TMC8_MOUSE
ID TMC8_MOUSE Reviewed; 722 AA.
AC Q7TN58; Q3TAL0; Q3UWI0; Q7TQ67;
DT 06-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 06-DEC-2005, sequence version 2.
DT 03-AUG-2022, entry version 120.
DE RecName: Full=Transmembrane channel-like protein 8;
DE AltName: Full=Epidermodysplasia verruciformis protein 2 homolog;
GN Name=Tmc8; Synonyms=Ever2;
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] (ISOFORM 2), AND NUCLEOTIDE SEQUENCE
RP [LARGE SCALE MRNA] OF 457-722.
RC STRAIN=C57BL/6J; TISSUE=Testis;
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 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT "Large-scale phosphorylation analysis of mouse liver.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-6; SER-18; SER-658; SER-663;
RP SER-673 AND SER-698, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP ANALYSIS].
RC TISSUE=Kidney, Lung, and 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).
CC -!- FUNCTION: Probable ion channel. {ECO:0000250}.
CC -!- SUBUNIT: Interacts with CIB1. {ECO:0000250|UniProtKB:Q8IU68}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250};
CC Multi-pass membrane protein {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q7TN58-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q7TN58-2; Sequence=VSP_016451;
CC -!- TISSUE SPECIFICITY: Expressed in thymus, lung, prostate, placenta,
CC testis and spleen. {ECO:0000269|PubMed:12812529,
CC ECO:0000269|PubMed:12906855}.
CC -!- SIMILARITY: Belongs to the TMC family. {ECO:0000305}.
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DR EMBL; AY236501; AAP69879.1; -; mRNA.
DR EMBL; AY263160; AAP78775.1; -; mRNA.
DR EMBL; AK136329; BAE22935.1; -; mRNA.
DR EMBL; AK171772; BAE42658.1; -; mRNA.
DR CCDS; CCDS25689.1; -. [Q7TN58-1]
DR CCDS; CCDS56824.1; -. [Q7TN58-2]
DR RefSeq; NP_001182019.1; NM_001195090.1.
DR RefSeq; NP_862904.1; NM_181856.2. [Q7TN58-1]
DR RefSeq; XP_006533187.1; XM_006533124.3. [Q7TN58-1]
DR AlphaFoldDB; Q7TN58; -.
DR STRING; 10090.ENSMUSP00000101941; -.
DR TCDB; 1.A.17.4.2; the calcium-dependent chloride channel (ca-clc) family.
DR GlyGen; Q7TN58; 3 sites.
DR iPTMnet; Q7TN58; -.
DR PhosphoSitePlus; Q7TN58; -.
DR EPD; Q7TN58; -.
DR jPOST; Q7TN58; -.
DR MaxQB; Q7TN58; -.
DR PaxDb; Q7TN58; -.
DR PRIDE; Q7TN58; -.
DR ProteomicsDB; 259248; -. [Q7TN58-1]
DR ProteomicsDB; 259249; -. [Q7TN58-2]
DR Antibodypedia; 32534; 198 antibodies from 28 providers.
DR DNASU; 217356; -.
DR Ensembl; ENSMUST00000050874; ENSMUSP00000051878; ENSMUSG00000050106. [Q7TN58-1]
DR Ensembl; ENSMUST00000106334; ENSMUSP00000101941; ENSMUSG00000050106. [Q7TN58-2]
DR Ensembl; ENSMUST00000119455; ENSMUSP00000113628; ENSMUSG00000050106. [Q7TN58-2]
DR GeneID; 217356; -.
DR KEGG; mmu:217356; -.
DR UCSC; uc007mns.2; mouse. [Q7TN58-1]
DR CTD; 147138; -.
DR MGI; MGI:2669037; Tmc8.
DR VEuPathDB; HostDB:ENSMUSG00000050106; -.
DR eggNOG; ENOG502RKT7; Eukaryota.
DR GeneTree; ENSGT01050000244894; -.
DR HOGENOM; CLU_013958_3_1_1; -.
DR InParanoid; Q7TN58; -.
DR OMA; TNTYLFY; -.
DR OrthoDB; 1048914at2759; -.
DR TreeFam; TF313462; -.
DR BioGRID-ORCS; 217356; 6 hits in 74 CRISPR screens.
DR ChiTaRS; Tmc8; mouse.
DR PRO; PR:Q7TN58; -.
DR Proteomes; UP000000589; Chromosome 11.
DR RNAct; Q7TN58; protein.
DR Bgee; ENSMUSG00000050106; Expressed in granulocyte and 61 other tissues.
DR ExpressionAtlas; Q7TN58; baseline and differential.
DR Genevisible; Q7TN58; MM.
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 GO; GO:0140311; F:protein sequestering activity; ISO:MGI.
DR GO; GO:0043120; F:tumor necrosis factor binding; ISO:MGI.
DR GO; GO:0032091; P:negative regulation of protein binding; ISO:MGI.
DR GO; GO:0031333; P:negative regulation of protein-containing complex assembly; ISO:MGI.
DR GO; GO:0001558; P:regulation of cell growth; ISO:MGI.
DR GO; GO:1902041; P:regulation of extrinsic apoptotic signaling pathway via death domain receptors; ISO:MGI.
DR GO; GO:0055069; P:zinc ion homeostasis; ISO:MGI.
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; Phosphoprotein; Reference proteome; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..722
FT /note="Transmembrane channel-like protein 8"
FT /id="PRO_0000185387"
FT TOPO_DOM 1..118
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 119..139
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 140..204
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 205..225
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 226..307
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 308..328
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 329..375
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 376..396
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 397..430
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 431..451
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 452..492
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 493..513
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 514..536
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 537..557
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 558..598
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 599..619
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 620..722
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 1..21
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 658..722
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..15
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 692..707
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 6
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 18
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 658
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 663
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 673
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 698
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT CARBOHYD 184
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 375
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 571
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT VAR_SEQ 154
FT /note="R -> TG (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_016451"
FT CONFLICT 179
FT /note="T -> A (in Ref. 3; BAE42658)"
FT /evidence="ECO:0000305"
FT CONFLICT 277..278
FT /note="ME -> VC (in Ref. 1; AAP69879)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 722 AA; 82329 MW; 33799843E88B6FD9 CRC64;
MFRQWSVQSG PAPRRPESQA ASEELWEQEV ERLCASRTPV RMLPYAMADK RFIRELREPE
GVKTTFWQRW HRPRRVARQH LREAEQRLAR GFGLWEGALY EIGGLFGTGI QSYFTFLRFL
LLLNLLTMLL TACFVLLPLV WLRPPELGPA LKLRLQCSSS PLPQSDIPRF HNPLWNILTG
RAFNNTYLFY GAYRAGPESS SEYSIRLAYL LSPMVCLLLC FCGILQRMAE GLPQQTLLGQ
RYRTPLSAKV FSSWDFCIRV WEAATIKKHE ISNELKMELE EGRRVELAQQ QTRAQKACRL
LTYLRTNILI VLLVVGAISA IFWATKYSQD NKEESLFLVL QYLPPGVISL VNFLGPQLFT
VLIQLENYPP GTEVNLTLIW CVVLKLASLG MFSFSLGQTV LCIGRNKTSC ESYGYNACDY
QCWENSVGEE LYKLIIFNFL LTVAFAFLVS LPRRLLVERF SGWFWTWLDR EEFLVPKNVL
DIVAAQTVTW MGLFYCPLLP LLNSVFLFLT FYIKKYTLLR NSRASPRRFR ASSSTFFFHL
VLLLGLLLAA VPLAYVISST HSSWDCGLFT NYSAPWQVVP ELVALQLPLP SQRALRYLSS
HAFSFPLLIL LSIVLTVCIS QSRANARAIQ GLRKQLVWQV QEKWHLVDDL SRLLPELSPE
PGSPHSRASR PRSFCPGFPC PGSPGPRTPR LAPSNRLSSS SLGAPSASVP ASRFHFPSRT
EL
