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ANO6_HUMAN
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   03-AUG-2022, entry version 149.
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; 129.
DR   IntAct; Q4KMQ2; 35.
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   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   EPD; Q4KMQ2; -.
DR   jPOST; Q4KMQ2; -.
DR   MassIVE; Q4KMQ2; -.
DR   MaxQB; Q4KMQ2; -.
DR   PaxDb; Q4KMQ2; -.
DR   PeptideAtlas; Q4KMQ2; -.
DR   PRIDE; Q4KMQ2; -.
DR   ProteomicsDB; 19131; -.
DR   ProteomicsDB; 19507; -.
DR   ProteomicsDB; 62203; -. [Q4KMQ2-1]
DR   ProteomicsDB; 62204; -. [Q4KMQ2-2]
DR   ABCD; Q4KMQ2; 1 sequenced antibody.
DR   Antibodypedia; 42608; 135 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   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; EKVTPRW; -.
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   SignaLink; Q4KMQ2; -.
DR   SIGNOR; Q4KMQ2; -.
DR   BioGRID-ORCS; 196527; 12 hits in 1085 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 190 other tissues.
DR   ExpressionAtlas; Q4KMQ2; baseline and differential.
DR   Genevisible; Q4KMQ2; HS.
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:UniProtKB.
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:intracellular calcium activated 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 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:0006812; P:cation transport; IDA:UniProtKB.
DR   GO; GO:1902476; P:chloride transmembrane transport; IGI:UniProtKB.
DR   GO; GO:0006821; P:chloride transport; IMP:UniProtKB.
DR   GO; GO:0002407; P:dendritic cell chemotaxis; IEA:InterPro.
DR   GO; GO:0034220; P: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 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   GO; GO:0055085; P:transmembrane transport; IBA:GO_Central.
DR   InterPro; IPR032394; Anoct_dimer.
DR   InterPro; IPR007632; Anoctamin.
DR   InterPro; IPR031295; Anoctamin-6.
DR   PANTHER; PTHR12308; PTHR12308; 1.
DR   PANTHER; PTHR12308:SF21; PTHR12308:SF21; 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   Reference proteome; Transmembrane; Transmembrane helix; Transport;
KW   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
 
 
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