TRML2_MOUSE
ID TRML2_MOUSE Reviewed; 329 AA.
AC Q2LA85; A6XA76;
DT 17-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 2.
DT 03-AUG-2022, entry version 111.
DE RecName: Full=Trem-like transcript 2 protein;
DE Short=TLT-2;
DE AltName: Full=Triggering receptor expressed on myeloid cells-like protein 2;
DE Flags: Precursor;
GN Name=Treml2; Synonyms=Tlt2;
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], FUNCTION, INDUCTION, SUBCELLULAR LOCATION, AND
RP TISSUE SPECIFICITY.
RC STRAIN=C57BL/6J; TISSUE=Spleen;
RX PubMed=16670310; DOI=10.4049/jimmunol.176.10.6012;
RA King R.G., Herrin B.R., Justement L.B.;
RT "Trem-like transcript 2 is expressed on cells of the myeloid/granuloid and
RT B lymphoid lineage and is up-regulated in response to inflammation.";
RL J. Immunol. 176:6012-6021(2006).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=C57BL/6J;
RA Melchior B., Carson M.J.;
RT "Trem-like transcripts expression in microglia and peripheral myeloid cells
RT display a common pattern.";
RL Submitted (JUN-2005) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Cell surface receptor that may play a role in the innate and
CC adaptive immune response. Acts as a counter-receptor for CD276 and
CC interaction with CD276 on T-cells enhances T-cell activation (By
CC similarity). {ECO:0000250, ECO:0000269|PubMed:16670310}.
CC -!- SUBUNIT: Interacts with CD276 and this interaction enhances T-cell
CC activation. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Single-pass type I
CC membrane protein {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Detected in B-lymphocytes and macrophages. Detected
CC in spleen, lymph nodes, blood, bone marrow and cells from the
CC peritoneal cavity (at protein level). {ECO:0000269|PubMed:16670310}.
CC -!- INDUCTION: Up-regulated in neutrophils and macrophages in response to
CC bacterial lipopolysaccharide (LPS) and inflammatory stimuly.
CC {ECO:0000269|PubMed:16670310}.
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; DQ341272; ABC68265.1; -; mRNA.
DR EMBL; DQ087184; ABA38680.1; -; mRNA.
DR CCDS; CCDS37646.1; -.
DR RefSeq; NP_001028577.2; NM_001033405.2.
DR RefSeq; XP_006524503.1; XM_006524440.2.
DR RefSeq; XP_006524504.1; XM_006524441.3.
DR AlphaFoldDB; Q2LA85; -.
DR SMR; Q2LA85; -.
DR BioGRID; 236663; 1.
DR STRING; 10090.ENSMUSP00000128215; -.
DR GlyGen; Q2LA85; 1 site.
DR PhosphoSitePlus; Q2LA85; -.
DR PaxDb; Q2LA85; -.
DR PRIDE; Q2LA85; -.
DR ProteomicsDB; 298236; -.
DR Antibodypedia; 30035; 169 antibodies from 26 providers.
DR DNASU; 328833; -.
DR Ensembl; ENSMUST00000233092; ENSMUSP00000156527; ENSMUSG00000071068.
DR GeneID; 328833; -.
DR KEGG; mmu:328833; -.
DR UCSC; uc008cxe.1; mouse.
DR CTD; 79865; -.
DR MGI; MGI:2147038; Treml2.
DR VEuPathDB; HostDB:ENSMUSG00000071068; -.
DR eggNOG; ENOG502SPIC; Eukaryota.
DR GeneTree; ENSGT00940000153835; -.
DR HOGENOM; CLU_044854_0_0_1; -.
DR InParanoid; Q2LA85; -.
DR OMA; LLWPQGC; -.
DR OrthoDB; 1378930at2759; -.
DR PhylomeDB; Q2LA85; -.
DR TreeFam; TF337556; -.
DR Reactome; R-MMU-198933; Immunoregulatory interactions between a Lymphoid and a non-Lymphoid cell.
DR BioGRID-ORCS; 328833; 1 hit in 73 CRISPR screens.
DR PRO; PR:Q2LA85; -.
DR Proteomes; UP000000589; Chromosome 17.
DR RNAct; Q2LA85; protein.
DR Bgee; ENSMUSG00000071068; Expressed in granulocyte and 25 other tissues.
DR ExpressionAtlas; Q2LA85; baseline and differential.
DR Genevisible; Q2LA85; MM.
DR GO; GO:0009986; C:cell surface; ISO:MGI.
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; ISO:MGI.
DR GO; GO:0042110; P:T cell activation; 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 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 Cell membrane; Disulfide bond; Glycoprotein; Immunoglobulin domain;
KW Membrane; Receptor; Reference proteome; Signal; Transmembrane;
KW Transmembrane helix.
FT SIGNAL 1..24
FT /evidence="ECO:0000255"
FT CHAIN 25..329
FT /note="Trem-like transcript 2 protein"
FT /id="PRO_0000253858"
FT TOPO_DOM 25..270
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 271..291
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 292..329
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 25..126
FT /note="Ig-like V-type"
FT REGION 202..259
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 261
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 46..110
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 61..68
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT CONFLICT 179
FT /note="M -> V (in Ref. 1; ABC68265)"
FT /evidence="ECO:0000305"
FT CONFLICT 203
FT /note="I -> T (in Ref. 1; ABC68265)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 329 AA; 37075 MW; 73C416AEAD0291D9 CRC64;
MEPWPLTFLL LLLLLLWLQG CVSGHSNENL YRKVWRREGE TLSVQCSYKN RRNLVEAKSW
CKVKKKKCDH NFTRSWVRGP SYSLRDDAKV KVVRITMEAL RVQDSGRYWC MRNTAGHFYP
LVGFQLEVYP ALTTERNVPH THLTNTPMDG FVTTGQVHIS DPHAPFTSDV TMFTSEVTMF
TSGLLTLASG TTTPTPVTGY SFIDTSGTVT EPERNTESQP ATLSPSNARS FSADPVTTST
MSRHQSSSLS TTGTCHPLTP NRSQETYIPA MVVVLTFLPA PVVLVVAYGF WKKRHMGRYN
LGSNYAKPWI HLPEGPETPW KPAWSKITQ
