T106B_MOUSE
ID T106B_MOUSE Reviewed; 275 AA.
AC Q80X71; Q9D737;
DT 27-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 123.
DE RecName: Full=Transmembrane protein 106B;
GN Name=Tmem106b;
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].
RC STRAIN=C57BL/6J; TISSUE=Tongue;
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 MRNA].
RC TISSUE=Olfactory epithelium;
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 [3]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA Thibault P.;
RT "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL Immunity 30:143-154(2009).
CC -!- FUNCTION: Involved in dendrite morphogenesis and maintenance by
CC regulating lysosomal trafficking via its interaction with MAP6. May act
CC by inhibiting retrograde transport of lysosomes along dendrites.
CC Required for dendrite branching (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Interacts with MAP6. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Late endosome membrane {ECO:0000250}; Single-pass
CC type II membrane protein. Lysosome membrane {ECO:0000250}; Single-pass
CC type II membrane protein. Membrane {ECO:0000250|UniProtKB:Q9NUM4};
CC Lipid-anchor {ECO:0000250|UniProtKB:Q9NUM4}.
CC -!- SIMILARITY: Belongs to the TMEM106 family. {ECO:0000305}.
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DR EMBL; AK009646; BAB26411.1; -; mRNA.
DR EMBL; BC050246; AAH50246.1; -; mRNA.
DR CCDS; CCDS19914.1; -.
DR RefSeq; NP_082268.2; NM_027992.3.
DR RefSeq; XP_006505232.1; XM_006505169.3.
DR AlphaFoldDB; Q80X71; -.
DR BioGRID; 215015; 1.
DR STRING; 10090.ENSMUSP00000031556; -.
DR GlyConnect; 2786; 6 N-Linked glycans (1 site).
DR GlyGen; Q80X71; 5 sites, 6 N-linked glycans (1 site).
DR iPTMnet; Q80X71; -.
DR PhosphoSitePlus; Q80X71; -.
DR SwissPalm; Q80X71; -.
DR EPD; Q80X71; -.
DR MaxQB; Q80X71; -.
DR PaxDb; Q80X71; -.
DR PeptideAtlas; Q80X71; -.
DR PRIDE; Q80X71; -.
DR ProteomicsDB; 253454; -.
DR Antibodypedia; 43908; 130 antibodies from 28 providers.
DR DNASU; 71900; -.
DR Ensembl; ENSMUST00000031556; ENSMUSP00000031556; ENSMUSG00000029571.
DR GeneID; 71900; -.
DR KEGG; mmu:71900; -.
DR UCSC; uc009ayk.2; mouse.
DR CTD; 54664; -.
DR MGI; MGI:1919150; Tmem106b.
DR VEuPathDB; HostDB:ENSMUSG00000029571; -.
DR eggNOG; ENOG502QQRZ; Eukaryota.
DR GeneTree; ENSGT00940000158360; -.
DR InParanoid; Q80X71; -.
DR OMA; QTSQERY; -.
DR OrthoDB; 1175832at2759; -.
DR PhylomeDB; Q80X71; -.
DR TreeFam; TF328907; -.
DR BioGRID-ORCS; 71900; 1 hit in 72 CRISPR screens.
DR ChiTaRS; Tmem106b; mouse.
DR PRO; PR:Q80X71; -.
DR Proteomes; UP000000589; Chromosome 6.
DR RNAct; Q80X71; protein.
DR Bgee; ENSMUSG00000029571; Expressed in vestibular membrane of cochlear duct and 233 other tissues.
DR ExpressionAtlas; Q80X71; baseline and differential.
DR Genevisible; Q80X71; MM.
DR GO; GO:0005768; C:endosome; ISO:MGI.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0031902; C:late endosome membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005765; C:lysosomal membrane; ISS:UniProtKB.
DR GO; GO:0005764; C:lysosome; IDA:UniProtKB.
DR GO; GO:0051117; F:ATPase binding; IPI:MGI.
DR GO; GO:0048813; P:dendrite morphogenesis; ISS:UniProtKB.
DR GO; GO:0007042; P:lysosomal lumen acidification; IMP:MGI.
DR GO; GO:1905146; P:lysosomal protein catabolic process; IMP:MGI.
DR GO; GO:0007041; P:lysosomal transport; IMP:MGI.
DR GO; GO:0032418; P:lysosome localization; ISS:UniProtKB.
DR GO; GO:0007040; P:lysosome organization; IMP:MGI.
DR GO; GO:0070050; P:neuron cellular homeostasis; IMP:MGI.
DR GO; GO:1900006; P:positive regulation of dendrite development; IMP:MGI.
DR GO; GO:0051345; P:positive regulation of hydrolase activity; IMP:MGI.
DR GO; GO:1905671; P:regulation of lysosome organization; IMP:MGI.
DR InterPro; IPR009790; TMEM106.
DR PANTHER; PTHR28556; PTHR28556; 1.
DR Pfam; PF07092; DUF1356; 1.
PE 1: Evidence at protein level;
KW Endosome; Glycoprotein; Lipoprotein; Lysosome; Membrane; Myristate;
KW Phosphoprotein; Reference proteome; Signal-anchor; Transmembrane;
KW Transmembrane helix; Transport.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:Q9NUM4"
FT CHAIN 2..275
FT /note="Transmembrane protein 106B"
FT /id="PRO_0000242651"
FT TOPO_DOM 2..97
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 98..118
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 119..275
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT REGION 1..24
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 34
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9NUM4"
FT LIPID 2
FT /note="N-myristoyl glycine"
FT /evidence="ECO:0000250|UniProtKB:Q9NUM4"
FT CARBOHYD 146
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 152
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 165
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 184
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 257
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CONFLICT 219
FT /note="S -> Y (in Ref. 1; BAB26411)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 275 AA; 31172 MW; 4075221F1280EC4A CRC64;
MGKSLSHLPL HSNKEDGYDG VTSTDNMRNG LVSSEVHNED GRNGDVSQFP YVEFTGRDSV
TCPTCQGTGR IPRGQENQLV ALIPYSDQRL RPRRTKLYVM ASVFVCLLLS GLAVFFLFPR
SIEVKYIGVK SAYVSYDAEK RTIYLNITNT LNITNNNYYS VEVENITAQV QFSKTVIGKA
RLNNITNIGP LDMKQIDYTV PTVIAEEMSY MYDFCTLLSI KVHNIVLMMQ VTVTTAYFGH
SEQISQERYQ YVDCGRNTTY QLAQSEYLNV LQPQQ
