ID   TREM1_PONAB             Reviewed;         231 AA.
AC   Q5RDA5;
DT   08-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT   21-DEC-2004, sequence version 1.
DT   03-AUG-2022, entry version 76.
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   Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Pongo.
OX   NCBI_TaxID=9601;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Heart;
RG   The German cDNA consortium;
RL   Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
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; CR858010; CAH90252.1; -; mRNA.
DR   RefSeq; NP_001127259.1; NM_001133787.1.
DR   RefSeq; XP_009240116.1; XM_009241841.1.
DR   AlphaFoldDB; Q5RDA5; -.
DR   SMR; Q5RDA5; -.
DR   STRING; 9601.ENSPPYP00000018559; -.
DR   Ensembl; ENSPPYT00000042526; ENSPPYP00000043121; ENSPPYG00000033253.
DR   GeneID; 100174314; -.
DR   KEGG; pon:100174314; -.
DR   CTD; 54210; -.
DR   eggNOG; ENOG502TE0T; Eukaryota.
DR   GeneTree; ENSGT00470000042299; -.
DR   InParanoid; Q5RDA5; -.
DR   TreeFam; TF339293; -.
DR   Proteomes; UP000001595; Chromosome 6.
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   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   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..231
FT                   /note="Triggering receptor expressed on myeloid cells 1"
FT                   /id="PRO_0000042799"
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..231
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          26..131
FT                   /note="Ig-like V-type"
FT   REGION          134..182
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CARBOHYD        188
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        191
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        41..110
FT                   /evidence="ECO:0000250|UniProtKB:Q9NP99"
SQ   SEQUENCE   231 AA;  25883 MW;  41DADA212BE21414 CRC64;
     MRKTRLWGLL WMFFVSELLA ATKLTEEKYE LKEGQTLDVK CDYMLEKFAS SRKAWQIIRD
     GEMPQTLACT ERPSHPVQVG RIILEDYHDH GLLHVRMTNL QVEDSGLYQC VIYQPPKEPH
     VLFDRIRLVV TKGSSGTPGS SENSTPNVYK TPPTTTKALR PLYTSPTTVT QAPPKSTADV
     STPDSEINLT NVTDIIRVPV FNIAILVAGG FLSKSLVFSV LFAVTLRSFV P