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Triggering receptor expressed on myeloid cells 1 (TREM-1) (Triggering receptor expressed on monocytes 1) (CD antigen CD354)

 TREM1_HUMAN             Reviewed;         234 AA.
Q9NP99; B4DWG2; K7EJW1; Q53FL8; Q5T2C9; Q86YU1;
19-JUL-2004, integrated into UniProtKB/Swiss-Prot.
01-OCT-2000, sequence version 1.
20-JUN-2018, entry version 152.
RecName: Full=Triggering receptor expressed on myeloid cells 1;
Short=TREM-1;
AltName: Full=Triggering receptor expressed on monocytes 1;
AltName: CD_antigen=CD354;
Flags: Precursor;
Name=TREM1;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, INDUCTION, TISSUE
SPECIFICITY, GLYCOSYLATION, AND INTERACTION WITH TYROBP/DAP12.
TISSUE=Monocyte, and Neutrophil;
PubMed=10799849; DOI=10.4049/jimmunol.164.10.4991;
Bouchon A., Dietrich J., Colonna M.;
"Inflammatory responses can be triggered by TREM-1, a novel receptor
expressed on neutrophils and monocytes.";
J. Immunol. 164:4991-4995(2000).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), AND TISSUE SPECIFICITY.
PubMed=11922939; DOI=10.1016/S0161-5890(02)00004-4;
Gingras M.-C., Lapillonne H., Margolin J.F.;
"TREM-1, MDL-1, and DAP12 expression is associated with a mature stage
of myeloid development.";
Mol. Immunol. 38:817-824(2002).
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
Begum N.A., Seya T.;
"Identification of a soluble form of TREM1 (sTREM1) from dendritic
cells.";
Submitted (JAN-2002) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
TISSUE=Synovium;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=14574404; DOI=10.1038/nature02055;
Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L.,
Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E.,
Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R.,
Almeida J.P., Ambrose K.D., Andrews T.D., Ashwell R.I.S.,
Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J.,
Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P.,
Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y.,
Burford D.C., Burrill W., Burton J., Carder C., Carter N.P.,
Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V.,
Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J.,
Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E.,
Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A.,
Frankland J., French L., Garner P., Garnett J., Ghori M.J.,
Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M.,
Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S.,
Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R.,
Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E.,
Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A.,
Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C.,
Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M.,
Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M.,
Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K.,
McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T.,
Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R.,
Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W.,
Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M.,
Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L.,
Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J.,
Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B.,
Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L.,
Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W.,
Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A.,
Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.;
"The DNA sequence and analysis of human chromosome 6.";
Nature 425:805-811(2003).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Lung;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-200, AND VARIANT SER-25.
TISSUE=Synovial cell;
Suzuki Y., Sugano S., Totoki Y., Toyoda A., Takeda T., Sakaki Y.,
Tanaka A., Yokoyama S.;
Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases.
[8]
FUNCTION.
PubMed=11323674; DOI=10.1038/35074114;
Bouchon A., Facchetti F., Weigand M.A., Colonna M.;
"TREM-1 amplifies inflammation and is a crucial mediator of septic
shock.";
Nature 410:1103-1107(2001).
[9]
X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF 17-134, AND DISULFIDE BOND.
PubMed=14656437; DOI=10.1016/j.str.2003.11.001;
Radaev S., Kattah M., Rostro B., Colonna M., Sun P.D.;
"Crystal structure of the human myeloid cell activating receptor TREM-
1.";
Structure 11:1527-1535(2003).
[10]
X-RAY CRYSTALLOGRAPHY (1.47 ANGSTROMS) OF 21-139, SUBUNIT, AND
DISULFIDE BOND.
PubMed=15351648; DOI=10.1016/j.jmb.2004.07.089;
Kelker M.S., Foss T.R., Peti W., Teyton L., Kelly J.W., Wuethrich K.,
Wilson I.A.;
"Crystal structure of human triggering receptor expressed on myeloid
cells 1 (TREM-1) at 1.47 A.";
J. Mol. Biol. 342:1237-1248(2004).
[11]
VARIANT [LARGE SCALE ANALYSIS] SER-97.
PubMed=16959974; DOI=10.1126/science.1133427;
Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D.,
Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S.,
Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J.,
Dawson D., Willson J.K.V., Gazdar A.F., Hartigan J., Wu L., Liu C.,
Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N.,
Vogelstein B., Kinzler K.W., Velculescu V.E.;
"The consensus coding sequences of human breast and colorectal
cancers.";
Science 314:268-274(2006).
-!- FUNCTION: Stimulates neutrophil and monocyte-mediated inflammatory
responses. Triggers release of pro-inflammatory chemokines and
cytokines, as well as increased surface expression of cell
activation markers. Amplifier of inflammatory responses that are
triggered by bacterial and fungal infections and is a crucial
mediator of septic shock. {ECO:0000269|PubMed:10799849,
ECO:0000269|PubMed:11323674}.
-!- SUBUNIT: Interacts with TYROBP/DAP12.
{ECO:0000269|PubMed:10799849, ECO:0000269|PubMed:15351648}.
-!- SUBCELLULAR LOCATION: Isoform 1: Cell membrane {ECO:0000305};
Single-pass type I membrane protein {ECO:0000305}.
-!- SUBCELLULAR LOCATION: Isoform 2: Secreted {ECO:0000305}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=3;
Name=1;
IsoId=Q9NP99-1; Sequence=Displayed;
Name=2; Synonyms=TREM-1sv, sTREM1;
IsoId=Q9NP99-2; Sequence=VSP_010790, VSP_010791;
Name=3;
IsoId=Q9NP99-3; Sequence=VSP_053939;
-!- TISSUE SPECIFICITY: Highly expressed in adult liver, lung and
spleen than in corresponding fetal tissue. Also expressed in the
lymph node, placenta, spinal cord and heart tissues. Expression is
more elevated in peripheral blood leukocytes than in the bone
marrow and in normal cells than malignant cells. Expressed at low
levels in the early development of the hematopoietic system and in
the promonocytic stage and at high levels in mature monocytes.
Strongly expressed in acute inflammatory lesions caused by
bacteria and fungi. Isoform 2 was detected in the lung, liver and
mature monocytes. {ECO:0000269|PubMed:10799849,
ECO:0000269|PubMed:11922939}.
-!- INDUCTION: Up-regulated by bacteria, fungi and bacterial
lipopolysaccharides (LPS). {ECO:0000269|PubMed:10799849}.
-!- PTM: Glycosylated. {ECO:0000269|PubMed:10799849}.
-----------------------------------------------------------------------
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EMBL; AF196329; AAF71694.1; -; mRNA.
EMBL; AF287008; AAF90197.1; -; mRNA.
EMBL; AY074783; AAL74018.1; -; mRNA.
EMBL; AK301519; BAG63024.1; -; mRNA.
EMBL; AL391903; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BC017773; AAH17773.1; -; mRNA.
EMBL; AK223264; BAD96984.1; -; mRNA.
CCDS; CCDS4854.1; -. [Q9NP99-1]
CCDS; CCDS56427.1; -. [Q9NP99-2]
CCDS; CCDS59499.1; -. [Q9NP99-3]
RefSeq; NP_001229518.1; NM_001242589.2. [Q9NP99-3]
RefSeq; NP_001229519.1; NM_001242590.2. [Q9NP99-2]
RefSeq; NP_061113.1; NM_018643.4. [Q9NP99-1]
RefSeq; XP_016866445.1; XM_017010956.1. [Q9NP99-1]
RefSeq; XP_016866446.1; XM_017010957.1. [Q9NP99-2]
UniGene; Hs.283022; -.
UniGene; Hs.435955; -.
PDB; 1Q8M; X-ray; 2.60 A; A/B/C/D=17-134.
PDB; 1SMO; X-ray; 1.47 A; A/B=21-139.
PDBsum; 1Q8M; -.
PDBsum; 1SMO; -.
ProteinModelPortal; Q9NP99; -.
SMR; Q9NP99; -.
BioGrid; 119926; 9.
IntAct; Q9NP99; 2.
STRING; 9606.ENSP00000244709; -.
ChEMBL; CHEMBL1697674; -.
DrugBank; DB01694; D-tartaric acid.
iPTMnet; Q9NP99; -.
PhosphoSitePlus; Q9NP99; -.
BioMuta; TREM1; -.
DMDM; 50401685; -.
PaxDb; Q9NP99; -.
PeptideAtlas; Q9NP99; -.
PRIDE; Q9NP99; -.
ProteomicsDB; 81942; -.
ProteomicsDB; 81943; -. [Q9NP99-2]
DNASU; 54210; -.
Ensembl; ENST00000244709; ENSP00000244709; ENSG00000124731. [Q9NP99-1]
Ensembl; ENST00000334475; ENSP00000334284; ENSG00000124731. [Q9NP99-2]
Ensembl; ENST00000591620; ENSP00000465345; ENSG00000124731. [Q9NP99-3]
GeneID; 54210; -.
KEGG; hsa:54210; -.
UCSC; uc003oqf.3; human. [Q9NP99-1]
CTD; 54210; -.
DisGeNET; 54210; -.
EuPathDB; HostDB:ENSG00000124731.12; -.
GeneCards; TREM1; -.
HGNC; HGNC:17760; TREM1.
HPA; HPA005563; -.
MIM; 605085; gene.
neXtProt; NX_Q9NP99; -.
OpenTargets; ENSG00000124731; -.
PharmGKB; PA38467; -.
eggNOG; ENOG410J3SD; Eukaryota.
eggNOG; ENOG4111ABH; LUCA.
GeneTree; ENSGT00470000042299; -.
HOGENOM; HOG000130964; -.
HOVERGEN; HBG068403; -.
InParanoid; Q9NP99; -.
KO; K14362; -.
OMA; MRKARLW; -.
PhylomeDB; Q9NP99; -.
TreeFam; TF339293; -.
Reactome; R-HSA-198933; Immunoregulatory interactions between a Lymphoid and a non-Lymphoid cell.
Reactome; R-HSA-202733; Cell surface interactions at the vascular wall.
Reactome; R-HSA-2172127; DAP12 interactions.
ChiTaRS; TREM1; human.
EvolutionaryTrace; Q9NP99; -.
GeneWiki; TREM1; -.
GenomeRNAi; 54210; -.
PRO; PR:Q9NP99; -.
Proteomes; UP000005640; Chromosome 6.
Bgee; ENSG00000124731; -.
CleanEx; HS_TREM1; -.
ExpressionAtlas; Q9NP99; baseline and differential.
Genevisible; Q9NP99; HS.
GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0005622; C:intracellular; IEA:GOC.
GO; GO:0005886; C:plasma membrane; TAS:Reactome.
GO; GO:0097110; F:scaffold protein binding; IPI:BHF-UCL.
GO; GO:0038023; F:signaling receptor activity; TAS:ProtInc.
GO; GO:0006959; P:humoral immune response; TAS:ProtInc.
GO; GO:0045087; P:innate immune response; TAS:Reactome.
GO; GO:0035556; P:intracellular signal transduction; TAS:ProtInc.
GO; GO:0050900; P:leukocyte migration; TAS:Reactome.
GO; GO:0050776; P:regulation of immune response; TAS:Reactome.
Gene3D; 2.60.40.10; -; 1.
InterPro; IPR036179; Ig-like_dom_sf.
InterPro; IPR013783; Ig-like_fold.
InterPro; IPR003599; Ig_sub.
InterPro; IPR013106; Ig_V-set.
Pfam; PF07686; V-set; 1.
SMART; SM00409; IG; 1.
SUPFAM; SSF48726; SSF48726; 1.
1: Evidence at protein level;
3D-structure; Alternative splicing; Cell membrane; Complete proteome;
Disulfide bond; Glycoprotein; Immunoglobulin domain; Membrane;
Polymorphism; Receptor; Reference proteome; Secreted; Signal;
Transmembrane; Transmembrane helix.
SIGNAL 1 20 {ECO:0000255}.
CHAIN 21 234 Triggering receptor expressed on myeloid
cells 1.
/FTId=PRO_0000014986.
TOPO_DOM 21 205 Extracellular. {ECO:0000255}.
TRANSMEM 206 226 Helical. {ECO:0000255}.
TOPO_DOM 227 234 Cytoplasmic. {ECO:0000255}.
DOMAIN 26 134 Ig-like V-type.
CARBOHYD 146 146 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 191 191 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 194 194 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 41 113 {ECO:0000244|PDB:1Q8M,
ECO:0000244|PDB:1SMO,
ECO:0000269|PubMed:14656437,
ECO:0000269|PubMed:15351648}.
VAR_SEQ 138 150 SGTPGSNENSTQN -> RCSTLSFSWLVDS (in
isoform 2). {ECO:0000303|PubMed:11922939,
ECO:0000303|PubMed:14702039,
ECO:0000303|Ref.3}.
/FTId=VSP_010790.
VAR_SEQ 151 234 Missing (in isoform 2).
{ECO:0000303|PubMed:11922939,
ECO:0000303|PubMed:14702039,
ECO:0000303|Ref.3}.
/FTId=VSP_010791.
VAR_SEQ 201 234 VPVFNIVILLAGGFLSKSLVFSVLFAVTLRSFVP -> YSF
QVPGPLVWTLSPLFPSLCAERM (in isoform 3).
{ECO:0000305}.
/FTId=VSP_053939.
VARIANT 25 25 T -> S (in dbSNP:rs2234237).
{ECO:0000269|Ref.7}.
/FTId=VAR_019333.
VARIANT 97 97 R -> S (in a breast cancer sample;
somatic mutation).
{ECO:0000269|PubMed:16959974}.
/FTId=VAR_035525.
VARIANT 135 135 K -> T (in dbSNP:rs34727391).
/FTId=VAR_049949.
VARIANT 214 214 F -> L (in dbSNP:rs2234245).
/FTId=VAR_033624.
CONFLICT 35 35 Q -> K (in Ref. 3; AAL74018).
{ECO:0000305}.
STRAND 22 30 {ECO:0000244|PDB:1SMO}.
STRAND 37 42 {ECO:0000244|PDB:1SMO}.
HELIX 45 48 {ECO:0000244|PDB:1SMO}.
STRAND 53 58 {ECO:0000244|PDB:1SMO}.
TURN 60 62 {ECO:0000244|PDB:1Q8M}.
STRAND 65 69 {ECO:0000244|PDB:1SMO}.
STRAND 80 82 {ECO:0000244|PDB:1SMO}.
STRAND 85 90 {ECO:0000244|PDB:1SMO}.
TURN 91 94 {ECO:0000244|PDB:1SMO}.
STRAND 95 100 {ECO:0000244|PDB:1SMO}.
HELIX 105 107 {ECO:0000244|PDB:1SMO}.
STRAND 109 115 {ECO:0000244|PDB:1SMO}.
STRAND 123 125 {ECO:0000244|PDB:1Q8M}.
STRAND 128 132 {ECO:0000244|PDB:1SMO}.
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


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