ANO8_MOUSE
ID ANO8_MOUSE Reviewed; 1060 AA.
AC Q6PB70; Q05CB5; Q69ZE4;
DT 05-SEP-2006, integrated into UniProtKB/Swiss-Prot.
DT 13-OCT-2009, sequence version 3.
DT 03-AUG-2022, entry version 115.
DE RecName: Full=Anoctamin-8;
DE AltName: Full=Transmembrane protein 16H;
GN Name=Ano8; Synonyms=Kiaa1623, Tmem16h;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Brain, and Mammary tumor;
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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-1057.
RC TISSUE=Embryonic tail;
RX PubMed=15368895; DOI=10.1093/dnares/11.3.205;
RA Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA Saga Y., Seino S., Nishimura M., Kaisho T., Hoshino K., Kitamura H.,
RA Nagase T., Ohara O., Koga H.;
RT "Prediction of the coding sequences of mouse homologues of KIAA gene: IV.
RT The complete nucleotide sequences of 500 mouse KIAA-homologous cDNAs
RT identified by screening of terminal sequences of cDNA clones randomly
RT sampled from size-fractionated libraries.";
RL DNA Res. 11:205-218(2004).
RN [3]
RP IDENTIFICATION.
RX PubMed=15647853;
RA Katoh M., Katoh M.;
RT "Identification and characterization of TMEM16H gene in silico.";
RL Int. J. Mol. Med. 15:353-358(2005).
RN [4]
RP DEVELOPMENTAL STAGE.
RX PubMed=18729231; DOI=10.1002/dvdy.21676;
RA Rock J.R., Harfe B.D.;
RT "Expression of TMEM16 paralogs during murine embryogenesis.";
RL Dev. Dyn. 237:2566-2574(2008).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-318 AND SER-665, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [6]
RP TISSUE SPECIFICITY.
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 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 [8]
RP METHYLATION [LARGE SCALE ANALYSIS] AT ARG-991 AND ARG-999, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, and Embryo;
RX PubMed=24129315; DOI=10.1074/mcp.o113.027870;
RA Guo A., Gu H., Zhou J., Mulhern D., Wang Y., Lee K.A., Yang V., Aguiar M.,
RA Kornhauser J., Jia X., Ren J., Beausoleil S.A., Silva J.C., Vemulapalli V.,
RA Bedford M.T., Comb M.J.;
RT "Immunoaffinity enrichment and mass spectrometry analysis of protein
RT methylation.";
RL Mol. Cell. Proteomics 13:372-387(2014).
CC -!- FUNCTION: Does not exhibit calcium-activated chloride channel (CaCC)
CC activity. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein.
CC Note=Shows predominantly an intracellular localization with a weak
CC expression in the cell membrane. {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Predominant expression seen in epithelial tissues.
CC {ECO:0000269|PubMed:20056604}.
CC -!- DEVELOPMENTAL STAGE: Detected in the mantle layer of the neural tube
CC and in the dorsal root ganglia at 14.5 dpc.
CC {ECO:0000269|PubMed:18729231}.
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 -!- SEQUENCE CAUTION:
CC Sequence=BAD32500.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; BC027735; AAH27735.1; -; mRNA.
DR EMBL; BC059855; AAH59855.1; -; mRNA.
DR EMBL; AK173222; BAD32500.1; ALT_INIT; Transcribed_RNA.
DR CCDS; CCDS52585.1; -.
DR RefSeq; NP_001158151.1; NM_001164679.1.
DR AlphaFoldDB; Q6PB70; -.
DR SMR; Q6PB70; -.
DR STRING; 10090.ENSMUSP00000091157; -.
DR GlyGen; Q6PB70; 1 site.
DR iPTMnet; Q6PB70; -.
DR PhosphoSitePlus; Q6PB70; -.
DR EPD; Q6PB70; -.
DR MaxQB; Q6PB70; -.
DR PaxDb; Q6PB70; -.
DR PeptideAtlas; Q6PB70; -.
DR PRIDE; Q6PB70; -.
DR ProteomicsDB; 281871; -.
DR Antibodypedia; 43758; 24 antibodies from 14 providers.
DR Ensembl; ENSMUST00000093450; ENSMUSP00000091157; ENSMUSG00000034863.
DR GeneID; 382014; -.
DR KEGG; mmu:382014; -.
DR UCSC; uc009mdl.2; mouse.
DR CTD; 57719; -.
DR MGI; MGI:2687327; Ano8.
DR VEuPathDB; HostDB:ENSMUSG00000034863; -.
DR eggNOG; KOG2513; Eukaryota.
DR GeneTree; ENSGT00940000157019; -.
DR HOGENOM; CLU_006685_2_1_1; -.
DR InParanoid; Q6PB70; -.
DR OMA; YWMENLR; -.
DR OrthoDB; 1263362at2759; -.
DR PhylomeDB; Q6PB70; -.
DR TreeFam; TF314265; -.
DR Reactome; R-MMU-2672351; Stimuli-sensing channels.
DR Reactome; R-MMU-381426; Regulation of Insulin-like Growth Factor (IGF) transport and uptake by Insulin-like Growth Factor Binding Proteins (IGFBPs).
DR Reactome; R-MMU-8957275; Post-translational protein phosphorylation.
DR BioGRID-ORCS; 382014; 4 hits in 73 CRISPR screens.
DR ChiTaRS; Ano8; mouse.
DR PRO; PR:Q6PB70; -.
DR Proteomes; UP000000589; Chromosome 8.
DR RNAct; Q6PB70; protein.
DR Bgee; ENSMUSG00000034863; Expressed in cortical plate and 95 other tissues.
DR ExpressionAtlas; Q6PB70; baseline and differential.
DR Genevisible; Q6PB70; MM.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR GO; GO:0006821; P:chloride transport; ISO:MGI.
DR GO; GO:0055085; P:transmembrane transport; IBA:GO_Central.
DR InterPro; IPR007632; Anoctamin.
DR InterPro; IPR031289; Anoctamin-8.
DR PANTHER; PTHR12308; PTHR12308; 1.
DR PANTHER; PTHR12308:SF33; PTHR12308:SF33; 1.
DR Pfam; PF04547; Anoctamin; 1.
PE 1: Evidence at protein level;
KW Acetylation; Cell membrane; Glycoprotein; Membrane; Methylation;
KW Phosphoprotein; Reference proteome; Transmembrane; Transmembrane helix.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:Q9HCE9"
FT CHAIN 2..1060
FT /note="Anoctamin-8"
FT /id="PRO_0000249004"
FT TOPO_DOM 2..244
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 245..265
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 266..281
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 282..302
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 303..356
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 357..377
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 378..400
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 401..421
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 422..437
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 438..458
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 459..745
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 746..766
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 767..802
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 803..823
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 824..836
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 837..857
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 858..1060
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 1..32
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 529..605
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 619..640
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 653..672
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 680..723
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 884..1060
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 559..579
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 580..601
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 884..931
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 975..989
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1041..1060
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000250|UniProtKB:Q9HCE9"
FT MOD_RES 318
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 665
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 796
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9HCE9"
FT MOD_RES 991
FT /note="Asymmetric dimethylarginine; alternate"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 991
FT /note="Omega-N-methylarginine; alternate"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 999
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT CARBOHYD 708
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CONFLICT 196
FT /note="I -> AV (in Ref. 2; BAD32500)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1060 AA; 119101 MW; B10687A73CD65802 CRC64;
MAEAASGAGD VTLEGERGKR PPPEGEPAAP ASGVLDKLFG KRLLQAGRYL VSHKAWMKTV
PTEDCDVLMT FPDTTDDHTL LWLLNHIRVG IPELIVQVRH HRHTRAYAFF VTATYESLLR
GADELGLRKA VKAEFGGGTR SFSCEEDFIY ENVESELRFF TSQERQSIIR FWLQNLRAKQ
GEALHNVRFL EDQPIIPELA ARGIIQQVFP VHEQRILNRL MKSWVQAVCE NQPLDDICDY
FGVKIAMYFA WLGFYTSAMV YPAVFGSVLY TFTEADQTSR DVSCVVFALF NVIWSTLFLE
EWKRRGAELA YKWGTLDSPG EAVEEPRPQF RGIRRISPIT RAEEFYYPPW KRLLFQLLVS
LPLCLACLIC VFILMLGCFQ LQELVLSVKG LPRLVRFLPK VMLALLVSVS AEGYKKLAVW
LNDMENYRLE STYERHLIIK VVLFQFVNSY LSLFYIGFYL KDMDRLKEML ATLLITRQLL
QNVREVLQPH LYRRLGSGEL GLRTILELAR ALLGLLNPLR PDPRRHLEAQ ADEGGAGSRR
CLGGGCGAPE EENEEEEEAA VERRPAGEGG EVPEGPRGGK EEDEEEDDDE DEDEEYEGEE
GSLLDCGLRL KKVSFAERGA GRRRPGPSPD GLLEEGSPTM VEKGLEPGVF TLAEEDDEPE
GPPGSPGPEP QTVLLRRARG EGRDQGPDGD RDTETGSGDA AGRQKRHNRS SWIDPPEEEH
SPQLTQAELE SCMKKYEDTF QDYQEMFVQF GYVVLFSSAF PLAALCALVN NLIEIRSDAF
KLCTGLQRPF GRRVESIGQW QKVMEAMGVL AIVVNCYLIG QCGQLQRLFP WLSPEAAIVS
VVVLEHLALL VKYLIHVAIP DIPGWVAEEM AKLEYQRREA FKRHERQAQQ RFQQQQRRRR
EEEERQRHAE QQARRERDTG GREEARAEAP GPDPVAERGA AKAKGSERPR RPGALLPPGP
VLRLKQIIPL QTRPPAPTGC APPPRSPADT RLPAFLSLRF LKAPERGPSP PRPGKLFAFS
AREPSANGAP GGGARAHRSA GDEPAAAEPE PRPEDAGHRP
