TRML2_HUMAN
ID TRML2_HUMAN Reviewed; 321 AA.
AC Q5T2D2; Q08AP8; Q08AP9; Q8IWY0; Q9H8E9;
DT 17-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 17-OCT-2006, sequence version 2.
DT 03-AUG-2022, entry version 142.
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=C6orf76, TLT2; ORFNames=UNQ6268/PRO20473;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=12645956; DOI=10.1002/immu.200310033;
RA Allcock R.J.N., Barrow A.D., Forbes S., Beck S., Trowsdale J.;
RT "The human TREM gene cluster at 6p21.1 encodes both activating and
RT inhibitory single IgV domain receptors and includes NKp44.";
RL Eur. J. Immunol. 33:567-577(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=12975309; DOI=10.1101/gr.1293003;
RA Clark H.F., Gurney A.L., Abaya E., Baker K., Baldwin D.T., Brush J.,
RA Chen J., Chow B., Chui C., Crowley C., Currell B., Deuel B., Dowd P.,
RA Eaton D., Foster J.S., Grimaldi C., Gu Q., Hass P.E., Heldens S., Huang A.,
RA Kim H.S., Klimowski L., Jin Y., Johnson S., Lee J., Lewis L., Liao D.,
RA Mark M.R., Robbie E., Sanchez C., Schoenfeld J., Seshagiri S., Simmons L.,
RA Singh J., Smith V., Stinson J., Vagts A., Vandlen R.L., Watanabe C.,
RA Wieand D., Woods K., Xie M.-H., Yansura D.G., Yi S., Yu G., Yuan J.,
RA Zhang M., Zhang Z., Goddard A.D., Wood W.I., Godowski P.J., Gray A.M.;
RT "The secreted protein discovery initiative (SPDI), a large-scale effort to
RT identify novel human secreted and transmembrane proteins: a bioinformatics
RT assessment.";
RL Genome Res. 13:2265-2270(2003).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT GLY-144.
RC TISSUE=Placenta;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=14574404; DOI=10.1038/nature02055;
RA Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L.,
RA Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R.,
RA Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D.,
RA Andrews T.D., Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J.,
RA Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H.,
RA Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J.,
RA Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P.,
RA Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V.,
RA Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J.,
RA Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E.,
RA Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J.,
RA French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J.,
RA Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C.,
RA Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A.,
RA Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R.,
RA Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M.,
RA Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K.,
RA Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R.,
RA Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M.,
RA Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A.,
RA Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L.,
RA Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I.,
RA Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y.,
RA Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E.,
RA Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A.,
RA Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W.,
RA Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M.,
RA West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J.,
RA Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M.,
RA Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I.,
RA Rogers J., Beck S.;
RT "The DNA sequence and analysis of human chromosome 6.";
RL Nature 425:805-811(2003).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [6]
RP FUNCTION, INDUCTION, TISSUE SPECIFICITY, AND INTERACTION WITH CD276.
RX PubMed=18650384; DOI=10.1073/pnas.0802423105;
RA Hashiguchi M., Kobori H., Ritprajak P., Kamimura Y., Kozono H., Azuma M.;
RT "Triggering receptor expressed on myeloid cell-like transcript 2 (TLT-2) is
RT a counter-receptor for B7-H3 and enhances T cell responses.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10495-10500(2008).
RN [7]
RP ERRATUM OF PUBMED:18650384.
RA Hashiguchi M., Kobori H., Ritprajak P., Kamimura Y., Kozono H., Azuma M.;
RL Proc. Natl. Acad. Sci. U.S.A. 105:14744-14744(2008).
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.
CC {ECO:0000269|PubMed:12645956, ECO:0000269|PubMed:18650384}.
CC -!- SUBUNIT: Interacts with CD276 and this interaction enhances T-cell
CC activation. {ECO:0000269|PubMed:18650384}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Single-pass type I
CC membrane protein {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Detected in cultured B-cells, T-cell leukemia and
CC monocyte leukemia. Expressed constitutively on CD8 T-cells and induced
CC on CD4 T-cells after activation. {ECO:0000269|PubMed:12645956,
CC ECO:0000269|PubMed:18650384}.
CC -!- INDUCTION: Induced in CD4 T-cells by concanavalin-A.
CC {ECO:0000269|PubMed:18650384}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAI25079.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=AAI25080.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=BAB14668.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AF534824; AAO15022.1; -; mRNA.
DR EMBL; AY358171; AAQ88538.1; -; mRNA.
DR EMBL; AK023755; BAB14668.1; ALT_INIT; mRNA.
DR EMBL; AL133404; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL391903; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC125078; AAI25079.1; ALT_INIT; mRNA.
DR EMBL; BC125079; AAI25080.1; ALT_INIT; mRNA.
DR CCDS; CCDS4853.2; -.
DR RefSeq; NP_079083.2; NM_024807.3.
DR AlphaFoldDB; Q5T2D2; -.
DR SMR; Q5T2D2; -.
DR BioGRID; 122953; 29.
DR IntAct; Q5T2D2; 8.
DR STRING; 9606.ENSP00000418767; -.
DR GlyConnect; 1980; 13 N-Linked glycans (1 site).
DR GlyGen; Q5T2D2; 1 site, 13 N-linked glycans (1 site).
DR iPTMnet; Q5T2D2; -.
DR PhosphoSitePlus; Q5T2D2; -.
DR BioMuta; TREML2; -.
DR DMDM; 116256100; -.
DR MassIVE; Q5T2D2; -.
DR PaxDb; Q5T2D2; -.
DR PeptideAtlas; Q5T2D2; -.
DR PRIDE; Q5T2D2; -.
DR ProteomicsDB; 64330; -.
DR Antibodypedia; 30035; 169 antibodies from 26 providers.
DR DNASU; 79865; -.
DR Ensembl; ENST00000483722.2; ENSP00000418767.1; ENSG00000112195.9.
DR GeneID; 79865; -.
DR KEGG; hsa:79865; -.
DR MANE-Select; ENST00000483722.2; ENSP00000418767.1; NM_024807.4; NP_079083.2.
DR UCSC; uc010jxm.3; human.
DR CTD; 79865; -.
DR DisGeNET; 79865; -.
DR GeneCards; TREML2; -.
DR HGNC; HGNC:21092; TREML2.
DR HPA; ENSG00000112195; Tissue enhanced (bone marrow, lymphoid tissue).
DR MIM; 609715; gene.
DR neXtProt; NX_Q5T2D2; -.
DR OpenTargets; ENSG00000112195; -.
DR PharmGKB; PA134921444; -.
DR VEuPathDB; HostDB:ENSG00000112195; -.
DR eggNOG; ENOG502SPIC; Eukaryota.
DR GeneTree; ENSGT00940000153835; -.
DR HOGENOM; CLU_044854_0_0_1; -.
DR InParanoid; Q5T2D2; -.
DR OMA; LLWPQGC; -.
DR OrthoDB; 1457971at2759; -.
DR PhylomeDB; Q5T2D2; -.
DR TreeFam; TF337556; -.
DR PathwayCommons; Q5T2D2; -.
DR Reactome; R-HSA-198933; Immunoregulatory interactions between a Lymphoid and a non-Lymphoid cell.
DR SignaLink; Q5T2D2; -.
DR BioGRID-ORCS; 79865; 57 hits in 1074 CRISPR screens.
DR GenomeRNAi; 79865; -.
DR Pharos; Q5T2D2; Tbio.
DR PRO; PR:Q5T2D2; -.
DR Proteomes; UP000005640; Chromosome 6.
DR RNAct; Q5T2D2; protein.
DR Bgee; ENSG00000112195; Expressed in blood and 82 other tissues.
DR Genevisible; Q5T2D2; HS.
DR GO; GO:0009986; C:cell surface; IDA:UniProtKB.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; TAS:Reactome.
DR GO; GO:0038023; F:signaling receptor activity; IDA:UniProtKB.
DR GO; GO:0042110; P:T cell activation; IDA:UniProtKB.
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 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..18
FT /evidence="ECO:0000255"
FT CHAIN 19..321
FT /note="Trem-like transcript 2 protein"
FT /id="PRO_0000253857"
FT TOPO_DOM 19..268
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 269..289
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 290..321
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 20..121
FT /note="Ig-like V-type"
FT REGION 189..241
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 89
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 41..105
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 56..63
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT VARIANT 19
FT /note="G -> C (in dbSNP:rs4418164)"
FT /id="VAR_059412"
FT VARIANT 50
FT /note="V -> M (in dbSNP:rs35512890)"
FT /id="VAR_055418"
FT VARIANT 144
FT /note="S -> G (in dbSNP:rs3747742)"
FT /evidence="ECO:0000269|PubMed:14702039"
FT /id="VAR_055419"
FT VARIANT 285
FT /note="V -> I (in dbSNP:rs35521209)"
FT /id="VAR_055420"
FT CONFLICT 23
FT /note="D -> G (in Ref. 5; AAI25080)"
FT /evidence="ECO:0000305"
FT CONFLICT 25
FT /note="V -> A (in Ref. 5; AAI25080)"
FT /evidence="ECO:0000305"
FT CONFLICT 59
FT /note="R -> K (in Ref. 3; BAB14668)"
FT /evidence="ECO:0000305"
FT CONFLICT 129
FT /note="T -> S (in Ref. 5; AAI25079)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 321 AA; 35127 MW; C273DABCED03F3E7 CRC64;
MAPAFLLLLL LWPQGCVSGP SADSVYTKVR LLEGETLSVQ CSYKGYKNRV EGKVWCKIRK
KKCEPGFARV WVKGPRYLLQ DDAQAKVVNI TMVALKLQDS GRYWCMRNTS GILYPLMGFQ
LDVSPAPQTE RNIPFTHLDN ILKSGTVTTG QAPTSGPDAP FTTGVMVFTP GLITLPRLLA
STRPASKTGY SFTATSTTSQ GPRRTMGSQT VTASPSNARD SSAGPESIST KSGDLSTRSP
TTGLCLTSRS LLNRLPSMPS IRHQDVYSTV LGVVLTLLVL MLIMVYGFWK KRHMASYSMC
SDPSTRDPPG RPEPYVEVYL I
