ID   TREM1_BOVIN             Reviewed;         232 AA.
AC   Q6QUN5;
DT   08-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   25-MAY-2022, entry version 86.
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   Bos taurus (Bovine).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Bovinae; Bos.
OX   NCBI_TaxID=9913;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RC   TISSUE=Bone marrow;
RX   PubMed=15451618; DOI=10.1016/j.vetimm.2004.05.007;
RA   Ramanathan B., Minton J.E., Ross C.R., Blecha F.;
RT   "Characterization of bovine cDNA encoding triggering receptor expressed on
RT   myeloid cells 1 (TREM-1).";
RL   Vet. Immunol. Immunopathol. 102:85-89(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. 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.
CC       {ECO:0000250|UniProtKB:Q9NP99}.
CC   -!- SUBUNIT: Monomer. Homomultimer; when activated. Interacts with
CC       TYROBP/DAP12. Interacts with TLR4. {ECO:0000250|UniProtKB:Q9NP99}.
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   -!- TISSUE SPECIFICITY: Detected in bone marrow, tongue, lung, liver,
CC       thymus, spleen, jejunum, ileum and lymph nodes.
CC       {ECO:0000269|PubMed:15451618}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AY525122; AAS66748.1; -; mRNA.
DR   RefSeq; NP_996853.1; NM_206970.1.
DR   AlphaFoldDB; Q6QUN5; -.
DR   SMR; Q6QUN5; -.
DR   STRING; 9913.ENSBTAP00000023397; -.
DR   PaxDb; Q6QUN5; -.
DR   GeneID; 404547; -.
DR   KEGG; bta:404547; -.
DR   CTD; 54210; -.
DR   eggNOG; ENOG502TE0T; Eukaryota.
DR   InParanoid; Q6QUN5; -.
DR   OrthoDB; 1472586at2759; -.
DR   Proteomes; UP000009136; Unplaced.
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: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; 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; 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   2: Evidence at transcript level;
KW   Adaptive immunity; Cell membrane; Disulfide bond; Glycoprotein; Immunity;
KW   Immunoglobulin domain; Innate immunity; Membrane; Receptor;
KW   Reference proteome; Signal; Transmembrane; Transmembrane helix.
FT   SIGNAL          1..20
FT                   /evidence="ECO:0000255"
FT   CHAIN           21..232
FT                   /note="Triggering receptor expressed on myeloid cells 1"
FT                   /id="PRO_0000042796"
FT   TOPO_DOM        21..203
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        204..224
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        225..232
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          21..125
FT                   /note="Ig-like V-type"
FT   REGION          152..186
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        156..172
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CARBOHYD        192
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        41..109
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
SQ   SEQUENCE   232 AA;  25381 MW;  F136AD41175546CD CRC64;
     MRKAGVWGLL WMLFIEEIQA AAEVFEEKCT LAEGQTLKVS CPTNTNIYSN SQKAWQRLKD
     NGEVQTLAIT EGSSQVRVGK YFLEDIPSEG MLQIQMANLQ VEDSGLYRCV ILGPSDPIIL
     FHPVRLVVTK NSLGTPASDE YPCQVSVQNP TPLPVTTKLR PRPRPRPKPV TQPIPTSADR
     LSSPGFTVTP TNVTHVNRAP GISIIIPAAC GLLSKTLVFI GLFAVTHRSF AS