.
GeneTreeiENSGT00840000129676.
HOGENOMiHOG000231806.
HOVERGENiHBG052360.
InParanoidiQ7L1W4.
OMAiQLFKCVK.
OrthoDBiEOG7Z3F3T.
PhylomeDBiQ7L1W4.
TreeFamiTF331443.

Family and domain databases

Gene3Di3.80.10.10. 2 hits.
InterProiIPR032675. L_dom-like.
IPR001611. Leu-rich_rpt.
IPR003591. Leu-rich_rpt_typical-subtyp.
IPR021040. LRRC8_Pannexin_like.
[Graphical view]
PfamiPF13855. LRR_8. 2 hits.
PF12534. Pannexin_like. 1 hit.
[Graphical view]
SMARTiSM00369. LRR_TYP. 7 hits.
[Graphical view]
SUPFAMiSSF52058. SSF52058. 1 hit.
PROSITEiPS51450. LRR. 9 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q7L1W4-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MFTLAEVASL NDIQPTYRIL KPWWDVFMDY LAVVMLMVAI FAGTMQLTKD
60 70 80 90 100
QVVCLPVLPS PVNSKAHTPP GNAEVTTNIP KMEAATNQDQ DGRTTNDISF
110 120 130 140 150
GTSAVTPDIP LRATYPRTDF ALPNQEAKKE KKDPTGRKTN LDFQQYVFIN
160 170 180 190 200
QMCYHLALPW YSKYFPYLAL IHTIILMVSS NFWFKYPKTC SKVEHFVSIL
210 220 230 240 250
GKCFESPWTT KALSETACED SEENKQRITG AQTLPKHVST SSDEGSPSAS
260 270 280 290 300
TPMINKTGFK FSAEKPVIEV PSMTILDKKD GEQAKALFEK VRKFRAHVED
310 320 330 340 350
SDLIYKLYVV QTVIKTAKFI FILCYTANFV NAISFEHVCK PKVEHLIGYE
360 370 380 390 400
VFECTHNMAY MLKKLLISYI SIICVYGFIC LYTLFWLFRI PLKEYSFEKV
410 420 430 440 450
REESSFSDIP DVKNDFAFLL HMVDQYDQLY SKRFGVFLSE VSENKLREIS
460 470 480 490 500
LNHEWTFEKL RQHISRNAQD KQELHLFMLS GVPDAVFDLT DLDVLKLELI
510 520 530 540 550
PEAKIPAKIS QMTNLQELHL CHCPAKVEQT AFSFLRDHLR CLHVKFTDVA
560 570 580 590 600
EIPAWVYLLK NLRELYLIGN LNSENNKMIG LESLRELRHL KILHVKSNLT
610 620 630 640 650
KVPSNITDVA PHLTKLVIHN DGTKLLVLNS LKKMMNVAEL ELQNCELERI
660 670 680 690 700
PHAIFSLSNL QELDLKSNNI RTIEEIISFQ HLKRLTCLKL WHNKIVTIPP
710 720 730 740 750
SITHVKNLES LYFSNNKLES LPVAVFSLQK LRCLDVSYNN ISMIPIEIGL
760 770 780 790 800
LQNLQHLHIT GNKVDILPKQ LFKCIKLRTL NLGQNCITSL PEKVGQLSQL
810 820 830 840 850
TQLELKGNCL DRLPAQLGQC RMLKKSGLVV EDHLFDTLPL EVKEALNQDI

NIPFANGI
Length:858
Mass (Da):98,201
Last modified:July 5, 2004 - v1
Checksum:i52A8B6EEF6F0FE2B
GO

Sequence cautioni

The sequence AAQ89233.1 differs from that shown. Reason: Erroneous initiation. Curated
The sequence BAA91631.1 differs from that shown. Reason: Erroneous initiation. Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti371 – 3711S → Y.
Corresponds to variant rs11552246 [ dbSNP | Ensembl ].
VAR_051132

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AL391497 Genomic DNA. Translation: CAH72226.1.
CH471097 Genomic DNA. Translation: EAW73130.1.
CH471097 Genomic DNA. Translation: EAW73131.1.
CH471097 Genomic DNA. Translation: EAW73132.1.
BC024159 mRNA. Translation: AAH24159.2.
AK001332 mRNA. Translation: BAA91631.1. Different initiation.
AY358874 mRNA. Translation: AAQ89233.1. Different initiation.
CCDSiCCDS726.1.
RefSeqiNP_001127951.1. NM_001134479.1.
NP_060573.2. NM_018103.4.
XP_011539991.1. XM_011541689.1.
XP_011539992.1. XM_011541690.1.
UniGeneiHs.482087.

Genome annotation databases

EnsembliENST00000337338; ENSP00000338887; ENSG00000171492.
ENST00000394593; ENSP00000378093; ENSG00000171492.
GeneIDi55144.
KEGGihsa:55144.
UCSCiuc001dnm.4. human.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AL391497 Genomic DNA. Translation: CAH72226.1.
CH471097 Genomic DNA. Translation: EAW73130.1.
CH471097 Genomic DNA. Translation: EAW73131.1.
CH471097 Genomic DNA. Translation: EAW73132.1.
BC024159 mRNA. Translation: AAH24159.2.
AK001332 mRNA. Translation: BAA91631.1. Different initiation.
AY358874 mRNA. Translation: AAQ89233.1. Different initiation.
CCDSiCCDS726.1.
RefSeqiNP_001127951.1. NM_001134479.1.
NP_060573.2. NM_018103.4.
XP_011539991.1. XM_011541689.1.
XP_011539992.1. XM_011541690.1.
UniGeneiHs.482087.

3D structure databases

ProteinModelPortaliQ7L1W4.
SMRiQ7L1W4. Positions 469-847.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi120447. 5 interactions.
DIPiDIP-31280N.
IntActiQ7L1W4. 1 interaction.
MINTiMINT-4995188.
STRINGi9606.ENSP00000338887.

Protein family/group databases

TCDBi1.A.25.3.1. the gap junction-forming innexin (innexin) family.

PTM databases

iPTMnetiQ7L1W4.
PhosphoSiteiQ7L1W4.

Polymorphism and mutation databases

BioMutaiLRRC8D.
DMDMi51701663.

Proteomic databases

EPDiQ7L1W4.
MaxQBiQ7L1W4.
PaxDbiQ7L1W4.
PRIDEiQ7L1W4.
TopDownProteomicsiQ7L1W4.

Protocols and materials databases

DNASUi55144.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000337338; ENSP00000338887; ENSG00000171492.
ENST00000394593; ENSP00000378093; ENSG00000171492.
GeneIDi55144.
KEGGihsa:55144.
UCSCiuc001dnm.4. human.

Organism-specific databases

CTDi55144.
GeneCardsiLRRC8D.
HGNCiHGNC:16992. LRRC8D.
HPAiHPA014745.
MIMi612890. gene.
neXtProtiNX_Q7L1W4.
PharmGKBiPA30464.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG0619. Eukaryota.
COG4886. LUCA.
GeneTreeiENSGT00840000129676.
HOGENOMiHOG000231806.
HOVERGENiHBG052360.
InParanoidiQ7L1W4.
OMAiQLFKCVK.
OrthoDBiEOG7Z3F3T.
PhylomeDBiQ7L1W4.
TreeFamiTF331443.

Miscellaneous databases

ChiTaRSiLRRC8D. human.
GeneWikiiLRRC8D.
GenomeRNAii55144.
NextBioi58848.
PROiQ7L1W4.
SOURCEiSearch...

Gene expression databases

BgeeiQ7L1W4.
CleanExiHS_LRRC8D.
ExpressionAtlasiQ7L1W4. baseline and differential.
GenevisibleiQ7L1W4. HS.

Family and domain databases

Gene3Di3.80.10.10. 2 hits.
InterProiIPR032675. L_dom-like.
IPR001611. Leu-rich_rpt.
IPR003591. Leu-rich_rpt_typical-subtyp.
IPR021040. LRRC8_Pannexin_like.
[Graphical view]
PfamiPF13855. LRR_8. 2 hits.
PF12534. Pannexin_like. 1 hit.
[Graphical view]
SMARTiSM00369. LRR_TYP. 7 hits.
[Graphical view]
SUPFAMiSSF52058. SSF52058. 1 hit.
PROSITEiPS51450. LRR. 9 hits.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "The DNA sequence and biological annotation of human chromosome 1."
    Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.
    , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.
    Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  3. "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].
    Tissue: Placenta.
  4. "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] OF 175-858.
  5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 335-858.
  6. "LRRC8 proteins share a common ancestor with pannexins, and may form hexameric channels involved in cell-cell communication."
    Abascal F., Zardoya R.
    Bioessays 34:551-560(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION.
  7. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-241 AND SER-242, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  8. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
    Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
    Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-246, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  9. "The protein synthesis inhibitor blasticidin S enters mammalian cells via leucine-rich repeat-containing protein 8D."
    Lee C.C., Freinkman E., Sabatini D.M., Ploegh H.L.
    J. Biol. Chem. 289:17124-17131(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION, TOPOLOGY, INTERACTION WITH LRRC8A; LRRC8B AND LRRC8C.
  10. "Identification of LRRC8 heteromers as an essential component of the volume-regulated anion channel VRAC."
    Voss F.K., Ullrich F., Muench J., Lazarow K., Lutter D., Mah N., Andrade-Navarro M.A., von Kries J.P., Stauber T., Jentsch T.J.
    Science 344:634-638(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH LRRC8A, SUBCELLULAR LOCATION.
  11. "Subunit composition of VRAC channels determines substrate specificity and cellular resistance to Pt-based anti-cancer drugs."
    Planells-Cases R., Lutter D., Guyader C., Gerhards N.M., Ullrich F., Elger D.A., Kucukosmanoglu A., Xu G., Voss F.K., Reincke S.M., Stauber T., Blomen V.A., Vis D.J., Wessels L.F., Brummelkamp T.R., Borst P., Rottenberg S., Jentsch T.J.
    EMBO J. 34:2993-3008(2015) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  12. "LRRC8 proteins form volume-regulated anion channels that sense ionic strength."
    Syeda R., Qiu Z., Dubin A.E., Murthy S.E., Florendo M.N., Mason D.E., Mathur J., Cahalan S.M., Peters E.C., Montal M., Patapoutian A.
    Cell 164:499-511(2016) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION, SUBUNIT, IDENTIFICATION BY MASS SPECTROMETRY, MUTAGENESIS OF THR-44.

Entry informationi

Entry nameiLRC8D_HUMAN
AccessioniPrimary (citable) accession number: Q7L1W4
Secondary accession number(s): D3DT29, Q6UWB2, Q9NVW3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 31, 2004
Last sequence update: July 5, 2004
Last modified: May 11, 2016
This is version 118 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

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Human chromosome 1
    Human chromosome 1: 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. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.