TREM1_MOUSE
ID TREM1_MOUSE Reviewed; 230 AA.
AC Q9JKE2; Q3TAL7;
DT 08-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 144.
DE RecName: Full=Triggering receptor expressed on myeloid cells 1;
DE Short=TREM-1;
DE AltName: CD_antigen=CD354;
DE Flags: Precursor;
GN Name=Trem1;
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].
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 [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Dendritic cell, and Spleen;
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 FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=23241959; DOI=10.1172/jci64181;
RA Klesney-Tait J., Keck K., Li X., Gilfillan S., Otero K., Baruah S.,
RA Meyerholz D.K., Varga S.M., Knudson C.J., Moninger T.O., Moreland J.,
RA Zabner J., Colonna M.;
RT "Transepithelial migration of neutrophils into the lung requires TREM-1.";
RL J. Clin. Invest. 123:138-149(2013).
RN [4]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=27328755; DOI=10.1038/srep28556;
RA Kozik J.H., Trautmann T., Carambia A., Preti M., Luetgehetmann M.,
RA Krech T., Wiegard C., Heeren J., Herkel J.;
RT "Attenuated viral hepatitis in Trem1-/- mice is associated with reduced
RT inflammatory activity of neutrophils.";
RL Sci. Rep. 6:28556-28556(2016).
RN [5]
RP X-RAY CRYSTALLOGRAPHY (1.76 ANGSTROMS) OF 21-134, SUBUNIT, AND DISULFIDE
RP BOND.
RX PubMed=15561137; DOI=10.1016/j.jmb.2004.10.009;
RA Kelker M.S., Debler E.W., Wilson I.A.;
RT "Crystal structure of mouse triggering receptor expressed on myeloid cells
RT 1 (TREM-1) at 1.76 A.";
RL J. Mol. Biol. 344:1175-1181(2004).
CC -!- FUNCTION: Cell surface receptor that plays important roles in innate
CC and adaptive immunity by amplifying inflammatory responses. Upon
CC activation by various ligands such as PGLYRP1, HMGB1 or HSP70,
CC multimerizes and forms a complex with transmembrane adapter
CC TYROBP/DAP12. 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. This cascade promotes the
CC neutrophil- and macrophage-mediated release of pro-inflammatory
CC cytokines and/or chemokines, as well as their migration and thereby
CC amplifies inflammatory responses that are triggered by bacterial and
CC fungal infections (PubMed:23241959, PubMed:27328755). By also promoting
CC the amplification of inflammatory signals that are initially triggered
CC by Toll-like receptor (TLR) and NOD-like receptor engagement, plays a
CC major role in the pathophysiology of acute and chronic inflammatory
CC diseases of different etiologies including septic shock and
CC atherosclerosis (By similarity). {ECO:0000250|UniProtKB:Q9NP99,
CC ECO:0000269|PubMed:23241959, ECO:0000269|PubMed:27328755}.
CC -!- SUBUNIT: Monomer (PubMed:15561137). Homomultimer; when activated.
CC Interacts with TYROBP/DAP12. Interacts with TLR4 (By similarity).
CC {ECO:0000250|UniProtKB:Q9NP99, ECO:0000269|PubMed:15561137}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q9NP99};
CC Single-pass type I membrane protein {ECO:0000250|UniProtKB:Q9NP99}.
CC Note=Recruited to lipid rafts when activated.
CC {ECO:0000250|UniProtKB:Q9NP99}.
CC -!- DISRUPTION PHENOTYPE: Deletion mutants do not show any influence of the
CC antiviral T-cell response. However, TREM1 deficiency impairs secretion
CC of CCL2 and TNF-alpha by neutrophils in response to viruses
CC (PubMed:27328755). TREM-1/3-deficient animals have decreased
CC neutrophils in the airway and these neutrophils have a defect in
CC transepithelial migration (PubMed:23241959).
CC {ECO:0000269|PubMed:23241959, ECO:0000269|PubMed:27328755}.
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DR EMBL; AF241219; AAF69834.1; -; mRNA.
DR EMBL; AK089439; BAC40884.1; -; mRNA.
DR EMBL; AK171753; BAE42651.1; -; mRNA.
DR CCDS; CCDS28860.1; -.
DR RefSeq; NP_067381.1; NM_021406.5.
DR PDB; 1U9K; X-ray; 1.76 A; A/B=21-134.
DR PDBsum; 1U9K; -.
DR AlphaFoldDB; Q9JKE2; -.
DR SMR; Q9JKE2; -.
DR STRING; 10090.ENSMUSP00000038636; -.
DR GlyGen; Q9JKE2; 1 site.
DR iPTMnet; Q9JKE2; -.
DR PhosphoSitePlus; Q9JKE2; -.
DR PaxDb; Q9JKE2; -.
DR PRIDE; Q9JKE2; -.
DR TopDownProteomics; Q9JKE2; -.
DR ABCD; Q9JKE2; 21 sequenced antibodies.
DR Antibodypedia; 1616; 710 antibodies from 40 providers.
DR DNASU; 58217; -.
DR Ensembl; ENSMUST00000048782; ENSMUSP00000038636; ENSMUSG00000042265.
DR GeneID; 58217; -.
DR KEGG; mmu:58217; -.
DR UCSC; uc029tij.2; mouse.
DR CTD; 54210; -.
DR MGI; MGI:1930005; Trem1.
DR VEuPathDB; HostDB:ENSMUSG00000042265; -.
DR eggNOG; ENOG502TE0T; Eukaryota.
DR GeneTree; ENSGT00470000042299; -.
DR HOGENOM; CLU_1170307_0_0_1; -.
DR InParanoid; Q9JKE2; -.
DR OMA; NIMKYAN; -.
DR OrthoDB; 1472586at2759; -.
DR PhylomeDB; Q9JKE2; -.
DR TreeFam; TF339293; -.
DR Reactome; R-MMU-198933; Immunoregulatory interactions between a Lymphoid and a non-Lymphoid cell.
DR Reactome; R-MMU-202733; Cell surface interactions at the vascular wall.
DR Reactome; R-MMU-2172127; DAP12 interactions.
DR BioGRID-ORCS; 58217; 1 hit in 74 CRISPR screens.
DR EvolutionaryTrace; Q9JKE2; -.
DR PRO; PR:Q9JKE2; -.
DR Proteomes; UP000000589; Chromosome 17.
DR RNAct; Q9JKE2; protein.
DR Bgee; ENSMUSG00000042265; Expressed in granulocyte and 19 other tissues.
DR ExpressionAtlas; Q9JKE2; baseline and differential.
DR Genevisible; Q9JKE2; MM.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0097110; F:scaffold protein binding; ISO:MGI.
DR GO; GO:0038023; F:signaling receptor activity; IEA:InterPro.
DR GO; GO:0002526; P:acute inflammatory response; IEA:InterPro.
DR GO; GO:0002250; P:adaptive immune response; IEA:UniProtKB-KW.
DR GO; GO:0045087; P:innate immune response; IEA:UniProtKB-KW.
DR GO; GO:0030593; P:neutrophil chemotaxis; IGI:MGI.
DR GO; GO:0072672; P:neutrophil extravasation; IGI:MGI.
DR GO; GO:1990266; P:neutrophil migration; IGI:MGI.
DR GO; GO:0070945; P:neutrophil-mediated killing of gram-negative bacterium; IGI:MGI.
DR GO; GO:0010666; P:positive regulation of cardiac muscle cell apoptotic process; ISO:MGI.
DR GO; GO:0001954; P:positive regulation of cell-matrix adhesion; ISO:MGI.
DR GO; GO:0010759; P:positive regulation of macrophage chemotaxis; ISO:MGI.
DR Gene3D; 2.60.40.10; -; 1.
DR InterPro; IPR007110; Ig-like_dom.
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.
DR PROSITE; PS50835; IG_LIKE; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Adaptive immunity; Cell membrane; Disulfide bond;
KW Glycoprotein; Immunity; Immunoglobulin domain; Innate immunity; Membrane;
KW Receptor; Reference proteome; Signal; Transmembrane; Transmembrane helix.
FT SIGNAL 1..20
FT /evidence="ECO:0000255"
FT CHAIN 21..230
FT /note="Triggering receptor expressed on myeloid cells 1"
FT /id="PRO_0000042797"
FT TOPO_DOM 21..202
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 203..223
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 224..230
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 21..124
FT /note="Ig-like V-type"
FT CARBOHYD 191
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 41..113
FT /evidence="ECO:0000269|PubMed:15561137,
FT ECO:0007744|PDB:1U9K"
FT CONFLICT 92
FT /note="S -> T (in Ref. 2; BAE42651)"
FT /evidence="ECO:0000305"
FT STRAND 27..32
FT /evidence="ECO:0007829|PDB:1U9K"
FT STRAND 37..42
FT /evidence="ECO:0007829|PDB:1U9K"
FT HELIX 45..48
FT /evidence="ECO:0007829|PDB:1U9K"
FT STRAND 51..57
FT /evidence="ECO:0007829|PDB:1U9K"
FT STRAND 65..69
FT /evidence="ECO:0007829|PDB:1U9K"
FT STRAND 78..82
FT /evidence="ECO:0007829|PDB:1U9K"
FT STRAND 85..90
FT /evidence="ECO:0007829|PDB:1U9K"
FT HELIX 91..93
FT /evidence="ECO:0007829|PDB:1U9K"
FT STRAND 95..100
FT /evidence="ECO:0007829|PDB:1U9K"
FT HELIX 105..107
FT /evidence="ECO:0007829|PDB:1U9K"
FT STRAND 109..116
FT /evidence="ECO:0007829|PDB:1U9K"
FT STRAND 129..134
FT /evidence="ECO:0007829|PDB:1U9K"
SQ SEQUENCE 230 AA; 25409 MW; 51A1B7FD095A1990 CRC64;
MRKAGLWGLL CVFFVSEVKA AIVLEEERYD LVEGQTLTVK CPFNIMKYAN SQKAWQRLPD
GKEPLTLVVT QRPFTRPSEV HMGKFTLKHD PSEAMLQVQM TDLQVTDSGL YRCVIYHPPN
DPVVLFHPVR LVVTKGSSDV FTPVIIPITR LTERPILITT KYSPSDTTTT RSLPKPTAVV
SSPGLGVTII NGTDADSVST SSVTISVICG LLSKSLVFII LFIVTKRTFG
