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ANO2_MOUSE
ID   ANO2_MOUSE              Reviewed;        1002 AA.
AC   Q8CFW1; C4N788; Q8C8N6;
DT   04-NOV-2008, integrated into UniProtKB/Swiss-Prot.
DT   03-NOV-2009, sequence version 2.
DT   03-AUG-2022, entry version 123.
DE   RecName: Full=Anoctamin-2 {ECO:0000250|UniProtKB:Q9NQ90};
DE   AltName: Full=Transmembrane protein 16B {ECO:0000312|EMBL:AAH33409.1};
GN   Name=Ano2 {ECO:0000250|UniProtKB:Q9NQ90};
GN   Synonyms=Tmem16b {ECO:0000312|EMBL:AAH33409.1};
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, GLYCOSYLATION, SUBCELLULAR LOCATION,
RP   SUBUNIT, INTERACTION WITH DLG4, MUTAGENESIS OF 1000-THR--ASN-1002, AND
RP   TISSUE SPECIFICITY.
RC   STRAIN=C57BL/6J; TISSUE=Retina;
RX   PubMed=19474308; DOI=10.1523/jneurosci.5546-08.2009;
RA   Stoehr H., Heisig J.B., Benz P.M., Schoeberl S., Milenkovic V.M.,
RA   Strauss O., Aartsen W.M., Wijnholds J., Weber B.H.F., Schulz H.L.;
RT   "TMEM16B, a novel protein with calcium-dependent chloride channel activity,
RT   associates with a presynaptic protein complex in photoreceptor terminals.";
RL   J. Neurosci. 29:6809-6818(2009).
RN   [2] {ECO:0000305, ECO:0000312|EMBL:BAC32073.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-543.
RC   STRAIN=C57BL/6J {ECO:0000312|EMBL:BAC32073.1};
RC   TISSUE=Retina {ECO:0000312|EMBL:BAC32073.1};
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA   Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA   Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA   Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA   Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA   Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA   Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA   Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA   Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA   Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA   Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA   Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA   Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA   Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA   Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA   Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA   Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA   Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA   Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA   Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA   van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA   Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA   Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA   Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA   Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA   Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA   Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA   Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA   Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3] {ECO:0000305, ECO:0000312|EMBL:AAH33409.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 59-1002.
RC   STRAIN=C57BL/6J {ECO:0000312|EMBL:AAH33409.1};
RC   TISSUE=Eye {ECO:0000312|EMBL:AAH33409.1};
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4] {ECO:0000305}
RP   DEVELOPMENTAL STAGE.
RX   PubMed=18729231; DOI=10.1002/dvdy.21676;
RA   Rock J.R., Harfe B.D.;
RT   "Expression of TMEM16 paralogs during murine embryogenesis.";
RL   Dev. Dyn. 237:2566-2574(2008).
RN   [5]
RP   FUNCTION, AND ACTIVITY REGULATION.
RX   PubMed=19475416; DOI=10.1007/s00424-009-0684-9;
RA   Pifferi S., Dibattista M., Menini A.;
RT   "TMEM16B induces chloride currents activated by calcium in mammalian
RT   cells.";
RL   Pflugers Arch. 458:1023-1038(2009).
RN   [6]
RP   FUNCTION, IDENTIFICATION BY MASS SPECTROMETRY, SUBCELLULAR LOCATION, AND
RP   TISSUE SPECIFICITY.
RX   PubMed=19561302; DOI=10.1073/pnas.0903304106;
RA   Stephan A.B., Shum E.Y., Hirsh S., Cygnar K.D., Reisert J., Zhao H.;
RT   "ANO2 is the cilial calcium-activated chloride channel that may mediate
RT   olfactory amplification.";
RL   Proc. Natl. Acad. Sci. U.S.A. 106:11776-11781(2009).
RN   [7]
RP   TISSUE SPECIFICITY.
RX   PubMed=20056604; DOI=10.1074/jbc.m109.065367;
RA   Schreiber R., Uliyakina I., Kongsuphol P., Warth R., Mirza M.,
RA   Martins J.R., Kunzelmann K.;
RT   "Expression and function of epithelial anoctamins.";
RL   J. Biol. Chem. 285:7838-7845(2010).
RN   [8]
RP   FUNCTION.
RX   PubMed=22075693; DOI=10.1152/ajpcell.00140.2011;
RA   Duran C., Qu Z., Osunkoya A.O., Cui Y., Hartzell H.C.;
RT   "ANOs 3-7 in the anoctamin/Tmem16 Cl- channel family are intracellular
RT   proteins.";
RL   Am. J. Physiol. 302:C482-C493(2012).
RN   [9]
RP   REVIEW.
RX   PubMed=22302790; DOI=10.1113/expphysiol.2011.058214;
RA   Winpenny J.P., Gray M.A.;
RT   "The anoctamin (TMEM16) gene family: calcium-activated chloride channels
RT   come of age.";
RL   Exp. Physiol. 97:175-176(2012).
RN   [10]
RP   REVIEW, AND FUNCTION.
RX   PubMed=21890523; DOI=10.1113/expphysiol.2011.058230;
RA   Pifferi S., Cenedese V., Menini A.;
RT   "Anoctamin 2/TMEM16B: a calcium-activated chloride channel in olfactory
RT   transduction.";
RL   Exp. Physiol. 97:193-199(2012).
CC   -!- FUNCTION: Calcium-activated chloride channel (CaCC) which may play a
CC       role in olfactory signal transduction. Odorant molecules bind to odor-
CC       sensing receptors (OSRs), leading to an increase in calcium entry that
CC       activates CaCC current which amplifies the depolarization of the OSR
CC       cells, ANO2 seems to be the underlying chloride channel involved in
CC       this process. May mediate light perception amplification in retina.
CC       {ECO:0000269|PubMed:19474308, ECO:0000269|PubMed:19475416,
CC       ECO:0000269|PubMed:19561302, ECO:0000269|PubMed:21890523,
CC       ECO:0000269|PubMed:22075693}.
CC   -!- ACTIVITY REGULATION: Channel activity is repressed by chloride
CC       inhibitors; strongly by niflumic acid (NFA), partially by flufenamic
CC       acid (FFA), and only slightly by meclofenamic acid (MFA), 5-Nitro-2-(3-
CC       phenylpropylamino)benzoic acid (NPPB), 4-acetamido-4'-isothiocyanato-
CC       stilben-2,2'-disulfonate (SITS), and 4,4'-diisothiocyanatostilbene-
CC       2,2'-disulfonic acid (DIDS). {ECO:0000269|PubMed:19475416}.
CC   -!- SUBUNIT: Component of a presynaptic protein complex recruited to
CC       specialized plasma membrane domains of photoreceptors. Interacts with
CC       DLG4 by its C-terminal region. {ECO:0000269|PubMed:19474308}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:19474308,
CC       ECO:0000269|PubMed:19561302}; Multi-pass membrane protein
CC       {ECO:0000269|PubMed:19474308, ECO:0000269|PubMed:19561302}.
CC   -!- TISSUE SPECIFICITY: Expressed in retina, especially in the
CC       photoreceptor synaptic terminals, and in olfactory epithelium,
CC       particularly in sensory neurons (OSNs) and cilia (at protein level).
CC       Also observed in retinal pigment epithelium (RPE), olfactory bulb,
CC       brain, and cortex. {ECO:0000269|PubMed:19474308,
CC       ECO:0000269|PubMed:19561302, ECO:0000269|PubMed:20056604}.
CC   -!- DEVELOPMENTAL STAGE: Detected in the mantle layer of the neural tube
CC       and in the dorsal root ganglia at 14.5 dpc. In developing skin,
CC       expression is restricted to basal layers of the epidermis at 16.5 dpc.
CC       {ECO:0000269|PubMed:18729231}.
CC   -!- PTM: Glycosylated. {ECO:0000269|PubMed:19474308}.
CC   -!- MISCELLANEOUS: The term 'anoctamin' was coined because these channels
CC       are anion selective and have eight (OCT) transmembrane segments. There
CC       is some dissatisfaction in the field with the Ano nomenclature because
CC       it is not certain that all the members of this family are anion
CC       channels or have the 8-transmembrane topology.
CC   -!- SIMILARITY: Belongs to the anoctamin family.
CC       {ECO:0000250|UniProtKB:Q9NQ90}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAH33409.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC       Sequence=BAC32073.1; Type=Miscellaneous discrepancy; Note=Probable cloning artifact.; Evidence={ECO:0000305};
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DR   EMBL; FJ384096; ACL36051.1; -; mRNA.
DR   EMBL; AK044763; BAC32073.1; ALT_SEQ; mRNA.
DR   EMBL; BC033409; AAH33409.1; ALT_INIT; mRNA.
DR   CCDS; CCDS39643.2; -.
DR   RefSeq; NP_705817.2; NM_153589.2.
DR   RefSeq; XP_006506182.1; XM_006506119.1.
DR   AlphaFoldDB; Q8CFW1; -.
DR   SMR; Q8CFW1; -.
DR   BioGRID; 232544; 2.
DR   STRING; 10090.ENSMUSP00000125303; -.
DR   BindingDB; Q8CFW1; -.
DR   ChEMBL; CHEMBL4739697; -.
DR   GlyGen; Q8CFW1; 4 sites.
DR   iPTMnet; Q8CFW1; -.
DR   PhosphoSitePlus; Q8CFW1; -.
DR   PaxDb; Q8CFW1; -.
DR   PRIDE; Q8CFW1; -.
DR   ProteomicsDB; 282107; -.
DR   Antibodypedia; 41841; 137 antibodies from 28 providers.
DR   DNASU; 243634; -.
DR   Ensembl; ENSMUST00000160496; ENSMUSP00000125303; ENSMUSG00000038115.
DR   GeneID; 243634; -.
DR   KEGG; mmu:243634; -.
DR   UCSC; uc009duv.1; mouse.
DR   CTD; 57101; -.
DR   MGI; MGI:2387214; Ano2.
DR   VEuPathDB; HostDB:ENSMUSG00000038115; -.
DR   eggNOG; KOG2514; Eukaryota.
DR   GeneTree; ENSGT00940000155840; -.
DR   HOGENOM; CLU_006685_1_2_1; -.
DR   InParanoid; Q8CFW1; -.
DR   OMA; HYVYVFD; -.
DR   OrthoDB; 1263362at2759; -.
DR   PhylomeDB; Q8CFW1; -.
DR   TreeFam; TF314265; -.
DR   Reactome; R-MMU-2672351; Stimuli-sensing channels.
DR   BioGRID-ORCS; 243634; 0 hits in 73 CRISPR screens.
DR   ChiTaRS; Ano2; mouse.
DR   PRO; PR:Q8CFW1; -.
DR   Proteomes; UP000000589; Chromosome 6.
DR   RNAct; Q8CFW1; protein.
DR   Bgee; ENSMUSG00000038115; Expressed in retinal neural layer and 41 other tissues.
DR   ExpressionAtlas; Q8CFW1; baseline and differential.
DR   GO; GO:0034707; C:chloride channel complex; IEA:UniProtKB-KW.
DR   GO; GO:0043005; C:neuron projection; IDA:MGI.
DR   GO; GO:0097730; C:non-motile cilium; IDA:MGI.
DR   GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR   GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR   GO; GO:0005254; F:chloride channel activity; IBA:GO_Central.
DR   GO; GO:0042802; F:identical protein binding; IPI:MGI.
DR   GO; GO:0005229; F:intracellular calcium activated chloride channel activity; IDA:UniProtKB.
DR   GO; GO:0046983; F:protein dimerization activity; IEA:InterPro.
DR   GO; GO:1902476; P:chloride transmembrane transport; IBA:GO_Central.
DR   GO; GO:0006821; P:chloride transport; IDA:MGI.
DR   GO; GO:0051649; P:establishment of localization in cell; IDA:MGI.
DR   GO; GO:0055085; P:transmembrane transport; IBA:GO_Central.
DR   InterPro; IPR032394; Anoct_dimer.
DR   InterPro; IPR007632; Anoctamin.
DR   InterPro; IPR031288; Anoctamin-2.
DR   PANTHER; PTHR12308; PTHR12308; 1.
DR   PANTHER; PTHR12308:SF20; PTHR12308:SF20; 1.
DR   Pfam; PF16178; Anoct_dimer; 1.
DR   Pfam; PF04547; Anoctamin; 1.
PE   1: Evidence at protein level;
KW   Calcium; Cell membrane; Chloride; Chloride channel; Glycoprotein;
KW   Ion channel; Ion transport; Membrane; Reference proteome; Transmembrane;
KW   Transmembrane helix; Transport.
FT   CHAIN           1..1002
FT                   /note="Anoctamin-2"
FT                   /id="PRO_0000353187"
FT   TOPO_DOM        1..364
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        365..385
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        386..433
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        434..454
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        455..536
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        537..557
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        558..580
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        581..601
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        602..621
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        622..642
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        643..746
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        747..767
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        768..799
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        800..820
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        821..905
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        906..926
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        927..1002
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   REGION          1..85
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          501..523
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          958..1002
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           1000..1002
FT                   /note="DLG4 binding (PDZ)"
FT   COMPBIAS        958..972
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        973..1002
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CARBOHYD        421
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        839
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        847
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        854
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   MUTAGEN         1000..1002
FT                   /note="Missing: Impaired interaction with DLG4."
FT                   /evidence="ECO:0000269|PubMed:19474308"
SQ   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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