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Anoctamin-3 (Transmembrane protein 16C)

 ANO3_HUMAN              Reviewed;         981 AA.
Q9BYT9; B7Z3F5;
16-JAN-2004, integrated into UniProtKB/Swiss-Prot.
18-MAY-2010, sequence version 2.
25-OCT-2017, entry version 121.
RecName: Full=Anoctamin-3;
AltName: Full=Transmembrane protein 16C;
Name=ANO3; Synonyms=C11orf25, TMEM16C; ORFNames=GENX-3947;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
Rosier M.F., Toselli E., Segurens-Soury B., Auffray C., Devignes M.D.;
"Predominant brain expression and full-length characterization of a
novel human 6.6-Kb transcript mapping at 11p14 in the telomeric part
of WAGR locus.";
Submitted (NOV-2000) to the EMBL/GenBank/DDBJ databases.
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
TISSUE=Hippocampus;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16554811; DOI=10.1038/nature04632;
Taylor T.D., Noguchi H., Totoki Y., Toyoda A., Kuroki Y., Dewar K.,
Lloyd C., Itoh T., Takeda T., Kim D.-W., She X., Barlow K.F.,
Bloom T., Bruford E., Chang J.L., Cuomo C.A., Eichler E.,
FitzGerald M.G., Jaffe D.B., LaButti K., Nicol R., Park H.-S.,
Seaman C., Sougnez C., Yang X., Zimmer A.R., Zody M.C., Birren B.W.,
Nusbaum C., Fujiyama A., Hattori M., Rogers J., Lander E.S.,
Sakaki Y.;
"Human chromosome 11 DNA sequence and analysis including novel gene
identification.";
Nature 440:497-500(2006).
[4]
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).
[5]
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).
[6]
TISSUE SPECIFICITY, AND VARIANTS DYT24 CYS-490; TRP-494; GLY-685 AND
ASN-862.
PubMed=23200863; DOI=10.1016/j.ajhg.2012.10.024;
Charlesworth G., Plagnol V., Holmstroem K.M., Bras J., Sheerin U.M.,
Preza E., Rubio-Agusti I., Ryten M., Schneider S.A., Stamelou M.,
Trabzuni D., Abramov A.Y., Bhatia K.P., Wood N.W.;
"Mutations in ANO3 cause dominant craniocervical dystonia: ion channel
implicated in pathogenesis.";
Am. J. Hum. Genet. 91:1041-1050(2012).
[7]
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).
[8]
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).
-!- FUNCTION: Has calcium-dependent phospholipid scramblase activity;
scrambles phosphatidylcholine and galactosylceramide. Seems to act
as potassium channel regulator and may inhibit pain signaling; can
facilitate KCNT1/Slack channel activity by promoting its full
single-channel conductance at very low sodium concentrations and
by increasing its sodium sensitivity (By similarity). Does not
exhibit calcium-activated chloride channel (CaCC) activity.
{ECO:0000250|UniProtKB:A2AHL1, ECO:0000269|PubMed:21984732}.
-!- SUBUNIT: Interacts with KCNT1/Slack.
{ECO:0000250|UniProtKB:A2AHL1}.
-!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass
membrane protein {ECO:0000305}. Note=Shows an intracellular
localization. {ECO:0000250}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=Q9BYT9-1; Sequence=Displayed;
Name=2;
IsoId=Q9BYT9-2; Sequence=VSP_056893;
Note=No experimental confirmation available.;
-!- TISSUE SPECIFICITY: Highly expressed in the forebrain striatum.
{ECO:0000269|PubMed:23200863}.
-!- DISEASE: Dystonia 24 (DYT24) [MIM:615034]: A form of dystonia, a
disorder defined by the presence of sustained involuntary muscle
contraction, often leading to abnormal postures. DYT24 is an
autosomal dominant focal dystonia affecting the neck, laryngeal
muscles, and muscles of the upper limbs.
{ECO:0000269|PubMed:23200863}. Note=The disease is caused by
mutations affecting the gene represented in this entry.
-!- 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}.
-----------------------------------------------------------------------
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EMBL; AJ300461; CAC32454.1; -; mRNA.
EMBL; AK295816; BAH12191.1; -; mRNA.
EMBL; AC021698; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC036114; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC079064; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC083755; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC099687; -; NOT_ANNOTATED_CDS; Genomic_DNA.
CCDS; CCDS31447.1; -. [Q9BYT9-1]
CCDS; CCDS81557.1; -. [Q9BYT9-2]
RefSeq; NP_001300655.1; NM_001313726.1.
RefSeq; NP_001300656.1; NM_001313727.1. [Q9BYT9-2]
RefSeq; NP_113606.2; NM_031418.3. [Q9BYT9-1]
RefSeq; XP_016873607.1; XM_017018118.1. [Q9BYT9-2]
UniGene; Hs.577269; -.
UniGene; Hs.91791; -.
ProteinModelPortal; Q9BYT9; -.
BioGrid; 122027; 8.
IntAct; Q9BYT9; 8.
STRING; 9606.ENSP00000256737; -.
TCDB; 1.A.17.1.20; the calcium-dependent chloride channel (ca-clc) family.
iPTMnet; Q9BYT9; -.
PhosphoSitePlus; Q9BYT9; -.
BioMuta; ANO3; -.
DMDM; 296434396; -.
PaxDb; Q9BYT9; -.
PeptideAtlas; Q9BYT9; -.
PRIDE; Q9BYT9; -.
Ensembl; ENST00000256737; ENSP00000256737; ENSG00000134343. [Q9BYT9-1]
Ensembl; ENST00000531568; ENSP00000432394; ENSG00000134343. [Q9BYT9-2]
GeneID; 63982; -.
KEGG; hsa:63982; -.
UCSC; uc001mqt.5; human. [Q9BYT9-1]
CTD; 63982; -.
DisGeNET; 63982; -.
EuPathDB; HostDB:ENSG00000134343.12; -.
GeneCards; ANO3; -.
H-InvDB; HIX0035914; -.
HGNC; HGNC:14004; ANO3.
HPA; HPA041629; -.
MalaCards; ANO3; -.
MIM; 610110; gene.
MIM; 615034; phenotype.
neXtProt; NX_Q9BYT9; -.
OpenTargets; ENSG00000134343; -.
Orphanet; 93962; Autosomal dominant cervical dystonia.
PharmGKB; PA25489; -.
eggNOG; KOG2514; Eukaryota.
eggNOG; ENOG410XS4S; LUCA.
GeneTree; ENSGT00760000119015; -.
HOGENOM; HOG000006509; -.
HOVERGEN; HBG069519; -.
InParanoid; Q9BYT9; -.
KO; K19498; -.
OMA; CKLINNG; -.
OrthoDB; EOG091G01JF; -.
PhylomeDB; Q9BYT9; -.
TreeFam; TF314265; -.
Reactome; R-HSA-2672351; Stimuli-sensing channels.
ChiTaRS; ANO3; human.
GenomeRNAi; 63982; -.
PRO; PR:Q9BYT9; -.
Proteomes; UP000005640; Chromosome 11.
Bgee; ENSG00000134343; -.
CleanEx; HS_ANO3; -.
ExpressionAtlas; Q9BYT9; baseline and differential.
Genevisible; Q9BYT9; HS.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0005886; C:plasma membrane; TAS:Reactome.
GO; GO:0005229; F:intracellular calcium activated chloride channel activity; TAS:Reactome.
GO; GO:0017128; F:phospholipid scramblase activity; IEA:Ensembl.
GO; GO:0046983; F:protein dimerization activity; IEA:InterPro.
GO; GO:0061591; P:calcium activated galactosylceramide scrambling; IEA:Ensembl.
GO; GO:0061590; P:calcium activated phosphatidylcholine scrambling; IEA:Ensembl.
GO; GO:0050982; P:detection of mechanical stimulus; IEA:Ensembl.
GO; GO:0016048; P:detection of temperature stimulus; IEA:Ensembl.
GO; GO:0034220; P:ion transmembrane transport; TAS:Reactome.
InterPro; IPR032394; Anoct_dimer.
InterPro; IPR007632; Anoctamin.
InterPro; IPR031292; Anoctamin-3.
PANTHER; PTHR12308; PTHR12308; 1.
PANTHER; PTHR12308:SF16; PTHR12308:SF16; 1.
Pfam; PF16178; Anoct_dimer; 1.
Pfam; PF04547; Anoctamin; 1.
1: Evidence at protein level;
Alternative splicing; Cell membrane; Complete proteome;
Disease mutation; Dystonia; Glycoprotein; Lipid transport; Membrane;
Polymorphism; Reference proteome; Transmembrane; Transmembrane helix;
Transport.
CHAIN 1 981 Anoctamin-3.
/FTId=PRO_0000072565.
TOPO_DOM 1 403 Cytoplasmic. {ECO:0000255}.
TRANSMEM 404 424 Helical. {ECO:0000255}.
TOPO_DOM 425 469 Extracellular. {ECO:0000255}.
TRANSMEM 470 490 Helical. {ECO:0000255}.
TOPO_DOM 491 550 Cytoplasmic. {ECO:0000255}.
TRANSMEM 551 571 Helical. {ECO:0000255}.
TOPO_DOM 572 592 Extracellular. {ECO:0000255}.
TRANSMEM 593 613 Helical. {ECO:0000255}.
TOPO_DOM 614 640 Cytoplasmic. {ECO:0000255}.
TRANSMEM 641 661 Helical. {ECO:0000255}.
TOPO_DOM 662 761 Extracellular. {ECO:0000255}.
TRANSMEM 762 782 Helical. {ECO:0000255}.
TOPO_DOM 783 810 Cytoplasmic. {ECO:0000255}.
TRANSMEM 811 831 Helical. {ECO:0000255}.
TOPO_DOM 832 914 Extracellular. {ECO:0000255}.
TRANSMEM 915 935 Helical. {ECO:0000255}.
TOPO_DOM 936 981 Cytoplasmic. {ECO:0000255}.
CARBOHYD 425 425 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 448 448 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 455 455 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 866 866 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
VAR_SEQ 1 146 Missing (in isoform 2).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_056893.
VARIANT 490 490 W -> C (in DYT24).
{ECO:0000269|PubMed:23200863}.
/FTId=VAR_069732.
VARIANT 494 494 R -> W (in DYT24; dbSNP:rs587776922).
{ECO:0000269|PubMed:23200863}.
/FTId=VAR_069733.
VARIANT 685 685 S -> G (in DYT24; dbSNP:rs587776923).
{ECO:0000269|PubMed:23200863}.
/FTId=VAR_069734.
VARIANT 781 781 L -> V (in dbSNP:rs11825056).
/FTId=VAR_057287.
VARIANT 862 862 K -> N (in DYT24).
{ECO:0000269|PubMed:23200863}.
/FTId=VAR_069735.
CONFLICT 162 162 K -> R (in Ref. 1; CAC32454).
{ECO:0000305}.
CONFLICT 176 176 Q -> P (in Ref. 1; CAC32454).
{ECO:0000305}.
CONFLICT 256 256 N -> D (in Ref. 1; CAC32454).
{ECO:0000305}.
SEQUENCE 981 AA; 114657 MW; FC7449D2D4810290 CRC64;
MVHHSGSIQS FKQQKGMNIS KSEITKETSL KPSRRSLPCL AQSYAYSKSL SQSTSLFQST
ESESQAPTSI TLISTDKAEQ VNTEENKNDS VLRCSFADLS DFCLALGKDK DYTDESEHAT
YDRSRLINDF VIKDKSEFKT KLSKNDMNYI ASSGPLFKDG KKRIDYILVY RKTNIQYDKR
NTFEKNLRAE GLMLEKEPAI ASPDIMFIKI HIPWDTLCKY AERLNIRMPF RKKCYYTDGR
SKSMGRMQTY FRRIKNWMAQ NPMVLDKSAF PDLEESDCYT GPFSRARIHH FIINNKDTFF
SNATRSRIVY HMLERTKYEN GISKVGIRKL INNGSYIAAF PPHEGAYKSS QPIKTHGPQN
NRHLLYERWA RWGMWYKHQP LDLIRLYFGE KIGLYFAWLG WYTGMLIPAA IVGLCVFFYG
LFTMNNSQVS QEICKATEVF MCPLCDKNCS LQRLNDSCIY AKVTYLFDNG GTVFFAIFMA
IWATVFLEFW KRRRSILTYT WDLIEWEEEE ETLRPQFEAK YYKMEIVNPI TGKPEPHQPS
SDKVTRLLVS VSGIFFMISL VITAVFGVVV YRLVVMEQFA SFKWNFIKQY WQFATSAAAV
CINFIIIMLL NLAYEKIAYL LTNLEYPRTE SEWENSFALK MFLFQFVNLN SSIFYIAFFL
GRFVGHPGKY NKLFDRWRLE ECHPSGCLID LCLQMGVIMF LKQIWNNFME LGYPLIQNWW
SRHKIKRGIH DASIPQWEND WNLQPMNLHG LMDEYLEMVL QFGFTTIFVA AFPLAPLLAL
LNNIIEIRLD AYKFVTQWRR PLPARATDIG IWLGILEGIG ILAVITNAFV IAITSDYIPR
FVYEYKYGPC ANHVEPSENC LKGYVNNSLS FFDLSELGMG KSGYCRYRDY RGPPWSSKPY
EFTLQYWHIL AARLAFIIVF EHLVFGIKSF IAYLIPDVPK GLHDRIRREK YLVQEMMYEA
ELEHLQQQRR KSGQPVHHEW P


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