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   08-NOV-2023, entry version 129.
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   BioGRID; 229898; 1.
DR   STRING; 10090.ENSMUSP00000026659; -.
DR   GlyCosmos; Q7TN60; 2 sites, No reported glycans.
DR   GlyGen; Q7TN60; 2 sites.
DR   iPTMnet; Q7TN60; -.
DR   PhosphoSitePlus; Q7TN60; -.
DR   EPD; Q7TN60; -.
DR   MaxQB; Q7TN60; -.
DR   PaxDb; 10090-ENSMUSP00000026659; -.
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   AGR; MGI:1098686; -.
DR   CTD; 11322; -.
DR   MGI; MGI:1098686; Tmc6.
DR   eggNOG; KOG1039; Eukaryota.
DR   InParanoid; Q7TN60; -.
DR   OrthoDB; 4121853at2759; -.
DR   PhylomeDB; Q7TN60; -.
DR   Reactome; R-MMU-6798695; Neutrophil degranulation.
DR   BioGRID-ORCS; 217353; 4 hits in 79 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:0031965; C:nuclear membrane; ISO:MGI.
DR   GO; GO:0005886; C:plasma membrane; IEA:InterPro.
DR   GO; GO:0008381; F:mechanosensitive monoatomic ion channel activity; IBA:GO_Central.
DR   InterPro; IPR038900; TMC.
DR   InterPro; IPR012496; TMC_dom.
DR   PANTHER; PTHR23302:SF4; TRANSMEMBRANE CHANNEL-LIKE PROTEIN 6; 1.
DR   PANTHER; PTHR23302; TRANSMEMBRANE CHANNEL-RELATED; 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
//