TM198_MOUSE
ID TM198_MOUSE Reviewed; 360 AA.
AC Q8BG75;
DT 18-MAR-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 116.
DE RecName: Full=Transmembrane protein 198;
GN Name=Tmem198;
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, Hypothalamus, and Visual cortex;
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).
CC -!- FUNCTION: Promotes LRP6 phosphorylation by casein kinases and thereby
CC plays a role in Wnt signaling. May be a membrane scaffold protein
CC involved in the self-aggregation of LRP6 to further enhance its
CC activity (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Interacts with LRP6. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane
CC protein {ECO:0000305}. Cell membrane {ECO:0000250}. Cytoplasmic vesicle
CC {ECO:0000250}. Note=Largely located to vesicle-like structures.
CC {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the TMEM198 family. {ECO:0000305}.
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DR EMBL; BC059868; AAH59868.1; -; mRNA.
DR EMBL; AK038957; BAC30183.1; -; mRNA.
DR EMBL; AK082334; BAC38470.1; -; mRNA.
DR EMBL; AK158863; BAE34699.1; -; mRNA.
DR CCDS; CCDS15076.1; -.
DR RefSeq; NP_796030.1; NM_177056.4.
DR AlphaFoldDB; Q8BG75; -.
DR STRING; 10090.ENSMUSP00000109205; -.
DR iPTMnet; Q8BG75; -.
DR PhosphoSitePlus; Q8BG75; -.
DR PaxDb; Q8BG75; -.
DR PeptideAtlas; Q8BG75; -.
DR PRIDE; Q8BG75; -.
DR ProteomicsDB; 260684; -.
DR Antibodypedia; 56764; 8 antibodies from 4 providers.
DR Ensembl; ENSMUST00000050899; ENSMUSP00000057865; ENSMUSG00000051703.
DR Ensembl; ENSMUST00000113575; ENSMUSP00000109205; ENSMUSG00000051703.
DR GeneID; 319998; -.
DR KEGG; mmu:319998; -.
DR UCSC; uc007bpl.2; mouse.
DR CTD; 130612; -.
DR MGI; MGI:2443133; Tmem198.
DR VEuPathDB; HostDB:ENSMUSG00000051703; -.
DR eggNOG; ENOG502QS1E; Eukaryota.
DR GeneTree; ENSGT00390000016940; -.
DR HOGENOM; CLU_043600_0_0_1; -.
DR InParanoid; Q8BG75; -.
DR OMA; CWLTWVV; -.
DR OrthoDB; 1509246at2759; -.
DR PhylomeDB; Q8BG75; -.
DR TreeFam; TF323324; -.
DR BioGRID-ORCS; 319998; 2 hits in 75 CRISPR screens.
DR PRO; PR:Q8BG75; -.
DR Proteomes; UP000000589; Chromosome 1.
DR RNAct; Q8BG75; protein.
DR Bgee; ENSMUSG00000051703; Expressed in visual cortex and 143 other tissues.
DR ExpressionAtlas; Q8BG75; baseline and differential.
DR Genevisible; Q8BG75; MM.
DR GO; GO:0031410; C:cytoplasmic vesicle; ISO:MGI.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR GO; GO:0090263; P:positive regulation of canonical Wnt signaling pathway; ISO:MGI.
DR GO; GO:0016055; P:Wnt signaling pathway; IEA:UniProtKB-KW.
DR InterPro; IPR025256; DUF4203.
DR InterPro; IPR040236; TMEM198.
DR PANTHER; PTHR31247; PTHR31247; 1.
DR Pfam; PF13886; DUF4203; 1.
PE 2: Evidence at transcript level;
KW Cell membrane; Cytoplasmic vesicle; Developmental protein; Membrane;
KW Reference proteome; Transmembrane; Transmembrane helix;
KW Wnt signaling pathway.
FT CHAIN 1..360
FT /note="Transmembrane protein 198"
FT /id="PRO_0000326031"
FT TRANSMEM 36..56
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 59..79
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 93..113
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 116..136
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 145..165
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 177..197
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 218..238
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 260..302
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 316..360
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 282..299
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 316..339
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 360 AA; 39752 MW; BAA607299E462B8C CRC64;
MPGTMETLRF QLLPPEPDDT FWGAPCEQPL ERRYQALPAL VCIMCCLFGV VYCFFGYRCF
KAVLFLTGLL FGSVVIFLLC YRERVLETQL SAGASAGIAL GIGLLCGLVA MLVRSVGLFL
VGLLLGLLLA AAALLGSAPY YQPGSVWGPL GLLLGGGLLC ALLTLRWPRP LTTLATAVTG
AALIATAADY FAELLLLGRY VVERLRAAPV PPLCWRSWAL LALWPLLSLM GVLVQWRVTT
ERDSHTEVVI SRQRRRVQLM RIRQQEERKE KRRKKRPPRA PPRGPRAPPR PGPPDPAYRR
RPVPIKRFNG DVLSPSYIQS FRDRQTGSSL SSFMASPTDT DYEYGSRGPL TACSGPPVRV
