TP8L3_MOUSE
ID TP8L3_MOUSE Reviewed; 204 AA.
AC Q3TBL6;
DT 29-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2005, sequence version 1.
DT 03-AUG-2022, entry version 109.
DE RecName: Full=Tumor necrosis factor alpha-induced protein 8-like protein 3;
DE Short=TNF alpha-induced protein 8-like protein 3;
DE Short=TNFAIP8-like protein 3;
GN Name=Tnfaip8l3;
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=NOD;
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].
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 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [4]
RP TISSUE SPECIFICITY, FUNCTION, DISRUPTION PHENOTYPE, MUTAGENESIS OF LYS-33;
RP LYS-34; LYS-38; LYS-42; LEU-60; ARG-93 AND ARG-109, AND SUBCELLULAR
RP LOCATION.
RX PubMed=25242044; DOI=10.1016/j.ccr.2014.07.025;
RA Fayngerts S.A., Wu J., Oxley C.L., Liu X., Vourekas A., Cathopoulis T.,
RA Wang Z., Cui J., Liu S., Sun H., Lemmon M.A., Zhang L., Shi Y., Chen Y.H.;
RT "TIPE3 is the transfer protein of lipid second messengers that promote
RT cancer.";
RL Cancer Cell 26:465-478(2014).
RN [5]
RP TISSUE SPECIFICITY, AND SUBCELLULAR LOCATION.
RX PubMed=25479791; DOI=10.1369/0022155414564871;
RA Cui J., Hao C., Zhang W., Shao J., Zhang N., Zhang G., Liu S.;
RT "Identical expression profiling of human and murine TIPE3 protein reveals
RT links to its functions.";
RL J. Histochem. Cytochem. 63:206-216(2015).
CC -!- FUNCTION: Acts as a lipid transfer protein. Preferentially captures and
CC shuttles two lipid second messengers, i.e., phosphatidylinositol
CC 4,5- bisphosphate and phosphatidylinositol 3,4,5-trisphosphate and
CC increases their levels in the plasma membrane. Additionally, may also
CC function as a lipid-presenting protein to enhance the activity of the
CC PI3K-AKT and MEK-ERK pathways. May act as a regulator of tumorigenesis
CC through its activation of phospholipid signaling.
CC {ECO:0000269|PubMed:25242044}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:25479791}. Cell
CC membrane {ECO:0000269|PubMed:25242044}. Note=On PDGF activation,
CC translocates from cytoplasm to plasma membrane.
CC {ECO:0000269|PubMed:25242044}.
CC -!- TISSUE SPECIFICITY: Widely expressed (at protein level).
CC {ECO:0000269|PubMed:25242044, ECO:0000269|PubMed:25479791}.
CC -!- DOMAIN: The N-terminal domain (AA 2-20) is essential for its effect on
CC cell growth and survival. {ECO:0000269|PubMed:25242044}.
CC -!- DISRUPTION PHENOTYPE: Deficient mice develop normally during the first
CC 3 months of life under pathogen-free conditions. However, following
CC subcutaneous injection of the carcinogen 3-methylcholanthrene,
CC deficient mice exhibit markedly delayed skin tumor onset and reduced
CC tumor size compared with wild-type mice. {ECO:0000269|PubMed:25479791}.
CC -!- SIMILARITY: Belongs to the TNFAIP8 family. {ECO:0000305}.
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DR EMBL; AK170374; BAE41754.1; -; mRNA.
DR EMBL; AK171174; BAE42293.1; -; mRNA.
DR EMBL; BC118003; AAI18004.1; -; mRNA.
DR EMBL; BC119769; AAI19770.1; -; mRNA.
DR CCDS; CCDS40641.1; -.
DR RefSeq; NP_001028707.1; NM_001033535.3.
DR AlphaFoldDB; Q3TBL6; -.
DR SMR; Q3TBL6; -.
DR STRING; 10090.ENSMUSP00000096356; -.
DR iPTMnet; Q3TBL6; -.
DR PhosphoSitePlus; Q3TBL6; -.
DR MaxQB; Q3TBL6; -.
DR PaxDb; Q3TBL6; -.
DR PRIDE; Q3TBL6; -.
DR ProteomicsDB; 297500; -.
DR Antibodypedia; 57338; 93 antibodies from 22 providers.
DR Ensembl; ENSMUST00000098760; ENSMUSP00000096356; ENSMUSG00000074345.
DR GeneID; 244882; -.
DR KEGG; mmu:244882; -.
DR UCSC; uc009pmt.2; mouse.
DR CTD; 388121; -.
DR MGI; MGI:2685363; Tnfaip8l3.
DR VEuPathDB; HostDB:ENSMUSG00000074345; -.
DR eggNOG; ENOG502QRE6; Eukaryota.
DR GeneTree; ENSGT00390000003488; -.
DR HOGENOM; CLU_085918_1_0_1; -.
DR InParanoid; Q3TBL6; -.
DR OMA; RMCEGIN; -.
DR OrthoDB; 1284744at2759; -.
DR PhylomeDB; Q3TBL6; -.
DR TreeFam; TF323415; -.
DR Reactome; R-MMU-1483255; PI Metabolism.
DR BioGRID-ORCS; 244882; 1 hit in 74 CRISPR screens.
DR PRO; PR:Q3TBL6; -.
DR Proteomes; UP000000589; Chromosome 9.
DR RNAct; Q3TBL6; protein.
DR Bgee; ENSMUSG00000074345; Expressed in dentate gyrus of hippocampal formation granule cell and 31 other tissues.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR GO; GO:0035091; F:phosphatidylinositol binding; IDA:UniProtKB.
DR GO; GO:0008526; F:phosphatidylinositol transfer activity; IMP:UniProtKB.
DR GO; GO:0048017; P:inositol lipid-mediated signaling; IDA:UniProtKB.
DR GO; GO:0015914; P:phospholipid transport; IDA:UniProtKB.
DR GO; GO:0070374; P:positive regulation of ERK1 and ERK2 cascade; IDA:UniProtKB.
DR GO; GO:0043552; P:positive regulation of phosphatidylinositol 3-kinase activity; IDA:UniProtKB.
DR GO; GO:0051897; P:positive regulation of protein kinase B signaling; IDA:UniProtKB.
DR GO; GO:0042981; P:regulation of apoptotic process; IEA:InterPro.
DR GO; GO:0019216; P:regulation of lipid metabolic process; IDA:UniProtKB.
DR Gene3D; 1.20.1440.160; -; 1.
DR InterPro; IPR008477; TNFAIP8-like.
DR InterPro; IPR038355; TNFAIP8_sf.
DR PANTHER; PTHR12757; PTHR12757; 1.
DR Pfam; PF05527; DUF758; 1.
PE 1: Evidence at protein level;
KW Cell membrane; Cytoplasm; Lipid transport; Membrane; Reference proteome;
KW Transport.
FT CHAIN 1..204
FT /note="Tumor necrosis factor alpha-induced protein 8-like
FT protein 3"
FT /id="PRO_0000331425"
FT REGION 1..20
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 21..204
FT /note="Binding to phosphoinositides"
FT MUTAGEN 33
FT /note="K->Q: Reduces binding to phosphoinositide; when
FT associated with GLN-34; GLN-38 AND GLN-42."
FT /evidence="ECO:0000269|PubMed:25242044"
FT MUTAGEN 34
FT /note="K->Q: Reduces binding to phosphoinositide; when
FT associated with GLN-33; GLN-38 AND GLN-42."
FT /evidence="ECO:0000269|PubMed:25242044"
FT MUTAGEN 38
FT /note="K->Q: Reduces binding to phosphoinositide; when
FT associated with GLN-33; GLN-34 AND GLN-42."
FT /evidence="ECO:0000269|PubMed:25242044"
FT MUTAGEN 42
FT /note="K->Q: Reduces binding to phosphoinositide; when
FT associated with GLN-33; GLN-34 AND GLN-38."
FT /evidence="ECO:0000269|PubMed:25242044"
FT MUTAGEN 60
FT /note="L->W: Reduces binding to phosphoinositide."
FT /evidence="ECO:0000269|PubMed:25242044"
FT MUTAGEN 93
FT /note="R->Q: Reduces binding to phosphoinositide; when
FT associated with GLN-109."
FT /evidence="ECO:0000269|PubMed:25242044"
FT MUTAGEN 109
FT /note="R->Q: Reduces binding to phosphoinositide; when
FT associated with GLN-93."
FT /evidence="ECO:0000269|PubMed:25242044"
SQ SEQUENCE 204 AA; 23243 MW; 2A5830746A4D8AE5 CRC64;
MDSDSGEQSE GEPGTAAGPH VFSSKNLALQ AQKKILSKIA SKTVANMLID DTSSEIFDEL
YKVTEIHTHN KKEAHKIMKD AIKVAIKIGI LYRNKQFSQE EVIIVEKLRK KLNQTAMTMV
SFYEVEYTFD TNVLSKLLHE CKDLVHELVQ RHLTPRTHGR INHVFNHFAD VEFLSTLYGP
HGNCRPNLKR ICEGINKLLD DKIL
