SHPK_MOUSE
ID SHPK_MOUSE Reviewed; 476 AA.
AC Q9D5J6; Q5SSE0;
DT 27-APR-2001, integrated into UniProtKB/Swiss-Prot.
DT 27-APR-2001, sequence version 1.
DT 03-AUG-2022, entry version 134.
DE RecName: Full=Sedoheptulokinase;
DE Short=SHK;
DE EC=2.7.1.14;
DE AltName: Full=Carbohydrate kinase-like protein;
GN Name=Shpk; Synonyms=Carkl;
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 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].
RC STRAIN=C57BL/6J; 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 [4]
RP FUNCTION, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=18775706; DOI=10.1016/j.febslet.2008.08.024;
RA Kardon T., Stroobant V., Veiga-da-Cunha M., Schaftingen E.V.;
RT "Characterization of mammalian sedoheptulokinase and mechanism of formation
RT of erythritol in sedoheptulokinase deficiency.";
RL FEBS Lett. 582:3330-3334(2008).
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brown adipose tissue, Kidney, and Liver;
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).
RN [6]
RP FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, MUTAGENESIS OF THR-14;
RP THR-15; TRP-125 AND GLN-126, AND INDUCTION.
RX PubMed=22682222; DOI=10.1016/j.cmet.2012.04.023;
RA Haschemi A., Kosma P., Gille L., Evans C.R., Burant C.F., Starkl P.,
RA Knapp B., Haas R., Schmid J.A., Jandl C., Amir S., Lubec G., Park J.,
RA Esterbauer H., Bilban M., Brizuela L., Pospisilik J.A., Otterbein L.E.,
RA Wagner O.;
RT "The sedoheptulose kinase CARKL directs macrophage polarization through
RT control of glucose metabolism.";
RL Cell Metab. 15:813-826(2012).
CC -!- FUNCTION: Acts as a modulator of macrophage activation through control
CC of glucose metabolism. {ECO:0000269|PubMed:18775706,
CC ECO:0000269|PubMed:22682222}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + sedoheptulose = ADP + D-sedoheptulose 7-phosphate +
CC H(+); Xref=Rhea:RHEA:23844, ChEBI:CHEBI:15378, ChEBI:CHEBI:16802,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:57483, ChEBI:CHEBI:456216;
CC EC=2.7.1.14; Evidence={ECO:0000269|PubMed:22682222};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.19 mM for sedoheptulose {ECO:0000269|PubMed:18775706};
CC Vmax=0.128 nmol/min/mg enzyme (at 30 degrees Celsius)
CC {ECO:0000269|PubMed:18775706};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:22682222}.
CC -!- INDUCTION: Up-regulated by IL-4 and IL-13. Down-regulated by LPS.
CC {ECO:0000269|PubMed:22682222}.
CC -!- SIMILARITY: Belongs to the FGGY kinase family. {ECO:0000305}.
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DR EMBL; AK015273; BAB29776.1; -; mRNA.
DR EMBL; AL663116; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL670399; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC054721; AAH54721.1; -; mRNA.
DR EMBL; BC056433; AAH56433.1; -; mRNA.
DR CCDS; CCDS25002.1; -.
DR RefSeq; NP_083307.1; NM_029031.3.
DR AlphaFoldDB; Q9D5J6; -.
DR SMR; Q9D5J6; -.
DR STRING; 10090.ENSMUSP00000006105; -.
DR iPTMnet; Q9D5J6; -.
DR PhosphoSitePlus; Q9D5J6; -.
DR EPD; Q9D5J6; -.
DR jPOST; Q9D5J6; -.
DR MaxQB; Q9D5J6; -.
DR PaxDb; Q9D5J6; -.
DR PeptideAtlas; Q9D5J6; -.
DR PRIDE; Q9D5J6; -.
DR ProteomicsDB; 257155; -.
DR DNASU; 74637; -.
DR Ensembl; ENSMUST00000006105; ENSMUSP00000006105; ENSMUSG00000005951.
DR GeneID; 74637; -.
DR KEGG; mmu:74637; -.
DR UCSC; uc007kag.1; mouse.
DR CTD; 23729; -.
DR MGI; MGI:1921887; Shpk.
DR VEuPathDB; HostDB:ENSMUSG00000005951; -.
DR eggNOG; KOG2517; Eukaryota.
DR GeneTree; ENSGT01000000214434; -.
DR HOGENOM; CLU_021676_1_1_1; -.
DR InParanoid; Q9D5J6; -.
DR OMA; SCSRETQ; -.
DR OrthoDB; 1027013at2759; -.
DR PhylomeDB; Q9D5J6; -.
DR TreeFam; TF315140; -.
DR BRENDA; 2.7.1.14; 3474.
DR Reactome; R-MMU-71336; Pentose phosphate pathway.
DR SABIO-RK; Q9D5J6; -.
DR BioGRID-ORCS; 74637; 4 hits in 71 CRISPR screens.
DR PRO; PR:Q9D5J6; -.
DR Proteomes; UP000000589; Chromosome 11.
DR RNAct; Q9D5J6; protein.
DR Bgee; ENSMUSG00000005951; Expressed in right kidney and 90 other tissues.
DR ExpressionAtlas; Q9D5J6; baseline and differential.
DR Genevisible; Q9D5J6; MM.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016773; F:phosphotransferase activity, alcohol group as acceptor; IBA:GO_Central.
DR GO; GO:0050277; F:sedoheptulokinase activity; IDA:UniProtKB.
DR GO; GO:0005975; P:carbohydrate metabolic process; IDA:UniProtKB.
DR GO; GO:0035963; P:cellular response to interleukin-13; IDA:UniProtKB.
DR GO; GO:0071353; P:cellular response to interleukin-4; IDA:UniProtKB.
DR GO; GO:0071222; P:cellular response to lipopolysaccharide; IDA:UniProtKB.
DR GO; GO:0006071; P:glycerol metabolic process; IBA:GO_Central.
DR GO; GO:0009052; P:pentose-phosphate shunt, non-oxidative branch; IDA:UniProtKB.
DR GO; GO:0016310; P:phosphorylation; IDA:UniProtKB.
DR GO; GO:0050727; P:regulation of inflammatory response; IDA:UniProtKB.
DR GO; GO:0043030; P:regulation of macrophage activation; IDA:UniProtKB.
DR CDD; cd07777; FGGY_SHK_like; 1.
DR InterPro; IPR043129; ATPase_NBD.
DR InterPro; IPR018484; Carb_kinase_FGGY_N.
DR InterPro; IPR042027; SHK.
DR Pfam; PF00370; FGGY_N; 1.
DR SUPFAM; SSF53067; SSF53067; 2.
PE 1: Evidence at protein level;
KW ATP-binding; Cytoplasm; Kinase; Nucleotide-binding; Reference proteome;
KW Transferase.
FT CHAIN 1..476
FT /note="Sedoheptulokinase"
FT /id="PRO_0000059565"
FT MUTAGEN 14
FT /note="T->M: Decreases sedoheptulose kinase activity; when
FT associated with K-15."
FT /evidence="ECO:0000269|PubMed:22682222"
FT MUTAGEN 15
FT /note="T->K: Decreases sedoheptulose kinase activity; when
FT associated with M-14."
FT /evidence="ECO:0000269|PubMed:22682222"
FT MUTAGEN 125
FT /note="W->D: Decreases sedoheptulose kinase activity."
FT /evidence="ECO:0000269|PubMed:22682222"
FT MUTAGEN 126
FT /note="Q->K: Decreases sedoheptulose kinase activity."
FT /evidence="ECO:0000269|PubMed:22682222"
SQ SEQUENCE 476 AA; 51303 MW; B3638772519DBA3C CRC64;
MASRPVTLGI DLGTTSVKAA LLEAAPSLPS GFVVLASCAR AARAETESAV AGPQGREQDV
TRIIQALNEC LDALPRQQLQ RVRGIGVSGQ MHGILFWKAG QGCEWMEGGP AFVFEPRAVS
HLVTWQDGRC NSSFLASLPK PDSHLSVATG FGCATIFWLL KNSPEFLKSY DAAGTIQDYV
VAMLCGLPRP LMSDQNAASW GYFNTQSQSW NLDTLEKAGF PIHLLPDIAE PGSMAGRTSH
TWFEIPKGTQ VGIALGDLQA SVYSCMGQRT DAVLNISTSV QLAASMPVGF QPLQTPDPAA
PVAFFPYFDR TYLGVAASLN GGNVLATFVH MLVQWMADLG LEVEESTVYS RMIQAAAQQK
DTHLTITPTV LGERHLPDQL ASVTRISSSD LSLGHVTRAL CRGIVQNLHS MLPFQQLKEW
GVARVVGSGS ALSRNEVLKQ EVQRAFPFPV CFGQDVDAAF GAALVMLQRD LSQKEP
