TMC1_DANRE
ID TMC1_DANRE Reviewed; 935 AA.
AC F1QFU0; A0A076V3V4; A2BFV3;
DT 25-OCT-2017, integrated into UniProtKB/Swiss-Prot.
DT 20-JAN-2016, sequence version 2.
DT 03-AUG-2022, entry version 64.
DE RecName: Full=Transmembrane channel-like protein 1 {ECO:0000303|PubMed:25114259};
GN Name=tmc1 {ECO:0000303|PubMed:25114259,
GN ECO:0000312|ZFIN:ZDB-GENE-060526-261};
GN ORFNames=si:229d2.1 {ECO:0000312|ZFIN:ZDB-GENE-060526-261};
OS Danio rerio (Zebrafish) (Brachydanio rerio).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Danionidae; Danioninae; Danio.
OX NCBI_TaxID=7955;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, INTERACTION WITH PCDH15A, TISSUE
RP SPECIFICITY, AND PHYLOGENETIC ANALYSIS.
RX PubMed=25114259; DOI=10.1073/pnas.1402152111;
RA Maeda R., Kindt K.S., Mo W., Morgan C.P., Erickson T., Zhao H.,
RA Clemens-Grisham R., Barr-Gillespie P.G., Nicolson T.;
RT "Tip-link protein protocadherin 15 interacts with transmembrane channel-
RT like proteins TMC1 and TMC2.";
RL Proc. Natl. Acad. Sci. U.S.A. 111:12907-12912(2014).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Tuebingen;
RX PubMed=23594743; DOI=10.1038/nature12111;
RA Howe K., Clark M.D., Torroja C.F., Torrance J., Berthelot C., Muffato M.,
RA Collins J.E., Humphray S., McLaren K., Matthews L., McLaren S., Sealy I.,
RA Caccamo M., Churcher C., Scott C., Barrett J.C., Koch R., Rauch G.J.,
RA White S., Chow W., Kilian B., Quintais L.T., Guerra-Assuncao J.A., Zhou Y.,
RA Gu Y., Yen J., Vogel J.H., Eyre T., Redmond S., Banerjee R., Chi J., Fu B.,
RA Langley E., Maguire S.F., Laird G.K., Lloyd D., Kenyon E., Donaldson S.,
RA Sehra H., Almeida-King J., Loveland J., Trevanion S., Jones M., Quail M.,
RA Willey D., Hunt A., Burton J., Sims S., McLay K., Plumb B., Davis J.,
RA Clee C., Oliver K., Clark R., Riddle C., Elliot D., Threadgold G.,
RA Harden G., Ware D., Begum S., Mortimore B., Kerry G., Heath P.,
RA Phillimore B., Tracey A., Corby N., Dunn M., Johnson C., Wood J., Clark S.,
RA Pelan S., Griffiths G., Smith M., Glithero R., Howden P., Barker N.,
RA Lloyd C., Stevens C., Harley J., Holt K., Panagiotidis G., Lovell J.,
RA Beasley H., Henderson C., Gordon D., Auger K., Wright D., Collins J.,
RA Raisen C., Dyer L., Leung K., Robertson L., Ambridge K., Leongamornlert D.,
RA McGuire S., Gilderthorp R., Griffiths C., Manthravadi D., Nichol S.,
RA Barker G., Whitehead S., Kay M., Brown J., Murnane C., Gray E.,
RA Humphries M., Sycamore N., Barker D., Saunders D., Wallis J., Babbage A.,
RA Hammond S., Mashreghi-Mohammadi M., Barr L., Martin S., Wray P.,
RA Ellington A., Matthews N., Ellwood M., Woodmansey R., Clark G., Cooper J.,
RA Tromans A., Grafham D., Skuce C., Pandian R., Andrews R., Harrison E.,
RA Kimberley A., Garnett J., Fosker N., Hall R., Garner P., Kelly D., Bird C.,
RA Palmer S., Gehring I., Berger A., Dooley C.M., Ersan-Urun Z., Eser C.,
RA Geiger H., Geisler M., Karotki L., Kirn A., Konantz J., Konantz M.,
RA Oberlander M., Rudolph-Geiger S., Teucke M., Lanz C., Raddatz G.,
RA Osoegawa K., Zhu B., Rapp A., Widaa S., Langford C., Yang F.,
RA Schuster S.C., Carter N.P., Harrow J., Ning Z., Herrero J., Searle S.M.,
RA Enright A., Geisler R., Plasterk R.H., Lee C., Westerfield M.,
RA de Jong P.J., Zon L.I., Postlethwait J.H., Nusslein-Volhard C.,
RA Hubbard T.J., Roest Crollius H., Rogers J., Stemple D.L.;
RT "The zebrafish reference genome sequence and its relationship to the human
RT genome.";
RL Nature 496:498-503(2013).
RN [3]
RP SUBCELLULAR LOCATION.
RX PubMed=28534737; DOI=10.7554/elife.28474;
RA Erickson T., Morgan C.P., Olt J., Hardy K., Busch-Nentwich E., Maeda R.,
RA Clemens R., Krey J.F., Nechiporuk A., Barr-Gillespie P.G., Marcotti W.,
RA Nicolson T.;
RT "Integration of Tmc1/2 into the mechanotransduction complex in zebrafish
RT hair cells is regulated by Transmembrane O-methyltransferase (Tomt).";
RL Elife 6:0-0(2017).
CC -!- FUNCTION: Probable ion channel required for the normal function of hair
CC cells (By similarity). Component of the hair cell's mechanotransduction
CC (MET) machinery (PubMed:25114259). {ECO:0000250|UniProtKB:Q8R4P5,
CC ECO:0000269|PubMed:25114259}.
CC -!- SUBUNIT: Interacts specifically with isoform CD3 of PCDH15A (via
CC cytoplasmic domain). {ECO:0000269|PubMed:25114259}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q8R4P5};
CC Multi-pass membrane protein {ECO:0000255|RuleBase:RU310713}.
CC Note=Localized to the hair bundles of the hair cells.
CC {ECO:0000269|PubMed:28534737}.
CC -!- TISSUE SPECIFICITY: In adults, expression is restricted to the hair
CC cells of inner ear and lateral line organ. Expressed at higher levels
CC in the larval lateral-line neuromasts than in the larval inner ear.
CC Expressed in the sensory hair cell patches of the ear at 4 days post
CC fertilization (dpf). {ECO:0000269|PubMed:25114259}.
CC -!- SIMILARITY: Belongs to the TMC family. {ECO:0000255|RuleBase:RU310713}.
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DR EMBL; KM115406; AIK19895.1; -; mRNA.
DR EMBL; BX296526; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; F1QFU0; -.
DR SMR; F1QFU0; -.
DR STRING; 7955.ENSDARP00000121310; -.
DR TCDB; 1.A.17.4.13; the calcium-dependent chloride channel (ca-clc) family.
DR PaxDb; F1QFU0; -.
DR ZFIN; ZDB-GENE-060526-261; tmc1.
DR eggNOG; ENOG502QQGX; Eukaryota.
DR HOGENOM; CLU_013958_2_1_1; -.
DR TreeFam; TF313462; -.
DR PRO; PR:F1QFU0; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; Unplaced.
DR GO; GO:0005887; C:integral component of plasma membrane; IEA:InterPro.
DR GO; GO:0032421; C:stereocilium bundle; IDA:UniProtKB.
DR GO; GO:0008381; F:mechanosensitive ion channel activity; IBA:GO_Central.
DR GO; GO:0050910; P:detection of mechanical stimulus involved in sensory perception of sound; ISS:UniProtKB.
DR GO; GO:0060005; P:vestibular reflex; IBA:GO_Central.
DR InterPro; IPR038900; TMC.
DR InterPro; IPR012496; TMC_dom.
DR PANTHER; PTHR23302; PTHR23302; 1.
DR Pfam; PF07810; TMC; 1.
PE 1: Evidence at protein level;
KW Cell membrane; Coiled coil; Ion channel; Ion transport; Membrane;
KW Reference proteome; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..935
FT /note="Transmembrane channel-like protein 1"
FT /id="PRO_0000441914"
FT TRANSMEM 317..337
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 360..380
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 393..413
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 486..506
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 531..551
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 566..586
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 694..714
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 755..775
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 813..833
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 1..21
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 37..204
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 874..935
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 37..78
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 79..96
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 97..159
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 169..188
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 886..928
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 935 AA; 107497 MW; 0D59876F78B258D7 CRC64;
MPRHKLIASE SDVSIEVDEG KDKESCVYYV EVEENCERGK IKQASRDGKR RRERNGETRR
KASEKRTNEG ESKKAEKKHE KGHRTARKAG EKHGKRQRRK NAGEEDAEDK SSKEKKNMKN
EKNKTLKLEE EKEKDVRKKK RKHVKNEEDE TNHEKTKQHL KEEKRRKKRK KPETTSESES
KSESESASES ESKNSPAVGV LGSLTPEELE NLKEAVEERK KLITQLKGKP WPMRRKLVVL
RESQEFVEKY EGALGKGKGR KLYAYKVMMM KKWMKFQRDF ENFKTACIPW EMKIKEIESH
FGSSVASYFI FLRWMYGINM ILFGLTFGLV MVPEALMGKP YGSLPRKTVP REEEASAMNF
AVLWDFGGYA KYSVLFYGYY NSQRAIGWLK FRMPLSYFLV GVGTVAYSYM VVIRTMARNA
NEEGGGDDTS FNFSWKTFTS WDYLIGNPET ADNKFASITT SFKEAIVEEQ ESRKDDNIHL
TRFLRVLANF LVLCCLAGSG YLIYFVVRRS QKFALEGLEN YGWWERNEVN MVMSLLGMFC
PMLFDVISTL ENYHPRIALQ WQLGRIFALF LGNLYTFIIA LMDAIQLKRA EEEIVKKNMT
IWQANLYNGT VPDNSTAPPL TVHPADVPRG PCWETMVGQE FVRLIISDTM TTYITLLIGD
FMRAVLVRFL NNCWCWDLEY GFPSYSEFDV SGNVLGLIFN QGMIWMGAFY APCLPALNLL
RLHVSMYLQC WAVMCCNVPQ ERVFKASGSN NFYMAMLLVI LFLSTLPAIY TIVSIPPSFD
CGPFSGKPRM FDVIQETLET DFPAWFSKVF SYASNPGLVL PFLLLLVLAI YYLQSTSKTY
KRVNMELKKK LQAQNEENKK KNKLAALKAA SDLEQARKAG EQRRNSISDL GVNEENPESH
VSSSHTSRPP ASRGHTSSGH LPGHPQQPQK NSKKR
