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Q9NQ90 (ANO2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 99. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Anoctamin-2
Alternative name(s):
Transmembrane protein 16B
Gene names
Name:ANO2
Synonyms:C12orf3, TMEM16B
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length1003 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

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. Ref.2 Ref.5 Ref.9 Ref.10

Enzyme 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) By similarity.

Subunit structure

Component of a presynaptic protein complex recruited to specialized plasma membrane domains of photoreceptors. Interacts with DLG4 by its C-terminus region By similarity. Ref.2

Subcellular location

Cell membrane; Multi-pass membrane protein Ref.5.

Tissue specificity

Retina, especially in the photoreceptor synaptic terminals. Ref.2

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.

Sequence similarities

Belongs to the anoctamin family.

Sequence caution

The sequence BAB14773.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q9NQ90-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Note: Splice site between exons 4 and 5 is non-canonical.
Isoform 2 (identifier: Q9NQ90-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-4: Missing.
     5-7: GPR → MPE
Note: Splice site between exons 4 and 5 is non-canonical.
Isoform 3 (identifier: Q9NQ90-3)

The sequence of this isoform differs from the canonical sequence as follows:
     1-4: Missing.
     5-7: GPR → MPE
     212-212: Missing.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 10031003Anoctamin-2
PRO_0000072564

Regions

Topological domain1 – 365365Cytoplasmic Potential
Transmembrane366 – 38621Helical; Potential
Topological domain387 – 43448Extracellular Potential
Transmembrane435 – 45521Helical; Potential
Topological domain456 – 53883Cytoplasmic Potential
Transmembrane539 – 55921Helical; Potential
Topological domain560 – 58223Extracellular Potential
Transmembrane583 – 60321Helical; Potential
Topological domain604 – 62320Cytoplasmic Potential
Transmembrane624 – 64421Helical; Potential
Topological domain645 – 748104Extracellular Potential
Transmembrane749 – 76921Helical; Potential
Topological domain770 – 80132Cytoplasmic Potential
Transmembrane802 – 82221Helical; Potential
Topological domain823 – 90785Extracellular Potential
Transmembrane908 – 92821Helical; Potential
Topological domain929 – 100375Cytoplasmic Potential
Motif1001 – 10033DLG4 binding (PDZ)

Amino acid modifications

Glycosylation4221N-linked (GlcNAc...) Potential
Glycosylation8411N-linked (GlcNAc...) Potential
Glycosylation8491N-linked (GlcNAc...) Potential
Glycosylation8561N-linked (GlcNAc...) Potential

Natural variations

Alternative sequence1 – 44Missing in isoform 2 and isoform 3.
VSP_040493
Alternative sequence5 – 73GPR → MPE in isoform 2 and isoform 3.
VSP_040494
Alternative sequence2121Missing in isoform 3.
VSP_040495
Natural variant1121V → A.
Corresponds to variant rs3741903 [ dbSNP | Ensembl ].
VAR_021932
Natural variant1471P → S.
Corresponds to variant rs3741901 [ dbSNP | Ensembl ].
VAR_057286
Natural variant4011M → I.
Corresponds to variant rs17788563 [ dbSNP | Ensembl ].
VAR_061853
Natural variant5051S → A.
Corresponds to variant rs1860961 [ dbSNP | Ensembl ].
VAR_020331

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified November 3, 2009. Version 2.
Checksum: 32939EADC8AFE5C8

FASTA1,003113,969
        10         20         30         40         50         60 
MATPGPRDIP LLPGSPRRLS PQAGSRGGQG PKHGQQCLKM PGPRAPGLQG GSNRDPGQPC 

        70         80         90        100        110        120 
GGESTRSSSV INNYLDANEP VSLEARLSRM HFHDSQRKVD YVLAYHYRKR GVHLAQGFPG 

       130        140        150        160        170        180 
HSLAIVSNGE TGKEPHAGGP GDIELGPLDA LEEERKEQRE EFEHNLMEAG LELEKDLENK 

       190        200        210        220        230        240 
SQGSIFVRIH APWQVLAREA EFLKIKVPTK KEMYEIKAGG SIAKKFSAAL QKLSSHLQPR 

       250        260        270        280        290        300 
VPEHSNNKMK NLSYPFSREK MYLYNIQEKD TFFDNATRSR IVHEILKRTA CSRANNTMGI 

       310        320        330        340        350        360 
NSLIANNIYE AAYPLHDGEY DSPEDDMNDR KLLYQEWARY GVFYKFQPID LIRKYFGEKI 

       370        380        390        400        410        420 
GLYFAWLGLY TSFLIPSSVI GVIVFLYGCA TIEEDIPSRE MCDQQNAFTM CPLCDKSCDY 

       430        440        450        460        470        480 
WNLSSACGTA QASHLFDNPA TVFFSIFMAL WATMFLENWK RLQMRLGYFW DLTGIEEEEE 

       490        500        510        520        530        540 
RAQEHSRPEY ETKVREKMLK ESNQSAVQKL ETNTTECGDE DDEDKLTWKD RFPGYLMNFA 

       550        560        570        580        590        600 
SILFMIALTF SIVFGVIVYR ITTAAALSLN KATRSNVRVT VTATAVIINL VVILILDEIY 

       610        620        630        640        650        660 
GAVAKWLTKI EVPKTEQTFE ERLILKAFLL KFVNAYSPIF YVAFFKGRFV GRPGSYVYVF 

       670        680        690        700        710        720 
DGYRMEECAP GGCLMELCIQ LSIIMLGKQL IQNNIFEIGV PKLKKLFRKL KDETEAGETD 

       730        740        750        760        770        780 
SAHSKHPEQW DLDYSLEPYT GLTPEYMEMI IQFGFVTLFV ASFPLAPVFA LLNNVIEVRL 

       790        800        810        820        830        840 
DAKKFVTELR RPDAVRTKDI GIWFDILSGI GKFSVISNAF VIAITSDFIP RLVYQYSYSH 

       850        860        870        880        890        900 
NGTLHGFVNH TLSFFNVSQL KEGTQPENSQ FDQEVQFCRF KDYREPPWAP NPYEFSKQYW 

       910        920        930        940        950        960 
FILSARLAFV IIFQNLVMFL SVLVDWMIPD IPTDISDQIK KEKSLLVDFF LKEEHEKLKL 

       970        980        990       1000 
MDEPALRSPG GGDRSRSRAA SSAPSGQSQL GSMMSSGSQH TNV 

« Hide

Isoform 2 [UniParc].

Checksum: B9B4F56161AE1B00
Show »

FASTA999113,616
Isoform 3 [UniParc].

Checksum: A1CC10B50E9A487A
Show »

FASTA998113,487

References

« Hide 'large scale' references
[1]"Transcripts in 12p13.3."
Lorenz B., White K.E., Econs M.J., Strom T.M.
Submitted (FEB-2000) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
Tissue: Retina.
[2]"TMEM16B, a novel protein with calcium-dependent chloride channel activity, associates with a presynaptic protein complex in photoreceptor terminals."
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.
J. Neurosci. 29:6809-6818(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, GLYCOSYLATION, SUBUNIT, TISSUE SPECIFICITY.
Tissue: Retina.
[3]"The finished DNA sequence of human chromosome 12."
Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R. expand/collapse author list , Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Montgomery K.T., Morgan M.B., Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z., Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H., Draper H., Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S., Kelly S.H., Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H., Santibanez J., Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q., Williams G.A., Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V., Bailey M., Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E., Burkett C.E., Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K., Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D., Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M., Dathorne S.R., David R., Davis C.M., Davy-Carroll L., Deshazo D.R., Donlin J.E., D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J., Escotto M., Flagg N., Forbes L.D., Gabisi A.M., Garza M., Hamilton C., Henderson N., Hernandez O., Hines S., Hogues M.E., Huang M., Idlebird D.G., Johnson R., Jolivet A., Jones S., Kagan R., King L.M., Leal B., Lebow H., Lee S., LeVan J.M., Lewis L.C., London P., Lorensuhewa L.M., Loulseged H., Lovett D.A., Lucier A., Lucier R.L., Ma J., Madu R.C., Mapua P., Martindale A.D., Martinez E., Massey E., Mawhiney S., Meador M.G., Mendez S., Mercado C., Mercado I.C., Merritt C.E., Miner Z.L., Minja E., Mitchell T., Mohabbat F., Mohabbat K., Montgomery B., Moore N., Morris S., Munidasa M., Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O., Nwokenkwo S., Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J., Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A., Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M., Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I., Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A., Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D., Trejos Z.Y., Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I., Vera V.A., Villasana D.M., Wang L., Ward-Moore S., Warren J.T., Wei X., White F., Williamson A.L., Wleczyk R., Wooden H.S., Wooden S.H., Yen J., Yoon L., Yoon V., Zorrilla S.E., Nelson D., Kucherlapati R., Weinstock G., Gibbs R.A.
Nature 440:346-351(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]"Complete sequencing and characterization of 21,243 full-length human cDNAs."
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. expand/collapse author list , 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.
Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 556-999 (ISOFORMS 1 AND 2).
Tissue: Retinoblastoma.
[5]"Expression and function of epithelial anoctamins."
Schreiber R., Uliyakina I., Kongsuphol P., Warth R., Mirza M., Martins J.R., Kunzelmann K.
J. Biol. Chem. 285:7838-7845(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION.
[6]"Physiological roles and diseases of Tmem16/Anoctamin proteins: are they all chloride channels?"
Duran C., Hartzell H.C.
Acta Pharmacol. Sin. 32:685-692(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: REVIEW.
[7]"Anoctamins."
Kunzelmann K., Tian Y., Martins J.R., Faria D., Kongsuphol P., Ousingsawat J., Thevenod F., Roussa E., Rock J., Schreiber R.
Pflugers Arch. 462:195-208(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: REVIEW.
[8]"The anoctamin (TMEM16) gene family: calcium-activated chloride channels come of age."
Winpenny J.P., Gray M.A.
Exp. Physiol. 97:175-176(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: REVIEW.
[9]"The anoctamin family: TMEM16A and TMEM16B as calcium-activated chloride channels."
Scudieri P., Sondo E., Ferrera L., Galietta L.J.
Exp. Physiol. 97:177-183(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: REVIEW, FUNCTION.
[10]"Anoctamin 2/TMEM16B: a calcium-activated chloride channel in olfactory transduction."
Pifferi S., Cenedese V., Menini A.
Exp. Physiol. 97:193-199(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: REVIEW, FUNCTION.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AJ272204 mRNA. Translation: CAC01125.1.
FJ384095 mRNA. Translation: ACL36050.1.
AC006431 Genomic DNA. No translation available.
AC006560 Genomic DNA. No translation available.
AC137627 Genomic DNA. No translation available.
AK024010 mRNA. Translation: BAB14773.1. Different initiation.
RefSeqNP_001265525.1. NM_001278596.1.
NP_001265526.1. NM_001278597.1.
UniGeneHs.148970.

3D structure databases

ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid121367. 1 interaction.
STRING9606.ENSP00000314048.

Protein family/group databases

TCDB1.A.17.1.3. the calcium-dependent chloride channel (ca-clc) family.

PTM databases

PhosphoSiteQ9NQ90.

Polymorphism databases

DMDM262527528.

Proteomic databases

PaxDbQ9NQ90.
PRIDEQ9NQ90.

Protocols and materials databases

DNASU57101.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000327087; ENSP00000314048; ENSG00000047617. [Q9NQ90-3]
ENST00000356134; ENSP00000348453; ENSG00000047617. [Q9NQ90-2]
GeneID57101.
KEGGhsa:57101.
UCSCuc001qnm.2. human. [Q9NQ90-3]

Organism-specific databases

CTD57101.
GeneCardsGC12M005671.
HGNCHGNC:1183. ANO2.
HPAHPA036276.
MIM610109. gene.
neXtProtNX_Q9NQ90.
PharmGKBPA25504.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG320103.
HOGENOMHOG000006509.
HOVERGENHBG069519.
InParanoidQ9NQ90.
OMADRFPGYL.
OrthoDBEOG7BS48W.
PhylomeDBQ9NQ90.
TreeFamTF314265.

Enzyme and pathway databases

ReactomeREACT_15518. Transmembrane transport of small molecules.

Gene expression databases

ArrayExpressQ9NQ90.
BgeeQ9NQ90.
CleanExHS_ANO2.
GenevestigatorQ9NQ90.

Family and domain databases

InterProIPR007632. Anoctamin.
[Graphical view]
PANTHERPTHR12308. PTHR12308. 1 hit.
PfamPF04547. Anoctamin. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

GenomeRNAi57101.
NextBio62929.
PROQ9NQ90.
SOURCESearch...

Entry information

Entry nameANO2_HUMAN
AccessionPrimary (citable) accession number: Q9NQ90
Secondary accession number(s): C4N787, Q9H847
Entry history
Integrated into UniProtKB/Swiss-Prot: January 16, 2004
Last sequence update: November 3, 2009
Last modified: April 16, 2014
This is version 99 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 12

Human chromosome 12: entries, gene names and cross-references to MIM