TKTL1_MOUSE
ID TKTL1_MOUSE Reviewed; 595 AA.
AC Q99MX0; B1AYP0; Q684Q5; Q8CDU7;
DT 09-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 2.
DT 03-AUG-2022, entry version 127.
DE RecName: Full=Transketolase-like protein 1;
DE EC=2.2.1.1;
DE AltName: Full=Transketolase 2;
DE Short=TK 2;
GN Name=Tktl1 {ECO:0000312|MGI:MGI:1933244};
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] {ECO:0000312|EMBL:AAK31950.1}
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Testis {ECO:0000312|EMBL:AAK31950.1};
RX PubMed=11279525; DOI=10.1038/86927;
RA Wang P.J., McCarrey J.R., Yang F., Page D.C.;
RT "An abundance of X-linked genes expressed in spermatogonia.";
RL Nat. Genet. 27:422-426(2001).
RN [2] {ECO:0000312|EMBL:BAC26508.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J {ECO:0000312|EMBL:BAC26508.1};
RC TISSUE=Egg {ECO:0000312|EMBL:BAE24155.1}, and
RC Testis {ECO:0000312|EMBL:BAC26508.1};
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 [3]
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 [4] {ECO:0000312|EMBL:CAF25311.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [5] {ECO:0000312|EMBL:AAI13769.1}
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 [6] {ECO:0000312|EMBL:CAF25311.1}
RP NUCLEOTIDE SEQUENCE [MRNA] OF 361-595.
RC STRAIN=NMRI {ECO:0000312|EMBL:CAF25311.1};
RC TISSUE=Testis {ECO:0000312|EMBL:CAF25311.1};
RA Kolb A.A., Mehrle A., Bechtel S., Wellenreuther R., Simpson J.,
RA Pepperkok R., Wiemann S., Poustka A.;
RT "Towards functional annotation of all Xq28 genes: expression and
RT intracellular localization analyses reveal novel candidates for disease
RT genes.";
RL Submitted (FEB-2004) to the EMBL/GenBank/DDBJ databases.
RN [7]
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: Catalyzes the transfer of a two-carbon ketol group from a
CC ketose donor to an aldose acceptor, via a covalent intermediate with
CC the cofactor thiamine pyrophosphate. {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 Evidence={ECO:0000250|UniProtKB:P51854};
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|UniProtKB:P23254};
CC Note=Binds 1 thiamine pyrophosphate per subunit.
CC {ECO:0000250|UniProtKB:P23254};
CC -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:P23254}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P51854}. Nucleus
CC {ECO:0000250|UniProtKB:P51854}. Note=Predominantly cytoplasmic and to a
CC lesser extent also nuclear. {ECO:0000250|UniProtKB:P51854}.
CC -!- SIMILARITY: Belongs to the transketolase family. {ECO:0000255}.
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DR EMBL; AF285571; AAK31950.1; -; mRNA.
DR EMBL; AK029546; BAC26508.1; -; mRNA.
DR EMBL; AK139841; BAE24155.1; -; mRNA.
DR EMBL; AL928731; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH466650; EDL29841.1; -; Genomic_DNA.
DR EMBL; BC113768; AAI13769.1; -; mRNA.
DR EMBL; AJ627042; CAF25311.1; -; mRNA.
DR CCDS; CCDS30221.1; -.
DR RefSeq; NP_113556.2; NM_031379.2.
DR AlphaFoldDB; Q99MX0; -.
DR SMR; Q99MX0; -.
DR BioGRID; 219939; 1.
DR STRING; 10090.ENSMUSP00000010127; -.
DR iPTMnet; Q99MX0; -.
DR PhosphoSitePlus; Q99MX0; -.
DR EPD; Q99MX0; -.
DR MaxQB; Q99MX0; -.
DR PaxDb; Q99MX0; -.
DR PeptideAtlas; Q99MX0; -.
DR PRIDE; Q99MX0; -.
DR ProteomicsDB; 262823; -.
DR Antibodypedia; 17549; 69 antibodies from 22 providers.
DR DNASU; 83553; -.
DR Ensembl; ENSMUST00000010127; ENSMUSP00000010127; ENSMUSG00000031397.
DR GeneID; 83553; -.
DR KEGG; mmu:83553; -.
DR UCSC; uc009tnx.1; mouse.
DR CTD; 8277; -.
DR MGI; MGI:1933244; Tktl1.
DR VEuPathDB; HostDB:ENSMUSG00000031397; -.
DR eggNOG; KOG0523; Eukaryota.
DR GeneTree; ENSGT00940000162426; -.
DR HOGENOM; CLU_009227_3_0_1; -.
DR InParanoid; Q99MX0; -.
DR OMA; SMSVEHC; -.
DR OrthoDB; 354970at2759; -.
DR PhylomeDB; Q99MX0; -.
DR TreeFam; TF313097; -.
DR BioGRID-ORCS; 83553; 0 hits in 73 CRISPR screens.
DR PRO; PR:Q99MX0; -.
DR Proteomes; UP000000589; Chromosome X.
DR RNAct; Q99MX0; protein.
DR Bgee; ENSMUSG00000031397; Expressed in cleaving embryo and 36 other tissues.
DR ExpressionAtlas; Q99MX0; baseline and differential.
DR Genevisible; Q99MX0; MM.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
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 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; 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.
PE 1: Evidence at protein level;
KW Calcium; Cytoplasm; Magnesium; Metal-binding; Nucleus; Reference proteome;
KW Thiamine pyrophosphate; Transferase.
FT CHAIN 1..595
FT /note="Transketolase-like protein 1"
FT /id="PRO_0000271265"
FT ACT_SITE 339
FT /note="Proton donor"
FT /evidence="ECO:0000250"
FT BINDING 93..95
FT /ligand="thiamine diphosphate"
FT /ligand_id="ChEBI:CHEBI:58937"
FT /evidence="ECO:0000250"
FT BINDING 125
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 155
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 155
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 217
FT /ligand="thiamine diphosphate"
FT /ligand_id="ChEBI:CHEBI:58937"
FT /evidence="ECO:0000250"
FT BINDING 365
FT /ligand="thiamine diphosphate"
FT /ligand_id="ChEBI:CHEBI:58937"
FT /evidence="ECO:0000250"
FT BINDING 389
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 397
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT CONFLICT 37
FT /note="K -> R (in Ref. 1; AAK31950 and 5; AAI13769)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 595 AA; 65245 MW; 5B19A5375A8CA474 CRC64;
MSEAEASSGM AHNAGPDEKT LQVLRDMANR LRIRSIKATN SSTTSYLIPC SNAEIMSVLF
FYTMRYKQED PENPDNDRCI LSKGLPFVNV ATGWPGQGLG AACGMAYTGK YFDQASYRVF
CLLGDEESTE GSVWEAFAFA SYYNLDNLMA IFDVNRIGHS SSMSVEHCIA IYQKRCEAFG
WNTYVVDGRD VKTLCHVFSQ AAQVRGKPTA VVAKTFKARG MPNVEDAESW YGRPMPKERA
DAIVKLIESQ IQTNKILVPS PPIEDSPQIN IMNICMTSPP VYVADDKVST QRACGLALAK
LGHENDRVIV LGSDTKNCNF SDIFKKEHPE RFIQCCIAEQ NMVNVALGCS TRDRTIVFAY
SFAAFFTRAF DQIRLGAISQ ININLIGCHC GVSTGDDNPY HMALEDLAMF RAIPNCVVFY
PSDAVSTEHA VYLAANTKEM CFIRTSQAET AIIYTTQETF QIGQAKVVRH SDNDKVIVIG
AGVTLHEALV AAAELSKEDI SIRVIDLFTI KPLDIATIIS NAKATGGRII TVEDHYPEGG
IGGAVCAAVS MEPNIVVHNL AVMDVPRSGR CNEALDFSGI SSRHIIVAVK CILMT
