T106A_MOUSE
ID T106A_MOUSE Reviewed; 261 AA.
AC Q8VC04; Q3U4J0; Q3U9D3; Q3UEA5; Q8CIC3;
DT 27-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 03-AUG-2022, entry version 125.
DE RecName: Full=Transmembrane protein 106A;
GN Name=Tmem106a;
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 [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J, and NOD; TISSUE=Amnion, Bone marrow, Placenta, and Spleen;
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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Czech II, and FVB/N; TISSUE=Liver, and Mammary tumor;
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 [3]
RP FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND INDUCTION BY
RP THIOGLYCOLLATE.
RX PubMed=26215746; DOI=10.1038/srep12461;
RA Dai H., Xu D., Su J., Jang J., Chen Y.;
RT "Transmembrane protein 106a activates mouse peritoneal macrophages via the
RT MAPK and NF-kappaB signaling pathways.";
RL Sci. Rep. 5:12461-12461(2015).
CC -!- FUNCTION: Activates macrophages and polarizes them into M1-like
CC macrophages through the activation of the MAPK and NF-kappaB signaling
CC pathway (PubMed:26215746). Upon activation, up-regulates the expression
CC of CD80, CD86, CD69 and MHC II on macrophages, and induces the release
CC of pro-inflammatory cytokines such as TNF, IL1B, IL6, CCL2 and nitric
CC oxide (PubMed:26215746). May play a role in inhibition of proliferation
CC and migration (By similarity). {ECO:0000250|UniProtKB:Q96A25,
CC ECO:0000269|PubMed:26215746}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:26215746};
CC Single-pass membrane protein {ECO:0000255}.
CC -!- TISSUE SPECIFICITY: Expressed in liver, spleen, lung, kidney, lymph
CC nodes and adipose tissue (at protein level) (PubMed:26215746).
CC Expressed by macrophages (PubMed:26215746).
CC {ECO:0000269|PubMed:26215746}.
CC -!- INDUCTION: Cell surface expression is increased by Thioglycollate in
CC elicited macrophages. {ECO:0000269|PubMed:26215746}.
CC -!- SIMILARITY: Belongs to the TMEM106 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAE29006.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=BAE30734.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AK146019; BAE26837.1; -; mRNA.
DR EMBL; AK149650; BAE29006.1; ALT_FRAME; mRNA.
DR EMBL; AK150285; BAE29440.1; -; mRNA.
DR EMBL; AK151842; BAE30734.1; ALT_FRAME; mRNA.
DR EMBL; AK152741; BAE31461.1; -; mRNA.
DR EMBL; AK154217; BAE32441.1; -; mRNA.
DR EMBL; AK169081; BAE40865.1; -; mRNA.
DR EMBL; AK170900; BAE42103.1; -; mRNA.
DR EMBL; AK172282; BAE42923.1; -; mRNA.
DR EMBL; BC022145; AAH22145.1; -; mRNA.
DR EMBL; BC033268; AAH33268.1; -; mRNA.
DR CCDS; CCDS25476.1; -.
DR RefSeq; NP_659079.1; NM_144830.3.
DR RefSeq; XP_006533101.1; XM_006533038.3.
DR RefSeq; XP_017169971.1; XM_017314482.1.
DR AlphaFoldDB; Q8VC04; -.
DR STRING; 10090.ENSMUSP00000045832; -.
DR iPTMnet; Q8VC04; -.
DR PhosphoSitePlus; Q8VC04; -.
DR EPD; Q8VC04; -.
DR MaxQB; Q8VC04; -.
DR PaxDb; Q8VC04; -.
DR PeptideAtlas; Q8VC04; -.
DR PRIDE; Q8VC04; -.
DR ProteomicsDB; 254801; -.
DR Antibodypedia; 61733; 64 antibodies from 19 providers.
DR DNASU; 217203; -.
DR Ensembl; ENSMUST00000039581; ENSMUSP00000045832; ENSMUSG00000034947.
DR Ensembl; ENSMUST00000100403; ENSMUSP00000097971; ENSMUSG00000034947.
DR GeneID; 217203; -.
DR KEGG; mmu:217203; -.
DR UCSC; uc007lpl.1; mouse.
DR CTD; 113277; -.
DR MGI; MGI:1922056; Tmem106a.
DR VEuPathDB; HostDB:ENSMUSG00000034947; -.
DR eggNOG; ENOG502RY0I; Eukaryota.
DR GeneTree; ENSGT00940000161546; -.
DR HOGENOM; CLU_089337_1_0_1; -.
DR InParanoid; Q8VC04; -.
DR OMA; CSYLCHS; -.
DR OrthoDB; 1175832at2759; -.
DR PhylomeDB; Q8VC04; -.
DR TreeFam; TF328907; -.
DR BioGRID-ORCS; 217203; 1 hit in 72 CRISPR screens.
DR ChiTaRS; Tmem106a; mouse.
DR PRO; PR:Q8VC04; -.
DR Proteomes; UP000000589; Chromosome 11.
DR RNAct; Q8VC04; protein.
DR Bgee; ENSMUSG00000034947; Expressed in right kidney and 135 other tissues.
DR ExpressionAtlas; Q8VC04; baseline and differential.
DR Genevisible; Q8VC04; MM.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR GO; GO:0035780; P:CD80 biosynthetic process; IDA:UniProtKB.
DR GO; GO:0035781; P:CD86 biosynthetic process; IDA:UniProtKB.
DR GO; GO:0045087; P:innate immune response; IEA:UniProtKB-KW.
DR GO; GO:0042116; P:macrophage activation; IDA:UniProtKB.
DR GO; GO:0043123; P:positive regulation of I-kappaB kinase/NF-kappaB signaling; IDA:UniProtKB.
DR GO; GO:0032731; P:positive regulation of interleukin-1 beta production; IDA:UniProtKB.
DR GO; GO:0032755; P:positive regulation of interleukin-6 production; IDA:UniProtKB.
DR GO; GO:0043410; P:positive regulation of MAPK cascade; IDA:UniProtKB.
DR GO; GO:0045348; P:positive regulation of MHC class II biosynthetic process; IDA:UniProtKB.
DR GO; GO:1904407; P:positive regulation of nitric oxide metabolic process; IDA:UniProtKB.
DR GO; GO:0032760; P:positive regulation of tumor necrosis factor production; IDA:UniProtKB.
DR InterPro; IPR009790; TMEM106.
DR PANTHER; PTHR28556; PTHR28556; 1.
DR Pfam; PF07092; DUF1356; 1.
PE 1: Evidence at protein level;
KW Cell membrane; Immunity; Innate immunity; Membrane; Reference proteome;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..261
FT /note="Transmembrane protein 106A"
FT /id="PRO_0000242138"
FT TRANSMEM 93..113
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 1..23
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 43
FT /note="S -> F (in Ref. 2; AAH33268)"
FT /evidence="ECO:0000305"
FT CONFLICT 75
FT /note="L -> M (in Ref. 1; BAE32441)"
FT /evidence="ECO:0000305"
FT CONFLICT 141
FT /note="T -> M (in Ref. 2; AAH33268)"
FT /evidence="ECO:0000305"
FT CONFLICT 247
FT /note="R -> T (in Ref. 1; BAE29006)"
FT /evidence="ECO:0000305"
FT CONFLICT 254
FT /note="H -> Q (in Ref. 1; BAE29006)"
FT /evidence="ECO:0000305"
FT CONFLICT 257
FT /note="L -> V (in Ref. 1; BAE29006)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 261 AA; 29109 MW; 51013C0D7E348D1B CRC64;
MGKAVSQLTS RKDEDKPILP DNPAMASQAA NYFSTGSSKP AHSCMPYEKA ASSSFVTCPT
CQGNGEIPQE QEKQLVALIP YGDQRLKPRR TKLFVFLSVA ICLLIFSLTI FFLYPRPIAV
RPVGLNSSTV TFEDAHVQLN TTNVLNIFNS NFYPITVTQL TAEVLHQASV VGQVTSSLRL
HIGPLASEQM PYEVASRILD ENTYKICTWP KIRVHHILLN IQGSLTCSFL SHPQQLPFES
FEYVDCRENM SLPHLELPRP A
