TMC6_MOUSE
ID TMC6_MOUSE Reviewed; 810 AA.
AC Q7TN60; B1ATB4; Q78JR7; Q7TQ68; Q8BP52; Q8C6Z5; Q99J32;
DT 06-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 06-DEC-2005, sequence version 2.
DT 03-AUG-2022, entry version 124.
DE RecName: Full=Transmembrane channel-like protein 6;
GN Name=Tmc6;
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), AND TISSUE SPECIFICITY.
RX PubMed=12906855; DOI=10.1016/s0888-7543(03)00154-x;
RA Kurima K., Yang Y., Sorber K., Griffith A.J.;
RT "Characterization of the transmembrane channel-like (TMC) gene family:
RT functional clues from hearing loss and epidermodysplasia verruciformis.";
RL Genomics 82:300-308(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND TISSUE SPECIFICITY.
RC STRAIN=C57BL/6J;
RX PubMed=12812529; DOI=10.1186/1471-2164-4-24;
RA Keresztes G., Mutai H., Heller S.;
RT "TMC and EVER genes belong to a larger novel family, the TMC gene family
RT encoding transmembrane proteins.";
RL BMC Genomics 4:24-24(2003).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 4).
RC STRAIN=C57BL/6J; TISSUE=Mammary gland;
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 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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3).
RC STRAIN=129, and FVB/N; TISSUE=Kidney, and Mammary gland;
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 [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-136, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Spleen;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [7]
RP METHYLATION [LARGE SCALE ANALYSIS] AT ARG-93, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, and Embryo;
RX PubMed=24129315; DOI=10.1074/mcp.o113.027870;
RA Guo A., Gu H., Zhou J., Mulhern D., Wang Y., Lee K.A., Yang V., Aguiar M.,
RA Kornhauser J., Jia X., Ren J., Beausoleil S.A., Silva J.C., Vemulapalli V.,
RA Bedford M.T., Comb M.J.;
RT "Immunoaffinity enrichment and mass spectrometry analysis of protein
RT methylation.";
RL Mol. Cell. Proteomics 13:372-387(2014).
CC -!- FUNCTION: Probable ion channel. {ECO:0000250}.
CC -!- SUBUNIT: Interacts with CIB1. {ECO:0000250|UniProtKB:Q7Z403}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250};
CC Multi-pass membrane protein {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1;
CC IsoId=Q7TN60-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q7TN60-2; Sequence=VSP_016444, VSP_016447;
CC Name=3;
CC IsoId=Q7TN60-3; Sequence=VSP_016443;
CC Name=4;
CC IsoId=Q7TN60-4; Sequence=VSP_016445, VSP_016446;
CC -!- TISSUE SPECIFICITY: Widely expressed. {ECO:0000269|PubMed:12812529,
CC ECO:0000269|PubMed:12906855}.
CC -!- SIMILARITY: Belongs to the TMC family. {ECO:0000305}.
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DR EMBL; AY236497; AAP69875.1; -; mRNA.
DR EMBL; AY263158; AAP78773.1; -; mRNA.
DR EMBL; AK052814; BAC35157.1; -; mRNA.
DR EMBL; AK077671; BAC36945.1; -; mRNA.
DR EMBL; AL645856; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC004840; AAH04840.2; -; mRNA.
DR EMBL; BC013502; AAH13502.1; -; mRNA.
DR EMBL; BC058195; AAH58195.1; -; mRNA.
DR CCDS; CCDS25687.1; -. [Q7TN60-1]
DR RefSeq; NP_663414.3; NM_145439.2.
DR RefSeq; NP_851838.1; NM_181321.3.
DR AlphaFoldDB; Q7TN60; -.
DR SMR; Q7TN60; -.
DR STRING; 10090.ENSMUSP00000026659; -.
DR GlyGen; Q7TN60; 2 sites.
DR iPTMnet; Q7TN60; -.
DR PhosphoSitePlus; Q7TN60; -.
DR EPD; Q7TN60; -.
DR MaxQB; Q7TN60; -.
DR PaxDb; Q7TN60; -.
DR PRIDE; Q7TN60; -.
DR ProteomicsDB; 259242; -. [Q7TN60-1]
DR ProteomicsDB; 259243; -. [Q7TN60-2]
DR ProteomicsDB; 259244; -. [Q7TN60-3]
DR ProteomicsDB; 259245; -. [Q7TN60-4]
DR DNASU; 217353; -.
DR GeneID; 217353; -.
DR KEGG; mmu:217353; -.
DR UCSC; uc007mnn.2; mouse. [Q7TN60-2]
DR UCSC; uc007mnr.2; mouse. [Q7TN60-4]
DR CTD; 11322; -.
DR MGI; MGI:1098686; Tmc6.
DR eggNOG; KOG1039; Eukaryota.
DR InParanoid; Q7TN60; -.
DR OrthoDB; 1048914at2759; -.
DR PhylomeDB; Q7TN60; -.
DR Reactome; R-MMU-6798695; Neutrophil degranulation.
DR BioGRID-ORCS; 217353; 4 hits in 74 CRISPR screens.
DR ChiTaRS; Tmc6; mouse.
DR PRO; PR:Q7TN60; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; Q7TN60; protein.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0005783; C:endoplasmic reticulum; ISO:MGI.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005794; C:Golgi apparatus; ISO:MGI.
DR GO; GO:0005887; C:integral component of plasma membrane; IEA:InterPro.
DR GO; GO:0031965; C:nuclear membrane; ISO:MGI.
DR GO; GO:0008381; F:mechanosensitive ion channel activity; 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 Alternative splicing; Endoplasmic reticulum; Glycoprotein; Ion channel;
KW Ion transport; Membrane; Methylation; Phosphoprotein; Reference proteome;
KW Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..810
FT /note="Transmembrane channel-like protein 6"
FT /id="PRO_0000185385"
FT TOPO_DOM 1..205
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 206..226
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 227..253
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 254..274
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 275..338
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 339..359
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 360..429
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 430..450
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 451..468
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 469..489
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 490..504
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 505..525
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 526..552
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 553..573
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 574..603
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 604..624
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 625..649
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 650..670
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 671..721
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 722..742
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 743..810
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT REGION 1..26
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 775..810
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 775..803
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 88
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q7Z403"
FT MOD_RES 93
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 104
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q7Z403"
FT MOD_RES 136
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT CARBOHYD 102
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 311
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT VAR_SEQ 1..360
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_016443"
FT VAR_SEQ 1..260
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_016444"
FT VAR_SEQ 297..328
FT /note="GRFTHTVMYYGYYSNSTLSPSCDAPREGGQCS -> VRPSAPALAKNWCQAC
FT PDSPGGLLPVPRYLYG (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_016445"
FT VAR_SEQ 329..810
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_016446"
FT VAR_SEQ 781..810
FT /note="RPGRTQDATEPPAWHEDGGDQKEPCNPRSP -> SKLGLVPSGHVCRSPAAA
FT VRAPHIETDVLKLKA (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_016447"
FT CONFLICT 2
FT /note="A -> T (in Ref. 1; AAP69875)"
FT /evidence="ECO:0000305"
FT CONFLICT 338
FT /note="M -> T (in Ref. 1; AAP69875)"
FT /evidence="ECO:0000305"
FT CONFLICT 365
FT /note="F -> L (in Ref. 3; BAC36945)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 810 AA; 90546 MW; 6A78987C46CD4FD5 CRC64;
MAQSLALALD VPETTGDEGL EPSPYEESEV HDSFHQLIQE QSLRVAEEGL ELLPLGLGRG
DQTLPGLEGA PALSSATLRI LASMPSRTIG RSRGAIISQY YNRTVRLRRR SSRPLLGNVV
PSARPSLRLY DLELDSTILE EDEKRSLLVK ELQGLSAAQR DHMVRNMPLS LGEKRCLREK
SWSPKGKRRH LQGRSGAFSC CSRLRYTCML ALHSLGLALL SGLYAARPWR YALKQIGGQF
GSSVLSYFLF LKTLLAFNAL MLLPLLAFLV GVQAAFPPDP AGPVPTFSGL ELLTGGGRFT
HTVMYYGYYS NSTLSPSCDA PREGGQCSPR LGSLPYNMPL AYLFTMGATF FLTCIILVYS
MSHSFGESYR VGSTKGIHAL TVFCSWDYKV TQKRASRVQQ DSICTQLKEL LAEWHLRKRP
RSVCGQLRQV VVLGLGWLLC LGSTMGCTVA VLTFSEVMIQ RPASGGQGVE ALALPLVVSV
LNLGASYLFR GLATLERHDS PVLEVYMAIC RNLILKMAVL GVLCYHWLGR RVATLQGQCW
EDFVGQELYR FMVVDFIFML LDSLFGELVW RLISEKKLKR GQKPEFDIAR NVLDLIYGQT
LTWLGVLFSP LLPAVQILRL LFLFHIKKAS LMANCQAPRR PWLASHMSTV FLTLLCFPSF
LGAAVFLCYA VWQVRPSSTC GPFRTLNTMY EAGTVWVRRL EHAGSGASWL PWLHHFLVEN
TFFLFLASAL LLAVIYFNIQ VVKGQRKVIC LLKEQIRNEG EDKIFLINKL HSVYEEEGRS
RPGRTQDATE PPAWHEDGGD QKEPCNPRSP
