TCL1A_MOUSE
ID TCL1A_MOUSE Reviewed; 116 AA.
AC P56280;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 15-JUL-1998, sequence version 1.
DT 03-AUG-2022, entry version 139.
DE RecName: Full=T-cell leukemia/lymphoma protein 1A;
DE AltName: Full=Oncogene TCL-1;
DE Short=Oncogene TCL1;
DE AltName: Full=Protein p14 TCL1;
GN Name=Tcl1a; Synonyms=Tcl1;
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].
RX PubMed=9285687; DOI=10.1038/sj.onc.1201246;
RA Narducci M.G., Virgilio L., Engiles J.B., Buchberg A.M., Billips L.,
RA Facchiano A., Croce C.M., Russo G., Rothstein J.L.;
RT "The murine Tcl1 oncogene: embryonic and lymphoid cell expression.";
RL Oncogene 15:919-926(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Egg;
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 SUBCELLULAR LOCATION.
RX PubMed=10716693; DOI=10.1073/pnas.97.7.3028;
RA Pekarsky Y., Koval A., Hallas C., Bichi R., Tresini M., Malstrom S.,
RA Russo G., Tsichlis P., Croce C.M.;
RT "Tcl1 enhances Akt kinase activity and mediates its nuclear
RT translocation.";
RL Proc. Natl. Acad. Sci. U.S.A. 97:3028-3033(2000).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS).
RX PubMed=11679718; DOI=10.1107/s090744490101352x;
RA Petock J.M., Torshin I.Y., Wang Y.-F., Du Bois G.C., Croce C.M.,
RA Harrison R.W., Weber I.T.;
RT "Structure of murine Tcl1 at 2.5 A resolution and implications for the TCL
RT oncogene family.";
RL Acta Crystallogr. D 57:1545-1551(2001).
CC -!- FUNCTION: Enhances the phosphorylation and activation of AKT1 and AKT2.
CC Enhances cell proliferation, stabilizes mitochondrial membrane
CC potential and promotes cell survival (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Homodimer. Interacts with AKT1, AKT2 and AKT3 (via PH domain).
CC Interacts with PNPT1; the interaction has no effect on PNPT1
CC exonuclease activity (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:10716693}. Nucleus
CC {ECO:0000269|PubMed:10716693}. Microsome {ECO:0000250}. Endoplasmic
CC reticulum {ECO:0000250}. Note=Microsomal fraction. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the TCL1 family. {ECO:0000305}.
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DR EMBL; AF031956; AAB87461.1; -; mRNA.
DR EMBL; Y15376; CAA75599.1; -; mRNA.
DR EMBL; BC052336; AAH52336.1; -; mRNA.
DR CCDS; CCDS36549.1; -.
DR RefSeq; NP_033363.1; NM_009337.3.
DR PDB; 1JNP; X-ray; 2.50 A; A/B=1-116.
DR PDBsum; 1JNP; -.
DR AlphaFoldDB; P56280; -.
DR SMR; P56280; -.
DR BioGRID; 204023; 1.
DR STRING; 10090.ENSMUSP00000036066; -.
DR iPTMnet; P56280; -.
DR PhosphoSitePlus; P56280; -.
DR REPRODUCTION-2DPAGE; P56280; -.
DR PaxDb; P56280; -.
DR PRIDE; P56280; -.
DR Antibodypedia; 65; 434 antibodies from 40 providers.
DR DNASU; 21432; -.
DR Ensembl; ENSMUST00000041316; ENSMUSP00000036066; ENSMUSG00000041359.
DR GeneID; 21432; -.
DR KEGG; mmu:21432; -.
DR UCSC; uc007oyd.2; mouse.
DR CTD; 21432; -.
DR MGI; MGI:1097166; Tcl1.
DR VEuPathDB; HostDB:ENSMUSG00000041359; -.
DR eggNOG; ENOG502TDVJ; Eukaryota.
DR GeneTree; ENSGT00390000006885; -.
DR HOGENOM; CLU_168379_0_1_1; -.
DR InParanoid; P56280; -.
DR OMA; LWIWERS; -.
DR PhylomeDB; P56280; -.
DR TreeFam; TF337903; -.
DR BioGRID-ORCS; 21432; 2 hits in 73 CRISPR screens.
DR ChiTaRS; Tcl1; mouse.
DR EvolutionaryTrace; P56280; -.
DR PRO; PR:P56280; -.
DR Proteomes; UP000000589; Chromosome 12.
DR RNAct; P56280; protein.
DR Bgee; ENSMUSG00000041359; Expressed in animal zygote and 17 other tissues.
DR ExpressionAtlas; P56280; baseline and differential.
DR Genevisible; P56280; MM.
DR GO; GO:0005938; C:cell cortex; IDA:MGI.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0005783; C:endoplasmic reticulum; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; IDA:MGI.
DR GO; GO:1990917; C:ooplasm; IDA:MGI.
DR GO; GO:0045120; C:pronucleus; IDA:MGI.
DR GO; GO:0032991; C:protein-containing complex; ISO:MGI.
DR GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR GO; GO:0019901; F:protein kinase binding; ISO:MGI.
DR GO; GO:0043539; F:protein serine/threonine kinase activator activity; ISO:MGI.
DR GO; GO:0032148; P:activation of protein kinase B activity; IMP:CACAO.
DR GO; GO:0071356; P:cellular response to tumor necrosis factor; ISO:MGI.
DR GO; GO:0043066; P:negative regulation of apoptotic process; ISO:MGI.
DR GO; GO:0010629; P:negative regulation of gene expression; IMP:MGI.
DR GO; GO:0008284; P:positive regulation of cell population proliferation; ISO:MGI.
DR GO; GO:0010918; P:positive regulation of mitochondrial membrane potential; ISO:MGI.
DR GO; GO:0033138; P:positive regulation of peptidyl-serine phosphorylation; ISO:MGI.
DR GO; GO:0071902; P:positive regulation of protein serine/threonine kinase activity; ISO:MGI.
DR GO; GO:0031334; P:positive regulation of protein-containing complex assembly; ISO:MGI.
DR GO; GO:2000036; P:regulation of stem cell population maintenance; IGI:MGI.
DR GO; GO:0035019; P:somatic stem cell population maintenance; IMP:MGI.
DR Gene3D; 2.40.15.10; -; 1.
DR InterPro; IPR004832; TCL1_MTCP1.
DR InterPro; IPR036672; TCL1_MTCP1_sf.
DR PANTHER; PTHR14060; PTHR14060; 1.
DR Pfam; PF01840; TCL1_MTCP1; 1.
DR SUPFAM; SSF50904; SSF50904; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Endoplasmic reticulum; Microsome; Nucleus;
KW Reference proteome.
FT CHAIN 1..116
FT /note="T-cell leukemia/lymphoma protein 1A"
FT /id="PRO_0000184489"
FT STRAND 16..20
FT /evidence="ECO:0007829|PDB:1JNP"
FT STRAND 22..24
FT /evidence="ECO:0007829|PDB:1JNP"
FT STRAND 26..28
FT /evidence="ECO:0007829|PDB:1JNP"
FT STRAND 33..40
FT /evidence="ECO:0007829|PDB:1JNP"
FT STRAND 42..44
FT /evidence="ECO:0007829|PDB:1JNP"
FT STRAND 46..51
FT /evidence="ECO:0007829|PDB:1JNP"
FT TURN 63..65
FT /evidence="ECO:0007829|PDB:1JNP"
FT STRAND 74..76
FT /evidence="ECO:0007829|PDB:1JNP"
FT STRAND 82..84
FT /evidence="ECO:0007829|PDB:1JNP"
FT STRAND 89..94
FT /evidence="ECO:0007829|PDB:1JNP"
FT STRAND 96..100
FT /evidence="ECO:0007829|PDB:1JNP"
FT STRAND 102..107
FT /evidence="ECO:0007829|PDB:1JNP"
SQ SEQUENCE 116 AA; 14112 MW; 46DEED2F973F389A CRC64;
MATQRAHRAE TPAHPNRLWI WEKHVYLDEF RRSWLPVVIK SNEKFQVILR QEDVTLGEAM
SPSQLVPYEL PLMWQLYPKD RYRSCDSMYW QILYHIKFRD VEDMLLELID SESNDE
