TREM3_MOUSE
ID TREM3_MOUSE Reviewed; 183 AA.
AC Q9JKE1;
DT 12-SEP-2018, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 151.
DE RecName: Full=Triggering receptor expressed on myeloid cells 3 {ECO:0000303|PubMed:11754004};
DE Short=TREM-3 {ECO:0000303|PubMed:11754004};
DE Flags: Precursor;
GN Name=Trem3 {ECO:0000303|PubMed:11754004, ECO:0000312|MGI:MGI:1930003};
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 {ECO:0000312|EMBL:AAF69835.1};
RN [1] {ECO:0000312|EMBL:AAF69835.1}
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Bouchon A., Colonna M.;
RL Submitted (MAR-2000) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000312|EMBL:BAC37636.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Bone;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3] {ECO:0000312|Proteomes:UP000000589}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [4] {ECO:0000312|EMBL:EDL23603.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [5] {ECO:0000312|EMBL:AAI27036.1}
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] {ECO:0000305}
RP FUNCTION, SUBUNIT, INTERACTION WITH TYROBP, SUBCELLULAR LOCATION, TISSUE
RP SPECIFICITY, AND INDUCTION.
RX PubMed=11754004;
RX DOI=10.1002/1521-4141(200201)32:1<59::aid-immu59>3.0.co;2-u;
RA Chung D.H., Seaman W.E., Daws M.R.;
RT "Characterization of TREM-3, an activating receptor on mouse macrophages:
RT definition of a family of single Ig domain receptors on mouse chromosome
RT 17.";
RL Eur. J. Immunol. 32:59-66(2002).
CC -!- FUNCTION: Forms a receptor signaling complex with TYROBP/DAP12 which
CC mediates activation of macrophages as part of the innate immune
CC response. {ECO:0000269|PubMed:11754004}.
CC -!- SUBUNIT: Interacts with TYROBP/DAP12. {ECO:0000269|PubMed:11754004}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:11754004};
CC Single-pass type I membrane protein {ECO:0000255}.
CC -!- TISSUE SPECIFICITY: Expressed in macrophages and in T-cells.
CC {ECO:0000269|PubMed:11754004}.
CC -!- INDUCTION: Induced by lipopolysaccharide (LPS). Interferon gamma (IFNG)
CC decreases expression. {ECO:0000269|PubMed:11754004}.
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DR EMBL; AF241220; AAF69835.1; -; mRNA.
DR EMBL; AK079407; BAC37636.1; -; mRNA.
DR EMBL; AC241601; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH466559; EDL23603.1; -; Genomic_DNA.
DR EMBL; BC127035; AAI27036.1; -; mRNA.
DR EMBL; BC127036; AAI27037.1; -; mRNA.
DR CCDS; CCDS28861.1; -.
DR RefSeq; NP_067382.1; NM_021407.3.
DR AlphaFoldDB; Q9JKE1; -.
DR SMR; Q9JKE1; -.
DR STRING; 10090.ENSMUSP00000044478; -.
DR GlyGen; Q9JKE1; 1 site.
DR MaxQB; Q9JKE1; -.
DR PaxDb; Q9JKE1; -.
DR PRIDE; Q9JKE1; -.
DR DNASU; 58218; -.
DR Ensembl; ENSMUST00000048065; ENSMUSP00000044478; ENSMUSG00000041754.
DR GeneID; 58218; -.
DR KEGG; mmu:58218; -.
DR UCSC; uc008cwy.2; mouse.
DR CTD; 58218; -.
DR MGI; MGI:1930003; Trem3.
DR VEuPathDB; HostDB:ENSMUSG00000041754; -.
DR eggNOG; ENOG502TE0T; Eukaryota.
DR GeneTree; ENSGT00470000042299; -.
DR HOGENOM; CLU_110755_0_0_1; -.
DR InParanoid; Q9JKE1; -.
DR OMA; TCGFILN; -.
DR OrthoDB; 1472586at2759; -.
DR PhylomeDB; Q9JKE1; -.
DR TreeFam; TF339293; -.
DR BioGRID-ORCS; 58218; 2 hits in 72 CRISPR screens.
DR PRO; PR:Q9JKE1; -.
DR Proteomes; UP000000589; Chromosome 17.
DR RNAct; Q9JKE1; protein.
DR Bgee; ENSMUSG00000041754; Expressed in granulocyte and 16 other tissues.
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:0016477; P:cell migration; IGI:MGI.
DR GO; GO:0030593; P:neutrophil chemotaxis; IGI:MGI.
DR GO; GO:0072672; P:neutrophil extravasation; IGI:MGI.
DR GO; GO:0070945; P:neutrophil-mediated killing of gram-negative bacterium; IGI:MGI.
DR GO; GO:0045089; P:positive regulation of innate immune response; IDA:UniProtKB.
DR Gene3D; 2.60.40.10; -; 1.
DR InterPro; IPR036179; Ig-like_dom_sf.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR013106; Ig_V-set.
DR Pfam; PF07686; V-set; 1.
DR SUPFAM; SSF48726; SSF48726; 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..19
FT /evidence="ECO:0000255"
FT CHAIN 20..183
FT /note="Triggering receptor expressed on myeloid cells 3"
FT /evidence="ECO:0000255"
FT /id="PRO_5015099788"
FT TOPO_DOM 20..138
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 139..159
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 160..183
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT DOMAIN 30..128
FT /note="Ig-like V-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT CARBOHYD 33
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 38..110
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
SQ SEQUENCE 183 AA; 20452 MW; B0F0E05B512754C7 CRC64;
MSPLLLWLGL MLCVSGLQAG DEEEHKCFLE GENLTLTCPY NIMLYSLSLK AWQRVRSHGS
PETLVLTNTR KADFNVARAG KYLLEDYPTE SVVKVTVTGL QRQDVGLYQC VVYLSPDNVI
ILRQRIRLAW CQGKPVMVIV LTCGFILNKG LVFSVLFVFL CKAGPKVLQP SKTSKVQGVS
EKQ
