ID ANO7_HUMAN Reviewed; 933 AA. AC Q6IWH7; Q6IWH6; DT 29-MAY-2007, integrated into UniProtKB/Swiss-Prot. DT 31-MAY-2011, sequence version 2. DT 27-MAR-2024, entry version 152. DE RecName: Full=Anoctamin-7; DE AltName: Full=Dresden transmembrane protein of the prostate; DE Short=D-TMPP; DE AltName: Full=IPCA-5; DE AltName: Full=New gene expressed in prostate; DE AltName: Full=Prostate cancer-associated protein 5; DE AltName: Full=Transmembrane protein 16G; GN Name=ANO7; Synonyms=NGEP, PCANAP5, TMEM16G; 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 [MRNA] (ISOFORMS 1 AND 2), VARIANT LYS-912, TISSUE RP SPECIFICITY, SUBCELLULAR LOCATION, AND TOPOLOGY. RX PubMed=14981236; DOI=10.1073/pnas.0308746101; RA Bera T.K., Das S., Maeda H., Beers R., Wolfgang C.D., Kumar V., Hahn Y., RA Lee B., Pastan I.; RT "NGEP, a gene encoding a membrane protein detected only in prostate cancer RT and normal prostate."; RL Proc. Natl. Acad. Sci. U.S.A. 101:3059-3064(2004). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=15815621; DOI=10.1038/nature03466; RA Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., RA Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., RA Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., RA Du H., Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., RA Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., RA Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., RA Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., RA Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., RA Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., RA McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., RA Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., RA Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., RA Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., RA Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., RA Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., RA Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., RA Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., RA Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., RA Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., RA Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., RA Wilson R.K.; RT "Generation and annotation of the DNA sequences of human chromosomes 2 and RT 4."; RL Nature 434:724-731(2005). RN [3] RP IDENTIFICATION. RX PubMed=10613842; DOI=10.1101/gr.9.12.1198; RA Walker M.G., Volkmuth W., Sprinzak E., Hodgson D., Klingler T.; RT "Prediction of gene function by genome-scale expression analysis: prostate RT cancer-associated genes."; RL Genome Res. 9:1198-1203(1999). RN [4] RP IDENTIFICATION. RX PubMed=15375614; RA Katoh M., Katoh M.; RT "Characterization of human TMEM16G gene in silico."; RL Int. J. Mol. Med. 14:759-764(2004). RN [5] RP ALTERNATIVE SPLICING (ISOFORM 3), TISSUE SPECIFICITY, AND INDUCTION BY RP ANDROGEN. RX PubMed=15761874; DOI=10.1002/pros.20250; RA Kiessling A., Weigle B., Fuessel S., Ebner R., Meye A., Rieger M.A., RA Schmitz M., Temme A., Bachmann M., Wirth M.P., Rieber E.P.; RT "D-TMPP: a novel androgen-regulated gene preferentially expressed in RT prostate and prostate cancer that is the first characterized member of an RT eukaryotic gene family."; RL Prostate 64:387-400(2005). RN [6] RP FUNCTION, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY. RX PubMed=17308099; DOI=10.1158/0008-5472.can-06-2673; RA Das S., Hahn Y., Nagata S., Willingham M.C., Bera T.K., Lee B., Pastan I.; RT "NGEP, a prostate-specific plasma membrane protein that promotes the RT association of LNCaP cells."; RL Cancer Res. 67:1594-1601(2007). RN [7] RP GLYCOSYLATION AT ASN-809 AND ASN-824, AND MEMBRANE TOPOLOGY. RX PubMed=18676855; DOI=10.1158/0008-5472.can-08-0870; RA Das S., Hahn Y., Walker D.A., Nagata S., Willingham M.C., Peehl D.M., RA Bera T.K., Lee B., Pastan I.; RT "Topology of NGEP, a prostate-specific cell:cell junction protein widely RT expressed in many cancers of different grade level."; RL Cancer Res. 68:6306-6312(2008). RN [8] RP 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 [9] 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 [10] 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 [11] RP ABSENCE OF CALCIUM-ACTIVATED CHLORIDE CHANNEL ACTIVITY, AND SUBCELLULAR RP 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 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). CC -!- FUNCTION: Has calcium-dependent phospholipid scramblase activity; CC scrambles phosphatidylserine, phosphatidylcholine and CC galactosylceramide (By similarity). Does not exhibit calcium-activated CC chloride channel (CaCC) activity (PubMed:22075693). May play a role in CC cell-cell interactions (PubMed:17308099). CC {ECO:0000250|UniProtKB:Q14AT5, ECO:0000269|PubMed:17308099, CC ECO:0000269|PubMed:22075693}. 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:Q14AT5}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38664; CC Evidence={ECO:0000250|UniProtKB:Q14AT5}; 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:Q14AT5}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38900; CC Evidence={ECO:0000250|UniProtKB:Q14AT5}; 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:Q14AT5}; CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:38573; CC Evidence={ECO:0000250|UniProtKB:Q14AT5}; CC -!- SUBCELLULAR LOCATION: [Isoform 1]: Cell membrane CC {ECO:0000269|PubMed:14981236, ECO:0000269|PubMed:17308099, CC ECO:0000269|PubMed:20056604, ECO:0000269|PubMed:22946059}; Multi-pass CC membrane protein {ECO:0000255}. Cell junction CC {ECO:0000269|PubMed:17308099}. Endoplasmic reticulum CC {ECO:0000269|PubMed:22075693}. Note=Concentrates at sites of cell-cell CC contact (PubMed:17308099). Shows an intracellular localization CC according to PubMed:22075693 and PubMed:20056604. CC {ECO:0000269|PubMed:17308099, ECO:0000269|PubMed:20056604, CC ECO:0000269|PubMed:22075693}. CC -!- SUBCELLULAR LOCATION: [Isoform 2]: Cytoplasm, cytosol CC {ECO:0000269|PubMed:14981236}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=3; CC Name=1; Synonyms=NGEP-L; CC IsoId=Q6IWH7-1; Sequence=Displayed; CC Name=2; Synonyms=NGEP-S; CC IsoId=Q6IWH7-2; Sequence=VSP_026004, VSP_026005, VSP_026006; CC Name=3; Synonyms=D-TMPP; CC IsoId=Q6IWH7-3; Sequence=VSP_026004, VSP_026007, VSP_026008; CC -!- TISSUE SPECIFICITY: Specifically expressed in epithelial cells of the CC prostate (at protein level). {ECO:0000269|PubMed:14981236, CC ECO:0000269|PubMed:15761874, ECO:0000269|PubMed:17308099}. CC -!- INDUCTION: Up-regulated by androgen. {ECO:0000269|PubMed:15761874}. CC -!- MISCELLANEOUS: The term 'anoctamin' was coined because these channels CC are anion selective and have eight (OCT) transmembrane segments. There CC is some dissatisfaction in the field with the Ano nomenclature because CC it is not certain that all the members of this family are anion CC channels or have the 8-transmembrane topology. CC -!- SIMILARITY: Belongs to the anoctamin family. {ECO:0000305}. CC -!- CAUTION: It is uncertain whether Met-1 or Met-55 is the initiator. CC {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AY617079; AAT40139.1; -; mRNA. DR EMBL; AY617080; AAT40140.1; -; mRNA. DR EMBL; AC005237; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AC104841; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AC111201; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR RefSeq; NP_001001666.1; NM_001001666.3. DR RefSeq; NP_001001891.2; NM_001001891.3. DR AlphaFoldDB; Q6IWH7; -. DR SMR; Q6IWH7; -. DR BioGRID; 119107; 69. DR STRING; 9606.ENSP00000274979; -. DR TCDB; 1.A.17.1.27; the calcium-dependent chloride channel (ca-clc) family. DR GlyCosmos; Q6IWH7; 2 sites, No reported glycans. DR GlyGen; Q6IWH7; 2 sites. DR iPTMnet; Q6IWH7; -. DR PhosphoSitePlus; Q6IWH7; -. DR BioMuta; ANO7; -. DR DMDM; 334302764; -. DR jPOST; Q6IWH7; -. DR MassIVE; Q6IWH7; -. DR PaxDb; 9606-ENSP00000274979; -. DR PeptideAtlas; Q6IWH7; -. DR ProteomicsDB; 66501; -. [Q6IWH7-1] DR ProteomicsDB; 66502; -. [Q6IWH7-2] DR ProteomicsDB; 66503; -. [Q6IWH7-3] DR Antibodypedia; 47723; 134 antibodies from 26 providers. DR DNASU; 50636; -. DR Ensembl; ENST00000274979.12; ENSP00000274979.8; ENSG00000146205.15. [Q6IWH7-1] DR GeneID; 50636; -. DR KEGG; hsa:50636; -. DR UCSC; uc002waw.4; human. [Q6IWH7-1] DR AGR; HGNC:31677; -. DR CTD; 50636; -. DR DisGeNET; 50636; -. DR GeneCards; ANO7; -. DR HGNC; HGNC:31677; ANO7. DR HPA; ENSG00000146205; Tissue enhanced (intestine, prostate, stomach). DR MIM; 605096; gene. DR neXtProt; NX_Q6IWH7; -. DR OpenTargets; ENSG00000146205; -. DR PharmGKB; PA32980; -. DR VEuPathDB; HostDB:ENSG00000146205; -. DR eggNOG; KOG2514; Eukaryota. DR GeneTree; ENSGT00940000158551; -. DR HOGENOM; CLU_1502990_0_0_1; -. DR InParanoid; Q6IWH7; -. DR OMA; KYEDAFI; -. DR OrthoDB; 534027at2759; -. DR PhylomeDB; Q6IWH7; -. DR TreeFam; TF314265; -. DR PathwayCommons; Q6IWH7; -. DR Reactome; R-HSA-2672351; Stimuli-sensing channels. DR Reactome; R-HSA-9733458; Induction of Cell-Cell Fusion. DR BioGRID-ORCS; 50636; 5 hits in 1149 CRISPR screens. DR ChiTaRS; ANO7; human. DR GenomeRNAi; 50636; -. DR Pharos; Q6IWH7; Tbio. DR PRO; PR:Q6IWH7; -. DR Proteomes; UP000005640; Chromosome 2. DR RNAct; Q6IWH7; Protein. DR Bgee; ENSG00000146205; Expressed in mucosa of transverse colon and 108 other cell types or tissues. DR ExpressionAtlas; Q6IWH7; baseline and differential. DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-SubCell. DR GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell. DR GO; GO:0005783; C:endoplasmic reticulum; IDA:UniProtKB. DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB. DR GO; GO:0005254; F:chloride channel activity; IBA:GO_Central. DR GO; GO:0005229; F:intracellular calcium activated chloride channel activity; IDA:UniProtKB. DR GO; GO:0046983; F:protein dimerization activity; IEA:InterPro. DR GO; GO:0061588; P:calcium activated phospholipid scrambling; IBA:GO_Central. DR GO; GO:1902476; P:chloride transmembrane transport; IBA:GO_Central. DR GO; GO:0006821; P:chloride transport; IDA:UniProtKB. DR GO; GO:0034220; P:monoatomic ion transmembrane transport; TAS:Reactome. DR InterPro; IPR032394; Anoct_dimer. DR InterPro; IPR007632; Anoctamin. DR InterPro; IPR049452; Anoctamin_TM. DR PANTHER; PTHR12308; ANOCTAMIN; 1. DR PANTHER; PTHR12308:SF22; ANOCTAMIN-7; 1. DR Pfam; PF16178; Anoct_dimer; 1. DR Pfam; PF04547; Anoctamin; 1. DR Genevisible; Q6IWH7; HS. PE 1: Evidence at protein level; KW Alternative splicing; Cell junction; Cell membrane; Cytoplasm; KW Endoplasmic reticulum; Glycoprotein; Lipid transport; Membrane; KW Reference proteome; Transmembrane; Transmembrane helix; Transport. FT CHAIN 1..933 FT /note="Anoctamin-7" FT /id="PRO_0000289326" FT TOPO_DOM 1..355 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT TRANSMEM 356..376 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 377..420 FT /note="Extracellular" FT /evidence="ECO:0000255" FT TRANSMEM 421..441 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 442..499 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT TRANSMEM 500..520 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 521..550 FT /note="Extracellular" FT /evidence="ECO:0000255" FT TRANSMEM 551..571 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 572..588 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT TRANSMEM 589..609 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 610..714 FT /note="Extracellular" FT /evidence="ECO:0000255" FT TRANSMEM 715..735 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 736..763 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT TRANSMEM 764..784 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 785..843 FT /note="Extracellular" FT /evidence="ECO:0000255" FT TRANSMEM 844..864 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 865..933 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT REGION 43..101 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 902..933 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 903..933 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT CARBOHYD 809 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000269|PubMed:18676855" FT CARBOHYD 824 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000269|PubMed:18676855" FT VAR_SEQ 110 FT /note="Missing (in isoform 2 and isoform 3)" FT /evidence="ECO:0000303|PubMed:14981236" FT /id="VSP_026004" FT VAR_SEQ 158..180 FT /note="QDVQDGNTTVHYALLSASWAVLC -> VRGGCHGQGPRPCIHSVTHDLAA FT (in isoform 2)" FT /evidence="ECO:0000303|PubMed:14981236" FT /id="VSP_026005" FT VAR_SEQ 181..933 FT /note="Missing (in isoform 2)" FT /evidence="ECO:0000303|PubMed:14981236" FT /id="VSP_026006" FT VAR_SEQ 859 FT /note="H -> VAEAPAGSPIHGMRPRPCALPNSSTW (in isoform 3)" FT /evidence="ECO:0000305" FT /id="VSP_026007" FT VAR_SEQ 860..933 FT /note="Missing (in isoform 3)" FT /evidence="ECO:0000305" FT /id="VSP_026008" FT VARIANT 67 FT /note="V -> I (in dbSNP:rs2302054)" FT /id="VAR_032616" FT VARIANT 912 FT /note="E -> K (in dbSNP:rs7590653)" FT /evidence="ECO:0000269|PubMed:14981236" FT /id="VAR_065166" SQ SEQUENCE 933 AA; 105532 MW; D6FD42578A4BD773 CRC64; MRMAATAWAG LQGPPLPTLC PAVRTGLYCR DQAHAERWAM TSETSSGSHC ARSRMLRRRA QEEDSTVLID VSPPEAEKRG SYGSTAHASE PGGQQAAACR AGSPAKPRIA DFVLVWEEDL KLDRQQDSAA RDRTDMHRTW RETFLDNLRA AGLCVDQQDV QDGNTTVHYA LLSASWAVLC YYAEDLRLKL PLQELPNQAS NWSAGLLAWL GIPNVLLEVV PDVPPEYYSC RFRVNKLPRF LGSDNQDTFF TSTKRHQILF EILAKTPYGH EKKNLLGIHQ LLAEGVLSAA FPLHDGPFKT PPEGPQAPRL NQRQVLFQHW ARWGKWNKYQ PLDHVRRYFG EKVALYFAWL GFYTGWLLPA AVVGTLVFLV GCFLVFSDIP TQELCGSKDS FEMCPLCLDC PFWLLSSACA LAQAGRLFDH GGTVFFSLFM ALWAVLLLEY WKRKSATLAY RWDCSDYEDT EERPRPQFAA SAPMTAPNPI TGEDEPYFPE RSRARRMLAG SVVIVVMVAV VVMCLVSIIL YRAIMAIVVS RSGNTLLAAW ASRIASLTGS VVNLVFILIL SKIYVSLAHV LTRWEMHRTQ TKFEDAFTLK VFIFQFVNFY SSPVYIAFFK GRFVGYPGNY HTLFGVRNEE CAAGGCLIEL AQELLVIMVG KQVINNMQEV LIPKLKGWWQ KFRLRSKKRK AGASAGASQG PWEDDYELVP CEGLFDEYLE MVLQFGFVTI FVAACPLAPL FALLNNWVEI RLDARKFVCE YRRPVAERAQ DIGIWFHILA GLTHLAVISN AFLLAFSSDF LPRAYYRWTR AHDLRGFLNF TLARAPSSFA AAHNRTCRYR AFRDDDGHYS QTYWNLLAIR LAFVIVFEHV VFSVGRLLDL LVPDIPESVE IKVKREYYLA KQALAENEVL FGTNGTKDEQ PEGSELSSHW TPFTVPKASQ LQQ //