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Transmembrane protein 108 (Retrolinkin)

 TM108_MOUSE             Reviewed;         574 AA.
Q8BHE4; Q80WR9;
27-JUN-2006, integrated into UniProtKB/Swiss-Prot.
01-MAR-2003, sequence version 1.
12-SEP-2018, entry version 96.
RecName: Full=Transmembrane protein 108;
AltName: Full=Retrolinkin {ECO:0000303|PubMed:17287360};
Name=Tmem108 {ECO:0000312|MGI:MGI:1932411};
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=C57BL/6J; TISSUE=Cerebellum, Heart, and Hippocampus;
PubMed=16141072; DOI=10.1126/science.1112014;
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
Hayashizaki Y.;
"The transcriptional landscape of the mammalian genome.";
Science 309:1559-1563(2005).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=C57BL/6J; TISSUE=Brain;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[3]
FUNCTION, DEVELOPMENTAL STAGE, TISSUE SPECIFICITY, INTERACTION WITH
DST, SUBCELLULAR LOCATION, AND GLYCOSYLATION.
PubMed=17287360; DOI=10.1073/pnas.0602222104;
Liu J.J., Ding J., Wu C., Bhagavatula P., Cui B., Chu S., Mobley W.C.,
Yang Y.;
"Retrolinkin, a membrane protein, plays an important role in
retrograde axonal transport.";
Proc. Natl. Acad. Sci. U.S.A. 104:2223-2228(2007).
[4]
FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND INTERACTION
WITH SH3GL2.
PubMed=21849472; DOI=10.1091/mbc.E11-04-0308;
Fu X., Yang Y., Xu C., Niu Y., Chen T., Zhou Q., Liu J.J.;
"Retrolinkin cooperates with endophilin A1 to mediate BDNF-TrkB early
endocytic trafficking and signaling from early endosomes.";
Mol. Biol. Cell 22:3684-3698(2011).
[5]
FUNCTION, AND INTERACTION WITH CYFIP2 AND CYFIP1.
PubMed=27605705; DOI=10.1091/mbc.E16-05-0326;
Xu C., Fu X., Zhu S., Liu J.J.;
"Retrolinkin recruits the WAVE1 protein complex to facilitate BDNF-
induced TrkB endocytosis and dendrite outgrowth.";
Mol. Biol. Cell 27:3342-3356(2016).
[6]
FUNCTION, DISRUPTION PHENOTYPE, SUBCELLULAR LOCATION, TISSUE
SPECIFICITY, AND DEVELOPMENTAL STAGE.
PubMed=28096412; DOI=10.1073/pnas.1618213114;
Jiao H.F., Sun X.D., Bates R., Xiong L., Zhang L., Liu F., Li L.,
Zhang H.S., Wang S.Q., Xiong M.T., Patel M., Stranahan A.M.,
Xiong W.C., Li B.M., Mei L.;
"Transmembrane protein 108 is required for glutamatergic transmission
in dentate gyrus.";
Proc. Natl. Acad. Sci. U.S.A. 114:1177-1182(2017).
-!- FUNCTION: Transmembrane protein required for proper cognitive
functions. Involved in the development of dentate gyrus (DG)
neuron circuitry, is neccessary for AMPA receptors surface
expression and proper excitatory postsynaptic currents of DG
granule neurons (PubMed:28096412). Regulates the organization and
stability of the microtubule network of sensory neurons to allow
axonal transport. Through the interaction with DST, mediates the
docking of the dynein/dynactin motor complex to vesicle cargos for
retrograde axonal transport (PubMed:17287360). In hippocampal
neurons, required for BDNF-dependent dendrite outgrowth
(PubMed:21849472). Cooperates with SH3GL2 and recruits the WAVE1
complex to facilitate actin-dependent BDNF:NTRK2 early endocytic
trafficking and mediate signaling from early endosomes
(PubMed:21849472, PubMed:27605705). {ECO:0000269|PubMed:17287360,
ECO:0000269|PubMed:21849472, ECO:0000269|PubMed:27605705,
ECO:0000269|PubMed:28096412}.
-!- SUBUNIT: Interacts with DST (isoform 1) (PubMed:17287360).
Interacts with SH3GL2 (PubMed:21849472). Interacts (via N-
terminus) with CYFIP1 and CYFIP2; the interactions associate
TMEM108 with the WAVE1 complex (PubMed:27605705).
{ECO:0000269|PubMed:17287360, ECO:0000269|PubMed:21849472,
ECO:0000269|PubMed:27605705}.
-!- SUBCELLULAR LOCATION: Membrane {ECO:0000269|PubMed:17287360};
Multi-pass membrane protein {ECO:0000255}. Cell junction, synapse,
postsynaptic cell membrane, postsynaptic density
{ECO:0000269|PubMed:28096412}. Endosome membrane
{ECO:0000269|PubMed:17287360}. Cell projection, axon
{ECO:0000269|PubMed:17287360, ECO:0000269|PubMed:21849472}. Cell
projection, dendrite {ECO:0000269|PubMed:21849472}. Early endosome
{ECO:0000269|PubMed:21849472}.
-!- TISSUE SPECIFICITY: Expressed in the nervous system tissues, such
as hippocampus and spinal cord, is barely detectable in peripheral
tissues such as heart, lung, liver, kidney and muscle
(PubMed:17287360, PubMed:28096412). In brain, highly expressed in
dentate gyrus neurons and expressed in cortex, olfactory bulb,
ammon's horn, cerebellum, hypothalamus and striatum
(PubMed:28096412, PubMed:21849472). {ECO:0000269|PubMed:17287360,
ECO:0000269|PubMed:21849472, ECO:0000269|PubMed:28096412}.
-!- DEVELOPMENTAL STAGE: In brain, detectable as early as E12 and the
level increases persistently through later embryonic stages to the
adult age (PubMed:17287360). In the hippocampus, undetectable at
postnatal day 1 (P1), detected at P7, the levels peak between P15
and P21 to remain at a high level during adulthood
(PubMed:28096412). {ECO:0000269|PubMed:17287360,
ECO:0000269|PubMed:28096412}.
-!- PTM: Glycosylated. {ECO:0000269|PubMed:17287360}.
-!- DISRUPTION PHENOTYPE: Mutants are viable and show no difference in
body weight or locomotor activity (PubMed:28096412). They are
impaired in sensorimotor gating, spatial recognition memory and
suppressed fear memory consolidation (PubMed:28096412). Spine
density of dentate gyrus granule neurons is significantly reduced
compare to wild-type animals, which is associated with decreased
spine width and increased spine length (PubMed:28096412).
{ECO:0000269|PubMed:28096412}.
-----------------------------------------------------------------------
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Distributed under the Creative Commons Attribution (CC BY 4.0) License
-----------------------------------------------------------------------
EMBL; AK044989; BAC32171.1; -; mRNA.
EMBL; AK141589; BAE24751.1; -; mRNA.
EMBL; AK052330; BAC34940.1; -; mRNA.
EMBL; AK047474; BAC33068.1; -; mRNA.
EMBL; BC052085; AAH52085.2; -; mRNA.
CCDS; CCDS23455.1; -.
RefSeq; NP_848753.1; NM_178638.4.
RefSeq; XP_006511931.1; XM_006511868.3.
RefSeq; XP_006511932.1; XM_006511869.3.
UniGene; Mm.384704; -.
ProteinModelPortal; Q8BHE4; -.
STRING; 10090.ENSMUSP00000046021; -.
iPTMnet; Q8BHE4; -.
PhosphoSitePlus; Q8BHE4; -.
PaxDb; Q8BHE4; -.
PRIDE; Q8BHE4; -.
Ensembl; ENSMUST00000049452; ENSMUSP00000046021; ENSMUSG00000042757.
Ensembl; ENSMUST00000189066; ENSMUSP00000141160; ENSMUSG00000042757.
Ensembl; ENSMUST00000189588; ENSMUSP00000140027; ENSMUSG00000042757.
GeneID; 81907; -.
KEGG; mmu:81907; -.
UCSC; uc009rgx.2; mouse.
CTD; 66000; -.
MGI; MGI:1932411; Tmem108.
eggNOG; ENOG410IEMG; Eukaryota.
eggNOG; ENOG410YCMK; LUCA.
GeneTree; ENSGT00390000000626; -.
HOGENOM; HOG000154603; -.
HOVERGEN; HBG094052; -.
InParanoid; Q8BHE4; -.
OMA; TWKPGTA; -.
OrthoDB; EOG091G06WN; -.
PhylomeDB; Q8BHE4; -.
TreeFam; TF336337; -.
PRO; PR:Q8BHE4; -.
Proteomes; UP000000589; Chromosome 9.
Bgee; ENSMUSG00000042757; Expressed in 194 organ(s), highest expression level in placenta.
CleanEx; MM_TMEM108; -.
ExpressionAtlas; Q8BHE4; baseline and differential.
Genevisible; Q8BHE4; MM.
GO; GO:0030424; C:axon; IDA:UniProtKB.
GO; GO:1904115; C:axon cytoplasm; IEA:GOC.
GO; GO:0030054; C:cell junction; IEA:UniProtKB-KW.
GO; GO:0030425; C:dendrite; IEA:UniProtKB-SubCell.
GO; GO:0005769; C:early endosome; IDA:UniProtKB.
GO; GO:0010008; C:endosome membrane; IDA:UniProtKB.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0014069; C:postsynaptic density; IDA:UniProtKB.
GO; GO:0045211; C:postsynaptic membrane; IEA:UniProtKB-KW.
GO; GO:0036477; C:somatodendritic compartment; IDA:UniProtKB.
GO; GO:1990416; P:cellular response to brain-derived neurotrophic factor stimulus; IMP:UniProtKB.
GO; GO:0097484; P:dendrite extension; IMP:UniProtKB.
GO; GO:0021542; P:dentate gyrus development; IMP:UniProtKB.
GO; GO:0098815; P:modulation of excitatory postsynaptic potential; IMP:UniProtKB.
GO; GO:0031175; P:neuron projection development; IMP:UniProtKB.
GO; GO:0051388; P:positive regulation of neurotrophin TRK receptor signaling pathway; IMP:UniProtKB.
GO; GO:0097106; P:postsynaptic density organization; IMP:UniProtKB.
GO; GO:0006898; P:receptor-mediated endocytosis; IMP:UniProtKB.
GO; GO:0008090; P:retrograde axonal transport; IDA:UniProtKB.
InterPro; IPR031508; TMEM108.
PANTHER; PTHR28673; PTHR28673; 1.
Pfam; PF15759; TMEM108; 1.
1: Evidence at protein level;
Cell junction; Cell membrane; Cell projection; Complete proteome;
Endosome; Glycoprotein; Membrane; Postsynaptic cell membrane;
Reference proteome; Synapse; Transmembrane; Transmembrane helix.
CHAIN 1 574 Transmembrane protein 108.
/FTId=PRO_0000243914.
TRANSMEM 9 29 Helical. {ECO:0000255}.
TRANSMEM 468 488 Helical. {ECO:0000255}.
REGION 31 169 Interaction with SH3GL2.
{ECO:0000269|PubMed:21849472}.
REGION 173 406 Interaction with DST (isoform 1).
{ECO:0000269|PubMed:17287360}.
REGION 489 574 Interaction with CYFIP2.
{ECO:0000269|PubMed:27605705}.
COMPBIAS 32 169 Pro-rich. {ECO:0000255|PROSITE-
ProRule:PRU00015}.
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


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