ID MCTS1_MOUSE Reviewed; 181 AA.
AC Q9DB27; Q3UUI6;
DT 22-JUL-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 24-JAN-2024, entry version 160.
DE RecName: Full=Malignant T-cell-amplified sequence 1;
DE Short=MCT-1;
DE AltName: Full=Multiple copies T-cell malignancies 1;
GN Name=Mcts1;
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] (ISOFORMS 1 AND 2).
RC STRAIN=C57BL/6J, and NOD; TISSUE=Cerebellum, Hypothalamus, and Thymus;
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 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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=FVB/N; TISSUE=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 [4]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, and Testis;
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).
CC -!- FUNCTION: Anti-oncogene that plays a role in cell cycle regulation;
CC decreases cell doubling time and anchorage-dependent growth; shortens
CC the duration of G1 transit time and G1/S transition. When
CC constitutively expressed, increases CDK4 and CDK6 kinases activity and
CC CCND1/cyclin D1 protein level, as well as G1 cyclin/CDK complex
CC formation. Involved in translation initiation; promotes recruitment of
CC aminoacetyled initiator tRNA to P site of 40S ribosomes. Can promote
CC release of deacylated tRNA and mRNA from recycled 40S subunits
CC following ABCE1-mediated dissociation of post-termination ribosomal
CC complexes into subunits. Plays a role as translation enhancer; recruits
CC the density-regulated protein/DENR and binds to the cap complex of the
CC 5'-terminus of mRNAs, subsequently altering the mRNA translation
CC profile; up-regulates protein levels of BCL2L2, TFDP1, MRE11, CCND1 and
CC E2F1, while mRNA levels remains constant. Hyperactivates DNA damage
CC signaling pathway; increased gamma-irradiation-induced phosphorylation
CC of histone H2AX, and induces damage foci formation. Increases the
CC overall number of chromosomal abnormalities such as larger chromosomes
CC formation and multiple chromosomal fusions when overexpressed in gamma-
CC irradiated cells. May play a role in promoting lymphoid tumor
CC development: lymphoid cell lines overexpressing MCTS1 exhibit increased
CC growth rates and display increased protection against apoptosis. May
CC contribute to the pathogenesis and progression of breast cancer via
CC promotion of angiogenesis through the decline of inhibitory
CC THBS1/thrombospondin-1, and inhibition of apoptosis. Involved in the
CC process of proteasome degradation to down-regulate Tumor suppressor
CC p53/TP53 in breast cancer cell; Positively regulates phosphorylation of
CC MAPK1 and MAPK3 (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Interacts (via PUA domain) with DENR. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9DB27-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9DB27-2; Sequence=VSP_034857;
CC -!- DOMAIN: The PUA RNA-binding domain is critical for cap binding, but not
CC sufficient for translation enhancer function. MCT1 N-terminal region is
CC required to enhance translation possibly through interaction with other
CC proteins (By similarity). {ECO:0000250}.
CC -!- PTM: Phosphorylation is critical for stabilization and promotion of
CC cell proliferation. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the MCTS1 family. {ECO:0000305}.
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DR EMBL; AK005292; BAB23936.1; -; mRNA.
DR EMBL; AK087975; BAC40069.1; -; mRNA.
DR EMBL; AK138385; BAE23639.1; -; mRNA.
DR EMBL; AL513356; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL845279; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC010486; AAH10486.1; -; mRNA.
DR CCDS; CCDS30094.1; -. [Q9DB27-1]
DR RefSeq; NP_081178.1; NM_026902.3. [Q9DB27-1]
DR RefSeq; XP_006541598.1; XM_006541535.2.
DR AlphaFoldDB; Q9DB27; -.
DR SMR; Q9DB27; -.
DR BioGRID; 213164; 38.
DR IntAct; Q9DB27; 1.
DR MINT; Q9DB27; -.
DR STRING; 10090.ENSMUSP00000000365; -.
DR iPTMnet; Q9DB27; -.
DR PhosphoSitePlus; Q9DB27; -.
DR SwissPalm; Q9DB27; -.
DR EPD; Q9DB27; -.
DR MaxQB; Q9DB27; -.
DR PaxDb; 10090-ENSMUSP00000000365; -.
DR PeptideAtlas; Q9DB27; -.
DR ProteomicsDB; 295718; -. [Q9DB27-1]
DR ProteomicsDB; 295719; -. [Q9DB27-2]
DR Pumba; Q9DB27; -.
DR Antibodypedia; 29908; 309 antibodies from 29 providers.
DR DNASU; 68995; -.
DR Ensembl; ENSMUST00000000365.3; ENSMUSP00000000365.3; ENSMUSG00000000355.14. [Q9DB27-1]
DR GeneID; 68995; -.
DR KEGG; mmu:68995; -.
DR UCSC; uc009tad.1; mouse. [Q9DB27-1]
DR UCSC; uc009tae.1; mouse. [Q9DB27-2]
DR AGR; MGI:1916245; -.
DR CTD; 28985; -.
DR MGI; MGI:1916245; Mcts1.
DR VEuPathDB; HostDB:ENSMUSG00000000355; -.
DR eggNOG; KOG2523; Eukaryota.
DR GeneTree; ENSGT00550000074964; -.
DR HOGENOM; CLU_090468_0_1_1; -.
DR InParanoid; Q9DB27; -.
DR OMA; SINKGHG; -.
DR OrthoDB; 5036262at2759; -.
DR PhylomeDB; Q9DB27; -.
DR TreeFam; TF315123; -.
DR BioGRID-ORCS; 68995; 13 hits in 78 CRISPR screens.
DR ChiTaRS; Mcts1; mouse.
DR PRO; PR:Q9DB27; -.
DR Proteomes; UP000000589; Chromosome X.
DR RNAct; Q9DB27; Protein.
DR Bgee; ENSMUSG00000000355; Expressed in facial nucleus and 247 other cell types or tissues.
DR Genevisible; Q9DB27; MM.
DR GO; GO:0022627; C:cytosolic small ribosomal subunit; IEA:Ensembl.
DR GO; GO:0003723; F:RNA binding; IEA:InterPro.
DR GO; GO:0003743; F:translation initiation factor activity; IEA:UniProtKB-KW.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0006974; P:DNA damage response; IEA:UniProtKB-KW.
DR GO; GO:0001731; P:formation of translation preinitiation complex; ISO:MGI.
DR GO; GO:0075522; P:IRES-dependent viral translational initiation; ISO:MGI.
DR GO; GO:0032790; P:ribosome disassembly; ISO:MGI.
DR CDD; cd11609; MCT1_N; 1.
DR CDD; cd21155; PUA_MCTS-1-like; 1.
DR Gene3D; 3.10.400.20; -; 1.
DR InterPro; IPR016437; MCT-1/Tma20.
DR InterPro; IPR041366; Pre-PUA.
DR InterPro; IPR002478; PUA.
DR InterPro; IPR015947; PUA-like_sf.
DR InterPro; IPR004521; Uncharacterised_CHP00451.
DR NCBIfam; TIGR00451; unchar_dom_2; 1.
DR PANTHER; PTHR22798:SF10; MALIGNANT T-CELL-AMPLIFIED SEQUENCE 1; 1.
DR PANTHER; PTHR22798; MCT-1 PROTEIN; 1.
DR Pfam; PF17832; Pre-PUA; 1.
DR Pfam; PF01472; PUA; 1.
DR PIRSF; PIRSF005067; Tma_RNA-bind_prd; 1.
DR SMART; SM00359; PUA; 1.
DR SUPFAM; SSF88697; PUA domain-like; 1.
DR PROSITE; PS50890; PUA; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cell cycle; Cytoplasm; DNA damage; Growth regulation;
KW Initiation factor; Phosphoprotein; Protein biosynthesis;
KW Reference proteome; Transcription; Transcription regulation;
KW Tumor suppressor.
FT CHAIN 1..181
FT /note="Malignant T-cell-amplified sequence 1"
FT /id="PRO_0000344787"
FT DOMAIN 92..171
FT /note="PUA"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00161"
FT MOD_RES 81
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9ULC4"
FT MOD_RES 118
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9ULC4"
FT VAR_SEQ 1..4
FT /note="MFKK -> MGKGR (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_034857"
SQ SEQUENCE 181 AA; 20555 MW; A8E02C2F992B74BD CRC64;
MFKKFDEKEN VSNCIQLKTS VIKGIKNQLL EQFPGIEPWL NQIMPKKDPV KIVRCHEHIE
ILTVNGELLF FRQREGPFYP TLRLLHKYPF ILPHQQVDKG AIKFVLSGAN IMCPGLTSPG
AKLYPAAVDT IVAIMAEGKQ HALCVGVMKM SAEDIEKVNK GIGIENIHYL NDGLWHMKTY
K
//
