TM154_MOUSE
ID TM154_MOUSE Reviewed; 181 AA.
AC Q8C4Q9; Q3TB17; Q3TCN6; Q3TD45; Q8CB06;
DT 17-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 115.
DE RecName: Full=Transmembrane protein 154;
DE Flags: Precursor;
GN Name=Tmem154;
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] (ISOFORMS 1 AND 2).
RC STRAIN=C57BL/6J, and NOD; TISSUE=Head, and Vagina;
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] (ISOFORM 1).
RC STRAIN=FVB/N-3; TISSUE=Mammary tumor;
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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-160 AND SER-177, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Mast cell;
RX PubMed=17947660; DOI=10.4049/jimmunol.179.9.5864;
RA Cao L., Yu K., Banh C., Nguyen V., Ritz A., Raphael B.J., Kawakami Y.,
RA Kawakami T., Salomon A.R.;
RT "Quantitative time-resolved phosphoproteomic analysis of mast cell
RT signaling.";
RL J. Immunol. 179:5864-5876(2007).
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass membrane
CC protein {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q8C4Q9-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8C4Q9-2; Sequence=VSP_024546, VSP_024547;
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DR EMBL; AK037111; BAC29708.1; -; mRNA.
DR EMBL; AK081441; BAC38221.1; -; mRNA.
DR EMBL; AK154236; BAE32454.1; -; mRNA.
DR EMBL; AK170385; BAE41759.1; -; mRNA.
DR EMBL; AK170626; BAE41920.1; -; mRNA.
DR EMBL; AK170665; BAE41946.1; -; mRNA.
DR EMBL; AK171510; BAE42497.1; -; mRNA.
DR EMBL; BC096432; AAH96432.1; -; mRNA.
DR EMBL; BC113174; AAI13175.1; -; mRNA.
DR EMBL; BC113175; AAI13176.1; -; mRNA.
DR CCDS; CCDS38467.1; -. [Q8C4Q9-1]
DR RefSeq; NP_796234.1; NM_177260.2. [Q8C4Q9-1]
DR AlphaFoldDB; Q8C4Q9; -.
DR STRING; 10090.ENSMUSP00000103310; -.
DR iPTMnet; Q8C4Q9; -.
DR PhosphoSitePlus; Q8C4Q9; -.
DR EPD; Q8C4Q9; -.
DR MaxQB; Q8C4Q9; -.
DR PaxDb; Q8C4Q9; -.
DR PeptideAtlas; Q8C4Q9; -.
DR PRIDE; Q8C4Q9; -.
DR ProteomicsDB; 259536; -. [Q8C4Q9-1]
DR Antibodypedia; 67855; 44 antibodies from 14 providers.
DR DNASU; 320782; -.
DR Ensembl; ENSMUST00000107682; ENSMUSP00000103310; ENSMUSG00000056498. [Q8C4Q9-1]
DR GeneID; 320782; -.
DR KEGG; mmu:320782; -.
DR UCSC; uc008pqi.1; mouse. [Q8C4Q9-2]
DR UCSC; uc008pqj.1; mouse. [Q8C4Q9-1]
DR CTD; 201799; -.
DR MGI; MGI:2444725; Tmem154.
DR VEuPathDB; HostDB:ENSMUSG00000056498; -.
DR eggNOG; ENOG502SASK; Eukaryota.
DR GeneTree; ENSGT00390000016183; -.
DR HOGENOM; CLU_126881_0_0_1; -.
DR InParanoid; Q8C4Q9; -.
DR OMA; MNRSADC; -.
DR OrthoDB; 1505523at2759; -.
DR PhylomeDB; Q8C4Q9; -.
DR TreeFam; TF336891; -.
DR BioGRID-ORCS; 320782; 3 hits in 72 CRISPR screens.
DR ChiTaRS; Tmem154; mouse.
DR PRO; PR:Q8C4Q9; -.
DR Proteomes; UP000000589; Chromosome 3.
DR RNAct; Q8C4Q9; protein.
DR Bgee; ENSMUSG00000056498; Expressed in granulocyte and 78 other tissues.
DR Genevisible; Q8C4Q9; MM.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR InterPro; IPR028064; TMEM154.
DR Pfam; PF15102; TMEM154; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Membrane; Phosphoprotein; Reference proteome; Signal;
KW Transmembrane; Transmembrane helix.
FT SIGNAL 1..22
FT /evidence="ECO:0000255"
FT CHAIN 23..181
FT /note="Transmembrane protein 154"
FT /id="PRO_0000284504"
FT TOPO_DOM 23..74
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 75..95
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 96..181
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 19..47
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 103..122
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 161..181
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 103..121
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 162..181
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 160
FT /note="Phosphotyrosine"
FT /evidence="ECO:0007744|PubMed:17947660"
FT MOD_RES 177
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17947660"
FT VAR_SEQ 120..121
FT /note="HE -> RE (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_024546"
FT VAR_SEQ 122..181
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_024547"
FT CONFLICT 105
FT /note="K -> E (in Ref. 1; BAC29708)"
FT /evidence="ECO:0000305"
FT CONFLICT 121
FT /note="E -> G (in Ref. 1; BAE41759)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 181 AA; 19879 MW; 39BFCB1F1A9B2744 CRC64;
MTVPCAALVL ALGLAFGQSS QGNDEESEYS GQSITEEENS EDETTRSALA TVTTEALAEN
VNSTHTNDTS NQVEFILMVA IPLAALLILL FMVLIATYFK SKRPKQEPSS QGSQSALQTH
ELGGETLKVP IFEEDTPSVM EIEMEELDKW MNSMNRNADY ECLPTLKEEK EPNPSPSDNE
S
