TMM98_MOUSE
ID TMM98_MOUSE Reviewed; 226 AA.
AC Q91X86;
DT 03-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 127.
DE RecName: Full=Transmembrane protein 98;
GN Name=Tmem98;
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=NOD; TISSUE=Thymus;
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].
RC STRAIN=FVB/N; TISSUE=Liver;
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 FUNCTION, TISSUE SPECIFICITY, AND SUBCELLULAR LOCATION.
RX PubMed=25946230; DOI=10.1089/jir.2014.0110;
RA Fu W., Cheng Y., Zhang Y., Mo X., Li T., Liu Y., Wang P., Pan W., Chen Y.,
RA Xue Y., Ma D., Zhang Y., Han W.;
RT "The Secreted Form of Transmembrane Protein 98 Promotes the Differentiation
RT of T Helper 1 Cells.";
RL J. Interferon Cytokine Res. 35:720-733(2015).
RN [5]
RP FUNCTION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, SUBCELLULAR LOCATION,
RP AND INTERACTION WITH MYRF.
RX PubMed=30249802; DOI=10.1523/jneurosci.0154-18.2018;
RA Huang H., Teng P., Du J., Meng J., Hu X., Tang T., Zhang Z., Qi Y.B.,
RA Qiu M.;
RT "Interactive Repression of MYRF Self-Cleavage and Activity in
RT Oligodendrocyte Differentiation by TMEM98 Protein.";
RL J. Neurosci. 38:9829-9839(2018).
CC -!- FUNCTION: Functions as a negative regulator of MYRF in oligodendrocyte
CC differentiation and myelination. Interacts with the C-terminal of MYRF
CC inhibiting MYRF self-cleavage and N-fragment nuclear translocation
CC (PubMed:25946230). The secreted form promotes differentiation of T
CC helper 1 cells (Th1) (PubMed:25946230). {ECO:0000269|PubMed:25946230}.
CC -!- SUBUNIT: Interacts (via N-terminal region) with MYRF; the interaction
CC inhibits MYRF self-cleavage. {ECO:0000269|PubMed:30249802}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000305|PubMed:30249802}; Single-pass type II membrane protein
CC {ECO:0000250|UniProtKB:Q9Y2Y6}. Cell membrane
CC {ECO:0000250|UniProtKB:Q9Y2Y6}; Single-pass type II membrane protein
CC {ECO:0000250|UniProtKB:Q9Y2Y6}. Secreted {ECO:0000269|PubMed:25946230}.
CC Secreted, extracellular exosome {ECO:0000250|UniProtKB:Q9Y2Y6}.
CC Note=Secreted by exosomes through a non-classical pathway.
CC {ECO:0000250|UniProtKB:Q9Y2Y6}.
CC -!- TISSUE SPECIFICITY: Expressed in differentiated oligodendrocytes in
CC early postanatal central nervous system tissues (PubMed:30249802).
CC Expressed by CD4(+) T cells, the expression increases upon activation
CC (at protein level) (PubMed:25946230). {ECO:0000269|PubMed:25946230,
CC ECO:0000269|PubMed:30249802}.
CC -!- DEVELOPMENTAL STAGE: In the spinal cord region, expression is initially
CC detected in the ventral white matter at 18.5 dpc, up-regulates rapidly
CC afterward, and peaks at early postnatal stages from P4 to P7. At P15,
CC expression starts to be detected in the gray matter of spinal cord but
CC gradually disappears thereafter. Also observed in corpus callosum and
CC the white matter of cerebellum at P15 stages.
CC {ECO:0000269|PubMed:30249802}.
CC -!- SIMILARITY: Belongs to the TMEM98 family. {ECO:0000305}.
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DR EMBL; AK153960; BAE32282.1; -; mRNA.
DR EMBL; AL663054; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC011208; AAH11208.1; -; mRNA.
DR CCDS; CCDS25135.1; -.
DR RefSeq; NP_083813.1; NM_029537.1.
DR AlphaFoldDB; Q91X86; -.
DR SMR; Q91X86; -.
DR STRING; 10090.ENSMUSP00000042825; -.
DR iPTMnet; Q91X86; -.
DR PhosphoSitePlus; Q91X86; -.
DR SwissPalm; Q91X86; -.
DR MaxQB; Q91X86; -.
DR PaxDb; Q91X86; -.
DR PeptideAtlas; Q91X86; -.
DR PRIDE; Q91X86; -.
DR ProteomicsDB; 259265; -.
DR Antibodypedia; 52106; 46 antibodies from 13 providers.
DR Ensembl; ENSMUST00000040865; ENSMUSP00000042825; ENSMUSG00000035413.
DR GeneID; 103743; -.
DR KEGG; mmu:103743; -.
DR UCSC; uc007kmj.1; mouse.
DR CTD; 26022; -.
DR MGI; MGI:1923457; Tmem98.
DR VEuPathDB; HostDB:ENSMUSG00000035413; -.
DR eggNOG; ENOG502QT8U; Eukaryota.
DR GeneTree; ENSGT00390000012062; -.
DR HOGENOM; CLU_084317_0_0_1; -.
DR InParanoid; Q91X86; -.
DR OMA; RHRYCRP; -.
DR OrthoDB; 1413051at2759; -.
DR PhylomeDB; Q91X86; -.
DR TreeFam; TF336444; -.
DR BioGRID-ORCS; 103743; 0 hits in 72 CRISPR screens.
DR ChiTaRS; Tmem98; mouse.
DR PRO; PR:Q91X86; -.
DR Proteomes; UP000000589; Chromosome 11.
DR RNAct; Q91X86; protein.
DR Bgee; ENSMUSG00000035413; Expressed in pigmented layer of retina and 230 other tissues.
DR Genevisible; Q91X86; MM.
DR GO; GO:0005783; C:endoplasmic reticulum; ISO:MGI.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IDA:UniProtKB.
DR GO; GO:0070062; C:extracellular exosome; ISS:UniProtKB.
DR GO; GO:0005615; C:extracellular space; IDA:UniProtKB.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR GO; GO:0031642; P:negative regulation of myelination; IMP:UniProtKB.
DR GO; GO:0048715; P:negative regulation of oligodendrocyte differentiation; IMP:UniProtKB.
DR GO; GO:1900181; P:negative regulation of protein localization to nucleus; IDA:UniProtKB.
DR GO; GO:0010955; P:negative regulation of protein processing; IDA:UniProtKB.
DR GO; GO:0045063; P:T-helper 1 cell differentiation; IDA:UniProtKB.
DR InterPro; IPR029668; TMEM98.
DR PANTHER; PTHR32510; PTHR32510; 1.
PE 1: Evidence at protein level;
KW Cell membrane; Endoplasmic reticulum; Membrane; Reference proteome;
KW Secreted; Transmembrane; Transmembrane helix.
FT CHAIN 1..226
FT /note="Transmembrane protein 98"
FT /id="PRO_0000251712"
FT TOPO_DOM 1..3
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:Q9Y2Y6"
FT TRANSMEM 4..24
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 25..226
FT /note="Extracellular"
FT /evidence="ECO:0000250|UniProtKB:Q9Y2Y6"
FT REGION 1..88
FT /note="Required for interaction with MYRF"
FT /evidence="ECO:0000269|PubMed:30249802"
FT REGION 207..226
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 226 AA; 24684 MW; 5F4FC338DA6598D9 CRC64;
METVVIVAIG VLATIFLASF AALVVVCRQR YCRPRDLLQR YDSKPIVDLI GAMETQSEPS
ELELDDVVIT NPHIEAILEN EDWIEDASGL MSHCIAILKI CHTLTEKLVA MTMGSGAKMK
TSASVSDIIV VAKRISPRVD DVVKSMYPPL DPKLLDARTT ALLLSVSHLV LVTRNACHLT
GGLDWIDQSL SAAEEHLEVL REAALASEPD KSLPNPEGFL QEQSAI
