ID ANO6_HUMAN Reviewed; 910 AA.
AC Q4KMQ2; A6NNM6; B9EGG0; E7ENK4; E9PB30; E9PCT2; Q8N3Q2;
DT 13-SEP-2005, integrated into UniProtKB/Swiss-Prot.
DT 17-OCT-2006, sequence version 2.
DT 02-OCT-2024, entry version 161.
DE RecName: Full=Anoctamin-6 {ECO:0000305};
DE AltName: Full=Small-conductance calcium-activated nonselective cation channel;
DE Short=SCAN channel;
DE AltName: Full=Transmembrane protein 16F;
GN Name=ANO6 {ECO:0000312|HGNC:HGNC:25240};
GN Synonyms=TMEM16F {ECO:0000303|PubMed:33827113};
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 GENOMIC DNA].
RX PubMed=16541075; DOI=10.1038/nature04569;
RA Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y.,
RA Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C.,
RA Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M., Kovar-Smith C.,
RA Lewis L.R., Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R.,
RA Montgomery K.T., Morgan M.B., Nazareth L.V., Scott G., Sodergren E.,
RA Song X.-Z., Steffen D., Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y.,
RA Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G.,
RA Chen Z., Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H.,
RA Draper H., Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S.,
RA Kelly S.H., Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M.,
RA Nguyen B.-V., Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H.,
RA Santibanez J., Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q.,
RA Williams G.A., Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V.,
RA Bailey M., Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E.,
RA Burkett C.E., Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K.,
RA Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D.,
RA Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M., Dathorne S.R.,
RA David R., Davis C.M., Davy-Carroll L., Deshazo D.R., Donlin J.E.,
RA D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J., Escotto M., Flagg N.,
RA Forbes L.D., Gabisi A.M., Garza M., Hamilton C., Henderson N.,
RA Hernandez O., Hines S., Hogues M.E., Huang M., Idlebird D.G., Johnson R.,
RA Jolivet A., Jones S., Kagan R., King L.M., Leal B., Lebow H., Lee S.,
RA LeVan J.M., Lewis L.C., London P., Lorensuhewa L.M., Loulseged H.,
RA Lovett D.A., Lucier A., Lucier R.L., Ma J., Madu R.C., Mapua P.,
RA Martindale A.D., Martinez E., Massey E., Mawhiney S., Meador M.G.,
RA Mendez S., Mercado C., Mercado I.C., Merritt C.E., Miner Z.L., Minja E.,
RA Mitchell T., Mohabbat F., Mohabbat K., Montgomery B., Moore N., Morris S.,
RA Munidasa M., Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O.,
RA Nwokenkwo S., Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J.,
RA Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A.,
RA Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M.,
RA Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I.,
RA Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A.,
RA Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D., Trejos Z.Y.,
RA Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I., Vera V.A.,
RA Villasana D.M., Wang L., Ward-Moore S., Warren J.T., Wei X., White F.,
RA Williamson A.L., Wleczyk R., Wooden H.S., Wooden S.H., Yen J., Yoon L.,
RA Yoon V., Zorrilla S.E., Nelson D., Kucherlapati R., Weinstock G.,
RA Gibbs R.A.;
RT "The finished DNA sequence of human chromosome 12.";
RL Nature 440:346-351(2006).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Placenta, and Testis;
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 772-910 (ISOFORM 1/2).
RC TISSUE=Adipose tissue;
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 [4]
RP TISSUE SPECIFICITY.
RX PubMed=15067359;
RA Katoh M., Katoh M.;
RT "Identification and characterization of TMEM16E and TMEM16F genes in
RT silico.";
RL Int. J. Oncol. 24:1345-1349(2004).
RN [5]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-493.
RC TISSUE=Liver;
RX PubMed=19159218; DOI=10.1021/pr8008012;
RA Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.;
RT "Glycoproteomics analysis of human liver tissue by combination of multiple
RT enzyme digestion and hydrazide chemistry.";
RL J. Proteome Res. 8:651-661(2009).
RN [6]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=20056604; DOI=10.1074/jbc.m109.065367;
RA Schreiber R., Uliyakina I., Kongsuphol P., Warth R., Mirza M.,
RA Martins J.R., Kunzelmann K.;
RT "Expression and function of epithelial anoctamins.";
RL J. Biol. Chem. 285:7838-7845(2010).
RN [7]
RP FUNCTION, SUBCELLULAR LOCATION, AND INVOLVEMENT IN SCOTT SYNDROME.
RX PubMed=21107324; DOI=10.1038/nature09583;
RA Suzuki J., Umeda M., Sims P.J., Nagata S.;
RT "Calcium-dependent phospholipid scrambling by TMEM16F.";
RL Nature 468:834-838(2010).
RN [8]
RP REVIEW.
RX PubMed=21642943; DOI=10.1038/aps.2011.48;
RA Duran C., Hartzell H.C.;
RT "Physiological roles and diseases of Tmem16/Anoctamin proteins: are they
RT all chloride channels?";
RL Acta Pharmacol. Sin. 32:685-692(2011).
RN [9]
RP REVIEW.
RX PubMed=21607626; DOI=10.1007/s00424-011-0975-9;
RA Kunzelmann K., Tian Y., Martins J.R., Faria D., Kongsuphol P.,
RA Ousingsawat J., Thevenod F., Roussa E., Rock J., Schreiber R.;
RT "Anoctamins.";
RL Pflugers Arch. 462:195-208(2011).
RN [10]
RP FUNCTION.
RX PubMed=22006324; DOI=10.1073/pnas.1108094108;
RA Martins J.R., Faria D., Kongsuphol P., Reisch B., Schreiber R.,
RA Kunzelmann K.;
RT "Anoctamin 6 is an essential component of the outwardly rectifying chloride
RT channel.";
RL Proc. Natl. Acad. Sci. U.S.A. 108:18168-18172(2011).
RN [11]
RP SUBCELLULAR LOCATION.
RX PubMed=22075693; DOI=10.1152/ajpcell.00140.2011;
RA Duran C., Qu Z., Osunkoya A.O., Cui Y., Hartzell H.C.;
RT "ANOs 3-7 in the anoctamin/Tmem16 Cl- channel family are intracellular
RT proteins.";
RL Am. J. Physiol. 302:C482-C493(2012).
RN [12]
RP REVIEW.
RX PubMed=22302790; DOI=10.1113/expphysiol.2011.058214;
RA Winpenny J.P., Gray M.A.;
RT "The anoctamin (TMEM16) gene family: calcium-activated chloride channels
RT come of age.";
RL Exp. Physiol. 97:175-176(2012).
RN [13]
RP REVIEW, AND ABSENCE OF CALCIUM-ACTIVATED CHLORIDE CHANNEL ACTIVITY.
RX PubMed=21984732; DOI=10.1113/expphysiol.2011.058198;
RA Scudieri P., Sondo E., Ferrera L., Galietta L.J.;
RT "The anoctamin family: TMEM16A and TMEM16B as calcium-activated chloride
RT channels.";
RL Exp. Physiol. 97:177-183(2012).
RN [14]
RP REVIEW, AND FUNCTION.
RX PubMed=21908539; DOI=10.1113/expphysiol.2011.058206;
RA Kunzelmann K., Schreiber R., Kmit A., Jantarajit W., Martins J.R.,
RA Faria D., Kongsuphol P., Ousingsawat J., Tian Y.;
RT "Expression and function of epithelial anoctamins.";
RL Exp. Physiol. 97:184-192(2012).
RN [15]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=22946059; DOI=10.1242/jcs.109553;
RA Tian Y., Schreiber R., Kunzelmann K.;
RT "Anoctamins are a family of Ca2+ activated Cl- channels.";
RL J. Cell Sci. 125:4991-4998(2012).
RN [16]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [17]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25944712; DOI=10.1002/pmic.201400617;
RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT "N-terminome analysis of the human mitochondrial proteome.";
RL Proteomics 15:2519-2524(2015).
RN [18]
RP FUNCTION (MICROBIAL INFECTION), AND INDUCTION BY SARS-COV-2 INFECTION
RP (MICROBIAL INFECTION).
RX PubMed=33827113; DOI=10.1038/s41586-021-03491-6;
RA Braga L., Ali H., Secco I., Chiavacci E., Neves G., Goldhill D., Penn R.,
RA Jimenez-Guardeno J.M., Ortega-Prieto A.M., Bussani R., Cannata A.,
RA Rizzari G., Collesi C., Schneider E., Arosio D., Shah A.M., Barclay W.S.,
RA Malim M.H., Burrone J., Giacca M.;
RT "Drugs that inhibit TMEM16 proteins block SARS-CoV-2 Spike-induced
RT syncytia.";
RL Nature 594:88-93(2021).
CC -!- FUNCTION: Small-conductance calcium-activated nonselective cation
CC (SCAN) channel which acts as a regulator of phospholipid scrambling in
CC platelets and osteoblasts. Phospholipid scrambling results in surface
CC exposure of phosphatidylserine which in platelets is essential to
CC trigger the clotting system whereas in osteoblasts is essential for the
CC deposition of hydroxyapatite during bone mineralization. Has calcium-
CC dependent phospholipid scramblase activity; scrambles
CC phosphatidylserine, phosphatidylcholine and galactosylceramide (By
CC similarity). Can generate outwardly rectifying chloride channel
CC currents in airway epithelial cells and Jurkat T lymphocytes.
CC {ECO:0000250|UniProtKB:Q6P9J9, ECO:0000269|PubMed:20056604,
CC ECO:0000269|PubMed:21107324, ECO:0000269|PubMed:21908539,
CC ECO:0000269|PubMed:22006324, ECO:0000269|PubMed:22946059}.
CC -!- FUNCTION: (Microbial infection) Upon SARS coronavirus-2/SARS-CoV-2
CC infection, is activated by spike protein which increases the amplitude
CC of spontaneous Ca(2+) signals and is required for spike-mediated
CC syncytia. {ECO:0000269|PubMed:33827113}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 1,2-diacyl-sn-glycero-3-phospho-L-serine(in) = a 1,2-diacyl-
CC sn-glycero-3-phospho-L-serine(out); Xref=Rhea:RHEA:38663,
CC ChEBI:CHEBI:57262; Evidence={ECO:0000250|UniProtKB:Q6P9J9};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38664;
CC Evidence={ECO:0000250|UniProtKB:Q6P9J9};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a beta-D-galactosyl-(1<->1')-N-acylsphing-4-enine(out) = a
CC beta-D-galactosyl-(1<->1')-N-acylsphing-4-enine(in);
CC Xref=Rhea:RHEA:38899, ChEBI:CHEBI:18390;
CC Evidence={ECO:0000250|UniProtKB:Q6P9J9};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38900;
CC Evidence={ECO:0000250|UniProtKB:Q6P9J9};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 1,2-diacyl-sn-glycero-3-phosphocholine(in) = a 1,2-diacyl-
CC sn-glycero-3-phosphocholine(out); Xref=Rhea:RHEA:38571,
CC ChEBI:CHEBI:57643; Evidence={ECO:0000250|UniProtKB:Q6P9J9};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:38573;
CC Evidence={ECO:0000250|UniProtKB:Q6P9J9};
CC -!- ACTIVITY REGULATION: Exhibits synergistic gating by Ca(2+) and voltage
CC (By similarity). Inhibited by some non-specific cation channel blockers
CC such as: ruthenium red, 2-aminoethyl diphenylborinate (2APB),
CC gadolinium and cadmium ions (By similarity).
CC {ECO:0000250|UniProtKB:Q6P9J9}.
CC -!- ACTIVITY REGULATION: (Microbial infection) Activated by SARS
CC coronavirus-2/SARS-CoV-2 spike protein. {ECO:0000269|PubMed:33827113}.
CC -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:Q6P9J9}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:20056604,
CC ECO:0000269|PubMed:21107324, ECO:0000269|PubMed:22075693,
CC ECO:0000269|PubMed:22946059}; Multi-pass membrane protein
CC {ECO:0000269|PubMed:20056604, ECO:0000269|PubMed:21107324,
CC ECO:0000269|PubMed:22075693, ECO:0000269|PubMed:22946059}. Note=Shows
CC an intracellular localization according to PubMed:22075693.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1;
CC IsoId=Q4KMQ2-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q4KMQ2-2; Sequence=VSP_042893;
CC Name=3;
CC IsoId=Q4KMQ2-3; Sequence=VSP_046819;
CC Name=4;
CC IsoId=Q4KMQ2-4; Sequence=VSP_046820;
CC -!- TISSUE SPECIFICITY: Expressed in embryonic stem cell, fetal liver,
CC retina, chronic myologenous leukemia and intestinal cancer.
CC {ECO:0000269|PubMed:15067359}.
CC -!- INDUCTION: (Microbial infection) Expression is induced by SARS
CC coronavirus-2/SARS-CoV-2 spike protein. {ECO:0000269|PubMed:33827113}.
CC -!- DISEASE: Scott syndrome (SCTS) [MIM:262890]: A mild bleeding disorder
CC due to impaired surface exposure of procoagulant phosphatidylserine
CC (PS) on platelets and other blood cells, following activation with
CC Ca(2+)-elevating agents. {ECO:0000269|PubMed:21107324}. Note=The
CC disease is caused by variants affecting the gene represented in this
CC entry.
CC -!- MISCELLANEOUS: The term 'anoctamin' was coined because these channels
CC are anion selective and are predicted to have eight (OCT) transmembrane
CC segments. There is some dissatisfaction in the field with the Ano
CC nomenclature because it is not certain that all the members of this
CC family are anion channels or have the 8-transmembrane topology.
CC {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the anoctamin family. {ECO:0000305}.
CC -!- CAUTION: Contains ten transmembrane regions, not eight as predicted.
CC {ECO:0000250|UniProtKB:Q6P9J9}.
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DR EMBL; AC009248; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC009778; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC063924; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC098410; AAH98410.1; -; mRNA.
DR EMBL; BC136445; AAI36446.1; -; mRNA.
DR EMBL; AL833405; CAD38638.1; -; mRNA.
DR CCDS; CCDS31782.1; -. [Q4KMQ2-1]
DR CCDS; CCDS44865.1; -. [Q4KMQ2-4]
DR CCDS; CCDS44866.1; -. [Q4KMQ2-3]
DR CCDS; CCDS55819.1; -. [Q4KMQ2-2]
DR RefSeq; NP_001020527.2; NM_001025356.2. [Q4KMQ2-1]
DR RefSeq; NP_001136150.1; NM_001142678.1. [Q4KMQ2-3]
DR RefSeq; NP_001136151.1; NM_001142679.1. [Q4KMQ2-4]
DR RefSeq; NP_001191732.1; NM_001204803.1. [Q4KMQ2-2]
DR AlphaFoldDB; Q4KMQ2; -.
DR SMR; Q4KMQ2; -.
DR BioGRID; 128218; 143.
DR IntAct; Q4KMQ2; 69.
DR MINT; Q4KMQ2; -.
DR STRING; 9606.ENSP00000409126; -.
DR TCDB; 1.A.17.1.4; the calcium-dependent chloride channel (ca-clc) family.
DR GlyConnect; 1014; 7 N-Linked glycans (2 sites).
DR GlyCosmos; Q4KMQ2; 6 sites, 7 glycans.
DR GlyGen; Q4KMQ2; 6 sites, 7 N-linked glycans (2 sites).
DR iPTMnet; Q4KMQ2; -.
DR PhosphoSitePlus; Q4KMQ2; -.
DR SwissPalm; Q4KMQ2; -.
DR BioMuta; ANO6; -.
DR DMDM; 116242820; -.
DR jPOST; Q4KMQ2; -.
DR MassIVE; Q4KMQ2; -.
DR PaxDb; 9606-ENSP00000409126; -.
DR PeptideAtlas; Q4KMQ2; -.
DR ProteomicsDB; 19131; -.
DR ProteomicsDB; 19507; -.
DR ProteomicsDB; 62203; -. [Q4KMQ2-1]
DR ProteomicsDB; 62204; -. [Q4KMQ2-2]
DR Pumba; Q4KMQ2; -.
DR ABCD; Q4KMQ2; 1 sequenced antibody.
DR Antibodypedia; 42608; 157 antibodies from 22 providers.
DR DNASU; 196527; -.
DR Ensembl; ENST00000320560.13; ENSP00000320087.8; ENSG00000177119.17. [Q4KMQ2-1]
DR Ensembl; ENST00000423947.7; ENSP00000409126.3; ENSG00000177119.17. [Q4KMQ2-2]
DR Ensembl; ENST00000425752.6; ENSP00000391417.2; ENSG00000177119.17. [Q4KMQ2-4]
DR Ensembl; ENST00000441606.2; ENSP00000413137.2; ENSG00000177119.17. [Q4KMQ2-3]
DR Ensembl; ENST00000680201.1; ENSP00000506222.1; ENSG00000177119.17. [Q4KMQ2-1]
DR GeneID; 196527; -.
DR KEGG; hsa:196527; -.
DR MANE-Select; ENST00000320560.13; ENSP00000320087.8; NM_001025356.3; NP_001020527.2.
DR UCSC; uc001roo.4; human. [Q4KMQ2-1]
DR AGR; HGNC:25240; -.
DR CTD; 196527; -.
DR DisGeNET; 196527; -.
DR GeneCards; ANO6; -.
DR HGNC; HGNC:25240; ANO6.
DR HPA; ENSG00000177119; Low tissue specificity.
DR MalaCards; ANO6; -.
DR MIM; 262890; phenotype.
DR MIM; 608663; gene.
DR neXtProt; NX_Q4KMQ2; -.
DR OpenTargets; ENSG00000177119; -.
DR Orphanet; 806; Scott syndrome.
DR PharmGKB; PA164715690; -.
DR VEuPathDB; HostDB:ENSG00000177119; -.
DR eggNOG; KOG2514; Eukaryota.
DR GeneTree; ENSGT00940000158969; -.
DR HOGENOM; CLU_006685_1_3_1; -.
DR InParanoid; Q4KMQ2; -.
DR OMA; HYTMDGY; -.
DR OrthoDB; 534027at2759; -.
DR PhylomeDB; Q4KMQ2; -.
DR TreeFam; TF314265; -.
DR PathwayCommons; Q4KMQ2; -.
DR Reactome; R-HSA-2672351; Stimuli-sensing channels.
DR Reactome; R-HSA-6798695; Neutrophil degranulation.
DR Reactome; R-HSA-9733458; Induction of Cell-Cell Fusion.
DR SignaLink; Q4KMQ2; -.
DR SIGNOR; Q4KMQ2; -.
DR BioGRID-ORCS; 196527; 14 hits in 1165 CRISPR screens.
DR ChiTaRS; ANO6; human.
DR GenomeRNAi; 196527; -.
DR Pharos; Q4KMQ2; Tbio.
DR PRO; PR:Q4KMQ2; -.
DR Proteomes; UP000005640; Chromosome 12.
DR RNAct; Q4KMQ2; protein.
DR Bgee; ENSG00000177119; Expressed in epithelial cell of pancreas and 192 other cell types or tissues.
DR ExpressionAtlas; Q4KMQ2; baseline and differential.
DR GO; GO:0009986; C:cell surface; HDA:UniProtKB.
DR GO; GO:0034707; C:chloride channel complex; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0016020; C:membrane; HDA:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IDA:HPA.
DR GO; GO:0035579; C:specific granule membrane; TAS:Reactome.
DR GO; GO:0070821; C:tertiary granule membrane; TAS:Reactome.
DR GO; GO:0005227; F:calcium-activated cation channel activity; IDA:UniProtKB.
DR GO; GO:0005254; F:chloride channel activity; IBA:GO_Central.
DR GO; GO:0005229; F:intracellularly calcium-gated chloride channel activity; IMP:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0017128; F:phospholipid scramblase activity; IMP:FlyBase.
DR GO; GO:0046983; F:protein dimerization activity; IEA:InterPro.
DR GO; GO:0005247; F:voltage-gated chloride channel activity; IMP:UniProtKB.
DR GO; GO:0005244; F:voltage-gated monoatomic ion channel activity; ISS:UniProtKB.
DR GO; GO:0002543; P:activation of blood coagulation via clotting cascade; IMP:UniProtKB.
DR GO; GO:0032060; P:bleb assembly; IMP:UniProtKB.
DR GO; GO:0007596; P:blood coagulation; ISS:UniProtKB.
DR GO; GO:0061590; P:calcium activated phosphatidylcholine scrambling; IBA:GO_Central.
DR GO; GO:0061589; P:calcium activated phosphatidylserine scrambling; IBA:GO_Central.
DR GO; GO:0070588; P:calcium ion transmembrane transport; IGI:UniProtKB.
DR GO; GO:1902476; P:chloride transmembrane transport; IMP:UniProtKB.
DR GO; GO:0006821; P:chloride transport; IMP:UniProtKB.
DR GO; GO:0034220; P:monoatomic ion transmembrane transport; TAS:Reactome.
DR GO; GO:0045794; P:negative regulation of cell volume; IMP:UniProtKB.
DR GO; GO:0097045; P:phosphatidylserine exposure on blood platelet; IMP:UniProtKB.
DR GO; GO:0017121; P:plasma membrane phospholipid scrambling; IMP:UniProtKB.
DR GO; GO:0046931; P:pore complex assembly; IMP:UniProtKB.
DR GO; GO:0043065; P:positive regulation of apoptotic process; ISS:UniProtKB.
DR GO; GO:0030501; P:positive regulation of bone mineralization; IMP:UniProtKB.
DR GO; GO:2000353; P:positive regulation of endothelial cell apoptotic process; IMP:UniProtKB.
DR GO; GO:0034767; P:positive regulation of monoatomic ion transmembrane transport; IMP:UniProtKB.
DR GO; GO:0090026; P:positive regulation of monocyte chemotaxis; IMP:UniProtKB.
DR GO; GO:0060100; P:positive regulation of phagocytosis, engulfment; ISS:UniProtKB.
DR GO; GO:1903766; P:positive regulation of potassium ion export across plasma membrane; ISS:BHF-UCL.
DR GO; GO:0035590; P:purinergic nucleotide receptor signaling pathway; IMP:UniProtKB.
DR GO; GO:0035725; P:sodium ion transmembrane transport; IGI:UniProtKB.
DR InterPro; IPR032394; Anoct_dimer.
DR InterPro; IPR007632; Anoctamin.
DR InterPro; IPR049452; Anoctamin_TM.
DR PANTHER; PTHR12308; ANOCTAMIN; 1.
DR PANTHER; PTHR12308:SF21; ANOCTAMIN-6; 1.
DR Pfam; PF16178; Anoct_dimer; 1.
DR Pfam; PF04547; Anoctamin; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Calcium; Cell membrane; Chloride; Chloride channel;
KW Disulfide bond; Glycoprotein; Host-virus interaction; Ion channel;
KW Ion transport; Lipid transport; Membrane; Metal-binding;
KW Proteomics identification; Reference proteome; Transmembrane;
KW Transmembrane helix; Transport; Voltage-gated channel.
FT CHAIN 1..910
FT /note="Anoctamin-6"
FT /id="PRO_0000191757"
FT TOPO_DOM 1..300
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 301..321
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:Q6P9J9"
FT TOPO_DOM 322..375
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 376..396
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:Q6P9J9"
FT TOPO_DOM 397..455
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 456..476
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:Q6P9J9"
FT TOPO_DOM 477..509
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 510..530
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:Q6P9J9"
FT TOPO_DOM 531..551
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 552..572
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:Q6P9J9"
FT TOPO_DOM 573..601
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 602..621
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:Q6P9J9"
FT TOPO_DOM 622..663
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 664..684
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:Q6P9J9"
FT TRANSMEM 685..705
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:Q6P9J9"
FT TOPO_DOM 706..722
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 723..743
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:Q6P9J9"
FT TOPO_DOM 744..836
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 837..857
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:Q6P9J9"
FT TOPO_DOM 858..910
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT BINDING 623
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:Q6P9J9"
FT BINDING 666
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:Q6P9J9"
FT BINDING 669
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:Q6P9J9"
FT CARBOHYD 329
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 361
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 493
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:19159218"
FT CARBOHYD 777
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 790
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 802
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 330..371
FT /evidence="ECO:0000250|UniProtKB:Q6P9J9"
FT DISULFID 337..364
FT /evidence="ECO:0000250|UniProtKB:Q6P9J9"
FT DISULFID 348..806
FT /evidence="ECO:0000250|UniProtKB:Q6P9J9"
FT DISULFID 351..355
FT /evidence="ECO:0000250|UniProtKB:Q6P9J9"
FT DISULFID 595..600
FT /evidence="ECO:0000250|UniProtKB:Q6P9J9"
FT VAR_SEQ 1..23
FT /note="MKKMSRNVLLQMEEEEDDDDGDI -> MFCAA (in isoform 3)"
FT /evidence="ECO:0000305"
FT /id="VSP_046819"
FT VAR_SEQ 23
FT /note="I -> IGDVPASRRPFLTPHTHLPSSL (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_042893"
FT VAR_SEQ 843..910
FT /note="HVIYSVKFFISYAIPDVSKRTKSKIQREKYLTQKLLHENHLKDMTKNMGVIA
FT ERMIEAVDNNLRPKSE -> YLALLPRLGHSGMILAHCNLRLPVDCCMCYRFVDEIRLL
FT EQLTSDFIDSLYYIFSISIISIFFSVTFFFLLLSLGPTPCFSVSNFLS (in
FT isoform 4)"
FT /evidence="ECO:0000305"
FT /id="VSP_046820"
FT VARIANT 128
FT /note="A -> T (in dbSNP:rs2162321)"
FT /id="VAR_028109"
FT CONFLICT 837
FT /note="F -> L (in Ref. 2; AAH98410)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 910 AA; 106165 MW; 8F7F1CB78FAAEB78 CRC64;
MKKMSRNVLL QMEEEEDDDD GDIVLENLGQ TIVPDLGSLE SQHDFRTPEF EEFNGKPDSL
FFNDGQRRID FVLVYEDESR KETNKKGTNE KQRRKRQAYE SNLICHGLQL EATRSVLDDK
LVFVKVHAPW EVLCTYAEIM HIKLPLKPND LKNRSSAFGT LNWFTKVLSV DESIIKPEQE
FFTAPFEKNR MNDFYIVDRD AFFNPATRSR IVYFILSRVK YQVINNVSKF GINRLVNSGI
YKAAFPLHDC KFRRQSEDPS CPNERYLLYR EWAHPRSIYK KQPLDLIRKY YGEKIGIYFA
WLGYYTQMLL LAAVVGVACF LYGYLNQDNC TWSKEVCHPD IGGKIIMCPQ CDRLCPFWKL
NITCESSKKL CIFDSFGTLV FAVFMGVWVT LFLEFWKRRQ AELEYEWDTV ELQQEEQARP
EYEARCTHVV INEITQEEER IPFTAWGKCI RITLCASAVF FWILLIIASV IGIIVYRLSV
FIVFSAKLPK NINGTDPIQK YLTPQTATSI TASIISFIII MILNTIYEKV AIMITNFELP
RTQTDYENSL TMKMFLFQFV NYYSSCFYIA FFKGKFVGYP GDPVYWLGKY RNEECDPGGC
LLELTTQLTI IMGGKAIWNN IQEVLLPWIM NLIGRFHRVS GSEKITPRWE QDYHLQPMGK
LGLFYEYLEM IIQFGFVTLF VASFPLAPLL ALVNNILEIR VDAWKLTTQF RRLVPEKAQD
IGAWQPIMQG IAILAVVTNA MIIAFTSDMI PRLVYYWSFS VPPYGDHTSY TMEGYINNTL
SIFKVADFKN KSKGNPYSDL GNHTTCRYRD FRYPPGHPQE YKHNIYYWHV IAAKLAFIIV
MEHVIYSVKF FISYAIPDVS KRTKSKIQRE KYLTQKLLHE NHLKDMTKNM GVIAERMIEA
VDNNLRPKSE
//