T150C_MOUSE
ID T150C_MOUSE Reviewed; 249 AA.
AC Q8C8S3; D3YVG3; Q3TL78; Q8K117;
DT 15-JUN-2010, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 121.
DE RecName: Full=Transmembrane protein 150C;
DE AltName: Full=Tentonin 3 {ECO:0000303|PubMed:27321926};
GN Name=Tmem150c; Synonyms=Ttn3 {ECO:0000303|PubMed:27321926};
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 [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC STRAIN=C57BL/6J; TISSUE=Retina;
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 [2]
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=C57BL/6J; TISSUE=Brain, and Eye;
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 [5]
RP SUBCELLULAR LOCATION, FUNCTION, TISSUE SPECIFICITY, AND DISRUPTION
RP PHENOTYPE.
RX PubMed=27321926; DOI=10.1016/j.neuron.2016.05.029;
RA Hong G.S., Lee B., Wee J., Chun H., Kim H., Jung J., Cha J.Y., Riew T.R.,
RA Kim G.H., Kim I.B., Oh U.;
RT "Tentonin 3/TMEM150c confers distinct mechanosensitive currents in dorsal-
RT root ganglion neurons with proprioceptive function.";
RL Neuron 91:107-118(2016).
RN [6]
RP FUNCTION.
RX PubMed=28426961; DOI=10.1016/j.neuron.2017.03.039;
RA Dubin A.E., Murthy S., Lewis A.H., Brosse L., Cahalan S.M., Grandl J.,
RA Coste B., Patapoutian A.;
RT "Endogenous piezo1 can confound mechanically activated channel
RT identification and characterization.";
RL Neuron 94:266-270(2017).
RN [7]
RP FUNCTION, AND MUTAGENESIS OF GLY-48; ALA-49; LYS-50 AND HIS-51.
RX PubMed=28426962; DOI=10.1016/j.neuron.2017.03.038;
RA Hong G.S., Lee B., Oh U.;
RT "Evidence for mechanosensitive channel activity of tentonin 3/TMEM150C.";
RL Neuron 94:271-273(2017).
CC -!- FUNCTION: Component of a mechanosensitive cation channel. Confers
CC mechanically activated (MA) currents with slow inactivation kinetics.
CC May contribute to proprioception (PubMed:27321926).
CC {ECO:0000269|PubMed:27321926}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:27321926};
CC Multi-pass membrane protein {ECO:0000250|UniProtKB:B9EJG8}. Lysosome
CC membrane {ECO:0000250|UniProtKB:B9EJG8}; Multi-pass membrane protein
CC {ECO:0000250|UniProtKB:B9EJG8}. Note=Localizes at the plasma membrane.
CC A portion co-localizes with LAMP1 lysosomal marker.
CC {ECO:0000250|UniProtKB:B9EJG8}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q8C8S3-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8C8S3-2; Sequence=VSP_039351;
CC -!- TISSUE SPECIFICITY: High expression in the epididymis, pancreas,
CC dorsal-root ganglion, eye, brain, and spinal cord. Expressed in muscle
CC spindle afferents (at protein level)(PubMed:27321926).
CC {ECO:0000269|PubMed:27321926}.
CC -!- DISRUPTION PHENOTYPE: Deficient mice exhibit loss of coordinated
CC movements and abnormal gait. {ECO:0000269|PubMed:27321926}.
CC -!- MISCELLANEOUS: Tentonin comes from the Greek 'tentono' meaning to
CC stretch.
CC -!- SIMILARITY: Belongs to the DRAM/TMEM150 family. {ECO:0000305}.
CC -!- CAUTION: The function of the TMEM150C complex is debated. One study
CC confirms that naive cells expressing TMEM150C is activated by
CC mechanically stimuli but this response is absent in CRISPR-Cas9 PIEZO1
CC knockout cell lines suggesting that TMEM150C is not sufficient to
CC function as mechanically activated channels but is a modulatory protein
CC of PIEZO1 (PubMed:28426961). In another study, based on coexpression of
CC TMEM150C and PEIZO1 and mutant variants of TMEM150C supports that
CC TMEM150C is a pore-forming unit, and not an amplifying adapter for
CC PIEZO1 activity (PubMed:28426962). {ECO:0000269|PubMed:28426961,
CC ECO:0000269|PubMed:28426962}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAE38914.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AK044570; BAC31985.1; -; mRNA.
DR EMBL; AK166646; BAE38914.1; ALT_INIT; mRNA.
DR EMBL; AC124480; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC125378; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH466529; EDL20303.1; -; Genomic_DNA.
DR EMBL; BC028943; AAH28943.1; -; mRNA.
DR EMBL; BC055321; AAH55321.1; -; mRNA.
DR CCDS; CCDS19461.1; -. [Q8C8S3-1]
DR RefSeq; NP_878261.1; NM_182841.1. [Q8C8S3-1]
DR RefSeq; XP_006534940.1; XM_006534877.3. [Q8C8S3-1]
DR RefSeq; XP_006534941.1; XM_006534878.1.
DR RefSeq; XP_006534944.1; XM_006534881.3. [Q8C8S3-2]
DR RefSeq; XP_011247728.1; XM_011249426.2.
DR AlphaFoldDB; Q8C8S3; -.
DR STRING; 10090.ENSMUSP00000057116; -.
DR PhosphoSitePlus; Q8C8S3; -.
DR MaxQB; Q8C8S3; -.
DR PaxDb; Q8C8S3; -.
DR PRIDE; Q8C8S3; -.
DR ProteomicsDB; 263215; -. [Q8C8S3-1]
DR ProteomicsDB; 263216; -. [Q8C8S3-2]
DR Antibodypedia; 58904; 15 antibodies from 8 providers.
DR DNASU; 231503; -.
DR Ensembl; ENSMUST00000063192; ENSMUSP00000057116; ENSMUSG00000050640. [Q8C8S3-1]
DR GeneID; 231503; -.
DR KEGG; mmu:231503; -.
DR UCSC; uc008yhc.1; mouse. [Q8C8S3-1]
DR UCSC; uc008yhf.1; mouse. [Q8C8S3-2]
DR CTD; 441027; -.
DR MGI; MGI:3041258; Tmem150c.
DR VEuPathDB; HostDB:ENSMUSG00000050640; -.
DR eggNOG; KOG4320; Eukaryota.
DR GeneTree; ENSGT01030000234578; -.
DR HOGENOM; CLU_059992_0_1_1; -.
DR InParanoid; Q8C8S3; -.
DR OMA; ILMAQDI; -.
DR OrthoDB; 1199230at2759; -.
DR PhylomeDB; Q8C8S3; -.
DR TreeFam; TF314508; -.
DR BioGRID-ORCS; 231503; 2 hits in 72 CRISPR screens.
DR ChiTaRS; Tmem150c; mouse.
DR PRO; PR:Q8C8S3; -.
DR Proteomes; UP000000589; Chromosome 5.
DR RNAct; Q8C8S3; protein.
DR Bgee; ENSMUSG00000050640; Expressed in retinal neural layer and 155 other tissues.
DR ExpressionAtlas; Q8C8S3; baseline and differential.
DR Genevisible; Q8C8S3; MM.
DR GO; GO:0005887; C:integral component of plasma membrane; ISS:UniProtKB.
DR GO; GO:0005765; C:lysosomal membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR GO; GO:0008381; F:mechanosensitive ion channel activity; IMP:UniProtKB.
DR GO; GO:0071260; P:cellular response to mechanical stimulus; IMP:UniProtKB.
DR GO; GO:0019230; P:proprioception; IMP:UniProtKB.
DR InterPro; IPR019402; Frag1/DRAM/Sfk1.
DR Pfam; PF10277; Frag1; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cell membrane; Lysosome; Membrane;
KW Reference proteome; Transmembrane; Transmembrane helix.
FT CHAIN 1..249
FT /note="Transmembrane protein 150C"
FT /id="PRO_0000395033"
FT TOPO_DOM 1..9
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 10..30
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 31..64
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 65..85
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 86..97
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 98..118
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 119..130
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 131..151
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 152..168
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 169..189
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 190..192
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 193..213
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 214..249
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:Q86TG1"
FT VAR_SEQ 122..249
FT /note="LTNDEEIHNVGTSLTFGFGTLTCWIQAALTLKVNIKNEGRRAGIPRVILSAV
FT ITLCVVLYFILMAQDIHMYAARVQWGLVMCFLAYFGTLAVEFRHYRYEIVCSEYQENFL
FT SFSESLSEASEYQTDQV -> VLPLAFLPPSSAGKIIRV (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_039351"
FT MUTAGEN 48
FT /note="G->A: Does not affect ion selectivity."
FT /evidence="ECO:0000269|PubMed:28426962"
FT MUTAGEN 48
FT /note="G->F: Does not affect ion selectivity."
FT /evidence="ECO:0000269|PubMed:28426962"
FT MUTAGEN 49
FT /note="A->K: Affects ion selectivity."
FT /evidence="ECO:0000269|PubMed:28426962"
FT MUTAGEN 50
FT /note="K->E: Does not affect ion selectivity."
FT /evidence="ECO:0000269|PubMed:28426962"
FT MUTAGEN 51
FT /note="H->D: Affects ion selectivity."
FT /evidence="ECO:0000269|PubMed:28426962"
SQ SEQUENCE 249 AA; 27759 MW; 9A0F302E178B6D5A CRC64;
MDGKKCSVWM FLPLVFTLFT SAGLWIVYFI AVEDDKILPL NSAARKSGAK HAPYISFAGD
DPPASCVFSQ VMNMAAFLAL VVAVLRFIQL KPKVLNPWLN ISGLAALCLA SFGMTLLGNF
QLTNDEEIHN VGTSLTFGFG TLTCWIQAAL TLKVNIKNEG RRAGIPRVIL SAVITLCVVL
YFILMAQDIH MYAARVQWGL VMCFLAYFGT LAVEFRHYRY EIVCSEYQEN FLSFSESLSE
ASEYQTDQV
