TM108_MOUSE
ID TM108_MOUSE Reviewed; 574 AA.
AC Q8BHE4; Q80WR9;
DT 27-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 117.
DE RecName: Full=Transmembrane protein 108;
DE AltName: Full=Retrolinkin {ECO:0000303|PubMed:17287360};
GN Name=Tmem108 {ECO:0000312|MGI:MGI:1932411};
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=Cerebellum, Heart, and Hippocampus;
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 STRAIN=C57BL/6J; TISSUE=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 [3]
RP FUNCTION, DEVELOPMENTAL STAGE, TISSUE SPECIFICITY, INTERACTION WITH DST,
RP SUBCELLULAR LOCATION, AND GLYCOSYLATION.
RX PubMed=17287360; DOI=10.1073/pnas.0602222104;
RA Liu J.J., Ding J., Wu C., Bhagavatula P., Cui B., Chu S., Mobley W.C.,
RA Yang Y.;
RT "Retrolinkin, a membrane protein, plays an important role in retrograde
RT axonal transport.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:2223-2228(2007).
RN [4]
RP FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND INTERACTION WITH
RP SH3GL2.
RX PubMed=21849472; DOI=10.1091/mbc.e11-04-0308;
RA Fu X., Yang Y., Xu C., Niu Y., Chen T., Zhou Q., Liu J.J.;
RT "Retrolinkin cooperates with endophilin A1 to mediate BDNF-TrkB early
RT endocytic trafficking and signaling from early endosomes.";
RL Mol. Biol. Cell 22:3684-3698(2011).
RN [5]
RP FUNCTION, AND INTERACTION WITH CYFIP2 AND CYFIP1.
RX PubMed=27605705; DOI=10.1091/mbc.e16-05-0326;
RA Xu C., Fu X., Zhu S., Liu J.J.;
RT "Retrolinkin recruits the WAVE1 protein complex to facilitate BDNF-induced
RT TrkB endocytosis and dendrite outgrowth.";
RL Mol. Biol. Cell 27:3342-3356(2016).
RN [6]
RP FUNCTION, DISRUPTION PHENOTYPE, SUBCELLULAR LOCATION, TISSUE SPECIFICITY,
RP AND DEVELOPMENTAL STAGE.
RX PubMed=28096412; DOI=10.1073/pnas.1618213114;
RA Jiao H.F., Sun X.D., Bates R., Xiong L., Zhang L., Liu F., Li L.,
RA Zhang H.S., Wang S.Q., Xiong M.T., Patel M., Stranahan A.M., Xiong W.C.,
RA Li B.M., Mei L.;
RT "Transmembrane protein 108 is required for glutamatergic transmission in
RT dentate gyrus.";
RL Proc. Natl. Acad. Sci. U.S.A. 114:1177-1182(2017).
CC -!- FUNCTION: Transmembrane protein required for proper cognitive
CC functions. Involved in the development of dentate gyrus (DG) neuron
CC circuitry, is necessary for AMPA receptors surface expression and
CC proper excitatory postsynaptic currents of DG granule neurons
CC (PubMed:28096412). Regulates the organization and stability of the
CC microtubule network of sensory neurons to allow axonal transport.
CC Through the interaction with DST, mediates the docking of the
CC dynein/dynactin motor complex to vesicle cargos for retrograde axonal
CC transport (PubMed:17287360). In hippocampal neurons, required for BDNF-
CC dependent dendrite outgrowth (PubMed:21849472). Cooperates with SH3GL2
CC and recruits the WAVE1 complex to facilitate actin-dependent BDNF:NTRK2
CC early endocytic trafficking and mediate signaling from early endosomes
CC (PubMed:21849472, PubMed:27605705). {ECO:0000269|PubMed:17287360,
CC ECO:0000269|PubMed:21849472, ECO:0000269|PubMed:27605705,
CC ECO:0000269|PubMed:28096412}.
CC -!- SUBUNIT: Interacts with DST (isoform 1) (PubMed:17287360). Interacts
CC with SH3GL2 (PubMed:21849472). Interacts (via N-terminus) with CYFIP1
CC and CYFIP2; the interactions associate TMEM108 with the WAVE1 complex
CC (PubMed:27605705). {ECO:0000269|PubMed:17287360,
CC ECO:0000269|PubMed:21849472, ECO:0000269|PubMed:27605705}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000269|PubMed:17287360}; Multi-
CC pass membrane protein {ECO:0000255}. Postsynaptic density
CC {ECO:0000269|PubMed:28096412}. Endosome membrane
CC {ECO:0000269|PubMed:17287360}. Cell projection, axon
CC {ECO:0000269|PubMed:17287360, ECO:0000269|PubMed:21849472}. Cell
CC projection, dendrite {ECO:0000269|PubMed:21849472}. Early endosome
CC {ECO:0000269|PubMed:21849472}.
CC -!- TISSUE SPECIFICITY: Expressed in the nervous system tissues, such as
CC hippocampus and spinal cord, is barely detectable in peripheral tissues
CC such as heart, lung, liver, kidney and muscle (PubMed:17287360,
CC PubMed:28096412). In brain, highly expressed in dentate gyrus neurons
CC and expressed in cortex, olfactory bulb, ammon's horn, cerebellum,
CC hypothalamus and striatum (PubMed:28096412, PubMed:21849472).
CC {ECO:0000269|PubMed:17287360, ECO:0000269|PubMed:21849472,
CC ECO:0000269|PubMed:28096412}.
CC -!- DEVELOPMENTAL STAGE: In brain, detectable as early as 12 dpc and the
CC level increases persistently through later embryonic stages to the
CC adult age (PubMed:17287360). In the hippocampus, undetectable at
CC postnatal day 1 (P1), detected at P7, the levels peak between P15 and
CC P21 to remain at a high level during adulthood (PubMed:28096412).
CC {ECO:0000269|PubMed:17287360, ECO:0000269|PubMed:28096412}.
CC -!- PTM: Glycosylated. {ECO:0000269|PubMed:17287360}.
CC -!- DISRUPTION PHENOTYPE: Mutants are viable and show no difference in body
CC weight or locomotor activity (PubMed:28096412). They are impaired in
CC sensorimotor gating, spatial recognition memory and suppressed fear
CC memory consolidation (PubMed:28096412). Spine density of dentate gyrus
CC granule neurons is significantly reduced compare to wild-type animals,
CC which is associated with decreased spine width and increased spine
CC length (PubMed:28096412). {ECO:0000269|PubMed:28096412}.
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DR EMBL; AK044989; BAC32171.1; -; mRNA.
DR EMBL; AK141589; BAE24751.1; -; mRNA.
DR EMBL; AK052330; BAC34940.1; -; mRNA.
DR EMBL; AK047474; BAC33068.1; -; mRNA.
DR EMBL; BC052085; AAH52085.2; -; mRNA.
DR CCDS; CCDS23455.1; -.
DR RefSeq; NP_848753.1; NM_178638.4.
DR RefSeq; XP_006511931.1; XM_006511868.3.
DR RefSeq; XP_006511932.1; XM_006511869.3.
DR AlphaFoldDB; Q8BHE4; -.
DR STRING; 10090.ENSMUSP00000140027; -.
DR iPTMnet; Q8BHE4; -.
DR PhosphoSitePlus; Q8BHE4; -.
DR PaxDb; Q8BHE4; -.
DR PRIDE; Q8BHE4; -.
DR ProteomicsDB; 262825; -.
DR Antibodypedia; 17731; 88 antibodies from 19 providers.
DR DNASU; 81907; -.
DR Ensembl; ENSMUST00000049452; ENSMUSP00000046021; ENSMUSG00000042757.
DR Ensembl; ENSMUST00000189066; ENSMUSP00000141160; ENSMUSG00000042757.
DR Ensembl; ENSMUST00000189588; ENSMUSP00000140027; ENSMUSG00000042757.
DR GeneID; 81907; -.
DR KEGG; mmu:81907; -.
DR UCSC; uc009rgx.2; mouse.
DR CTD; 66000; -.
DR MGI; MGI:1932411; Tmem108.
DR VEuPathDB; HostDB:ENSMUSG00000042757; -.
DR eggNOG; ENOG502RXTY; Eukaryota.
DR GeneTree; ENSGT00390000000626; -.
DR HOGENOM; CLU_040547_1_0_1; -.
DR InParanoid; Q8BHE4; -.
DR OMA; KPMGATS; -.
DR OrthoDB; 1160560at2759; -.
DR PhylomeDB; Q8BHE4; -.
DR TreeFam; TF336337; -.
DR BioGRID-ORCS; 81907; 1 hit in 70 CRISPR screens.
DR ChiTaRS; Tmem108; mouse.
DR PRO; PR:Q8BHE4; -.
DR Proteomes; UP000000589; Chromosome 9.
DR RNAct; Q8BHE4; protein.
DR Bgee; ENSMUSG00000042757; Expressed in placenta labyrinth and 179 other tissues.
DR ExpressionAtlas; Q8BHE4; baseline and differential.
DR Genevisible; Q8BHE4; MM.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0030424; C:axon; IDA:UniProtKB.
DR GO; GO:1904115; C:axon cytoplasm; IEA:GOC.
DR GO; GO:0030425; C:dendrite; IEA:UniProtKB-SubCell.
DR GO; GO:0005769; C:early endosome; IDA:UniProtKB.
DR GO; GO:0010008; C:endosome membrane; IDA:UniProtKB.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0014069; C:postsynaptic density; IDA:UniProtKB.
DR GO; GO:0036477; C:somatodendritic compartment; IDA:UniProtKB.
DR GO; GO:1990416; P:cellular response to brain-derived neurotrophic factor stimulus; IMP:UniProtKB.
DR GO; GO:0097484; P:dendrite extension; IMP:UniProtKB.
DR GO; GO:0021542; P:dentate gyrus development; IMP:UniProtKB.
DR GO; GO:0098815; P:modulation of excitatory postsynaptic potential; IMP:UniProtKB.
DR GO; GO:0031175; P:neuron projection development; IMP:UniProtKB.
DR GO; GO:0051388; P:positive regulation of neurotrophin TRK receptor signaling pathway; IMP:UniProtKB.
DR GO; GO:0097106; P:postsynaptic density organization; IMP:UniProtKB.
DR GO; GO:0006898; P:receptor-mediated endocytosis; IMP:UniProtKB.
DR GO; GO:0008090; P:retrograde axonal transport; IDA:UniProtKB.
DR InterPro; IPR031508; TMEM108.
DR PANTHER; PTHR28673; PTHR28673; 1.
DR Pfam; PF15759; TMEM108; 1.
PE 1: Evidence at protein level;
KW Cell projection; Endosome; Glycoprotein; Membrane; Reference proteome;
KW Synapse; Transmembrane; Transmembrane helix.
FT CHAIN 1..574
FT /note="Transmembrane protein 108"
FT /id="PRO_0000243914"
FT TRANSMEM 9..29
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 468..488
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 31..169
FT /note="Interaction with SH3GL2"
FT /evidence="ECO:0000269|PubMed:21849472"
FT REGION 32..417
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 173..406
FT /note="Interaction with DST (isoform 1)"
FT /evidence="ECO:0000269|PubMed:17287360"
FT REGION 489..574
FT /note="Interaction with CYFIP2"
FT /evidence="ECO:0000269|PubMed:27605705"
FT COMPBIAS 36..104
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 117..158
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 240..269
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 304..366
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 383..404
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 574 AA; 59642 MW; 29901D7013C07DC1 CRC64;
MKRSLQALYC QLLSFLLTLA LTKALVLAVH EPSPRESLQT LPSGSPPGTM VTAPHSPTRL
SSVLTLNPTP DGPSSQAAAT LETTVSHPEG HPPTDTTSTV MGTAAVPHPE SPLPTGSPPA
AMTTTPSHSE SLPPGDATPT TTLPTKPAGT TSRPTVAPRA TTRRPPRPPG SSRKGAGGST
RTLTPVPGGH LARKESQRGR NQSSAHLGPK RPLGKIFQIY KGNFTGSAEP DPSALTPRTP
LGGYFSSTQP QTVSPATAPR STSRVPPTTS LVPVKDKPGF IRSNQGSGPI LTSPGGEPAA
TAATGAPAST QPAPVPSQSP HGDVQDSASH SDSWLAVTPD TDRPTSASSG VFTAATGPTQ
AAFDATVSAP SPGIPQGPSA TPQAPTRPSG VSESTVSPAE EEAEASPTTT DRGPRPLSTV
LSTATGNFLN RLVPAGTWKP GTVANISHVA EGDKPQHRAT ICLSKMDIAW VIVAISVPIS
SCSVLLTVCC MRRKKKTANP ENNLSYWNNA ITMDYFNRHA VELPREIQSL ETSEDQLSEP
RSPANGDYRD TGMVLVNPFC QETLFVGNDQ VSEI
