TRML1_MOUSE
ID TRML1_MOUSE Reviewed; 317 AA.
AC Q8K558; B2RRH0; Q9D3N6;
DT 17-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 17-OCT-2006, sequence version 2.
DT 03-AUG-2022, entry version 120.
DE RecName: Full=Trem-like transcript 1 protein;
DE Short=TLT-1;
DE AltName: Full=Triggering receptor expressed on myeloid cells-like protein 1;
DE Flags: Precursor;
GN Name=Treml1; Synonyms=Tlt1;
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] (ISOFORMS 1 AND 2), FUNCTION, PHOSPHORYLATION,
RP INTERACTION WITH PTPN6, AND TISSUE SPECIFICITY.
RC STRAIN=C57BL/6J; TISSUE=Bone marrow;
RX PubMed=12393607; DOI=10.1182/blood-2002-02-0523;
RA Washington A.V., Quigley L., McVicar D.W.;
RT "Initial characterization of TREM-like transcript (TLT)-1: a putative
RT inhibitory receptor within the TREM cluster.";
RL Blood 100:3822-3824(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=C57BL/6J; TISSUE=Head;
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] (ISOFORM 1).
RC 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).
RN [4]
RP SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=15100151; DOI=10.1182/blood-2004-01-0315;
RA Washington A.V., Schubert R.L., Quigley L., Disipio T., Feltz R., Cho E.H.,
RA McVicar D.W.;
RT "A TREM family member, TLT-1, is found exclusively in the alpha-granules of
RT megakaryocytes and platelets.";
RL Blood 104:1042-1047(2004).
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT "Large-scale phosphorylation analysis of mouse liver.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-283, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Lung, and Spleen;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: Cell surface receptor that may play a role in the innate and
CC adaptive immune response. {ECO:0000269|PubMed:12393607}.
CC -!- SUBUNIT: When phosphorylated, interacts with PTPN11 (By similarity).
CC When phosphorylated, interacts with PTPN6. {ECO:0000250,
CC ECO:0000269|PubMed:12393607}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:15100151};
CC Single-pass type I membrane protein {ECO:0000269|PubMed:15100151}.
CC Cytoplasm {ECO:0000269|PubMed:15100151}. Note=Sequestered in
CC cytoplasmic vesicles in resting platelets. Transported to the cell
CC surface after stimulation by thrombin. Soluble fragments can be
CC released into the serum by proteolysis. {ECO:0000250|UniProtKB:Q86YW5}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q8K558-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8K558-2; Sequence=VSP_021127;
CC -!- TISSUE SPECIFICITY: Highly expressed in bone marrow leukocytes, splenic
CC megakaryocytes and platelets. Detected in brain, liver and in
CC peritoneal monocytes. {ECO:0000269|PubMed:12393607,
CC ECO:0000269|PubMed:15100151}.
CC -!- PTM: Phosphorylated on tyrosine residues.
CC {ECO:0000269|PubMed:12393607}.
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DR EMBL; AY078502; AAL85488.1; -; mRNA.
DR EMBL; AY286071; AAP33393.1; -; mRNA.
DR EMBL; AK017256; BAB30655.1; -; mRNA.
DR EMBL; BC138399; AAI38400.1; -; mRNA.
DR CCDS; CCDS28866.1; -. [Q8K558-2]
DR CCDS; CCDS89114.1; -. [Q8K558-1]
DR RefSeq; NP_001276380.1; NM_001289451.1.
DR RefSeq; NP_001276386.1; NM_001289457.1. [Q8K558-1]
DR RefSeq; NP_082039.1; NM_027763.2. [Q8K558-2]
DR AlphaFoldDB; Q8K558; -.
DR SMR; Q8K558; -.
DR BioGRID; 214639; 1.
DR IntAct; Q8K558; 1.
DR MINT; Q8K558; -.
DR STRING; 10090.ENSMUSP00000024792; -.
DR iPTMnet; Q8K558; -.
DR PhosphoSitePlus; Q8K558; -.
DR CPTAC; non-CPTAC-3886; -.
DR MaxQB; Q8K558; -.
DR PaxDb; Q8K558; -.
DR PeptideAtlas; Q8K558; -.
DR PRIDE; Q8K558; -.
DR ProteomicsDB; 298234; -. [Q8K558-1]
DR ProteomicsDB; 298235; -. [Q8K558-2]
DR Antibodypedia; 2655; 289 antibodies from 31 providers.
DR DNASU; 71326; -.
DR Ensembl; ENSMUST00000024792; ENSMUSP00000024792; ENSMUSG00000023993. [Q8K558-1]
DR Ensembl; ENSMUST00000224001; ENSMUSP00000153300; ENSMUSG00000023993. [Q8K558-2]
DR GeneID; 71326; -.
DR KEGG; mmu:71326; -.
DR UCSC; uc008cxm.2; mouse. [Q8K558-2]
DR UCSC; uc008cxn.2; mouse. [Q8K558-1]
DR CTD; 340205; -.
DR MGI; MGI:1918576; Treml1.
DR VEuPathDB; HostDB:ENSMUSG00000023993; -.
DR eggNOG; ENOG502SRZV; Eukaryota.
DR GeneTree; ENSGT00470000042300; -.
DR HOGENOM; CLU_077694_1_0_1; -.
DR InParanoid; Q8K558; -.
DR OMA; IQVQCHY; -.
DR OrthoDB; 1390184at2759; -.
DR PhylomeDB; Q8K558; -.
DR TreeFam; TF337145; -.
DR Reactome; R-MMU-198933; Immunoregulatory interactions between a Lymphoid and a non-Lymphoid cell.
DR BioGRID-ORCS; 71326; 1 hit in 71 CRISPR screens.
DR PRO; PR:Q8K558; -.
DR Proteomes; UP000000589; Chromosome 17.
DR RNAct; Q8K558; protein.
DR Bgee; ENSMUSG00000023993; Expressed in bone marrow and 28 other tissues.
DR ExpressionAtlas; Q8K558; baseline and differential.
DR Genevisible; Q8K558; MM.
DR GO; GO:0009986; C:cell surface; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0005794; C:Golgi apparatus; ISO:MGI.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0016607; C:nuclear speck; ISO:MGI.
DR GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR GO; GO:0031091; C:platelet alpha granule; IDA:UniProtKB.
DR GO; GO:0038023; F:signaling receptor activity; TAS:MGI.
DR GO; GO:0004888; F:transmembrane signaling receptor activity; IBA:GO_Central.
DR GO; GO:0019722; P:calcium-mediated signaling; ISO:MGI.
DR GO; GO:0009968; P:negative regulation of signal transduction; TAS:MGI.
DR GO; GO:0030168; P:platelet activation; IEP:UniProtKB.
DR GO; GO:0042060; P:wound healing; NAS:UniProtKB.
DR Gene3D; 2.60.40.10; -; 1.
DR InterPro; IPR036179; Ig-like_dom_sf.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR003599; Ig_sub.
DR SMART; SM00409; IG; 1.
DR SUPFAM; SSF48726; SSF48726; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cell membrane; Cytoplasm; Disulfide bond;
KW Immunoglobulin domain; Lipoprotein; Membrane; Palmitate; Phosphoprotein;
KW Receptor; Reference proteome; Signal; Transmembrane; Transmembrane helix.
FT SIGNAL 1..20
FT /evidence="ECO:0000255"
FT CHAIN 21..317
FT /note="Trem-like transcript 1 protein"
FT /id="PRO_0000253856"
FT TOPO_DOM 21..175
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 176..196
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 197..317
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 21..122
FT /note="Ig-like V-type"
FT REGION 147..166
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 212..278
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 295..317
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 284..289
FT /note="ITIM"
FT COMPBIAS 260..275
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 283
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT LIPID 208
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000250"
FT DISULFID 39..105
FT /evidence="ECO:0000250"
FT DISULFID 53..60
FT /evidence="ECO:0000250"
FT VAR_SEQ 173
FT /note="S -> RCQKQC (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:12393607"
FT /id="VSP_021127"
SQ SEQUENCE 317 AA; 33522 MW; 097E16B34D03E87B CRC64;
MDCYLLLLLL LLGLAGQGSA DSHPEVLQAP VGSSILVQCH YRLQDVRALK VWCQFLQEGC
HPLVTSAVDR RAPGNGRIFL TDLGGGLLQV EMVTLQEEDT GEYGCVVEGA AGPQTLHRVS
LLVLPPVPGP REGEEAEDEK ETYRIGTGSL LEDPSLDPSA SAGPHEFRRR ENSIPLIWGA
VLLLALVVVA VVIFAVMARK KGNRLVVCGP SQSTGVPGMD PPSAAHRSSD SGLPSDIPHV
RLDSPPSFDS IYTGSSLDPP SSEPPAPPSQ PPLPPKVLMS SKSVTYATVV FPGGDKGKIA
SCEPVQDPPN SQTPPSK
