ANO9_MOUSE
ID ANO9_MOUSE Reviewed; 747 AA.
AC P86044;
DT 04-NOV-2008, integrated into UniProtKB/Swiss-Prot.
DT 04-NOV-2008, sequence version 1.
DT 03-AUG-2022, entry version 80.
DE RecName: Full=Anoctamin-9 {ECO:0000250|UniProtKB:A1A5B4};
DE AltName: Full=Transmembrane protein 16J {ECO:0000250|UniProtKB:A1A5B4};
GN Name=Ano9 {ECO:0000250|UniProtKB:A1A5B4};
GN Synonyms=Tmem16j {ECO:0000250|UniProtKB:A1A5B4};
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 [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [2] {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 [3]
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 [4]
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 [5]
RP FUNCTION, CATALYTIC ACTIVITY, AND TISSUE SPECIFICITY.
RX PubMed=23532839; DOI=10.1074/jbc.m113.457937;
RA Suzuki J., Fujii T., Imao T., Ishihara K., Kuba H., Nagata S.;
RT "Calcium-dependent phospholipid scramblase activity of TMEM16 protein
RT family members.";
RL J. Biol. Chem. 288:13305-13316(2013).
CC -!- FUNCTION: Has calcium-dependent phospholipid scramblase activity;
CC scrambles phosphatidylserine, phosphatidylcholine and
CC galactosylceramide (PubMed:23532839). Does not exhibit calcium-
CC activated chloride channel (CaCC) activity (By similarity). Can inhibit
CC the activity of ANO1 (By similarity). {ECO:0000250|UniProtKB:A1A5B4,
CC ECO:0000269|PubMed:23532839}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 1,2-diacyl-sn-glycero-3-phospho-L-serine(in) = a 1,2-diacyl-
CC sn-glycero-3-phospho-L-serine(out); Xref=Rhea:RHEA:38663,
CC ChEBI:CHEBI:57262; Evidence={ECO:0000269|PubMed:23532839};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38664;
CC Evidence={ECO:0000305|PubMed:23532839};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a beta-D-galactosyl-(1<->1')-N-acylsphing-4-enine(out) = a
CC beta-D-galactosyl-(1<->1')-N-acylsphing-4-enine(in);
CC Xref=Rhea:RHEA:38899, ChEBI:CHEBI:18390;
CC Evidence={ECO:0000269|PubMed:23532839};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38900;
CC Evidence={ECO:0000305|PubMed:23532839};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 1,2-diacyl-sn-glycero-3-phosphocholine(in) = a 1,2-diacyl-
CC sn-glycero-3-phosphocholine(out); Xref=Rhea:RHEA:38571,
CC ChEBI:CHEBI:57643; Evidence={ECO:0000269|PubMed:23532839};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:38573;
CC Evidence={ECO:0000305|PubMed:23532839};
CC -!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein.
CC Note=Shows predominantly an intracellular localization with a weak
CC expression in the cell membrane. {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Predominant expression seen in epithelial tissues.
CC {ECO:0000269|PubMed:20056604, ECO:0000269|PubMed:23532839}.
CC -!- DEVELOPMENTAL STAGE: In the developing respiratory system, expression
CC is restricted to the lung epithelium at 14.5 dpc. At 14.5 dpc and 16.5
CC dpc, expressed in the epithelium of the esophagus, small intestine,
CC stomach and pancreas. At 16.5 dpc, detected in bronchial epithelium. In
CC the developing skeleton, expressed in the perichondria of developing
CC ribs at 14.5 dpc. In developing skin, expression is detected in the
CC most suprabasal layers at 16.5 dpc. {ECO:0000269|PubMed:18729231}.
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:A1A5B4}.
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DR EMBL; AC109272; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR CCDS; CCDS52438.1; -.
DR RefSeq; NP_848468.2; NM_178381.3.
DR AlphaFoldDB; P86044; -.
DR SMR; P86044; -.
DR STRING; 10090.ENSMUSP00000067689; -.
DR SwissLipids; SLP:000000376; -.
DR GlyGen; P86044; 4 sites.
DR iPTMnet; P86044; -.
DR PhosphoSitePlus; P86044; -.
DR PaxDb; P86044; -.
DR PeptideAtlas; P86044; -.
DR PRIDE; P86044; -.
DR ProteomicsDB; 296313; -.
DR Antibodypedia; 58906; 75 antibodies from 20 providers.
DR DNASU; 71345; -.
DR Ensembl; ENSMUST00000067836; ENSMUSP00000067689; ENSMUSG00000054662.
DR GeneID; 71345; -.
DR KEGG; mmu:71345; -.
DR UCSC; uc012fwo.1; mouse.
DR CTD; 338440; -.
DR MGI; MGI:1918595; Ano9.
DR VEuPathDB; HostDB:ENSMUSG00000054662; -.
DR eggNOG; KOG2514; Eukaryota.
DR GeneTree; ENSGT00940000158300; -.
DR HOGENOM; CLU_006685_3_1_1; -.
DR InParanoid; P86044; -.
DR OMA; MAIWTTL; -.
DR OrthoDB; 1263362at2759; -.
DR PhylomeDB; P86044; -.
DR TreeFam; TF314265; -.
DR Reactome; R-MMU-2672351; Stimuli-sensing channels.
DR BioGRID-ORCS; 71345; 3 hits in 72 CRISPR screens.
DR ChiTaRS; Ano9; mouse.
DR PRO; PR:P86044; -.
DR Proteomes; UP000000589; Chromosome 7.
DR RNAct; P86044; protein.
DR Bgee; ENSMUSG00000054662; Expressed in lip and 79 other tissues.
DR Genevisible; P86044; MM.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; ISO: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:0017128; F:phospholipid scramblase activity; IDA:MGI.
DR GO; GO:0061591; P:calcium activated galactosylceramide scrambling; IDA:MGI.
DR GO; GO:0061590; P:calcium activated phosphatidylcholine scrambling; IDA:MGI.
DR GO; GO:0061589; P:calcium activated phosphatidylserine scrambling; IDA:MGI.
DR GO; GO:1902476; P:chloride transmembrane transport; IBA:GO_Central.
DR GO; GO:0006821; P:chloride transport; ISO:MGI.
DR GO; GO:0051649; P:establishment of localization in cell; IDA:MGI.
DR GO; GO:0006629; P:lipid metabolic process; IEA:UniProtKB-KW.
DR GO; GO:1902939; P:negative regulation of intracellular calcium activated chloride channel activity; ISO:MGI.
DR GO; GO:0055085; P:transmembrane transport; IBA:GO_Central.
DR InterPro; IPR007632; Anoctamin.
DR InterPro; IPR031290; Anoctamin-9.
DR PANTHER; PTHR12308; PTHR12308; 1.
DR PANTHER; PTHR12308:SF37; PTHR12308:SF37; 1.
DR Pfam; PF04547; Anoctamin; 1.
PE 1: Evidence at protein level;
KW Cell membrane; Glycoprotein; Lipid metabolism; Lipid transport; Membrane;
KW Reference proteome; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..747
FT /note="Anoctamin-9"
FT /id="PRO_0000353191"
FT TOPO_DOM 1..193
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 194..214
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 215..259
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 260..280
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 281..326
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 327..347
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 348..364
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 365..385
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 386..414
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 415..435
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 436..543
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 544..564
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 565..595
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 596..616
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 617..695
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 696..716
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 717..747
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT CARBOHYD 630
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 643
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 665
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 681
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 747 AA; 87180 MW; 42B4CA02516A54C4 CRC64;
MQDDESSQIF MGPEGDQLPL VEMGSCKPEA SDQWDCVLVA DLQTLKIQKH AQKQLQFLEN
LESNGFHFKM LKDQKKVFFG IRADSDVIDK YRTLLMNPED SGSRDEQSFN IATTRIRIVS
FVVNNKLKPG DTFEDLVKDG VFETMFLLHK GEQNLKNIWA RWRNMFEPQP IDEIREYFGE
KVALYFTWLG WYTYMLVPAA VVGLIVFLSG FALFDSSQIS KEICSANDIF MCPLGDHSHR
YLRLSEMCTF AKLTHLFDNE GTVLFAIFMA LWATVFLEIW KRKRAHEVQS WKLYEWDEEE
EEMALELINS PHYKLKDHRH SYLSSTIILI LSLFMICLMI GMAHVLVVYR VLAGALFSSL
VKQQVTTAVV VTGAVVHYII IVIMTKVNKY VALKLCKFEE SGTFSEQERK FTVKFFILQF
FAHFSSLIYI AFILGRINGH PGKSTRLAGL WKLEECHLSG CMMDLFIQMA IIMGLKQTLS
NCVEYLCPLL AHKWRLMWAS KHGHMSKDPE LKEWQRNYYM NPINTFSLFD EFMEMMIQYG
FTTIFVAAFP LAPLLALFSN LVEIRLDAIK MVRLQRRLVP RKAKDIGTWL QVLETIGVLA
VIANGMVIAF TSEFIPRVVY KYHYGPCRTN RTFTDDCLTN YVNHSLSVFY TKHFNDHSRM
EGQENVTVCR YRDYRNEHDY NLSEQFWFIL AIRLTFVILF EHFALCIKLI AAWFVPDVPQ
KVKNEVLQEK YDRIRHRMRF SSRSTDV
