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Transmembrane O-methyltransferase homolog (EC 2.1.1.6) (Protein mercury)

 TOMT_DANRE              Reviewed;         259 AA.
A0A193KX02;
25-OCT-2017, integrated into UniProtKB/Swiss-Prot.
05-OCT-2016, sequence version 1.
23-MAY-2018, entry version 12.
RecName: Full=Transmembrane O-methyltransferase homolog {ECO:0000305};
EC=2.1.1.6 {ECO:0000250|UniProtKB:P21964};
AltName: Full=Protein mercury {ECO:0000303|PubMed:9491988};
Name=tomt {ECO:0000303|PubMed:28534737,
ECO:0000312|ZFIN:ZDB-GENE-160629-1};
Synonyms=mrc {ECO:0000303|PubMed:9491988};
Danio rerio (Zebrafish) (Brachydanio rerio).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
Cyprinidae; Danio.
NCBI_TaxID=7955;
[1]
NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, AND
DEVELOPMENTAL STAGE.
PubMed=28534737; DOI=10.7554/eLife.28474;
Erickson T., Morgan C.P., Olt J., Hardy K., Busch-Nentwich E.,
Maeda R., Clemens R., Krey J.F., Nechiporuk A., Barr-Gillespie P.G.,
Marcotti W., Nicolson T.;
"Integration of Tmc1/2 into the mechanotransduction complex in
zebrafish hair cells is regulated by Transmembrane O-methyltransferase
(Tomt).";
Elife 6:0-0(2017).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=Tuebingen;
PubMed=23594743; DOI=10.1038/nature12111;
Howe K., Clark M.D., Torroja C.F., Torrance J., Berthelot C.,
Muffato M., Collins J.E., Humphray S., McLaren K., Matthews L.,
McLaren S., Sealy I., Caccamo M., Churcher C., Scott C., Barrett J.C.,
Koch R., Rauch G.J., White S., Chow W., Kilian B., Quintais L.T.,
Guerra-Assuncao J.A., Zhou Y., Gu Y., Yen J., Vogel J.H., Eyre T.,
Redmond S., Banerjee R., Chi J., Fu B., Langley E., Maguire S.F.,
Laird G.K., Lloyd D., Kenyon E., Donaldson S., Sehra H.,
Almeida-King J., Loveland J., Trevanion S., Jones M., Quail M.,
Willey D., Hunt A., Burton J., Sims S., McLay K., Plumb B., Davis J.,
Clee C., Oliver K., Clark R., Riddle C., Eliott D., Threadgold G.,
Harden G., Ware D., Mortimer B., Kerry G., Heath P., Phillimore B.,
Tracey A., Corby N., Dunn M., Johnson C., Wood J., Clark S., Pelan S.,
Griffiths G., Smith M., Glithero R., Howden P., Barker N., Stevens C.,
Harley J., Holt K., Panagiotidis G., Lovell J., Beasley H.,
Henderson C., Gordon D., Auger K., Wright D., Collins J., Raisen C.,
Dyer L., Leung K., Robertson L., Ambridge K., Leongamornlert D.,
McGuire S., Gilderthorp R., Griffiths C., Manthravadi D., Nichol S.,
Barker G., Whitehead S., Kay M., Brown J., Murnane C., Gray E.,
Humphries M., Sycamore N., Barker D., Saunders D., Wallis J.,
Babbage A., Hammond S., Mashreghi-Mohammadi M., Barr L., Martin S.,
Wray P., Ellington A., Matthews N., Ellwood M., Woodmansey R.,
Clark G., Cooper J., Tromans A., Grafham D., Skuce C., Pandian R.,
Andrews R., Harrison E., Kimberley A., Garnett J., Fosker N., Hall R.,
Garner P., Kelly D., Bird C., Palmer S., Gehring I., Berger A.,
Dooley C.M., Ersan-Urun Z., Eser C., Geiger H., Geisler M.,
Karotki L., Kirn A., Konantz J., Konantz M., Oberlander M.,
Rudolph-Geiger S., Teucke M., Osoegawa K., Zhu B., Rapp A., Widaa S.,
Langford C., Yang F., Carter N.P., Harrow J., Ning Z., Herrero J.,
Searle S.M., Enright A., Geisler R., Plasterk R.H., Lee C.,
Westerfield M., de Jong P.J., Zon L.I., Postlethwait J.H.,
Nusslein-Volhard C., Hubbard T.J., Roest Crollius H., Rogers J.,
Stemple D.L.;
"The zebrafish reference genome sequence and its relationship to the
human genome.";
Nature 496:498-503(2013).
[3]
IDENTIFICATION, AND DISRUPTION PHENOTYPE.
PubMed=9491988;
Nicolson T., Ruesch A., Friedrich R.W., Granato M., Ruppersberg J.P.,
Nuesslein-Volhard C.;
"Genetic analysis of vertebrate sensory hair cell mechanosensation:
the zebrafish circler mutants.";
Neuron 20:271-283(1998).
-!- FUNCTION: Catalyzes the O-methylation, and thereby the
inactivation, of catecholamine neurotransmitters and catechol
hormones (By similarity). Required for auditory function.
Component of the hair cell's mechanotransduction (MET) machinery.
Involved in the assembly of the asymmetric tip-link MET complex.
Required for transportation of TMC1 and TMC2 proteins into the
mechanically sensitive stereocilia of the hair cells. The function
in MET is independent of the enzymatic activity (PubMed:28534737).
{ECO:0000250|UniProtKB:P21964, ECO:0000269|PubMed:28534737}.
-!- CATALYTIC ACTIVITY: S-adenosyl-L-methionine + a catechol = S-
adenosyl-L-homocysteine + a guaiacol.
{ECO:0000250|UniProtKB:P21964}.
-!- SUBCELLULAR LOCATION: Endoplasmic reticulum
{ECO:0000269|PubMed:28534737}. Golgi apparatus
{ECO:0000269|PubMed:28534737}. Basolateral cell membrane
{ECO:0000269|PubMed:28534737}. Note=Enriched in an apical membrane
compartment above the nucleus in the hair cells. Not detectable in
the hair bundle. May be present at lower levels in the endoplasmic
reticulum and the basolateral membrane.
{ECO:0000269|PubMed:28534737}.
-!- DEVELOPMENTAL STAGE: At 28 hr post-fertilization (hpf), expressed
exclusively in the hair cells of the anterior and posterior
maculae in the developing ear. At 4 days post-fertilization (dpf),
expressed specifically in hair cells of the inner ear and lateral
line organ. {ECO:0000269|PubMed:28534737}.
-!- DISRUPTION PHENOTYPE: Originally identified in a genetic screen
for genes required for hearing and balance. The mercury circler
mutant phenotype is characterized by balance defects, an absence
of the acoustic startle reflex, failure to inflate the swim
bladder, lack of hair cell-dependent calcium responses in the
hindbrain, and undetectable microphonic currents. No morphological
defects in the sensory hair cell bundles nor epithelium.
{ECO:0000269|PubMed:9491988}.
-!- SIMILARITY: Belongs to the class I-like SAM-binding
methyltransferase superfamily. Cation-dependent O-
methyltransferase family. {ECO:0000305}.
-!- CAUTION: Despite its name, the zebrafish TOMT protein is not
predicted to contain a transmembrane region in contrast to primate
orthologs. {ECO:0000305}.
-----------------------------------------------------------------------
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Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; KX066099; ANO40802.1; -; mRNA.
EMBL; CZQB01095947; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CZQB01095951; -; NOT_ANNOTATED_CDS; Genomic_DNA.
UniGene; Dr.138523; -.
UniGene; Dr.141301; -.
SMR; A0A193KX02; -.
ZFIN; ZDB-GENE-160629-1; tomt.
PRO; PR:A0A193KX02; -.
Proteomes; UP000000437; Unplaced.
GO; GO:0016323; C:basolateral plasma membrane; IDA:UniProtKB.
GO; GO:0005783; C:endoplasmic reticulum; IDA:UniProtKB.
GO; GO:0005794; C:Golgi apparatus; IDA:UniProtKB.
GO; GO:0016206; F:catechol O-methyltransferase activity; ISS:UniProtKB.
GO; GO:0102084; F:L-dopa O-methyltransferase activity; IEA:UniProtKB-EC.
GO; GO:0102938; F:orcinol O-methyltransferase activity; IEA:UniProtKB-EC.
GO; GO:0031223; P:auditory behavior; IMP:UniProtKB.
GO; GO:0042424; P:catecholamine catabolic process; ISS:UniProtKB.
GO; GO:0050974; P:detection of mechanical stimulus involved in sensory perception; IMP:ZFIN.
GO; GO:0006897; P:endocytosis; IMP:ZFIN.
GO; GO:0035315; P:hair cell differentiation; IMP:ZFIN.
GO; GO:0060122; P:inner ear receptor cell stereocilium organization; IMP:ZFIN.
GO; GO:0048884; P:neuromast development; IMP:ZFIN.
GO; GO:0042135; P:neurotransmitter catabolic process; IEA:UniProtKB-KW.
GO; GO:0007605; P:sensory perception of sound; IEA:UniProtKB-KW.
InterPro; IPR002935; O-MeTrfase_3.
InterPro; IPR029063; SAM-dependent_MTases.
InterPro; IPR033025; TOMT.
PANTHER; PTHR43836:SF1; PTHR43836:SF1; 1.
Pfam; PF01596; Methyltransf_3; 1.
SUPFAM; SSF53335; SSF53335; 1.
PROSITE; PS51682; SAM_OMT_I; 1.
2: Evidence at transcript level;
Catecholamine metabolism; Cell membrane; Complete proteome; Deafness;
Endoplasmic reticulum; Golgi apparatus; Hearing; Membrane;
Methyltransferase; Neurotransmitter degradation; Reference proteome;
S-adenosyl-L-methionine; Transferase.
CHAIN 1 259 Transmembrane O-methyltransferase
homolog.
/FTId=PRO_0000441917.
REGION 1 45 Sufficient for localization to the Golgi
apparatus. {ECO:0000269|PubMed:28534737}.
REGION 107 108 S-adenosyl-L-methionine binding.
{ECO:0000255|PROSITE-ProRule:PRU01019}.
BINDING 83 83 S-adenosyl-L-methionine; via amide
nitrogen. {ECO:0000255|PROSITE-
ProRule:PRU01019}.
BINDING 105 105 S-adenosyl-L-methionine.
{ECO:0000255|PROSITE-ProRule:PRU01019}.
BINDING 113 113 S-adenosyl-L-methionine.
{ECO:0000255|PROSITE-ProRule:PRU01019}.
BINDING 131 131 S-adenosyl-L-methionine.
{ECO:0000255|PROSITE-ProRule:PRU01019}.
BINDING 161 161 S-adenosyl-L-methionine; via amide
nitrogen. {ECO:0000255|PROSITE-
ProRule:PRU01019}.
SEQUENCE 259 AA; 29608 MW; EFED3342D025C6D4 CRC64;
MVSPAIALAF LPLLLTLIIR YRYYFVLLYR AVLTRWVRDC LSGISREERA FQYILTHATP
GDSQSILDTF DTWCSKVEFI SNIGPKKGKI LDRLLQENCP ITVLELGTHC GYSTVRMARS
LPIGARIYSV EMDQRNAQVA EKIIRLAGFD DDMVELIQRP SDEVIPRLRE DLGVERLDLV
LMDHWKRCYL PDLHLLEDSG LIGQGSIILA DNVIFPGAPN FLRYARRCGL YEVRVHRATL
EYMRGIPDGM AELTYIGIK


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