TREM1_HUMAN
ID TREM1_HUMAN Reviewed; 234 AA.
AC Q9NP99; B4DWG2; K7EJW1; Q53FL8; Q5T2C9; Q86YU1;
DT 19-JUL-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 175.
DE RecName: Full=Triggering receptor expressed on myeloid cells 1;
DE Short=TREM-1;
DE AltName: Full=Triggering receptor expressed on monocytes 1;
DE AltName: CD_antigen=CD354;
DE Flags: Precursor;
GN Name=TREM1;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION (ISOFORM 1), INDUCTION,
RP TISSUE SPECIFICITY, GLYCOSYLATION, AND INTERACTION WITH TYROBP/DAP12.
RC TISSUE=Monocyte, and Neutrophil;
RX PubMed=10799849; DOI=10.4049/jimmunol.164.10.4991;
RA Bouchon A., Dietrich J., Colonna M.;
RT "Inflammatory responses can be triggered by TREM-1, a novel receptor
RT expressed on neutrophils and monocytes.";
RL J. Immunol. 164:4991-4995(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), AND TISSUE SPECIFICITY.
RX PubMed=11922939; DOI=10.1016/s0161-5890(02)00004-4;
RA Gingras M.-C., Lapillonne H., Margolin J.F.;
RT "TREM-1, MDL-1, and DAP12 expression is associated with a mature stage of
RT myeloid development.";
RL Mol. Immunol. 38:817-824(2002).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
RA Begum N.A., Seya T.;
RT "Identification of a soluble form of TREM1 (sTREM1) from dendritic cells.";
RL Submitted (JAN-2002) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Synovium;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=14574404; DOI=10.1038/nature02055;
RA Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L.,
RA Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R.,
RA Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D.,
RA Andrews T.D., Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J.,
RA Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H.,
RA Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J.,
RA Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P.,
RA Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V.,
RA Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J.,
RA Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E.,
RA Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J.,
RA French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J.,
RA Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C.,
RA Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A.,
RA Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R.,
RA Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M.,
RA Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K.,
RA Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R.,
RA Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M.,
RA Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A.,
RA Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L.,
RA Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I.,
RA Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y.,
RA Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E.,
RA Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A.,
RA Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W.,
RA Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M.,
RA West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J.,
RA Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M.,
RA Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I.,
RA Rogers J., Beck S.;
RT "The DNA sequence and analysis of human chromosome 6.";
RL Nature 425:805-811(2003).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Lung;
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 [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-200, AND VARIANT SER-25.
RC TISSUE=Synovial cell;
RA Suzuki Y., Sugano S., Totoki Y., Toyoda A., Takeda T., Sakaki Y.,
RA Tanaka A., Yokoyama S.;
RL Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases.
RN [8]
RP FUNCTION.
RX PubMed=11323674; DOI=10.1038/35074114;
RA Bouchon A., Facchetti F., Weigand M.A., Colonna M.;
RT "TREM-1 amplifies inflammation and is a crucial mediator of septic shock.";
RL Nature 410:1103-1107(2001).
RN [9]
RP FUNCTION (ISOFORM 1).
RX PubMed=17568691; DOI=10.1016/j.imlet.2007.04.011;
RA El Mezayen R., El Gazzar M., Seeds M.C., McCall C.E., Dreskin S.C.,
RA Nicolls M.R.;
RT "Endogenous signals released from necrotic cells augment inflammatory
RT responses to bacterial endotoxin.";
RL Immunol. Lett. 111:36-44(2007).
RN [10]
RP FUNCTION (ISOFORM 1), INTERACTION WITH TLR4, AND SUBCELLULAR LOCATION
RP (ISOFORM 1).
RX PubMed=17098818; DOI=10.1093/intimm/dxl119;
RA Fortin C.F., Lesur O., Fulop T. Jr.;
RT "Effects of TREM-1 activation in human neutrophils: activation of signaling
RT pathways, recruitment into lipid rafts and association with TLR4.";
RL Int. Immunol. 19:41-50(2007).
RN [11]
RP FUNCTION (ISOFORM 1).
RX PubMed=21659545; DOI=10.1182/blood-2010-11-317016;
RA Ormsby T., Schlecker E., Ferdin J., Tessarz A.S., Angelisova P.,
RA Koepruelue A.D., Borte M., Warnatz K., Schulze I., Ellmeier W., Horejsi V.,
RA Cerwenka A.;
RT "Btk is a positive regulator in the TREM-1/DAP12 signaling pathway.";
RL Blood 118:936-945(2011).
RN [12]
RP FUNCTION (ISOFORM 1), SUBCELLULAR LOCATION (ISOFORM 1), AND INTERACTION
RP WITH TLR4.
RX PubMed=21393102; DOI=10.1684/ecn.2011.0274;
RA Arts R.J., Joosten L.A., Dinarello C.A., Kullberg B.J., van der Meer J.W.,
RA Netea M.G.;
RT "TREM-1 interaction with the LPS/TLR4 receptor complex.";
RL Eur. Cytokine Netw. 22:11-14(2011).
RN [13]
RP INTERACTION WITH PGLYRP1, AND FUNCTION (ISOFORM 1).
RX PubMed=25595774; DOI=10.4049/jimmunol.1402303;
RA Read C.B., Kuijper J.L., Hjorth S.A., Heipel M.D., Tang X., Fleetwood A.J.,
RA Dantzler J.L., Grell S.N., Kastrup J., Wang C., Brandt C.S., Hansen A.J.,
RA Wagtmann N.R., Xu W., Stennicke V.W.;
RT "Cutting Edge: identification of neutrophil PGLYRP1 as a ligand for TREM-
RT 1.";
RL J. Immunol. 194:1417-1421(2015).
RN [14]
RP FUNCTION (ISOFORM 2), AND SUBCELLULAR LOCATION (ISOFORM 2).
RX PubMed=26561551; DOI=10.4049/jimmunol.1402713;
RA Baruah S., Keck K., Vrenios M., Pope M.R., Pearl M., Doerschug K.,
RA Klesney-Tait J.;
RT "Identification of a Novel Splice Variant Isoform of TREM-1 in Human
RT Neutrophil Granules.";
RL J. Immunol. 195:5725-5731(2015).
RN [15]
RP FUNCTION (ISOFORM 1), AND SUBUNIT.
RX PubMed=29568119; DOI=10.1038/s41423-018-0003-5;
RA Carrasco K., Boufenzer A., Jolly L., Le Cordier H., Wang G., Heck A.J.,
RA Cerwenka A., Vinolo E., Nazabal A., Kriznik A., Launay P., Gibot S.,
RA Derive M.;
RT "TREM-1 multimerization is essential for its activation on monocytes and
RT neutrophils.";
RL Cell. Mol. Immunol. 16:460-472(2019).
RN [16]
RP X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF 17-134, AND DISULFIDE BOND.
RX PubMed=14656437; DOI=10.1016/j.str.2003.11.001;
RA Radaev S., Kattah M., Rostro B., Colonna M., Sun P.D.;
RT "Crystal structure of the human myeloid cell activating receptor TREM-1.";
RL Structure 11:1527-1535(2003).
RN [17]
RP X-RAY CRYSTALLOGRAPHY (1.47 ANGSTROMS) OF 21-139, SUBUNIT, AND DISULFIDE
RP BOND.
RX PubMed=15351648; DOI=10.1016/j.jmb.2004.07.089;
RA Kelker M.S., Foss T.R., Peti W., Teyton L., Kelly J.W., Wuethrich K.,
RA Wilson I.A.;
RT "Crystal structure of human triggering receptor expressed on myeloid cells
RT 1 (TREM-1) at 1.47 A.";
RL J. Mol. Biol. 342:1237-1248(2004).
RN [18]
RP VARIANT [LARGE SCALE ANALYSIS] SER-97.
RX PubMed=16959974; DOI=10.1126/science.1133427;
RA Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D.,
RA Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P.,
RA Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V.,
RA Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H.,
RA Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W.,
RA Velculescu V.E.;
RT "The consensus coding sequences of human breast and colorectal cancers.";
RL Science 314:268-274(2006).
CC -!- FUNCTION: [Isoform 1]: Cell surface receptor that plays important roles
CC in innate and adaptive immunity by amplifying inflammatory responses
CC (PubMed:10799849, PubMed:21393102). Upon activation by various ligands
CC such as PGLYRP1, HMGB1 or HSP70, multimerizes and forms a complex with
CC transmembrane adapter TYROBP/DAP12 (PubMed:25595774, PubMed:17568691,
CC PubMed:29568119). In turn, initiates a SYK-mediated cascade of tyrosine
CC phosphorylation, activating multiple downstream mediators such as BTK,
CC MAPK1, MAPK3 or phospholipase C-gamma (PubMed:21659545,
CC PubMed:14656437). This cascade promotes the neutrophil- and macrophage-
CC mediated release of pro-inflammatory cytokines and/or chemokines, as
CC well as their migration and thereby amplifies inflammatory responses
CC that are triggered by bacterial and fungal infections (PubMed:17568691,
CC PubMed:17098818). By also promoting the amplification of inflammatory
CC signals that are initially triggered by Toll-like receptor (TLR) and
CC NOD-like receptor engagement, plays a major role in the pathophysiology
CC of acute and chronic inflammatory diseases of different etiologies
CC including septic shock and atherosclerosis (PubMed:21393102,
CC PubMed:11323674). {ECO:0000269|PubMed:10799849,
CC ECO:0000269|PubMed:11323674, ECO:0000269|PubMed:14656437,
CC ECO:0000269|PubMed:17098818, ECO:0000269|PubMed:17568691,
CC ECO:0000269|PubMed:21393102, ECO:0000269|PubMed:21659545,
CC ECO:0000269|PubMed:25595774, ECO:0000269|PubMed:29568119}.
CC -!- FUNCTION: [Isoform 2]: Acts as a decoy receptor, counterbalancing TREM1
CC pro-inflammatory activity through the neutralization of its lignad.
CC {ECO:0000269|PubMed:26561551}.
CC -!- SUBUNIT: Monomer (PubMed:29568119). Homomultimer; when activated
CC (PubMed:29568119). Interacts with TYROBP/DAP12 (PubMed:10799849,
CC PubMed:15351648). Interacts with TLR4 (PubMed:17098818,
CC PubMed:21393102). {ECO:0000269|PubMed:10799849,
CC ECO:0000269|PubMed:15351648, ECO:0000269|PubMed:17098818,
CC ECO:0000269|PubMed:21393102, ECO:0000269|PubMed:29568119}.
CC -!- SUBCELLULAR LOCATION: [Isoform 1]: Cell membrane
CC {ECO:0000269|PubMed:17098818, ECO:0000269|PubMed:21393102}; Single-pass
CC type I membrane protein {ECO:0000305}. Note=Recruited to lipid rafts
CC when activated. {ECO:0000269|PubMed:17098818}.
CC -!- SUBCELLULAR LOCATION: [Isoform 2]: Secreted
CC {ECO:0000269|PubMed:26561551}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q9NP99-1; Sequence=Displayed;
CC Name=2; Synonyms=TREM-1sv, sTREM1;
CC IsoId=Q9NP99-2; Sequence=VSP_010790, VSP_010791;
CC Name=3;
CC IsoId=Q9NP99-3; Sequence=VSP_053939;
CC -!- TISSUE SPECIFICITY: Mostly expressed by immune cells of the myeloid
CC lineage, such as monocytes, macrophages, neutrophils and dendritic
CC cells (PubMed:10799849). Expression is associated with a mature stage
CC of myeloid development (PubMed:11922939). Highly expressed in adult
CC liver, lung and spleen than in corresponding fetal tissue. Also
CC expressed in the lymph node, placenta, spinal cord and heart tissues.
CC Isoform 2 was detected in the lung, liver and mature monocytes.
CC {ECO:0000269|PubMed:10799849, ECO:0000269|PubMed:11922939,
CC ECO:0000269|PubMed:21393102}.
CC -!- INDUCTION: Up-regulated by bacteria, fungi and bacterial
CC lipopolysaccharides (LPS). {ECO:0000269|PubMed:10799849}.
CC -!- PTM: Glycosylated. {ECO:0000269|PubMed:10799849}.
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DR EMBL; AF196329; AAF71694.1; -; mRNA.
DR EMBL; AF287008; AAF90197.1; -; mRNA.
DR EMBL; AY074783; AAL74018.1; -; mRNA.
DR EMBL; AK301519; BAG63024.1; -; mRNA.
DR EMBL; AL391903; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC017773; AAH17773.1; -; mRNA.
DR EMBL; AK223264; BAD96984.1; -; mRNA.
DR CCDS; CCDS4854.1; -. [Q9NP99-1]
DR CCDS; CCDS56427.1; -. [Q9NP99-2]
DR CCDS; CCDS59499.1; -. [Q9NP99-3]
DR RefSeq; NP_001229518.1; NM_001242589.2. [Q9NP99-3]
DR RefSeq; NP_001229519.1; NM_001242590.2. [Q9NP99-2]
DR RefSeq; NP_061113.1; NM_018643.4. [Q9NP99-1]
DR RefSeq; XP_016866445.1; XM_017010956.1. [Q9NP99-1]
DR RefSeq; XP_016866446.1; XM_017010957.1. [Q9NP99-2]
DR PDB; 1Q8M; X-ray; 2.60 A; A/B/C/D=17-134.
DR PDB; 1SMO; X-ray; 1.47 A; A/B=21-139.
DR PDBsum; 1Q8M; -.
DR PDBsum; 1SMO; -.
DR AlphaFoldDB; Q9NP99; -.
DR SMR; Q9NP99; -.
DR BioGRID; 119926; 17.
DR IntAct; Q9NP99; 3.
DR STRING; 9606.ENSP00000244709; -.
DR ChEMBL; CHEMBL1697674; -.
DR DrugBank; DB01694; D-tartaric acid.
DR GlyGen; Q9NP99; 3 sites.
DR iPTMnet; Q9NP99; -.
DR PhosphoSitePlus; Q9NP99; -.
DR BioMuta; TREM1; -.
DR DMDM; 50401685; -.
DR jPOST; Q9NP99; -.
DR MassIVE; Q9NP99; -.
DR PaxDb; Q9NP99; -.
DR PeptideAtlas; Q9NP99; -.
DR PRIDE; Q9NP99; -.
DR ProteomicsDB; 81942; -. [Q9NP99-1]
DR ProteomicsDB; 81943; -. [Q9NP99-2]
DR Antibodypedia; 1616; 710 antibodies from 40 providers.
DR DNASU; 54210; -.
DR Ensembl; ENST00000244709.9; ENSP00000244709.3; ENSG00000124731.13. [Q9NP99-1]
DR Ensembl; ENST00000334475.10; ENSP00000334284.5; ENSG00000124731.13. [Q9NP99-2]
DR Ensembl; ENST00000591620.1; ENSP00000465345.1; ENSG00000124731.13. [Q9NP99-3]
DR GeneID; 54210; -.
DR KEGG; hsa:54210; -.
DR MANE-Select; ENST00000244709.9; ENSP00000244709.3; NM_018643.5; NP_061113.1.
DR UCSC; uc003oqf.3; human. [Q9NP99-1]
DR CTD; 54210; -.
DR DisGeNET; 54210; -.
DR GeneCards; TREM1; -.
DR HGNC; HGNC:17760; TREM1.
DR HPA; ENSG00000124731; Tissue enhanced (bone marrow, lung, lymphoid tissue).
DR MIM; 605085; gene.
DR neXtProt; NX_Q9NP99; -.
DR OpenTargets; ENSG00000124731; -.
DR PharmGKB; PA38467; -.
DR VEuPathDB; HostDB:ENSG00000124731; -.
DR eggNOG; ENOG502TE0T; Eukaryota.
DR GeneTree; ENSGT00470000042299; -.
DR HOGENOM; CLU_1170307_0_0_1; -.
DR InParanoid; Q9NP99; -.
DR OMA; YRCVICQ; -.
DR PhylomeDB; Q9NP99; -.
DR TreeFam; TF339293; -.
DR PathwayCommons; Q9NP99; -.
DR Reactome; R-HSA-198933; Immunoregulatory interactions between a Lymphoid and a non-Lymphoid cell.
DR Reactome; R-HSA-202733; Cell surface interactions at the vascular wall.
DR Reactome; R-HSA-2172127; DAP12 interactions.
DR SignaLink; Q9NP99; -.
DR BioGRID-ORCS; 54210; 11 hits in 1074 CRISPR screens.
DR ChiTaRS; TREM1; human.
DR EvolutionaryTrace; Q9NP99; -.
DR GeneWiki; TREM1; -.
DR GenomeRNAi; 54210; -.
DR Pharos; Q9NP99; Tbio.
DR PRO; PR:Q9NP99; -.
DR Proteomes; UP000005640; Chromosome 6.
DR RNAct; Q9NP99; protein.
DR Bgee; ENSG00000124731; Expressed in monocyte and 119 other tissues.
DR ExpressionAtlas; Q9NP99; baseline and differential.
DR Genevisible; Q9NP99; HS.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; TAS:Reactome.
DR GO; GO:0097110; F:scaffold protein binding; IPI:BHF-UCL.
DR GO; GO:0038023; F:signaling receptor activity; TAS:ProtInc.
DR GO; GO:0002526; P:acute inflammatory response; IEA:InterPro.
DR GO; GO:0002250; P:adaptive immune response; IEA:UniProtKB-KW.
DR GO; GO:0006959; P:humoral immune response; TAS:ProtInc.
DR GO; GO:0045087; P:innate immune response; IEA:UniProtKB-KW.
DR GO; GO:0035556; P:intracellular signal transduction; TAS:ProtInc.
DR GO; GO:0030593; P:neutrophil chemotaxis; IBA:GO_Central.
DR GO; GO:0070945; P:neutrophil-mediated killing of gram-negative bacterium; IBA:GO_Central.
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 InterPro; IPR013106; Ig_V-set.
DR InterPro; IPR039141; TREM1.
DR PANTHER; PTHR19357:SF0; PTHR19357:SF0; 1.
DR Pfam; PF07686; V-set; 1.
DR SMART; SM00409; IG; 1.
DR SUPFAM; SSF48726; SSF48726; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Adaptive immunity; Alternative splicing; Cell membrane;
KW Disulfide bond; Glycoprotein; Immunity; Immunoglobulin domain;
KW Innate immunity; Membrane; Receptor; Reference proteome; Secreted; Signal;
KW Transmembrane; Transmembrane helix.
FT SIGNAL 1..20
FT /evidence="ECO:0000255"
FT CHAIN 21..234
FT /note="Triggering receptor expressed on myeloid cells 1"
FT /id="PRO_0000014986"
FT TOPO_DOM 21..205
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 206..226
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 227..234
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 26..134
FT /note="Ig-like V-type"
FT CARBOHYD 146
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 191
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 194
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 41..113
FT /evidence="ECO:0000269|PubMed:14656437,
FT ECO:0000269|PubMed:15351648, ECO:0007744|PDB:1Q8M,
FT ECO:0007744|PDB:1SMO"
FT VAR_SEQ 138..150
FT /note="SGTPGSNENSTQN -> RCSTLSFSWLVDS (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:11922939,
FT ECO:0000303|PubMed:14702039, ECO:0000303|Ref.3"
FT /id="VSP_010790"
FT VAR_SEQ 151..234
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:11922939,
FT ECO:0000303|PubMed:14702039, ECO:0000303|Ref.3"
FT /id="VSP_010791"
FT VAR_SEQ 201..234
FT /note="VPVFNIVILLAGGFLSKSLVFSVLFAVTLRSFVP -> YSFQVPGPLVWTLS
FT PLFPSLCAERM (in isoform 3)"
FT /evidence="ECO:0000305"
FT /id="VSP_053939"
FT VARIANT 25
FT /note="T -> S (in dbSNP:rs2234237)"
FT /evidence="ECO:0000269|Ref.7"
FT /id="VAR_019333"
FT VARIANT 97
FT /note="R -> S (in a breast cancer sample; somatic
FT mutation)"
FT /evidence="ECO:0000269|PubMed:16959974"
FT /id="VAR_035525"
FT VARIANT 135
FT /note="K -> T (in dbSNP:rs34727391)"
FT /id="VAR_049949"
FT VARIANT 214
FT /note="F -> L (in dbSNP:rs2234245)"
FT /id="VAR_033624"
FT CONFLICT 35
FT /note="Q -> K (in Ref. 3; AAL74018)"
FT /evidence="ECO:0000305"
FT STRAND 22..30
FT /evidence="ECO:0007829|PDB:1SMO"
FT STRAND 37..42
FT /evidence="ECO:0007829|PDB:1SMO"
FT HELIX 45..48
FT /evidence="ECO:0007829|PDB:1SMO"
FT STRAND 53..58
FT /evidence="ECO:0007829|PDB:1SMO"
FT TURN 60..62
FT /evidence="ECO:0007829|PDB:1Q8M"
FT STRAND 65..69
FT /evidence="ECO:0007829|PDB:1SMO"
FT STRAND 80..82
FT /evidence="ECO:0007829|PDB:1SMO"
FT STRAND 85..90
FT /evidence="ECO:0007829|PDB:1SMO"
FT TURN 91..94
FT /evidence="ECO:0007829|PDB:1SMO"
FT STRAND 95..100
FT /evidence="ECO:0007829|PDB:1SMO"
FT HELIX 105..107
FT /evidence="ECO:0007829|PDB:1SMO"
FT STRAND 109..115
FT /evidence="ECO:0007829|PDB:1SMO"
FT STRAND 123..125
FT /evidence="ECO:0007829|PDB:1Q8M"
FT STRAND 128..132
FT /evidence="ECO:0007829|PDB:1SMO"
SQ SEQUENCE 234 AA; 26387 MW; AA114696E35D4D45 CRC64;
MRKTRLWGLL WMLFVSELRA ATKLTEEKYE LKEGQTLDVK CDYTLEKFAS SQKAWQIIRD
GEMPKTLACT ERPSKNSHPV QVGRIILEDY HDHGLLRVRM VNLQVEDSGL YQCVIYQPPK
EPHMLFDRIR LVVTKGFSGT PGSNENSTQN VYKIPPTTTK ALCPLYTSPR TVTQAPPKST
ADVSTPDSEI NLTNVTDIIR VPVFNIVILL AGGFLSKSLV FSVLFAVTLR SFVP
