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 29-MAY-2013, entry version 87.
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;
OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC Muroidea; Muridae; 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.,
RA Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA 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.,
RA Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA 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
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
CC -!- FUNCTION: Plays an essential role in total transketolase activity
CC and cell proliferation in cancer cells; after transfection with
CC anti-TKTL1 siRNA, total transketolase activity dramatically
CC decreases and proliferation was significantly inhibited in cancer
CC cells. Plays a pivotal role in carcinogenesis (By similarity).
CC -!- CATALYTIC ACTIVITY: Sedoheptulose 7-phosphate + D-glyceraldehyde
CC 3-phosphate = D-ribose 5-phosphate + D-xylulose 5-phosphate.
CC -!- COFACTOR: Binds 1 magnesium ion per subunit. Can also utilize
CC other divalent metal cations, such as Ca(2+), Mn(2+) and Co(2+)
CC (By similarity).
CC -!- COFACTOR: Binds 1 thiamine pyrophosphate per subunit (By
CC similarity).
CC -!- SUBUNIT: Homodimer (By similarity).
CC -!- SIMILARITY: Belongs to the transketolase family.
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DR EMBL; AK016603; BAB30335.1; -; mRNA.
DR EMBL; BC132110; AAI32111.1; -; mRNA.
DR EMBL; BC132298; AAI32299.1; -; mRNA.
DR IPI; IPI00317015; -.
DR RefSeq; NP_001258503.1; NM_001271574.1.
DR RefSeq; NP_083203.2; NM_028927.3.
DR UniGene; Mm.483195; -.
DR UniGene; Mm.483407; -.
DR UniGene; Mm.487219; -.
DR ProteinModelPortal; Q9D4D4; -.
DR SMR; Q9D4D4; 8-622.
DR PhosphoSite; Q9D4D4; -.
DR PaxDb; Q9D4D4; -.
DR PRIDE; Q9D4D4; -.
DR Ensembl; ENSMUST00000002025; ENSMUSP00000002025; ENSMUSG00000025519.
DR GeneID; 74419; -.
DR KEGG; mmu:74419; -.
DR UCSC; uc009lvq.1; mouse.
DR CTD; 84076; -.
DR MGI; MGI:1921669; Tktl2.
DR eggNOG; COG0021; -.
DR GeneTree; ENSGT00390000005240; -.
DR HOGENOM; HOG000243868; -.
DR HOVERGEN; HBG004036; -.
DR InParanoid; Q9D4D4; -.
DR KO; K00615; -.
DR OrthoDB; EOG4R23TG; -.
DR NextBio; 340709; -.
DR Bgee; Q9D4D4; -.
DR CleanEx; MM_TKTL2; -.
DR Genevestigator; Q9D4D4; -.
DR GO; GO:0005737; C:cytoplasm; IEA:Compara.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004802; F:transketolase activity; IEA:EC.
DR Gene3D; 3.40.50.920; -; 1.
DR InterPro; IPR009014; Transketo_C/Pyr-ferredox_oxred.
DR InterPro; IPR015941; Transketolase-like_C.
DR InterPro; IPR005475; Transketolase-like_Pyr-bd.
DR InterPro; IPR020826; Transketolase_BS.
DR InterPro; IPR005476; 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; SSF52922; Transketo_C_like; 1.
DR PROSITE; PS00801; TRANSKETOLASE_1; FALSE_NEG.
DR PROSITE; PS00802; TRANSKETOLASE_2; 1.
PE 2: Evidence at transcript level;
KW Calcium; Complete proteome; Magnesium; Metal-binding;
KW Reference proteome; Thiamine pyrophosphate; Transferase.
FT CHAIN 1 627 Transketolase-like protein 2.
FT /FTId=PRO_0000285201.
FT NP_BIND 125 127 Thiamine pyrophosphate (By similarity).
FT ACT_SITE 371 371 Proton donor (By similarity).
FT METAL 157 157 Magnesium (By similarity).
FT METAL 187 187 Magnesium (By similarity).
FT METAL 189 189 Magnesium; via carbonyl oxygen (By
FT similarity).
FT BINDING 39 39 Substrate (By similarity).
FT BINDING 42 42 Thiamine pyrophosphate (By similarity).
FT BINDING 79 79 Thiamine pyrophosphate (By similarity).
FT BINDING 158 158 Thiamine pyrophosphate; via amide
FT nitrogen (By similarity).
FT BINDING 187 187 Thiamine pyrophosphate (By similarity).
FT BINDING 249 249 Thiamine pyrophosphate (By similarity).
FT BINDING 263 263 Substrate (By similarity).
FT BINDING 263 263 Thiamine pyrophosphate (By similarity).
FT BINDING 323 323 Substrate (By similarity).
FT BINDING 350 350 Substrate (By similarity).
FT BINDING 371 371 Thiamine pyrophosphate (By similarity).
FT BINDING 397 397 Thiamine pyrophosphate (By similarity).
FT BINDING 421 421 Substrate (By similarity).
FT BINDING 429 429 Substrate (By similarity).
FT BINDING 433 433 Thiamine pyrophosphate (By similarity).
FT BINDING 479 479 Substrate (By similarity).
FT SITE 39 39 Important for catalytic activity (By
FT similarity).
FT SITE 263 263 Important for catalytic activity (By
FT similarity).
FT CONFLICT 14 14 L -> F (in Ref. 2; AAI32299/AAI32111).
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
//
