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Anoctamin-2 (Transmembrane protein 16B)

 ANO2_MOUSE              Reviewed;        1002 AA.
Q8CFW1; C4N788; Q8C8N6;
04-NOV-2008, integrated into UniProtKB/Swiss-Prot.
03-NOV-2009, sequence version 2.
12-SEP-2018, entry version 104.
RecName: Full=Anoctamin-2 {ECO:0000250|UniProtKB:Q9NQ90};
AltName: Full=Transmembrane protein 16B {ECO:0000312|EMBL:AAH33409.1};
Name=Ano2 {ECO:0000250|UniProtKB:Q9NQ90};
Synonyms=Tmem16b {ECO:0000312|EMBL:AAH33409.1};
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, GLYCOSYLATION, SUBCELLULAR
LOCATION, SUBUNIT, INTERACTION WITH DLG4, MUTAGENESIS OF
1000-THR--ASN-1002, AND TISSUE SPECIFICITY.
STRAIN=C57BL/6J; TISSUE=Retina;
PubMed=19474308; DOI=10.1523/JNEUROSCI.5546-08.2009;
Stoehr H., Heisig J.B., Benz P.M., Schoeberl S., Milenkovic V.M.,
Strauss O., Aartsen W.M., Wijnholds J., Weber B.H.F., Schulz H.L.;
"TMEM16B, a novel protein with calcium-dependent chloride channel
activity, associates with a presynaptic protein complex in
photoreceptor terminals.";
J. Neurosci. 29:6809-6818(2009).
[2] {ECO:0000305, ECO:0000312|EMBL:BAC32073.1}
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-543.
STRAIN=C57BL/6J {ECO:0000312|EMBL:BAC32073.1};
TISSUE=Retina {ECO:0000312|EMBL:BAC32073.1};
PubMed=16141072; DOI=10.1126/science.1112014;
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
Hayashizaki Y.;
"The transcriptional landscape of the mammalian genome.";
Science 309:1559-1563(2005).
[3] {ECO:0000305, ECO:0000312|EMBL:AAH33409.1}
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 59-1002.
STRAIN=C57BL/6J {ECO:0000312|EMBL:AAH33409.1};
TISSUE=Eye {ECO:0000312|EMBL:AAH33409.1};
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[4] {ECO:0000305}
DEVELOPMENTAL STAGE.
PubMed=18729231; DOI=10.1002/dvdy.21676;
Rock J.R., Harfe B.D.;
"Expression of TMEM16 paralogs during murine embryogenesis.";
Dev. Dyn. 237:2566-2574(2008).
[5]
FUNCTION, AND ACTIVITY REGULATION.
PubMed=19475416; DOI=10.1007/s00424-009-0684-9;
Pifferi S., Dibattista M., Menini A.;
"TMEM16B induces chloride currents activated by calcium in mammalian
cells.";
Pflugers Arch. 458:1023-1038(2009).
[6]
FUNCTION, IDENTIFICATION BY MASS SPECTROMETRY, SUBCELLULAR LOCATION,
AND TISSUE SPECIFICITY.
PubMed=19561302; DOI=10.1073/pnas.0903304106;
Stephan A.B., Shum E.Y., Hirsh S., Cygnar K.D., Reisert J., Zhao H.;
"ANO2 is the cilial calcium-activated chloride channel that may
mediate olfactory amplification.";
Proc. Natl. Acad. Sci. U.S.A. 106:11776-11781(2009).
[7]
TISSUE SPECIFICITY.
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).
[8]
FUNCTION.
PubMed=22075693; DOI=10.1152/ajpcell.00140.2011;
Duran C., Qu Z., Osunkoya A.O., Cui Y., Hartzell H.C.;
"ANOs 3-7 in the anoctamin/Tmem16 Cl- channel family are intracellular
proteins.";
Am. J. Physiol. 302:C482-C493(2012).
[9]
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).
[10]
REVIEW, AND FUNCTION.
PubMed=21890523; DOI=10.1113/expphysiol.2011.058230;
Pifferi S., Cenedese V., Menini A.;
"Anoctamin 2/TMEM16B: a calcium-activated chloride channel in
olfactory transduction.";
Exp. Physiol. 97:193-199(2012).
-!- FUNCTION: Calcium-activated chloride channel (CaCC) which may play
a role in olfactory signal transduction. Odorant molecules bind to
odor-sensing receptors (OSRs), leading to an increase in calcium
entry that activates CaCC current which amplifies the
depolarization of the OSR cells, ANO2 seems to be the underlying
chloride channel involved in this process. May mediate light
perception amplification in retina. {ECO:0000269|PubMed:19474308,
ECO:0000269|PubMed:19475416, ECO:0000269|PubMed:19561302,
ECO:0000269|PubMed:21890523, ECO:0000269|PubMed:22075693}.
-!- ACTIVITY REGULATION: Channel activity is repressed by chloride
inhibitors; strongly by niflumic acid (NFA), partially by
flufenamic acid (FFA), and only slightly by meclofenamic acid
(MFA), 5-Nitro-2-(3-phenylpropylamino)benzoic acid (NPPB), 4-
acetamido-4'-isothiocyanato-stilben-2,2'-disulfonate (SITS), and
4,4'-diisothiocyanatostilbene-2,2'-disulfonic acid (DIDS).
{ECO:0000269|PubMed:19475416}.
-!- SUBUNIT: Component of a presynaptic protein complex recruited to
specialized plasma membrane domains of photoreceptors. Interacts
with DLG4 by its C-terminal region. {ECO:0000269|PubMed:19474308}.
-!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:19474308,
ECO:0000269|PubMed:19561302}; Multi-pass membrane protein
{ECO:0000269|PubMed:19474308, ECO:0000269|PubMed:19561302}.
-!- TISSUE SPECIFICITY: Expressed in retina, especially in the
photoreceptor synaptic terminals, and in olfactory epithelium,
particularly in sensory neurons (OSNs) and cilia (at protein
level). Also observed in retinal pigment epithelium (RPE),
olfactory bulb, brain, and cortex. {ECO:0000269|PubMed:19474308,
ECO:0000269|PubMed:19561302, ECO:0000269|PubMed:20056604}.
-!- DEVELOPMENTAL STAGE: Detected in the mantle layer of the neural
tube and in the dorsal root ganglia at E14.5. In developing skin,
expression is restricted to basal layers of the epidermis at
E16.5. {ECO:0000269|PubMed:18729231}.
-!- PTM: Glycosylated. {ECO:0000269|PubMed:19474308}.
-!- 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:0000250|UniProtKB:Q9NQ90}.
-!- SEQUENCE CAUTION:
Sequence=AAH33409.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
Sequence=BAC32073.1; Type=Miscellaneous discrepancy; Note=Probable cloning artifact.; Evidence={ECO:0000305};
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EMBL; FJ384096; ACL36051.1; -; mRNA.
EMBL; AK044763; BAC32073.1; ALT_SEQ; mRNA.
EMBL; BC033409; AAH33409.1; ALT_INIT; mRNA.
CCDS; CCDS39643.2; -.
RefSeq; NP_705817.2; NM_153589.2.
RefSeq; XP_006506182.1; XM_006506119.1.
UniGene; Mm.333398; -.
STRING; 10090.ENSMUSP00000125303; -.
iPTMnet; Q8CFW1; -.
PhosphoSitePlus; Q8CFW1; -.
PaxDb; Q8CFW1; -.
PRIDE; Q8CFW1; -.
Ensembl; ENSMUST00000160496; ENSMUSP00000125303; ENSMUSG00000038115.
GeneID; 243634; -.
KEGG; mmu:243634; -.
UCSC; uc009duv.1; mouse.
CTD; 57101; -.
MGI; MGI:2387214; Ano2.
eggNOG; KOG2514; Eukaryota.
eggNOG; ENOG410XS4S; LUCA.
GeneTree; ENSGT00760000119015; -.
HOGENOM; HOG000006509; -.
HOVERGEN; HBG069519; -.
InParanoid; Q8CFW1; -.
KO; K19497; -.
OMA; DEDKLTW; -.
OrthoDB; EOG091G01JF; -.
TreeFam; TF314265; -.
Reactome; R-MMU-2672351; Stimuli-sensing channels.
ChiTaRS; Ano2; mouse.
PRO; PR:Q8CFW1; -.
Proteomes; UP000000589; Chromosome 6.
Bgee; ENSMUSG00000038115; Expressed in 23 organ(s), highest expression level in olfactory epithelium.
ExpressionAtlas; Q8CFW1; baseline and differential.
GO; GO:0034707; C:chloride channel complex; IEA:UniProtKB-KW.
GO; GO:0097730; C:non-motile cilium; IDA:MGI.
GO; GO:0005654; C:nucleoplasm; ISO:MGI.
GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
GO; GO:0005229; F:intracellular calcium activated chloride channel activity; IDA:UniProtKB.
GO; GO:0046982; F:protein heterodimerization activity; IPI:MGI.
GO; GO:0042803; F:protein homodimerization activity; IPI:MGI.
GO; GO:0006821; P:chloride transport; IDA:MGI.
InterPro; IPR032394; Anoct_dimer.
InterPro; IPR007632; Anoctamin.
InterPro; IPR031288; Anoctamin-2.
PANTHER; PTHR12308; PTHR12308; 1.
PANTHER; PTHR12308:SF20; PTHR12308:SF20; 1.
Pfam; PF16178; Anoct_dimer; 1.
Pfam; PF04547; Anoctamin; 1.
1: Evidence at protein level;
Calcium; Cell membrane; Chloride; Chloride channel; Complete proteome;
Glycoprotein; Ion channel; Ion transport; Membrane;
Reference proteome; Transmembrane; Transmembrane helix; Transport.
CHAIN 1 1002 Anoctamin-2.
/FTId=PRO_0000353187.
TOPO_DOM 1 364 Cytoplasmic. {ECO:0000255}.
TRANSMEM 365 385 Helical. {ECO:0000255}.
TOPO_DOM 386 433 Extracellular. {ECO:0000255}.
TRANSMEM 434 454 Helical. {ECO:0000255}.
TOPO_DOM 455 536 Cytoplasmic. {ECO:0000255}.
TRANSMEM 537 557 Helical. {ECO:0000255}.
TOPO_DOM 558 580 Extracellular. {ECO:0000255}.
TRANSMEM 581 601 Helical. {ECO:0000255}.
TOPO_DOM 602 621 Cytoplasmic. {ECO:0000255}.
TRANSMEM 622 642 Helical. {ECO:0000255}.
TOPO_DOM 643 746 Extracellular. {ECO:0000255}.
TRANSMEM 747 767 Helical. {ECO:0000255}.
TOPO_DOM 768 799 Cytoplasmic. {ECO:0000255}.
TRANSMEM 800 820 Helical. {ECO:0000255}.
TOPO_DOM 821 905 Extracellular. {ECO:0000255}.
TRANSMEM 906 926 Helical. {ECO:0000255}.
TOPO_DOM 927 1002 Cytoplasmic. {ECO:0000255}.
MOTIF 1000 1002 DLG4 binding (PDZ).
CARBOHYD 421 421 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 839 839 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 847 847 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 854 854 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
MUTAGEN 1000 1002 Missing: Impaired interaction with DLG4.
{ECO:0000269|PubMed:19474308}.
SEQUENCE 1002 AA; 114134 MW; 8514FC9CC13F78C7 CRC64;
MAAPGLRDIP LLPGSPRRLS SRTVARGSQG PKHGQQYLKV PGHRAPGQRD NSSLHPSQVS
RRESSRDRSV INNYLDANEP PSSEARLSRM HFHDNQRKVD YVLAYHYRKR GAHLGHGSPG
HSLAVISNGE TGKERHGGGP GDVELGPLDA LEEERREQRD EFEHNLMAAG LELEKDLESK
SQGSVFVRIH APWQVLAREA EFLKIKVPTK KMYEIKAGGS IAKKFSAILQ TLSSPLQPRV
PEHSNNRMKN LSYPFSREKM YLYNIQEKDT FFDNATRSRI VHEILKRTAC SRANNTMGIN
SLIANNIYEA AYPLHDGEYD SPGDDMNDRK LLYQEWARYG VFYKFQPIDL IRKYFGEKIG
LYFAWLGLYT SFLIPSSVIG VIVFLYGCAT IEEDIPSKEM CDHQNAFTMC PLCDKSCDYW
NLSSACGTAR ASHLFDNPAT VFFSIFMALW ATMFLENWKR LQMRLGYFWD LTGIEEEEER
SQEHSRPEYE TKVREKLLKE SGKSAVQKLE ANSPEDDEDD EDKLTWKDRF PGYLMNFASI
LFMIALTFSI VFGVIVYRIT TAAALSLNKA TRSNVRVTVT ATAVIINLVV ILILDEIYGA
VAKWLTKIEV PKTEQTFEER LILKAFLLKF VNAYSPIFYV AFFKGRFVGR PGSYVYVFDG
YRMEECAPGG CLMELCIQLS IIMLGKQLIQ NNIFEIGVPK LKKLFRKLKD ETEPGESDPD
HSKRPEQWDL DHSLEPYTGL TPEYMEMIIQ FGFVTLFVAS FPLAPVFALL NNVIEVRLDA
KKFVTELRRP DAVRTKDIGI WFDILSGIGK FSVIINAFVI AVTSDFIPRL VYQYSYSHNG
TLHGFVNHTL SFFNVSQLKE GTQPENSQFD QEVQFCRFKD YREPPWAPNP YEFSKQYWSV
LSARLAFVII FQNLVMFLSV LVDWMIPDIP TDISDQIKKE KSLLVDFFLK EEHEKVKLAD
EPTQRSQGGG DRSRRSRAAS SAPSGRSQPG SIASSGSQHT NV


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