TM266_MOUSE
ID TM266_MOUSE Reviewed; 538 AA.
AC Q8BZB3; B1B1B3; Q6NVG3;
DT 27-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT 09-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 122.
DE RecName: Full=Transmembrane protein 266 {ECO:0000305};
GN Name=Tmem266 {ECO:0000312|MGI:MGI:2142980};
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] (ISOFORM 1).
RC STRAIN=C57BL/6J; TISSUE=Cerebellum;
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 MRNA] (ISOFORM 2).
RC STRAIN=C57BL/6J; TISSUE=Embryonic brain;
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 [4]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
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 [5]
RP SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=25165868; DOI=10.1371/journal.pone.0105926;
RA Kim I.H., Hevezi P., Varga C., Pathak M.M., Hong L., Ta D., Tran C.T.,
RA Zlotnik A., Soltesz I., Tombola F.;
RT "Evidence for functional diversity between the voltage-gated proton channel
RT Hv1 and its closest related protein HVRP1.";
RL PLoS ONE 9:E105926-E105926(2014).
CC -!- FUNCTION: Voltage-sensor protein present on the post-synaptic side of
CC glutamatergic mossy fibers and granule cells in the cerebellum. Despite
CC the presence of a voltage-sensor segment, does not form a functional
CC ion channel and its precise role remains unclear. Undergoes both rapid
CC and slow structural rearrangements in response to changes in voltage.
CC Contains a zinc-binding site that can regulate the slow conformational
CC transition. {ECO:0000250|UniProtKB:Q2M3C6}.
CC -!- SUBUNIT: Homodimer; disulfide-linked. {ECO:0000250|UniProtKB:Q2M3C6}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q2M3C6};
CC Multi-pass membrane protein {ECO:0000255}. Cell projection, dendrite
CC {ECO:0000269|PubMed:25165868}. Perikaryon
CC {ECO:0000250|UniProtKB:Q2M3C6}. Note=Present in the dendrites and soma
CC of cerebellar granule neurons, but not in their axon.
CC {ECO:0000250|UniProtKB:Q2M3C6}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q8BZB3-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8BZB3-2; Sequence=VSP_022109, VSP_022110, VSP_019514,
CC VSP_019515;
CC -!- TISSUE SPECIFICITY: In brain, present in the granule layer of the
CC cerebellar cortex (PubMed:25165868). Localizes on the post-synaptic
CC side of glutamatergic mossy fibers and granule cells in the cerebellum
CC (at protein level) (PubMed:25165868). {ECO:0000269|PubMed:25165868}.
CC -!- DOMAIN: The transmembrane segment S4 functions as voltage-sensor and is
CC characterized by a series of positively charged amino acids at every
CC third position. Transplantation of the transmembrane segment S4 into
CC HVCN1, generates a functional voltage-activated proton channel.
CC {ECO:0000250|UniProtKB:Q2M3C6}.
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DR EMBL; AK036040; BAC29283.1; -; mRNA.
DR EMBL; CT025532; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC068128; AAH68128.1; -; mRNA.
DR CCDS; CCDS23203.1; -. [Q8BZB3-1]
DR RefSeq; NP_766511.1; NM_172923.3. [Q8BZB3-1]
DR RefSeq; XP_011241048.1; XM_011242746.2.
DR AlphaFoldDB; Q8BZB3; -.
DR STRING; 10090.ENSMUSP00000034862; -.
DR iPTMnet; Q8BZB3; -.
DR PhosphoSitePlus; Q8BZB3; -.
DR PaxDb; Q8BZB3; -.
DR PeptideAtlas; Q8BZB3; -.
DR PRIDE; Q8BZB3; -.
DR ProteomicsDB; 260697; -. [Q8BZB3-1]
DR ProteomicsDB; 260698; -. [Q8BZB3-2]
DR Antibodypedia; 27411; 106 antibodies from 21 providers.
DR DNASU; 244886; -.
DR Ensembl; ENSMUST00000034862; ENSMUSP00000034862; ENSMUSG00000032313. [Q8BZB3-1]
DR Ensembl; ENSMUST00000085754; ENSMUSP00000082906; ENSMUSG00000032313. [Q8BZB3-2]
DR GeneID; 244886; -.
DR KEGG; mmu:244886; -.
DR UCSC; uc009psj.1; mouse. [Q8BZB3-2]
DR UCSC; uc009psk.1; mouse. [Q8BZB3-1]
DR CTD; 123591; -.
DR MGI; MGI:2142980; Tmem266.
DR VEuPathDB; HostDB:ENSMUSG00000032313; -.
DR eggNOG; ENOG502QRI0; Eukaryota.
DR GeneTree; ENSGT00940000156738; -.
DR HOGENOM; CLU_933712_0_0_1; -.
DR InParanoid; Q8BZB3; -.
DR OMA; PAREDDM; -.
DR OrthoDB; 826861at2759; -.
DR PhylomeDB; Q8BZB3; -.
DR TreeFam; TF332271; -.
DR BioGRID-ORCS; 244886; 0 hits in 40 CRISPR screens.
DR PRO; PR:Q8BZB3; -.
DR Proteomes; UP000000589; Chromosome 9.
DR RNAct; Q8BZB3; protein.
DR Bgee; ENSMUSG00000032313; Expressed in cerebellar cortex and 61 other tissues.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0030425; C:dendrite; ISS:UniProtKB.
DR GO; GO:0005887; C:integral component of plasma membrane; ISS:UniProtKB.
DR GO; GO:0043204; C:perikaryon; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR GO; GO:0042803; F:protein homodimerization activity; ISS:UniProtKB.
DR GO; GO:0006811; P:ion transport; IEA:InterPro.
DR GO; GO:0055085; P:transmembrane transport; IEA:InterPro.
DR Gene3D; 1.20.120.350; -; 1.
DR InterPro; IPR005821; Ion_trans_dom.
DR InterPro; IPR042857; TMEM266.
DR InterPro; IPR027359; Volt_channel_dom_sf.
DR PANTHER; PTHR46842; PTHR46842; 1.
DR Pfam; PF00520; Ion_trans; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cell membrane; Cell projection; Coiled coil;
KW Disulfide bond; Membrane; Reference proteome; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..538
FT /note="Transmembrane protein 266"
FT /id="PRO_0000244096"
FT TOPO_DOM 1..102
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 103..123
FT /note="Helical; Name=Segment S1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 124..130
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 131..151
FT /note="Helical; Name=Segment S2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 152..169
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 170..190
FT /note="Helical; Name=Segment S3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 191..199
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 200..220
FT /note="Helical; Name=Segment S4"
FT /evidence="ECO:0000250|UniProtKB:Q2M3C6"
FT TOPO_DOM 221..538
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT REGION 380..435
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 453..483
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 232..278
FT /evidence="ECO:0000255"
FT COMPBIAS 380..420
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 1..65
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_022109"
FT VAR_SEQ 66..76
FT /note="SNLDEEYQREG -> MMLFQPHRAFR (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_022110"
FT VAR_SEQ 341..363
FT /note="DSGAPEPAVCVVTTAAIDIHQPN -> GKSGLGLFACTMQPQDTCDPSKP
FT (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_019514"
FT VAR_SEQ 364..538
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_019515"
SQ SEQUENCE 538 AA; 58897 MW; D3F14858BD140C65 CRC64;
MALVTSFNMA NPQPAIEGGI SEVEIISQQV DEETKSIAPV QLVNFAYRDL PLAAVDLSTG
GSQLLSNLDE EYQREGSDWL KPCCGKRAAV WQVFLLSASL NSFLVACVIL VVILLTLELL
IDTKLLQFSN AFQFAGVIHW ISLVILSVFF SETVLRIVVL GIWDYIENKI EVFDGAVIIL
SLAPMVASTV ANGPRSPWDA ISLIIMFRIW RVKRVIDAYV LPVKLEMEMV TQQYEKAKAI
QDEQLERLTQ ICQEQGFEIR QLRAHLAQQD LDLAAEREAA LQAPHVLSQP RSRYKVVEAG
TWAEETAAES IVEELRPSQE ATVKDDMNSY ISQYYNGPSS DSGAPEPAVC VVTTAAIDIH
QPNVPSDLFS VDLPLKLSGN STCASATSET TSHSTCGSVT RAQSASSQTL GSSTDCSTPR
EELLPSKPRS SPLPLLLPPQ QLVAEATVQD LMSSLSKDPC PSHKALDPAP LAQPTPLGSV
QTSPELEHRV SLFNQKNQEA LPVLQINPVI HLQPTAGLEE KFRSLESKEP KLHTVPEA
