TM135_MOUSE
ID TM135_MOUSE Reviewed; 458 AA.
AC Q9CYV5; Q8BSY5; Q8CCZ6; Q8CE78;
DT 17-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 123.
DE RecName: Full=Transmembrane protein 135 {ECO:0000312|MGI:MGI:1920009};
DE AltName: Full=Peroxisomal membrane protein 52 {ECO:0000303|PubMed:17768142};
DE Short=PMP52 {ECO:0000303|PubMed:17768142};
GN Name=Tmem135 {ECO:0000312|MGI:MGI:1920009};
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 [MRNA].
RC STRAIN=BALB/cJ; TISSUE=Heart;
RA Leu M., Ehler E., Perriard J.-C.;
RT "Cloning of a putative transmembrane protein.";
RL Submitted (JUN-2001) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Medulla oblongata, Placenta, and Skin;
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J, and FVB/N; TISSUE=Brain, and Salivary gland;
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 SUBCELLULAR LOCATION.
RX PubMed=17768142; DOI=10.1074/mcp.m700169-mcp200;
RA Wiese S., Gronemeyer T., Ofman R., Kunze M., Grou C.P., Almeida J.A.,
RA Eisenacher M., Stephan C., Hayen H., Schollenberger L., Korosec T.,
RA Waterham H.R., Schliebs W., Erdmann R., Berger J., Meyer H.E., Just W.,
RA Azevedo J.E., Wanders R.J., Warscheid B.;
RT "Proteomics characterization of mouse kidney peroxisomes by tandem mass
RT spectrometry and protein correlation profiling.";
RL Mol. Cell. Proteomics 6:2045-2057(2007).
RN [5]
RP INDUCTION.
RX PubMed=21151927; DOI=10.1371/journal.pone.0014228;
RA Exil V.J., Silva Avila D., Benedetto A., Exil E.A., Adams M.R., Au C.,
RA Aschner M.;
RT "Stressed-induced TMEM135 protein is part of a conserved genetic network
RT involved in fat storage and longevity regulation in Caenorhabditis
RT elegans.";
RL PLoS ONE 5:E14228-E14228(2010).
RN [6]
RP FUNCTION, SUBCELLULAR LOCATION, AND DISRUPTION PHENOTYPE.
RX PubMed=27863209; DOI=10.7554/elife.19264;
RA Lee W.H., Higuchi H., Ikeda S., Macke E.L., Takimoto T., Pattnaik B.R.,
RA Liu C., Chu L.F., Siepka S.M., Krentz K.J., Rubinstein C.D., Kalejta R.F.,
RA Thomson J.A., Mullins R.F., Takahashi J.S., Pinto L.H., Ikeda A.;
RT "Mouse Tmem135 mutation reveals a mechanism involving mitochondrial
RT dynamics that leads to age-dependent retinal pathologies.";
RL Elife 5:0-0(2016).
CC -!- FUNCTION: Involved in mitochondrial metabolism by regulating the
CC balance between mitochondrial fusion and fission (PubMed:27863209). May
CC act as a regulator of mitochondrial fission that promotes DNM1L-
CC dependent fission through activation of DNM1L (PubMed:27863209). May be
CC involved in peroxisome organization (By similarity).
CC {ECO:0000250|UniProtKB:Q5U4F4, ECO:0000269|PubMed:27863209}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion membrane
CC {ECO:0000305|PubMed:27863209}; Multi-pass membrane protein
CC {ECO:0000305}. Peroxisome membrane {ECO:0000305|PubMed:17768142};
CC Multi-pass membrane protein {ECO:0000255}.
CC -!- INDUCTION: Up-regulated following cold exposure and upon fasting.
CC {ECO:0000269|PubMed:21151927}.
CC -!- DISRUPTION PHENOTYPE: Age-dependent pathologies, characterized by
CC accelerated aging in the retina similar to macular degeneration of the
CC retina (PubMed:27863209). Retina show higher sensitivity to oxidative
CC stress (PubMed:27863209). Defects are caused by impaired balance
CC between mitochondrial fusion and fission (PubMed:27863209).
CC {ECO:0000269|PubMed:27863209}.
CC -!- SIMILARITY: Belongs to the TMEM135 family. {ECO:0000305}.
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DR EMBL; AY040841; AAK84685.1; -; mRNA.
DR EMBL; AK013269; BAB28760.1; -; mRNA.
DR EMBL; AK028401; BAC25933.1; -; mRNA.
DR EMBL; AK028846; BAC26151.1; -; mRNA.
DR EMBL; AK031818; BAC27564.1; -; mRNA.
DR EMBL; BC033279; AAH33279.1; -; mRNA.
DR EMBL; BC050931; AAH50931.1; -; mRNA.
DR CCDS; CCDS21440.1; -.
DR RefSeq; NP_082619.3; NM_028343.4.
DR AlphaFoldDB; Q9CYV5; -.
DR STRING; 10090.ENSMUSP00000042783; -.
DR iPTMnet; Q9CYV5; -.
DR PhosphoSitePlus; Q9CYV5; -.
DR SwissPalm; Q9CYV5; -.
DR EPD; Q9CYV5; -.
DR jPOST; Q9CYV5; -.
DR MaxQB; Q9CYV5; -.
DR PaxDb; Q9CYV5; -.
DR PeptideAtlas; Q9CYV5; -.
DR PRIDE; Q9CYV5; -.
DR ProteomicsDB; 260678; -.
DR Antibodypedia; 31460; 51 antibodies from 19 providers.
DR DNASU; 72759; -.
DR Ensembl; ENSMUST00000041968; ENSMUSP00000042783; ENSMUSG00000039428.
DR GeneID; 72759; -.
DR KEGG; mmu:72759; -.
DR UCSC; uc009ifw.2; mouse.
DR CTD; 65084; -.
DR MGI; MGI:1920009; Tmem135.
DR VEuPathDB; HostDB:ENSMUSG00000039428; -.
DR eggNOG; KOG1398; Eukaryota.
DR GeneTree; ENSGT00390000000303; -.
DR HOGENOM; CLU_046474_0_0_1; -.
DR InParanoid; Q9CYV5; -.
DR OMA; TDKCVNA; -.
DR OrthoDB; 706534at2759; -.
DR PhylomeDB; Q9CYV5; -.
DR TreeFam; TF314580; -.
DR BioGRID-ORCS; 72759; 4 hits in 72 CRISPR screens.
DR ChiTaRS; Tmem135; mouse.
DR PRO; PR:Q9CYV5; -.
DR Proteomes; UP000000589; Chromosome 7.
DR RNAct; Q9CYV5; protein.
DR Bgee; ENSMUSG00000039428; Expressed in epithelium of small intestine and 241 other tissues.
DR ExpressionAtlas; Q9CYV5; baseline and differential.
DR Genevisible; Q9CYV5; MM.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005811; C:lipid droplet; IDA:MGI.
DR GO; GO:0031966; C:mitochondrial membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005739; C:mitochondrion; IDA:UniProtKB.
DR GO; GO:0005778; C:peroxisomal membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005777; C:peroxisome; IDA:UniProtKB.
DR GO; GO:0008340; P:determination of adult lifespan; ISO:MGI.
DR GO; GO:0007031; P:peroxisome organization; ISS:UniProtKB.
DR GO; GO:0010628; P:positive regulation of gene expression; ISO:MGI.
DR GO; GO:0010884; P:positive regulation of lipid storage; ISO:MGI.
DR GO; GO:0010918; P:positive regulation of mitochondrial membrane potential; ISO:MGI.
DR GO; GO:0090140; P:regulation of mitochondrial fission; IMP:UniProtKB.
DR GO; GO:0009409; P:response to cold; IDA:MGI.
DR GO; GO:0032094; P:response to food; IDA:MGI.
DR InterPro; IPR026749; Tmem135.
DR InterPro; IPR031926; TMEM135_N.
DR PANTHER; PTHR12459; PTHR12459; 1.
DR Pfam; PF15982; TMEM135_C_rich; 1.
PE 2: Evidence at transcript level;
KW Membrane; Mitochondrion; Peroxisome; Reference proteome; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..458
FT /note="Transmembrane protein 135"
FT /id="PRO_0000284623"
FT TRANSMEM 68..88
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 96..116
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 149..169
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 298..318
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 331..351
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 377..397
FT /note="Helical"
FT /evidence="ECO:0000255"
FT CONFLICT 167
FT /note="F -> L (in Ref. 2; BAC26151)"
FT /evidence="ECO:0000305"
FT CONFLICT 230
FT /note="V -> E (in Ref. 2; BAC25933)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 458 AA; 52364 MW; 9D3563140233D472 CRC64;
MAALSKSIPH NCYEIGHTWH PSCRVSFLQI TWGALEESLR IYAPLYLIAA VLRKRKLEYY
LYKLLPEILQ SASFLTANGA LYITFFCILR KILGKFYSWT PGFGAALPAS YVAILIERKS
RRGLLTIYMA NLATETLFRM GVARGTITTL RNGEVLLFCI TAAMYMFFFR CKDGLKGFTF
SALRFIVGKE EIPTHSYSPE TAYAKVEQKR EKHKGTPRAM SIIALVRTLV DSVCKHGPRH
RCCKHYEDNC ISYCIKGFIR MFSVGYLIQC CLRIPSAFRH LFTEPSRLLS LFYNKENFQL
GAFLGSFVSI YKGTSCFLRW IRNLDDELHA IVAGFLAGVS MMFYKSTTIS MYLASKLVET
MYFKGIEAGK VPYFPQADTI IYSISTAICF HAAVMEVQNL RPSYWKFLLR LTKGRFALMN
RKALDVFGTG ASREFHNFIP RLDPRYTVVT PELPIDFS
