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Anoctamin-8 (Transmembrane protein 16H)

 ANO8_HUMAN              Reviewed;        1232 AA.
Q9HCE9; A6NIJ0;
05-SEP-2006, integrated into UniProtKB/Swiss-Prot.
05-SEP-2006, sequence version 3.
05-DEC-2018, entry version 120.
RecName: Full=Anoctamin-8;
AltName: Full=Transmembrane protein 16H;
Name=ANO8; Synonyms=KIAA1623, TMEM16H;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Brain;
PubMed=10997877; DOI=10.1093/dnares/7.4.271;
Nagase T., Kikuno R., Nakayama M., Hirosawa M., Ohara O.;
"Prediction of the coding sequences of unidentified human genes.
XVIII. The complete sequences of 100 new cDNA clones from brain which
code for large proteins in vitro.";
DNA Res. 7:273-281(2000).
[2]
SEQUENCE REVISION.
PubMed=12168954; DOI=10.1093/dnares/9.3.99;
Nakajima D., Okazaki N., Yamakawa H., Kikuno R., Ohara O., Nagase T.;
"Construction of expression-ready cDNA clones for KIAA genes: manual
curation of 330 KIAA cDNA clones.";
DNA Res. 9:99-106(2002).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15057824; DOI=10.1038/nature02399;
Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J.,
Lamerdin J.E., Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M.,
Aerts A., Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E.,
Caenepeel S., Carrano A.V., Caoile C., Chan Y.M., Christensen M.,
Cleland C.A., Copeland A., Dalin E., Dehal P., Denys M., Detter J.C.,
Escobar J., Flowers D., Fotopulos D., Garcia C., Georgescu A.M.,
Glavina T., Gomez M., Gonzales E., Groza M., Hammon N., Hawkins T.,
Haydu L., Ho I., Huang W., Israni S., Jett J., Kadner K., Kimball H.,
Kobayashi A., Larionov V., Leem S.-H., Lopez F., Lou Y., Lowry S.,
Malfatti S., Martinez D., McCready P.M., Medina C., Morgan J.,
Nelson K., Nolan M., Ovcharenko I., Pitluck S., Pollard M.,
Popkie A.P., Predki P., Quan G., Ramirez L., Rash S., Retterer J.,
Rodriguez A., Rogers S., Salamov A., Salazar A., She X., Smith D.,
Slezak T., Solovyev V., Thayer N., Tice H., Tsai M., Ustaszewska A.,
Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J., Dubchak I.,
Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E.,
Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M.,
Rubin E.M., Lucas S.M.;
"The DNA sequence and biology of human chromosome 19.";
Nature 428:529-535(2004).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[5]
ALTERNATIVE SPLICING (ISOFORMS 1 AND 2), AND TISSUE SPECIFICITY.
PubMed=15647853;
Katoh M., Katoh M.;
"Identification and characterization of TMEM16H gene in silico.";
Int. J. Mol. Med. 15:353-358(2005).
[6]
ABSENCE OF CALCIUM-ACTIVATED CHLORIDE CHANNEL ACTIVITY, AND
SUBCELLULAR LOCATION.
PubMed=20056604; DOI=10.1074/jbc.M109.065367;
Schreiber R., Uliyakina I., Kongsuphol P., Warth R., Mirza M.,
Martins J.R., Kunzelmann K.;
"Expression and function of epithelial anoctamins.";
J. Biol. Chem. 285:7838-7845(2010).
[7]
REVIEW.
PubMed=21642943; DOI=10.1038/aps.2011.48;
Duran C., Hartzell H.C.;
"Physiological roles and diseases of Tmem16/Anoctamin proteins: are
they all chloride channels?";
Acta Pharmacol. Sin. 32:685-692(2011).
[8]
ABSENCE OF CALCIUM-ACTIVATED CHLORIDE CHANNEL ACTIVITY.
PubMed=22178883; DOI=10.1159/000335765;
Ousingsawat J., Kongsuphol P., Schreiber R., Kunzelmann K.;
"CFTR and TMEM16A are separate but functionally related Cl-channels.";
Cell. Physiol. Biochem. 28:715-724(2011).
[9]
REVIEW.
PubMed=21607626; DOI=10.1007/s00424-011-0975-9;
Kunzelmann K., Tian Y., Martins J.R., Faria D., Kongsuphol P.,
Ousingsawat J., Thevenod F., Roussa E., Rock J., Schreiber R.;
"Anoctamins.";
Pflugers Arch. 462:195-208(2011).
[10]
REVIEW.
PubMed=22302790; DOI=10.1113/expphysiol.2011.058214;
Winpenny J.P., Gray M.A.;
"The anoctamin (TMEM16) gene family: calcium-activated chloride
channels come of age.";
Exp. Physiol. 97:175-176(2012).
[11]
REVIEW, AND ABSENCE OF CALCIUM-ACTIVATED CHLORIDE CHANNEL ACTIVITY.
PubMed=21984732; DOI=10.1113/expphysiol.2011.058198;
Scudieri P., Sondo E., Ferrera L., Galietta L.J.;
"The anoctamin family: TMEM16A and TMEM16B as calcium-activated
chloride channels.";
Exp. Physiol. 97:177-183(2012).
[12]
SUBCELLULAR LOCATION.
PubMed=22946059; DOI=10.1242/jcs.109553;
Tian Y., Schreiber R., Kunzelmann K.;
"Anoctamins are a family of Ca2+ activated Cl- channels.";
J. Cell Sci. 125:4991-4998(2012).
[13]
ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22814378; DOI=10.1073/pnas.1210303109;
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E.,
Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
Aldabe R.;
"N-terminal acetylome analyses and functional insights of the N-
terminal acetyltransferase NatB.";
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
[14]
PHOSPHORYLATION AT SER-801.
PubMed=26091039; DOI=10.1016/j.cell.2015.05.028;
Tagliabracci V.S., Wiley S.E., Guo X., Kinch L.N., Durrant E., Wen J.,
Xiao J., Cui J., Nguyen K.B., Engel J.L., Coon J.J., Grishin N.,
Pinna L.A., Pagliarini D.J., Dixon J.E.;
"A single kinase generates the majority of the secreted
phosphoproteome.";
Cell 161:1619-1632(2015).
-!- FUNCTION: Does not exhibit calcium-activated chloride channel
(CaCC) activity.
-!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:20056604,
ECO:0000269|PubMed:22946059}; Multi-pass membrane protein
{ECO:0000269|PubMed:20056604, ECO:0000269|PubMed:22946059}.
Note=Shows predominantly an intracellular localization with a weak
expression in the cell membrane.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=Q9HCE9-1; Sequence=Displayed;
Name=2;
IsoId=Q9HCE9-2; Sequence=VSP_020351, VSP_020352;
-!- TISSUE SPECIFICITY: Expressed in embryonic stem cells, fetal brain
and neural tissues. {ECO:0000269|PubMed:15647853}.
-!- MISCELLANEOUS: The term 'anoctamin' was coined because these
channels are anion selective and have eight (OCT) transmembrane
segments. There is some dissatisfaction in the field with the Ano
nomenclature because it is not certain that all the members of
this family are anion channels or have the 8-transmembrane
topology.
-!- SIMILARITY: Belongs to the anoctamin family. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=BAB13449.2; Type=Erroneous initiation; Note=Translation N-terminally shortened.; Evidence={ECO:0000305};
-----------------------------------------------------------------------
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EMBL; AB046843; BAB13449.2; ALT_INIT; mRNA.
EMBL; AC010463; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471106; EAW84595.1; -; Genomic_DNA.
CCDS; CCDS32949.1; -. [Q9HCE9-1]
RefSeq; NP_066010.1; NM_020959.2. [Q9HCE9-1]
RefSeq; XP_016882537.1; XM_017027048.1. [Q9HCE9-2]
UniGene; Hs.590990; -.
ProteinModelPortal; Q9HCE9; -.
BioGrid; 121742; 1.
IntAct; Q9HCE9; 1.
iPTMnet; Q9HCE9; -.
PhosphoSitePlus; Q9HCE9; -.
BioMuta; ANO8; -.
DMDM; 114152287; -.
EPD; Q9HCE9; -.
MaxQB; Q9HCE9; -.
PaxDb; Q9HCE9; -.
PeptideAtlas; Q9HCE9; -.
PRIDE; Q9HCE9; -.
ProteomicsDB; 81695; -.
ProteomicsDB; 81696; -. [Q9HCE9-2]
Ensembl; ENST00000159087; ENSP00000159087; ENSG00000074855. [Q9HCE9-1]
GeneID; 57719; -.
KEGG; hsa:57719; -.
UCSC; uc002ngf.2; human. [Q9HCE9-1]
CTD; 57719; -.
EuPathDB; HostDB:ENSG00000074855.10; -.
GeneCards; ANO8; -.
HGNC; HGNC:29329; ANO8.
HPA; HPA031787; -.
HPA; HPA049206; -.
MIM; 610216; gene.
neXtProt; NX_Q9HCE9; -.
OpenTargets; ENSG00000074855; -.
PharmGKB; PA164715790; -.
eggNOG; KOG2513; Eukaryota.
eggNOG; ENOG410XPYE; LUCA.
GeneTree; ENSGT00940000157019; -.
HOGENOM; HOG000033952; -.
HOVERGEN; HBG100443; -.
InParanoid; Q9HCE9; -.
KO; K19502; -.
OMA; IMSHKSW; -.
OrthoDB; EOG091G06A3; -.
PhylomeDB; Q9HCE9; -.
TreeFam; TF314265; -.
Reactome; R-HSA-2672351; Stimuli-sensing channels.
Reactome; R-HSA-381426; Regulation of Insulin-like Growth Factor (IGF) transport and uptake by Insulin-like Growth Factor Binding Proteins (IGFBPs).
Reactome; R-HSA-8957275; Post-translational protein phosphorylation.
ChiTaRS; ANO8; human.
GenomeRNAi; 57719; -.
PRO; PR:Q9HCE9; -.
Proteomes; UP000005640; Chromosome 19.
Bgee; ENSG00000074855; Expressed in 105 organ(s), highest expression level in left adrenal gland.
CleanEx; HS_ANO8; -.
ExpressionAtlas; Q9HCE9; baseline and differential.
Genevisible; Q9HCE9; HS.
GO; GO:0005788; C:endoplasmic reticulum lumen; TAS:Reactome.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
GO; GO:0005229; F:intracellular calcium activated chloride channel activity; IMP:UniProtKB.
GO; GO:0044267; P:cellular protein metabolic process; TAS:Reactome.
GO; GO:0006821; P:chloride transport; IMP:UniProtKB.
GO; GO:0034220; P:ion transmembrane transport; TAS:Reactome.
GO; GO:0043687; P:post-translational protein modification; TAS:Reactome.
InterPro; IPR007632; Anoctamin.
InterPro; IPR031289; Anoctamin-8.
PANTHER; PTHR12308; PTHR12308; 1.
PANTHER; PTHR12308:SF33; PTHR12308:SF33; 1.
Pfam; PF04547; Anoctamin; 1.
1: Evidence at protein level;
Acetylation; Alternative splicing; Cell membrane; Complete proteome;
Membrane; Methylation; Phosphoprotein; Reference proteome;
Transmembrane; Transmembrane helix.
INIT_MET 1 1 Removed. {ECO:0000244|PubMed:22814378}.
CHAIN 2 1232 Anoctamin-8.
/FTId=PRO_0000249003.
TOPO_DOM 2 244 Extracellular. {ECO:0000255}.
TRANSMEM 245 265 Helical. {ECO:0000255}.
TOPO_DOM 266 281 Cytoplasmic. {ECO:0000255}.
TRANSMEM 282 302 Helical. {ECO:0000255}.
TOPO_DOM 303 356 Extracellular. {ECO:0000255}.
TRANSMEM 357 377 Helical. {ECO:0000255}.
TOPO_DOM 378 400 Cytoplasmic. {ECO:0000255}.
TRANSMEM 401 421 Helical. {ECO:0000255}.
TOPO_DOM 422 437 Extracellular. {ECO:0000255}.
TRANSMEM 438 458 Helical. {ECO:0000255}.
TOPO_DOM 459 750 Cytoplasmic. {ECO:0000255}.
TRANSMEM 751 771 Helical. {ECO:0000255}.
TOPO_DOM 772 807 Extracellular. {ECO:0000255}.
TRANSMEM 808 828 Helical. {ECO:0000255}.
TOPO_DOM 829 841 Cytoplasmic. {ECO:0000255}.
TRANSMEM 842 862 Helical. {ECO:0000255}.
TOPO_DOM 863 1232 Extracellular. {ECO:0000255}.
COMPBIAS 353 518 Leu-rich.
COMPBIAS 533 580 Gly-rich.
COMPBIAS 554 673 Glu-rich.
COMPBIAS 1130 1222 Pro-rich.
MOD_RES 2 2 N-acetylalanine.
{ECO:0000244|PubMed:22814378}.
MOD_RES 318 318 Phosphoserine.
{ECO:0000250|UniProtKB:Q6PB70}.
MOD_RES 669 669 Phosphoserine.
{ECO:0000250|UniProtKB:Q6PB70}.
MOD_RES 801 801 Phosphoserine; by FAM20C.
{ECO:0000269|PubMed:26091039}.
MOD_RES 1020 1020 Asymmetric dimethylarginine; alternate.
{ECO:0000250|UniProtKB:Q6PB70}.
MOD_RES 1020 1020 Omega-N-methylarginine; alternate.
{ECO:0000250|UniProtKB:Q6PB70}.
VAR_SEQ 1112 1114 TAL -> HKL (in isoform 2). {ECO:0000305}.
/FTId=VSP_020351.
VAR_SEQ 1115 1232 Missing (in isoform 2). {ECO:0000305}.
/FTId=VSP_020352.
SEQUENCE 1232 AA; 136034 MW; 1802BC3544A9234C CRC64;
MAEAASGAGG TSLEGERGKR PPPEGEPAAP ASGVLDKLFG KRLLQAGRYL VSHKAWMKTV
PTENCDVLMT FPDTTDDHTL LWLLNHIRVG IPELIVQVRH HRHTRAYAFF VTATYESLLR
GADELGLRKA VKAEFGGGTR GFSCEEDFIY ENVESELRFF TSQERQSIIR FWLQNLRAKQ
GEALHNVRFL EDQPIIPELA ARGIIQQVFP VHEQRILNRL MKSWVQAVCE NQPLDDICDY
FGVKIAMYFA WLGFYTSAMV YPAVFGSVLY TFTEADQTSR DVSCVVFALF NVIWSTLFLE
EWKRRGAELA YKWGTLDSPG EAVEEPRPQF RGVRRISPIT RAEEFYYPPW KRLLFQLLVS
LPLCLACLVC VFLLMLGCFQ LQELVLSVKG LPRLARFLPK VMLALLVSVS AEGYKKLAIW
LNDMENYRLE SAYEKHLIIK VVLFQFVNSY LSLFYIGFYL KDMERLKEML ATLLITRQFL
QNVREVLQPH LYRRLGRGEL GLRAVWELAR ALLGLLSLRR PAPRRLEPQA DEGGGGGSGG
GGRRCLSGGC GAPEEEEEAA LVERRRAGEG GEEGDGPPGG KEEDEDDEEE EDEEEEEDEE
EGEEGGLLDC GLRLKKVSFA ERGAGRRRPG PSPEALLEEG SPTMVEKGLE PGVFTLAEED
DEAEGAPGSP EREPPAILFR RAGGEGRDQG PDGGPDPEPG SNSDSTRRQR RQNRSSWIDP
PEEEHSPQLT QAELESCMKK YEDTFQDYQE MFVQFGYVVL FSSAFPLAAL CALVNNLIEI
RSDAFKLCTG LQRPFGQRVE SIGQWQKVME AMGVLAIVVN CYLIGQCGQL QRLFPWLSPE
AAIVSVVVLE HFALLLKYLI HVAIPDIPGW VAEEMAKLEY QRREAFKRHE RQAQHRYQQQ
QRRRREEEER QRHAEHHARR EHDSGGREEA RAEGSGLDPA TSSEKASAKA KGSTAGGHGP
ERPKRPGSLL APNNVMKLKQ IIPLQGKFLS SGATSSLAAA GAGATTRPPP AQSPTGSDTR
LPAFLSFKFL KSPETRRDSE RSHSPPKAFH AGKLFPFGGT RAEPGSNGAG GQARPDGTPS
SGSSRVQRSG PVDEALAEEL EAPRPEEEGS GTALAPVGAP ALRTRRSRSP APPPPMPLPR
PPTPPAGCWQ WDGPWGCGGE GAAPRQALAA AECPPCAMAG PPPAPQPLPG DASFYSLPPP
PLPPTSDPLE TPAPSPSPSP SPQAVCWPSG WH


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