ANO5_MOUSE
ID ANO5_MOUSE Reviewed; 904 AA.
AC Q75UR0; Q2VPA8; Q3V657; Q8CC04;
DT 13-SEP-2005, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 121.
DE RecName: Full=Anoctamin-5;
DE AltName: Full=Gnathodiaphyseal dysplasia 1 protein homolog;
DE AltName: Full=Transmembrane protein 16E;
GN Name=Ano5; Synonyms=Gdd1, Tmem16e;
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] (ISOFORM 1), ALTERNATIVE SPLICING, TISSUE
RP SPECIFICITY, AND INDUCTION.
RC STRAIN=BALB/cJ; TISSUE=Skeletal muscle;
RX PubMed=15124103; DOI=10.1086/421527;
RA Tsutsumi S., Kamata N., Vokes T.J., Maruoka Y., Nakakuki K., Enomoto S.,
RA Omura K., Amagasa T., Nagayama M., Saito-Ohara F., Inazawa J., Moritani M.,
RA Yamaoka T., Inoue H., Itakura M.;
RT "The novel gene encoding a putative transmembrane protein is mutated in
RT gnathodiaphyseal dysplasia (GDD).";
RL Am. J. Hum. Genet. 74:1255-1261(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), ALTERNATIVE SPLICING, TISSUE
RP SPECIFICITY, AND INDUCTION.
RC STRAIN=BDF1; TISSUE=Skeletal muscle;
RX PubMed=15882990; DOI=10.1016/j.bbrc.2005.03.226;
RA Tsutsumi S., Inoue H., Sakamoto Y., Mizuta K., Kamata N., Itakura M.;
RT "Molecular cloning and characterization of the murine gnathodiaphyseal
RT dysplasia gene GDD1.";
RL Biochem. Biophys. Res. Commun. 331:1099-1106(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC STRAIN=C57BL/6J; TISSUE=Diencephalon;
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
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 [5]
RP SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RX PubMed=17418107; DOI=10.1016/j.bbrc.2007.03.108;
RA Mizuta K., Tsutsumi S., Inoue H., Sakamoto Y., Miyatake K., Miyawaki K.,
RA Noji S., Kamata N., Itakura M.;
RT "Molecular characterization of GDD1/TMEM16E, the gene product responsible
RT for autosomal dominant gnathodiaphyseal dysplasia.";
RL Biochem. Biophys. Res. Commun. 357:126-132(2007).
RN [6]
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 [7]
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).
CC -!- FUNCTION: Does not exhibit calcium-activated chloride channel (CaCC)
CC activity. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000269|PubMed:17418107}; Multi-pass membrane protein
CC {ECO:0000269|PubMed:17418107}. Cell membrane
CC {ECO:0000269|PubMed:17418107}; Multi-pass membrane protein
CC {ECO:0000255}. Note=Colocalized with CALR/calreticulin. Shows an
CC intracellular localization. {ECO:0000250|UniProtKB:Q75V66}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Comment=At least 14 isoforms are produced using different
CC combinations of exons 4, 6, 16, 20 and 21.;
CC Name=1;
CC IsoId=Q75UR0-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q75UR0-2; Sequence=VSP_015628, VSP_015629, VSP_015630,
CC VSP_015631;
CC Name=3;
CC IsoId=Q75UR0-3; Sequence=VSP_035571, VSP_035572;
CC -!- TISSUE SPECIFICITY: Highly expressed in skeletal muscle, bone tissues
CC and thyroid gland. {ECO:0000269|PubMed:15124103,
CC ECO:0000269|PubMed:15882990, ECO:0000269|PubMed:17418107,
CC ECO:0000269|PubMed:20056604}.
CC -!- DEVELOPMENTAL STAGE: In the developing embryo, expressed mainly in
CC differentiating and developing somites and is associated with myotomal
CC somite lineages. {ECO:0000269|PubMed:17418107}.
CC -!- INDUCTION: Up-regulated during the course of myogenic differentiation.
CC Down-regulated during osteoblastic differentiation.
CC {ECO:0000269|PubMed:15124103, ECO:0000269|PubMed:15882990}.
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. {ECO:0000305}.
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DR EMBL; AB125740; BAD17873.1; -; mRNA.
DR EMBL; AB206762; BAE44438.1; -; mRNA.
DR EMBL; AK034197; BAC28628.1; -; mRNA.
DR EMBL; BC109163; AAI09164.2; -; mRNA.
DR CCDS; CCDS39968.1; -. [Q75UR0-1]
DR CCDS; CCDS85311.1; -. [Q75UR0-3]
DR RefSeq; NP_001258808.1; NM_001271879.1. [Q75UR0-3]
DR RefSeq; NP_808362.2; NM_177694.6. [Q75UR0-1]
DR AlphaFoldDB; Q75UR0; -.
DR SMR; Q75UR0; -.
DR STRING; 10090.ENSMUSP00000046884; -.
DR TCDB; 1.A.17.1.2; the calcium-dependent chloride channel (ca-clc) family.
DR GlyGen; Q75UR0; 6 sites.
DR iPTMnet; Q75UR0; -.
DR PhosphoSitePlus; Q75UR0; -.
DR PaxDb; Q75UR0; -.
DR PRIDE; Q75UR0; -.
DR Antibodypedia; 53749; 79 antibodies from 18 providers.
DR Ensembl; ENSMUST00000043944; ENSMUSP00000046884; ENSMUSG00000055489. [Q75UR0-1]
DR Ensembl; ENSMUST00000207044; ENSMUSP00000147243; ENSMUSG00000055489. [Q75UR0-2]
DR Ensembl; ENSMUST00000207717; ENSMUSP00000146783; ENSMUSG00000055489. [Q75UR0-3]
DR GeneID; 233246; -.
DR KEGG; mmu:233246; -.
DR UCSC; uc009hcc.2; mouse. [Q75UR0-1]
DR UCSC; uc009hce.2; mouse. [Q75UR0-2]
DR UCSC; uc033izs.1; mouse. [Q75UR0-3]
DR CTD; 203859; -.
DR MGI; MGI:3576659; Ano5.
DR VEuPathDB; HostDB:ENSMUSG00000055489; -.
DR eggNOG; KOG2514; Eukaryota.
DR GeneTree; ENSGT00940000155692; -.
DR HOGENOM; CLU_006685_1_4_1; -.
DR InParanoid; Q75UR0; -.
DR OMA; LRNVQYW; -.
DR OrthoDB; 1263362at2759; -.
DR PhylomeDB; Q75UR0; -.
DR TreeFam; TF314265; -.
DR Reactome; R-MMU-2672351; Stimuli-sensing channels.
DR BioGRID-ORCS; 233246; 2 hits in 73 CRISPR screens.
DR PRO; PR:Q75UR0; -.
DR Proteomes; UP000000589; Chromosome 7.
DR RNAct; Q75UR0; protein.
DR Bgee; ENSMUSG00000055489; Expressed in quadriceps femoris and 48 other tissues.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR GO; GO:0031982; C:vesicle; IDA:MGI.
DR GO; GO:0005254; F:chloride channel activity; IBA:GO_Central.
DR GO; GO:0005229; F:intracellular calcium activated chloride channel activity; IEA:Ensembl.
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; ISO:MGI.
DR GO; GO:0055085; P:transmembrane transport; IBA:GO_Central.
DR InterPro; IPR032394; Anoct_dimer.
DR InterPro; IPR007632; Anoctamin.
DR InterPro; IPR031294; Anoctamin-5.
DR PANTHER; PTHR12308; PTHR12308; 1.
DR PANTHER; PTHR12308:SF23; PTHR12308:SF23; 1.
DR Pfam; PF16178; Anoct_dimer; 1.
DR Pfam; PF04547; Anoctamin; 1.
PE 2: Evidence at transcript level;
KW Alternative splicing; Cell membrane; Endoplasmic reticulum; Glycoprotein;
KW Membrane; Reference proteome; Transmembrane; Transmembrane helix.
FT CHAIN 1..904
FT /note="Anoctamin-5"
FT /id="PRO_0000191756"
FT TOPO_DOM 1..290
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 291..311
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 312..371
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 372..392
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 393..453
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 454..474
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 475..502
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 503..523
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 524..548
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 549..569
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 570..667
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 668..688
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 689..723
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 724..744
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 745..825
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 826..846
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 847..904
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT CARBOHYD 326
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 357
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 371
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 759
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 769
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 782
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT VAR_SEQ 1..33
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_015628"
FT VAR_SEQ 34..52
FT /note="DLQSPPEKRFNLFLRRRLM -> MNLGSKETSFLIPEDLQSP (in
FT isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_015629"
FT VAR_SEQ 39..52
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_035571"
FT VAR_SEQ 535..570
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_035572"
FT VAR_SEQ 796..805
FT /note="RYRDYRYPPD -> STSCFCLNFY (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_015630"
FT VAR_SEQ 806..904
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_015631"
SQ SEQUENCE 904 AA; 106214 MW; 347FA6BC33FA0042 CRC64;
MVEQEGLTAK EIDYAFQQNE NLGSKETSFL IPEDLQSPPE KRFNLFLRRR LMFQRSEHSK
DSVFFRDGIR QIDFVLSYVE DLKKDGELKA ERRREFEQNL RKTGLDLETE DKLNSEDGKT
YFVKIHAPWE VLVTYAEVLG IKMPIKLSDI PRPKYPPLSY MLGAVKLPSS VKYPTPEYFT
AQFSRHRQEL FLIEDEATFF PSSTRNRIVY YILSRCPFGV EEGKKKIGIE RLLNSNTYLS
AYPLHDGQYW KPSKTTRPNE RYNLCKNWAR FSYFYKEQPF HLIRNYFGEK IGIYFVFLGY
YTEMLLFAAL VGLACFIYGL LSMENNRTST EICDPDIGGQ MIMCPLCDEV CDYWRLNTTC
LHSKFSHLFD NESTVFFALF MGIWVTLFLE FWKQRQARLE YEWDLVDFEE EQQQLQLRPE
FEAMCKHKKM NPVTKEMEPH MPLCHRIPWY FVSGTTVTFG MALLLSSMVS ILIYRLSVFA
TFASFMESEA TLQSVKSFFT PQLATALSGS CLNCIVILIL NFFYEKISAW ITKMEIPRTH
QEYESSLTLK MFLFQFVNYY SSCFYVAFFK GKFVGYPGSY TYMFNIWRSE ECGPAGCLIE
LTTQLTIIMI GKQIFGNIHE AFQPLIFNWW RRRRARTHSE KLYSRWEQDH DLQVYGHRGL
FYEYLETVIQ FGFATLFVAS FPLAPLFALM NNIMGIRVDA WKLTTQYRRP VAAKAHSIGV
WQDILFGMAI VSVATNAFIV SFTSDIIPRL VYFYAYSTNS TEPLSGYVNN SLSVFLIADF
PNHTVPMEKK DFVTCRYRDY RYPPDHEDKY SHNMQFWHVL AAKMTFIIVM EHVVFLFKFL
LAWLIPDVPK DVVEKIKREK LMTIKIIHDF ELNKLKENLD VEYGNIMKNV LVDEDNSLKA
KTTV
