TKTL2_MOUSE
ID TKTL2_MOUSE Reviewed; 627 AA.
AC Q9D4D4; A2RSH3;
DT 01-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 131.
DE RecName: Full=Transketolase-like protein 2;
DE EC=2.2.1.1;
GN Name=Tktl2;
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; TISSUE=Testis;
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 TISSUE=Brain;
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=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: Plays an essential role in total transketolase activity and
CC cell proliferation in cancer cells; after transfection with anti-TKTL1
CC siRNA, total transketolase activity dramatically decreases and
CC proliferation was significantly inhibited in cancer cells. Plays a
CC pivotal role in carcinogenesis (By similarity). {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=D-glyceraldehyde 3-phosphate + D-sedoheptulose 7-phosphate =
CC aldehydo-D-ribose 5-phosphate + D-xylulose 5-phosphate;
CC Xref=Rhea:RHEA:10508, ChEBI:CHEBI:57483, ChEBI:CHEBI:57737,
CC ChEBI:CHEBI:58273, ChEBI:CHEBI:59776; EC=2.2.1.1;
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000250};
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250};
CC Name=Co(2+); Xref=ChEBI:CHEBI:48828; Evidence={ECO:0000250};
CC Note=Binds 1 Mg(2+) ion per subunit. Can also utilize other divalent
CC metal cations, such as Ca(2+), Mn(2+) and Co(2+). {ECO:0000250};
CC -!- COFACTOR:
CC Name=thiamine diphosphate; Xref=ChEBI:CHEBI:58937;
CC Evidence={ECO:0000250};
CC Note=Binds 1 thiamine pyrophosphate per subunit. {ECO:0000250};
CC -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the transketolase family. {ECO:0000305}.
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DR EMBL; AK016603; BAB30335.1; -; mRNA.
DR EMBL; BC132110; AAI32111.1; -; mRNA.
DR EMBL; BC132298; AAI32299.1; -; mRNA.
DR CCDS; CCDS22334.1; -.
DR RefSeq; NP_001258503.1; NM_001271574.1.
DR RefSeq; NP_083203.2; NM_028927.3.
DR AlphaFoldDB; Q9D4D4; -.
DR SMR; Q9D4D4; -.
DR BioGRID; 216735; 3.
DR STRING; 10090.ENSMUSP00000002025; -.
DR iPTMnet; Q9D4D4; -.
DR PhosphoSitePlus; Q9D4D4; -.
DR jPOST; Q9D4D4; -.
DR PaxDb; Q9D4D4; -.
DR PeptideAtlas; Q9D4D4; -.
DR PRIDE; Q9D4D4; -.
DR ProteomicsDB; 258890; -.
DR GeneID; 74419; -.
DR KEGG; mmu:74419; -.
DR UCSC; uc009lvq.2; mouse.
DR CTD; 84076; -.
DR MGI; MGI:1921669; Tktl2.
DR eggNOG; KOG0523; Eukaryota.
DR InParanoid; Q9D4D4; -.
DR OrthoDB; 354970at2759; -.
DR PhylomeDB; Q9D4D4; -.
DR TreeFam; TF313097; -.
DR BioGRID-ORCS; 74419; 3 hits in 73 CRISPR screens.
DR PRO; PR:Q9D4D4; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; Q9D4D4; protein.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0030976; F:thiamine pyrophosphate binding; IBA:GO_Central.
DR GO; GO:0004802; F:transketolase activity; IBA:GO_Central.
DR CDD; cd02012; TPP_TK; 1.
DR Gene3D; 3.40.50.920; -; 1.
DR InterPro; IPR029061; THDP-binding.
DR InterPro; IPR009014; Transketo_C/PFOR_II.
DR InterPro; IPR005475; Transketolase-like_Pyr-bd.
DR InterPro; IPR020826; Transketolase_BS.
DR InterPro; IPR033248; Transketolase_C.
DR InterPro; IPR005474; Transketolase_N.
DR Pfam; PF02779; Transket_pyr; 1.
DR Pfam; PF02780; Transketolase_C; 1.
DR Pfam; PF00456; Transketolase_N; 1.
DR SMART; SM00861; Transket_pyr; 1.
DR SUPFAM; SSF52518; SSF52518; 2.
DR SUPFAM; SSF52922; SSF52922; 1.
DR PROSITE; PS00802; TRANSKETOLASE_2; 1.
PE 1: Evidence at protein level;
KW Calcium; Magnesium; Metal-binding; Reference proteome;
KW Thiamine pyrophosphate; Transferase.
FT CHAIN 1..627
FT /note="Transketolase-like protein 2"
FT /id="PRO_0000285201"
FT ACT_SITE 371
FT /note="Proton donor"
FT /evidence="ECO:0000250"
FT BINDING 39
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 42
FT /ligand="thiamine diphosphate"
FT /ligand_id="ChEBI:CHEBI:58937"
FT /evidence="ECO:0000250"
FT BINDING 79
FT /ligand="thiamine diphosphate"
FT /ligand_id="ChEBI:CHEBI:58937"
FT /evidence="ECO:0000250"
FT BINDING 125..127
FT /ligand="thiamine diphosphate"
FT /ligand_id="ChEBI:CHEBI:58937"
FT /evidence="ECO:0000250"
FT BINDING 157
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 158
FT /ligand="thiamine diphosphate"
FT /ligand_id="ChEBI:CHEBI:58937"
FT /evidence="ECO:0000250"
FT BINDING 187
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 187
FT /ligand="thiamine diphosphate"
FT /ligand_id="ChEBI:CHEBI:58937"
FT /evidence="ECO:0000250"
FT BINDING 189
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 249
FT /ligand="thiamine diphosphate"
FT /ligand_id="ChEBI:CHEBI:58937"
FT /evidence="ECO:0000250"
FT BINDING 263
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 263
FT /ligand="thiamine diphosphate"
FT /ligand_id="ChEBI:CHEBI:58937"
FT /evidence="ECO:0000250"
FT BINDING 323
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 350
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 371
FT /ligand="thiamine diphosphate"
FT /ligand_id="ChEBI:CHEBI:58937"
FT /evidence="ECO:0000250"
FT BINDING 397
FT /ligand="thiamine diphosphate"
FT /ligand_id="ChEBI:CHEBI:58937"
FT /evidence="ECO:0000250"
FT BINDING 421
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 429
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 433
FT /ligand="thiamine diphosphate"
FT /ligand_id="ChEBI:CHEBI:58937"
FT /evidence="ECO:0000250"
FT BINDING 479
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT SITE 39
FT /note="Important for catalytic activity"
FT /evidence="ECO:0000250"
FT SITE 263
FT /note="Important for catalytic activity"
FT /evidence="ECO:0000250"
FT CONFLICT 14
FT /note="L -> F (in Ref. 2; AAI32299/AAI32111)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 627 AA; 68447 MW; 87499ECAEB2950AE CRC64;
MALARDAKLE SDTLQVLQDV ANRLRIHSIR ATCACSSGHP TSCCSVAEIM AVLFFHTMRY
KQADPEHPDN DRFVLSKGHA APILYAVWVE VGRICESDLL NLRKIHCDLE GHPTPRLSFV
DVATGSLGQG LGAACGMAYT GKYFDKASYR VFCLMGDGES SEGSVWEALA FASHYNLDNL
VAIFDVNRLG QSGTAPLEHC TAVYEKRCQA FGWNTYVVDG HDVEALCQAF WKAAQVKNKP
TALIAKTFKG RGIPNVEDAE NWHGKPMPKD RADGIVKLIE NRIQTNRNLT PKPPIEDSPR
ISMSNTKMTS LPVYKLGDMI ATREAYGLAL AKLGQSNQRV IVLDGDTKNS TFSEVFKKEH
PERFIECFIA EQNMVSVALG CATRGRTIAF VSTFAAFLTR AFDQIRMGAI SQTNINFVGS
HCGVSVGEDG PSQMALEDLA MFRSIPNCTV FYPSDAVSTE HAVYLAANTK GMCFIRTTRP
KTAVIYTAEE NFVIGQAKVI RQSAVDKVTV IGAGVTLHEA LVAAEELSQQ GIFIRVIDLF
TIKPLDAVTI IQSAKATGGQ IITVEDHYRE GGIGEAVCAA ISREPDIVVR QLAVTEVPRS
GKPSELLDMF GISARHIIAA VKDTVMK
