TREM1_PIG
ID TREM1_PIG Reviewed; 238 AA.
AC Q6TYI6;
DT 08-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 100.
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 Sus scrofa (Pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX NCBI_TaxID=9823;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
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}.
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DR EMBL; AY382476; AAQ83838.1; -; mRNA.
DR RefSeq; NP_998921.1; NM_213756.1.
DR AlphaFoldDB; Q6TYI6; -.
DR SMR; Q6TYI6; -.
DR STRING; 9823.ENSSSCP00000030720; -.
DR PaxDb; Q6TYI6; -.
DR Ensembl; ENSSSCT00005062763; ENSSSCP00005038794; ENSSSCG00005039233.
DR Ensembl; ENSSSCT00025077021; ENSSSCP00025033376; ENSSSCG00025056327.
DR Ensembl; ENSSSCT00030090753; ENSSSCP00030041790; ENSSSCG00030064941.
DR Ensembl; ENSSSCT00045020223; ENSSSCP00045013886; ENSSSCG00045011920.
DR Ensembl; ENSSSCT00050006643; ENSSSCP00050002880; ENSSSCG00050004829.
DR Ensembl; ENSSSCT00060071570; ENSSSCP00060030868; ENSSSCG00060052590.
DR Ensembl; ENSSSCT00065096170; ENSSSCP00065042079; ENSSSCG00065070055.
DR GeneID; 396601; -.
DR KEGG; ssc:396601; -.
DR CTD; 54210; -.
DR eggNOG; ENOG502TE0T; Eukaryota.
DR HOGENOM; CLU_1170307_0_0_1; -.
DR InParanoid; Q6TYI6; -.
DR OMA; YRCVICQ; -.
DR OrthoDB; 1472586at2759; -.
DR Reactome; R-SSC-198933; Immunoregulatory interactions between a Lymphoid and a non-Lymphoid cell.
DR Reactome; R-SSC-202733; Cell surface interactions at the vascular wall.
DR Reactome; R-SSC-2172127; DAP12 interactions.
DR ChiTaRS; TREM1; pig.
DR Proteomes; UP000008227; Unplaced.
DR Proteomes; UP000314985; Unplaced.
DR Genevisible; Q6TYI6; SS.
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; IEA:Ensembl.
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..238
FT /note="Triggering receptor expressed on myeloid cells 1"
FT /id="PRO_0000042798"
FT TOPO_DOM 21..210
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 211..231
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 232..238
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 21..129
FT /note="Ig-like V-type"
FT REGION 141..169
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 141..166
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 135
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 198
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 41..113
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
SQ SEQUENCE 238 AA; 26428 MW; 63822ABB5BB480CB CRC64;
MRSARLGRLL WMLFITEIQA ATELPEEKYI LAEGETLNVN CPVTVGVYSN SRKAWQKLNR
NGKFQTLAIT ERVSGQVSKV QVGKIFLTDE PSEGMLHVQM TNVQAEDSGL YRCVIYQPPK
DPIILFYPVR LVVTNYSSGT PASAETPTQS CSPTTTLPPT TTTNRHRPRP RTVRTVTQFL
TDFTTSLSSP GLKVTLTNVT DITRDTEISL ILPAVCGLLS KSLVFIVLFV VTRMSFTP
