LRC8E_HUMAN
ID LRC8E_HUMAN Reviewed; 796 AA.
AC Q6NSJ5; B3KR78; Q2YDY3; Q7L236; Q8N3B0; Q9H5H8;
DT 07-FEB-2006, integrated into UniProtKB/Swiss-Prot.
DT 18-MAY-2010, sequence version 2.
DT 03-AUG-2022, entry version 162.
DE RecName: Full=Volume-regulated anion channel subunit LRRC8E {ECO:0000305};
DE AltName: Full=Leucine-rich repeat-containing protein 8E {ECO:0000303|PubMed:22532330};
GN Name=LRRC8E {ECO:0000303|PubMed:22532330, ECO:0000312|HGNC:HGNC:26272};
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Tongue;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT THR-190.
RC TISSUE=Esophageal carcinoma, and Melanoma;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15057824; DOI=10.1038/nature02399;
RA Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J., Lamerdin J.E.,
RA Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M., Aerts A.,
RA Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E., Caenepeel S.,
RA Carrano A.V., Caoile C., Chan Y.M., Christensen M., Cleland C.A.,
RA Copeland A., Dalin E., Dehal P., Denys M., Detter J.C., Escobar J.,
RA Flowers D., Fotopulos D., Garcia C., Georgescu A.M., Glavina T., Gomez M.,
RA Gonzales E., Groza M., Hammon N., Hawkins T., Haydu L., Ho I., Huang W.,
RA Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Larionov V.,
RA Leem S.-H., Lopez F., Lou Y., Lowry S., Malfatti S., Martinez D.,
RA McCready P.M., Medina C., Morgan J., Nelson K., Nolan M., Ovcharenko I.,
RA Pitluck S., Pollard M., Popkie A.P., Predki P., Quan G., Ramirez L.,
RA Rash S., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A.,
RA She X., Smith D., Slezak T., Solovyev V., Thayer N., Tice H., Tsai M.,
RA Ustaszewska A., Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J.,
RA Dubchak I., Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E.,
RA Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M.,
RA Rubin E.M., Lucas S.M.;
RT "The DNA sequence and biology of human chromosome 19.";
RL Nature 428:529-535(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Kidney, Lung, and Placenta;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [6]
RP IDENTIFICATION.
RX PubMed=22532330; DOI=10.1002/bies.201100173;
RA Abascal F., Zardoya R.;
RT "LRRC8 proteins share a common ancestor with pannexins, and may form
RT hexameric channels involved in cell-cell communication.";
RL Bioessays 34:551-560(2012).
RN [7]
RP FUNCTION, CATALYTIC ACTIVITY, INTERACTION WITH LRRC8A, AND SUBCELLULAR
RP LOCATION.
RX PubMed=24790029; DOI=10.1126/science.1252826;
RA Voss F.K., Ullrich F., Muench J., Lazarow K., Lutter D., Mah N.,
RA Andrade-Navarro M.A., von Kries J.P., Stauber T., Jentsch T.J.;
RT "Identification of LRRC8 heteromers as an essential component of the
RT volume-regulated anion channel VRAC.";
RL Science 344:634-638(2014).
RN [8]
RP FUNCTION, SUBCELLULAR LOCATION, SUBUNIT, IDENTIFICATION BY MASS
RP SPECTROMETRY, AND MUTAGENESIS OF THR-44.
RX PubMed=26824658; DOI=10.1016/j.cell.2015.12.031;
RA Syeda R., Qiu Z., Dubin A.E., Murthy S.E., Florendo M.N., Mason D.E.,
RA Mathur J., Cahalan S.M., Peters E.C., Montal M., Patapoutian A.;
RT "LRRC8 proteins form volume-regulated anion channels that sense ionic
RT strength.";
RL Cell 164:499-511(2016).
RN [9]
RP FUNCTION, SUBUNIT, AND SUBCELLULAR LOCATION.
RX PubMed=28193731; DOI=10.1242/jcs.196253;
RA Lutter D., Ullrich F., Lueck J.C., Kempa S., Jentsch T.J.;
RT "Selective transport of neurotransmitters and modulators by distinct
RT volume-regulated LRRC8 anion channels.";
RL J. Cell Sci. 130:1122-1133(2017).
RN [10]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=33171122; DOI=10.1016/j.molcel.2020.10.021;
RA Lahey L.J., Mardjuki R.E., Wen X., Hess G.T., Ritchie C., Carozza J.A.,
RA Boehnert V., Maduke M., Bassik M.C., Li L.;
RT "LRRC8A:C/E heteromeric channels are ubiquitous transporters of cGAMP.";
RL Mol. Cell 0:0-0(2020).
RN [11]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=33139539; DOI=10.1073/pnas.2016539117;
RA Li P., Hu M., Wang C., Feng X., Zhao Z., Yang Y., Sahoo N., Gu M., Yang Y.,
RA Xiao S., Sah R., Cover T.L., Chou J., Geha R., Benavides F., Hume R.I.,
RA Xu H.;
RT "LRRC8 family proteins within lysosomes regulate cellular osmoregulation
RT and enhance cell survival to multiple physiological stresses.";
RL Proc. Natl. Acad. Sci. U.S.A. 117:29155-29165(2020).
CC -!- FUNCTION: Non-essential component of the volume-regulated anion channel
CC (VRAC, also named VSOAC channel), an anion channel required to maintain
CC a constant cell volume in response to extracellular or intracellular
CC osmotic changes (PubMed:24790029, PubMed:26824658, PubMed:28193731).
CC The VRAC channel conducts iodide better than chloride and can also
CC conduct organic osmolytes like taurine (PubMed:24790029,
CC PubMed:26824658). Mediates efflux of amino acids, such as aspartate, in
CC response to osmotic stress (PubMed:28193731). The VRAC channel also
CC mediates transport of immunoreactive cyclic dinucleotide GMP-AMP (2'-
CC 3'-cGAMP), an immune messenger produced in response to DNA virus in the
CC cytosol (PubMed:33171122). Channel activity requires LRRC8A plus at
CC least one other family member (LRRC8B, LRRC8C, LRRC8D or LRRC8E);
CC channel characteristics depend on the precise subunit composition
CC (PubMed:24790029, PubMed:26824658, PubMed:28193731). Also plays a role
CC in lysosome homeostasis by forming functional lysosomal VRAC channels
CC in response to low cytoplasmic ionic strength condition: lysosomal VRAC
CC channels are necessary for the formation of large lysosome-derived
CC vacuoles, which store and then expel excess water to maintain cytosolic
CC water homeostasis (PubMed:33139539). {ECO:0000269|PubMed:24790029,
CC ECO:0000269|PubMed:26824658, ECO:0000269|PubMed:28193731,
CC ECO:0000269|PubMed:33139539, ECO:0000269|PubMed:33171122}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=chloride(in) = chloride(out); Xref=Rhea:RHEA:29823,
CC ChEBI:CHEBI:17996; Evidence={ECO:0000305|PubMed:24790029};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=iodide(out) = iodide(in); Xref=Rhea:RHEA:66324,
CC ChEBI:CHEBI:16382; Evidence={ECO:0000305|PubMed:24790029};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=taurine(out) = taurine(in); Xref=Rhea:RHEA:66328,
CC ChEBI:CHEBI:507393; Evidence={ECO:0000305|PubMed:24790029};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2',3'-cGAMP(out) = 2',3'-cGAMP(in); Xref=Rhea:RHEA:66320,
CC ChEBI:CHEBI:143093; Evidence={ECO:0000269|PubMed:33171122};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:66321;
CC Evidence={ECO:0000269|PubMed:33171122};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:66322;
CC Evidence={ECO:0000269|PubMed:33171122};
CC -!- SUBUNIT: Heterohexamer (Probable). Oligomerizes with other LRRC8
CC proteins (LRRC8A, LRRC8C, LRRC8D and/or LRRC8B) to form a heterohexamer
CC (PubMed:24790029, PubMed:26824658, PubMed:28193731). Detected in a
CC channel complex that contains LRRC8A, LRRC8C and LRRC8E
CC (PubMed:28193731). In vivo, the subunit composition may depend
CC primarily on expression levels, and heterooligomeric channels
CC containing various proportions of the different LRRC8 proteins may
CC coexist (Probable). {ECO:0000269|PubMed:24790029,
CC ECO:0000269|PubMed:26824658, ECO:0000269|PubMed:28193731, ECO:0000305}.
CC -!- INTERACTION:
CC Q6NSJ5; P81274: GPSM2; NbExp=3; IntAct=EBI-8647013, EBI-618655;
CC Q6NSJ5; Q8IWT6: LRRC8A; NbExp=3; IntAct=EBI-8647013, EBI-10970086;
CC Q6NSJ5; Q5PRF9: SAMD4B; NbExp=3; IntAct=EBI-8647013, EBI-1047489;
CC Q6NSJ5; Q9C040: TRIM2; NbExp=6; IntAct=EBI-8647013, EBI-749840;
CC Q6NSJ5; O75382: TRIM3; NbExp=3; IntAct=EBI-8647013, EBI-2129889;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:24790029,
CC ECO:0000269|PubMed:26824658, ECO:0000269|PubMed:28193731}; Multi-pass
CC membrane protein {ECO:0000305}. Endoplasmic reticulum membrane
CC {ECO:0000305|PubMed:24790029}. Lysosome membrane
CC {ECO:0000269|PubMed:33139539}; Multi-pass membrane protein
CC {ECO:0000305}. Endoplasmic reticulum membrane
CC {ECO:0000269|PubMed:33139539}; Multi-pass membrane protein
CC {ECO:0000305}. Note=In the absence of LRRC8A, resides primarily in the
CC endoplasmic reticulum (PubMed:24790029, PubMed:33139539). Requires
CC LRRC8A for localization at the cell membrane or lysosome membrane
CC (PubMed:24790029, PubMed:33139539). {ECO:0000269|PubMed:24790029,
CC ECO:0000269|PubMed:33139539}.
CC -!- DOMAIN: The volume-regulated anion channel (VRAC) channel forms a
CC trimer of dimers, with symmetry mismatch between the pore-forming
CC domain and the cytosolic LRR repeats, a topology similar to gap
CC junction proteins. {ECO:0000250|UniProtKB:Q8IWT6}.
CC -!- SIMILARITY: Belongs to the LRRC8 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB15648.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAB15648.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence.; Evidence={ECO:0000305};
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DR EMBL; AK027073; BAB15648.1; ALT_SEQ; mRNA.
DR EMBL; AK091134; BAG52290.1; -; mRNA.
DR EMBL; AL834474; CAD39133.1; -; mRNA.
DR EMBL; BX538180; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; AC010336; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471139; EAW68969.1; -; Genomic_DNA.
DR EMBL; BC022216; AAH22216.2; -; mRNA.
DR EMBL; BC070089; AAH70089.1; -; mRNA.
DR EMBL; BC108252; AAI08253.1; -; mRNA.
DR CCDS; CCDS12189.1; -.
DR RefSeq; NP_001255213.1; NM_001268284.2.
DR RefSeq; NP_001255214.1; NM_001268285.2.
DR RefSeq; NP_079337.2; NM_025061.5.
DR RefSeq; XP_011526621.1; XM_011528319.2.
DR AlphaFoldDB; Q6NSJ5; -.
DR SMR; Q6NSJ5; -.
DR BioGRID; 123131; 117.
DR CORUM; Q6NSJ5; -.
DR DIP; DIP-61363N; -.
DR IntAct; Q6NSJ5; 25.
DR MINT; Q6NSJ5; -.
DR STRING; 9606.ENSP00000479953; -.
DR TCDB; 1.A.25.3.1; the gap junction-forming innexin (innexin) family.
DR GlyGen; Q6NSJ5; 2 sites.
DR iPTMnet; Q6NSJ5; -.
DR PhosphoSitePlus; Q6NSJ5; -.
DR BioMuta; LRRC8E; -.
DR DMDM; 296434573; -.
DR EPD; Q6NSJ5; -.
DR jPOST; Q6NSJ5; -.
DR MassIVE; Q6NSJ5; -.
DR MaxQB; Q6NSJ5; -.
DR PaxDb; Q6NSJ5; -.
DR PeptideAtlas; Q6NSJ5; -.
DR PRIDE; Q6NSJ5; -.
DR ProteomicsDB; 66639; -.
DR Antibodypedia; 12282; 59 antibodies from 15 providers.
DR DNASU; 80131; -.
DR Ensembl; ENST00000306708.11; ENSP00000306524.5; ENSG00000171017.11.
DR Ensembl; ENST00000618098.4; ENSP00000479953.1; ENSG00000171017.11.
DR GeneID; 80131; -.
DR KEGG; hsa:80131; -.
DR MANE-Select; ENST00000306708.11; ENSP00000306524.5; NM_025061.6; NP_079337.2.
DR UCSC; uc002mir.4; human.
DR CTD; 80131; -.
DR DisGeNET; 80131; -.
DR GeneCards; LRRC8E; -.
DR HGNC; HGNC:26272; LRRC8E.
DR HPA; ENSG00000171017; Low tissue specificity.
DR MIM; 612891; gene.
DR neXtProt; NX_Q6NSJ5; -.
DR OpenTargets; ENSG00000171017; -.
DR PharmGKB; PA142671537; -.
DR VEuPathDB; HostDB:ENSG00000171017; -.
DR eggNOG; KOG0619; Eukaryota.
DR GeneTree; ENSGT00940000159311; -.
DR HOGENOM; CLU_019019_0_0_1; -.
DR InParanoid; Q6NSJ5; -.
DR OMA; EYSFEQV; -.
DR OrthoDB; 192398at2759; -.
DR PhylomeDB; Q6NSJ5; -.
DR TreeFam; TF331443; -.
DR PathwayCommons; Q6NSJ5; -.
DR Reactome; R-HSA-5223345; Miscellaneous transport and binding events.
DR SignaLink; Q6NSJ5; -.
DR BioGRID-ORCS; 80131; 9 hits in 1070 CRISPR screens.
DR ChiTaRS; LRRC8E; human.
DR GeneWiki; LRRC8E; -.
DR GenomeRNAi; 80131; -.
DR Pharos; Q6NSJ5; Tbio.
DR PRO; PR:Q6NSJ5; -.
DR Proteomes; UP000005640; Chromosome 19.
DR RNAct; Q6NSJ5; protein.
DR Bgee; ENSG00000171017; Expressed in secondary oocyte and 127 other tissues.
DR ExpressionAtlas; Q6NSJ5; baseline and differential.
DR Genevisible; Q6NSJ5; HS.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0030176; C:integral component of endoplasmic reticulum membrane; IDA:UniProtKB.
DR GO; GO:1905103; C:integral component of lysosomal membrane; IDA:UniProtKB.
DR GO; GO:0005887; C:integral component of plasma membrane; IDA:UniProtKB.
DR GO; GO:0034702; C:ion channel complex; IMP:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR GO; GO:0005225; F:volume-sensitive anion channel activity; IDA:UniProtKB.
DR GO; GO:0098656; P:anion transmembrane transport; IMP:UniProtKB.
DR GO; GO:0015810; P:aspartate transmembrane transport; IMP:UniProtKB.
DR GO; GO:0006884; P:cell volume homeostasis; IDA:UniProtKB.
DR GO; GO:0071470; P:cellular response to osmotic stress; IMP:UniProtKB.
DR GO; GO:0140361; P:cyclic-GMP-AMP transmembrane import across plasma membrane; IDA:UniProtKB.
DR Gene3D; 3.80.10.10; -; 2.
DR InterPro; IPR001611; Leu-rich_rpt.
DR InterPro; IPR003591; Leu-rich_rpt_typical-subtyp.
DR InterPro; IPR032675; LRR_dom_sf.
DR InterPro; IPR021040; LRRC8_Pannexin-like.
DR Pfam; PF13855; LRR_8; 2.
DR Pfam; PF12534; Pannexin_like; 1.
DR SMART; SM00369; LRR_TYP; 7.
DR PROSITE; PS51450; LRR; 8.
PE 1: Evidence at protein level;
KW Cell membrane; Disulfide bond; Endoplasmic reticulum; Glycoprotein;
KW Ion channel; Ion transport; Leucine-rich repeat; Lysosome; Membrane;
KW Reference proteome; Repeat; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..796
FT /note="Volume-regulated anion channel subunit LRRC8E"
FT /id="PRO_0000076250"
FT TOPO_DOM 1..22
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 23..43
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 44..116
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 117..137
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 138..265
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 266..286
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 287..313
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 314..334
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 335..796
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REPEAT 508..529
FT /note="LRR 1"
FT REPEAT 536..557
FT /note="LRR 2"
FT REPEAT 559..579
FT /note="LRR 3"
FT REPEAT 583..604
FT /note="LRR 4"
FT REPEAT 606..627
FT /note="LRR 5"
FT REPEAT 631..652
FT /note="LRR 6"
FT REPEAT 654..675
FT /note="LRR 7"
FT REPEAT 677..698
FT /note="LRR 8"
FT REPEAT 700..721
FT /note="LRR 9"
FT REPEAT 723..744
FT /note="LRR 10"
FT REPEAT 746..767
FT /note="LRR 11"
FT CARBOHYD 63
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 302
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 54..301
FT /evidence="ECO:0000250|UniProtKB:Q80WG5"
FT VARIANT 160
FT /note="P -> L (in dbSNP:rs3745377)"
FT /id="VAR_060437"
FT VARIANT 181
FT /note="E -> G (in dbSNP:rs2042919)"
FT /id="VAR_059695"
FT VARIANT 190
FT /note="M -> T (in dbSNP:rs2115108)"
FT /evidence="ECO:0000269|PubMed:17974005"
FT /id="VAR_059696"
FT VARIANT 433
FT /note="V -> I (in dbSNP:rs36038711)"
FT /id="VAR_056930"
FT MUTAGEN 44
FT /note="T->C: Alters channel anion selectivity."
FT /evidence="ECO:0000269|PubMed:26824658"
FT CONFLICT 31
FT /note="L -> P (in Ref. 2; BX538180)"
FT /evidence="ECO:0000305"
FT CONFLICT 115
FT /note="A -> T (in Ref. 5; AAH70089)"
FT /evidence="ECO:0000305"
FT CONFLICT 244
FT /note="H -> R (in Ref. 2; BX538180)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 796 AA; 90247 MW; CB23AF612D1472C6 CRC64;
MIPVAEFKQF TEQQPAFKVL KPWWDVLAEY LTVAMLMIGV FGCTLQVTQD KIICLPNHEL
QENLSEAPCQ QLLPRGIPEQ IGALQEVKGL KNNLDLQQYS FINQLCYETA LHWYAKYFPY
LVVIHTLIFM VCTSFWFKFP GTSSKIEHFI SILGKCFDSP WTTRALSEVS GENQKGPAAT
ERAAATIVAM AGTGPGKAGE GEKEKVLAEP EKVVTEPPVV TLLDKKEGEQ AKALFEKVKK
FRMHVEEGDI LYTMYIRQTV LKVCKFLAIL VYNLVYVEKI SFLVACRVET SEVTGYASFC
CNHTKAHLFS KLAFCYISFV CIYGLTCIYT LYWLFHRPLK EYSFRSVREE TGMGDIPDVK
NDFAFMLHLI DQYDSLYSKR FAVFLSEVSE SRLKQLNLNH EWTPEKLRQK LQRNAAGRLE
LALCMLPGLP DTVFELSEVE SLRLEAICDI TFPPGLSQLV HLQELSLLHS PARLPFSLQV
FLRDHLKVMR VKCEELREVP LWVFGLRGLE ELHLEGLFPQ ELARAATLES LRELKQLKVL
SLRSNAGKVP ASVTDVAGHL QRLSLHNDGA RLVALNSLKK LAALRELELV ACGLERIPHA
VFSLGALQEL DLKDNHLRSI EEILSFQHCR KLVTLRLWHN QIAYVPEHVR KLRSLEQLYL
SYNKLETLPS QLGLCSGLRL LDVSHNGLHS LPPEVGLLQN LQHLALSYNA LEALPEELFF
CRKLRTLLLG DNQLSQLSPH VGALRALSRL ELKGNRLEAL PEELGNCGGL KKAGLLVEDT
LYQGLPAEVR DKMEEE
