TMC2B_DANRE
ID TMC2B_DANRE Reviewed; 892 AA.
AC F1QZE9; A0A076V6D3; F1QW55;
DT 25-OCT-2017, integrated into UniProtKB/Swiss-Prot.
DT 20-JAN-2016, sequence version 2.
DT 03-AUG-2022, entry version 68.
DE RecName: Full=Transmembrane channel-like protein 2-B {ECO:0000303|PubMed:25114259};
GN Name=tmc2b {ECO:0000303|PubMed:25114259}; Synonyms=si:229d2.2;
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], TISSUE 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 -!- SUBCELLULAR LOCATION: Membrane {ECO:0000255|RuleBase:RU310713}; Multi-
CC pass membrane protein {ECO:0000255|RuleBase:RU310713}. Note=Localized
CC to the hair bundles of the hair cells. {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 {ECO:0000269|PubMed:25114259}.
CC -!- SIMILARITY: Belongs to the TMC family. {ECO:0000255|RuleBase:RU310713}.
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DR EMBL; BX296526; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; KM115408; AIK19897.1; -; mRNA.
DR RefSeq; NP_001289152.1; NM_001302223.1.
DR AlphaFoldDB; F1QZE9; -.
DR SMR; F1QZE9; -.
DR STRING; 7955.ENSDARP00000044470; -.
DR TCDB; 1.A.17.4.13; the calcium-dependent chloride channel (ca-clc) family.
DR PaxDb; F1QZE9; -.
DR GeneID; 567304; -.
DR KEGG; dre:567304; -.
DR CTD; 567304; -.
DR ZFIN; ZDB-GENE-060526-262; tmc2b.
DR eggNOG; ENOG502QVCF; Eukaryota.
DR InParanoid; F1QZE9; -.
DR OrthoDB; 310839at2759; -.
DR TreeFam; TF313462; -.
DR PRO; PR:F1QZE9; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; Unplaced.
DR GO; GO:0005887; C:integral component of plasma membrane; IEA:InterPro.
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; IMP:ZFIN.
DR GO; GO:0048839; P:inner ear development; IEP:UniProtKB.
DR GO; GO:0042472; P:inner ear morphogenesis; IEP:UniProtKB.
DR GO; GO:0048884; P:neuromast development; IEP: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 2: Evidence at transcript level;
KW Membrane; Reference proteome; Transmembrane; Transmembrane helix.
FT CHAIN 1..892
FT /note="Transmembrane channel-like protein 2-B"
FT /id="PRO_0000441916"
FT TRANSMEM 235..255
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 275..295
FT /note="Helical"
FT /evidence="ECO:0000255|RuleBase:RU310713"
FT TRANSMEM 308..328
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 403..423
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 444..464
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 482..502
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 616..636
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 671..691
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 736..756
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 29..125
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 772..791
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 796..892
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 75..98
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 99..115
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 858..876
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 747
FT /note="Missing (in Ref. 2; BX296526)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 892 AA; 102045 MW; 6E8EDD4E8BCBEF99 CRC64;
MCVLQLGWKW MQNLIVEVMW TQKEEQKAGI NQNLRREEGK PNQQTVWRRA KKRRMNRRAR
GEAGGRSKKM RMRVRKNRRE EERKLSIPGR EQQRKTSQRR RSPSSCSSSS DNNSDDESMS
EGEMARLKEE VEEKKKLIAT LRNKPWRMKR RLKCLKEAQE FVEKFEGALG KGKGRRLYAF
KVMMTKKLIK FNRDFENFKT ACIPWESRIK EVESHFGSSV ASYFIFLRWM YGLNLVLFGF
MFGLVVIPEL LMGIPYGSIP RKTVPREEQD SAMDFSVLFE FGGYCKYSIL FYGFYNNQRT
IGFLQFRLPL SYLLVGVGIF GYSLMVVIRT MARNANEGGD GGDEGNFTFC WKLFTSWDYL
IGNPETADNK FASTTTSFKE SIVDEQENLK DENIHLRRFL RLLANVLILC CLAGSGYLIY
AVVKRSQDFA KRDRNELTWL QKNEVEIVMS LLGLVCPPLF EAIAELEDYH PRIALKWQLG
RIFALFLGNL YTFLFALFDE VNGKLENEKQ IKNQTVWALK EYYANYTLQY NITENIPPPN
IAPADVIRGP CWETEVGIEF VKLTVSDIQV TYLTILIGDF LRALIVRFLN YCWCWDLEAG
FPSYAEFDIS GNVLGLIFNQ GMIWMGAFYA PGLVGINVLR LLSSMYYQCW AVMACNVPHE
RVFKASRSNN FYMGLLLLVL FLSLMPVIYS IMTLPPSFDC GPFSGKDKMY DVITETIDKD
LPPFMADIFS YASNPGLIIS VVLLMVWLAI YYLNAVSKAY QNSNLELKRK MQMQRDEEKN
RRNNKDSTNQ VMKDLEDLLP NKSLIPPPSV EETEKPAEQP SKSSKVTGKP GAAASGKGVH
VQKDVSLAAA NPRAPVTRAP GPRQPGPLPG NPRGPPPGQG MGRGRGGPPP RR
