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Anoctamin-4 (Transmembrane protein 16D)

 ANO4_MOUSE              Reviewed;         955 AA.
Q8C5H1; Q8CA37;
04-NOV-2008, integrated into UniProtKB/Swiss-Prot.
04-NOV-2008, sequence version 2.
28-MAR-2018, entry version 91.
RecName: Full=Anoctamin-4 {ECO:0000250|UniProtKB:Q32M45};
AltName: Full=Transmembrane protein 16D {ECO:0000250|UniProtKB:Q32M45};
Name=Ano4 {ECO:0000250|UniProtKB:Q32M45};
Synonyms=Tmem16d {ECO:0000312|MGI:MGI:2443344};
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1] {ECO:0000305, ECO:0000312|EMBL:BAC37238.1}
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 3).
STRAIN=C57BL/6J {ECO:0000312|EMBL:BAC37238.1};
TISSUE=Cerebellum {ECO:0000312|EMBL:BAC37238.1}, and
Spinal cord {ECO:0000312|EMBL:BAC30429.1};
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).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=C57BL/6J;
PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
Lindblad-Toh K., Eichler E.E., Ponting C.P.;
"Lineage-specific biology revealed by a finished genome assembly of
the mouse.";
PLoS Biol. 7:E1000112-E1000112(2009).
[3]
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).
[4]
ABSENCE OF CALCIUM-ACTIVATED CHLORIDE CHANNEL ACTIVITY, AND
SUBCELLULAR LOCATION.
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).
[5]
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).
[6]
FUNCTION, AND TISSUE SPECIFICITY.
PubMed=23532839; DOI=10.1074/jbc.M113.457937;
Suzuki J., Fujii T., Imao T., Ishihara K., Kuba H., Nagata S.;
"Calcium-dependent phospholipid scramblase activity of TMEM16 protein
family members.";
J. Biol. Chem. 288:13305-13316(2013).
-!- FUNCTION: Has calcium-dependent phospholipid scramblase activity;
scrambles phosphatidylserine, phosphatidylcholine and
galactosylceramide. Does not exhibit calcium-activated chloride
channel (CaCC) activity. {ECO:0000269|PubMed:23532839}.
-!- SUBCELLULAR LOCATION: Cell membrane
{ECO:0000250|UniProtKB:Q32M45}; Multi-pass membrane protein
{ECO:0000250|UniProtKB:Q32M45}. Note=Shows an intracellular
localization according to PubMed:22075693.
{ECO:0000269|PubMed:22075693}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=3;
Name=1;
IsoId=Q8C5H1-1; Sequence=Displayed;
Note=Gene prediction based on similarity to human ortholog.
{ECO:0000305};
Name=2 {ECO:0000269|PubMed:16141072};
IsoId=Q8C5H1-2; Sequence=VSP_052962, VSP_052963;
Note=May be due to an intron retention. No experimental
confirmation available.;
Name=3 {ECO:0000269|PubMed:16141072};
IsoId=Q8C5H1-3; Sequence=VSP_052960, VSP_052961;
Note=No experimental confirmation available. {ECO:0000305};
-!- TISSUE SPECIFICITY: Predominantly expressed in neuronal tissues.
Expressed at low levels in ovary, uterus, heart and brain.
{ECO:0000269|PubMed:20056604, ECO:0000269|PubMed:23532839}.
-!- 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:Q32M45}.
-----------------------------------------------------------------------
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EMBL; AK039728; BAC30429.1; -; mRNA.
EMBL; AK078364; BAC37238.1; -; mRNA.
EMBL; AC124504; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC132383; -; NOT_ANNOTATED_CDS; Genomic_DNA.
CCDS; CCDS24114.2; -. [Q8C5H1-1]
RefSeq; NP_001264117.1; NM_001277188.1. [Q8C5H1-1]
RefSeq; XP_006513821.1; XM_006513758.3. [Q8C5H1-1]
UniGene; Mm.236464; -.
UniGene; Mm.417681; -.
ProteinModelPortal; Q8C5H1; -.
STRING; 10090.ENSMUSP00000043478; -.
SwissLipids; SLP:000000374; -.
PhosphoSitePlus; Q8C5H1; -.
PaxDb; Q8C5H1; -.
PRIDE; Q8C5H1; -.
Ensembl; ENSMUST00000181976; ENSMUSP00000138792; ENSMUSG00000035189. [Q8C5H1-3]
Ensembl; ENSMUST00000182341; ENSMUSP00000138193; ENSMUSG00000035189. [Q8C5H1-1]
GeneID; 320091; -.
KEGG; mmu:320091; -.
UCSC; uc007gsa.1; mouse. [Q8C5H1-1]
UCSC; uc007gsb.1; mouse. [Q8C5H1-2]
UCSC; uc007gsc.1; mouse. [Q8C5H1-3]
CTD; 121601; -.
MGI; MGI:2443344; Ano4.
eggNOG; KOG2514; Eukaryota.
eggNOG; ENOG410XS4S; LUCA.
GeneTree; ENSGT00760000119015; -.
HOGENOM; HOG000006509; -.
HOVERGEN; HBG069519; -.
InParanoid; Q8C5H1; -.
KO; K19499; -.
OMA; HHILQRV; -.
OrthoDB; EOG091G01JF; -.
PhylomeDB; Q8C5H1; -.
Reactome; R-MMU-2672351; Stimuli-sensing channels.
PRO; PR:Q8C5H1; -.
Proteomes; UP000000589; Chromosome 10.
Bgee; ENSMUSG00000035189; -.
ExpressionAtlas; Q8C5H1; baseline and differential.
Genevisible; Q8C5H1; MM.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0005622; C:intracellular; IDA:UniProtKB.
GO; GO:0005886; C:plasma membrane; ISO:MGI.
GO; GO:0017128; F:phospholipid scramblase activity; IDA:MGI.
GO; GO:0046983; F:protein dimerization activity; IEA:InterPro.
GO; GO:0061591; P:calcium activated galactosylceramide scrambling; IDA:MGI.
GO; GO:0061590; P:calcium activated phosphatidylcholine scrambling; IDA:MGI.
GO; GO:0061589; P:calcium activated phosphatidylserine scrambling; IDA:MGI.
GO; GO:0006821; P:chloride transport; ISO:MGI.
InterPro; IPR032394; Anoct_dimer.
InterPro; IPR007632; Anoctamin.
InterPro; IPR031293; Anoctamin-4.
PANTHER; PTHR12308; PTHR12308; 1.
PANTHER; PTHR12308:SF28; PTHR12308:SF28; 1.
Pfam; PF16178; Anoct_dimer; 1.
Pfam; PF04547; Anoctamin; 1.
2: Evidence at transcript level;
Alternative splicing; Cell membrane; Complete proteome; Glycoprotein;
Lipid transport; Membrane; Reference proteome; Transmembrane;
Transmembrane helix; Transport.
CHAIN 1 955 Anoctamin-4.
/FTId=PRO_0000353190.
TOPO_DOM 1 352 Cytoplasmic. {ECO:0000255}.
TRANSMEM 353 373 Helical. {ECO:0000255}.
TOPO_DOM 374 424 Extracellular. {ECO:0000255}.
TRANSMEM 425 445 Helical. {ECO:0000255}.
TOPO_DOM 446 505 Cytoplasmic. {ECO:0000255}.
TRANSMEM 506 526 Helical. {ECO:0000255}.
TOPO_DOM 527 547 Extracellular. {ECO:0000255}.
TRANSMEM 548 568 Helical. {ECO:0000255}.
TOPO_DOM 569 595 Cytoplasmic. {ECO:0000255}.
TRANSMEM 596 616 Helical. {ECO:0000255}.
TOPO_DOM 617 715 Extracellular. {ECO:0000255}.
TRANSMEM 716 736 Helical. {ECO:0000255}.
TOPO_DOM 737 768 Cytoplasmic. {ECO:0000255}.
TRANSMEM 769 789 Helical. {ECO:0000255}.
TOPO_DOM 790 885 Extracellular. {ECO:0000255}.
TRANSMEM 886 906 Helical. {ECO:0000255}.
TOPO_DOM 907 955 Cytoplasmic. {ECO:0000255}.
COMPBIAS 462 467 Poly-Glu.
CARBOHYD 544 544 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 824 824 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 837 837 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
VAR_SEQ 245 245 H -> Q (in isoform 3).
{ECO:0000303|PubMed:16141072}.
/FTId=VSP_052960.
VAR_SEQ 246 955 Missing (in isoform 3).
{ECO:0000303|PubMed:16141072}.
/FTId=VSP_052961.
VAR_SEQ 438 439 AT -> GK (in isoform 2).
{ECO:0000303|PubMed:16141072}.
/FTId=VSP_052962.
VAR_SEQ 440 955 Missing (in isoform 2).
{ECO:0000303|PubMed:16141072}.
/FTId=VSP_052963.
CONFLICT 214 214 P -> H (in Ref. 1; BAC30429).
{ECO:0000305}.
SEQUENCE 955 AA; 111544 MW; DE3F0B931B21FB6A CRC64;
MEASSSGITN GKNKVFHAEG GLDLQSHQLD MQILPDGPKS DVDFSEILNA IQEMAKDVNI
LFDELEAVNS PCKDDDSLLH PGNLTSTSED TSRLEAGGET VRERNKSNGL YFRDGKCRID
YILVYRKSNP QTEKREVFER NIRAEGLQME KESSLINSDI IFVKLHAPWE VLGRYAEQMN
VRMPFRRKIY YLPRRYKFMS RIDKQISRFR RWLPKKPMRL DKETLPDLEE NDCYTAPFSQ
QRIHHFIIHN KDTFFNNATR SRIVHHILQR IKYEEGKNKI GLNRLLTNGS YEAAFPLHEG
SYRSKNSIKT HGAVNHRHLL YECWASWGVW YKYQPLDLVR RYFGEKIGLY FAWLGWYTGM
LFPAAFIGLF VFLYGVTTLD HCQVSKEVCQ ATDIIMCPVC DKYCPFMRLS DSCVYAKVTH
LFDNGATVFF AVFMAVWATV FLEFWKRRRA VIAYDWDLID WEEEEEEIRP QFEAKYSKKE
RMNPISGKPE PYQAFTDKCS RLIVSASGIF FMICVVIAAV FGIVIYRVVT VSTFAAFKWA
LIRNNSQVAT TGTAVCINFC IIMLLNVLYE KVALLLTNLE QPRTESEWEN SFTLKMFLFQ
FVNLNSSTFY IAFFLGRFTG HPGAYLRLIN RWRLEECHPS GCLIDLCMQM GIIMVLKQTW
NNFMELGYPL IQNWWTRRKV RQEHGTERKI NFPQWEKDYN LQPMNAYGLF DEYLEMILQF
GFTTIFVAAF PLAPLLALLN NIIEIRLDAY KFVTQWRRPL ASRAKDIGIW YGILEGIGIL
SVITNAFVIA ITSDFIPRLV YAYKYGPCAG QGEAGQKCMV GYVNASLSVF RISDFENRSE
PESDGSEFSG TPLKYCRYRD YRDPPHSLAP YGYTLQFWHV LAARLAFIIV FEHLVFCIKH
LISYLIPDLP KDLRDRMRRE KYLIQEMMYE AELERLQKER KERKKNGKAH HNEWP


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