ADPGK_MOUSE
ID ADPGK_MOUSE Reviewed; 496 AA.
AC Q8VDL4; Q8C7Y9; Q9D0H2;
DT 26-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT 26-APR-2005, sequence version 2.
DT 03-AUG-2022, entry version 130.
DE RecName: Full=ADP-dependent glucokinase;
DE Short=ADP-GK;
DE Short=ADPGK;
DE EC=2.7.1.147;
DE Flags: Precursor;
GN Name=Adpgk;
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; TISSUE=Cerebellum, and Vagina;
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] (ISOFORM 3).
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 [3]
RP CHARACTERIZATION, SUBUNIT, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=14975750; DOI=10.1016/j.bbrc.2004.01.103;
RA Ronimus R.S., Morgan H.W.;
RT "Cloning and biochemical characterization of a novel mouse ADP-dependent
RT glucokinase.";
RL Biochem. Biophys. Res. Commun. 315:652-658(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: Catalyzes the phosphorylation of D-glucose to D-glucose 6-
CC phosphate using ADP as the phosphate donor. GDP and CDP can replace
CC ADP, but with reduced efficiency.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ADP + D-glucose = AMP + D-glucose 6-phosphate + H(+);
CC Xref=Rhea:RHEA:11460, ChEBI:CHEBI:4167, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:61548, ChEBI:CHEBI:456215, ChEBI:CHEBI:456216;
CC EC=2.7.1.147;
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000255|PROSITE-ProRule:PRU00584};
CC Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000255|PROSITE-
CC ProRule:PRU00584};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=96 uM for D-glucose (at 37 degrees Celsius)
CC {ECO:0000269|PubMed:14975750};
CC KM=0.28 mM for ADP (at 37 degrees Celsius)
CC {ECO:0000269|PubMed:14975750};
CC KM=20 mM for ADP (at 37 degrees Celsius)
CC {ECO:0000269|PubMed:14975750};
CC Vmax=160 umol/min/mg enzyme with glucose and ADP as substrates (at 37
CC degrees Celsius) {ECO:0000269|PubMed:14975750};
CC pH dependence:
CC Optimum pH is 5.75-6.5 and 8.75-9.0. {ECO:0000269|PubMed:14975750};
CC -!- PATHWAY: Carbohydrate degradation; glycolysis. {ECO:0000255|PROSITE-
CC ProRule:PRU00584}.
CC -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:14975750}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q8VDL4-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8VDL4-2; Sequence=VSP_013555, VSP_013556;
CC Name=3;
CC IsoId=Q8VDL4-3; Sequence=VSP_013557;
CC -!- SIMILARITY: Belongs to the ADP-dependent glucokinase family.
CC {ECO:0000305}.
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DR EMBL; AK011434; BAB27619.1; -; mRNA.
DR EMBL; AK048904; BAC33486.1; -; mRNA.
DR EMBL; BC021526; AAH21526.1; -; mRNA.
DR CCDS; CCDS23248.1; -. [Q8VDL4-1]
DR CCDS; CCDS90583.1; -. [Q8VDL4-3]
DR RefSeq; NP_082397.1; NM_028121.2.
DR PDB; 5CCF; X-ray; 2.10 A; A=51-496.
DR PDB; 5CK7; X-ray; 2.99 A; A=51-496.
DR PDBsum; 5CCF; -.
DR PDBsum; 5CK7; -.
DR AlphaFoldDB; Q8VDL4; -.
DR SMR; Q8VDL4; -.
DR BioGRID; 215179; 4.
DR STRING; 10090.ENSMUSP00000026266; -.
DR PhosphoSitePlus; Q8VDL4; -.
DR SwissPalm; Q8VDL4; -.
DR EPD; Q8VDL4; -.
DR jPOST; Q8VDL4; -.
DR MaxQB; Q8VDL4; -.
DR PaxDb; Q8VDL4; -.
DR PeptideAtlas; Q8VDL4; -.
DR PRIDE; Q8VDL4; -.
DR ProteomicsDB; 296113; -. [Q8VDL4-1]
DR ProteomicsDB; 296114; -. [Q8VDL4-2]
DR ProteomicsDB; 296115; -. [Q8VDL4-3]
DR DNASU; 72141; -.
DR GeneID; 72141; -.
DR KEGG; mmu:72141; -.
DR UCSC; uc009pxo.1; mouse. [Q8VDL4-2]
DR CTD; 83440; -.
DR MGI; MGI:1919391; Adpgk.
DR eggNOG; KOG4184; Eukaryota.
DR InParanoid; Q8VDL4; -.
DR OrthoDB; 1036373at2759; -.
DR PhylomeDB; Q8VDL4; -.
DR TreeFam; TF313401; -.
DR BRENDA; 2.7.1.147; 3474.
DR Reactome; R-MMU-70171; Glycolysis.
DR SABIO-RK; Q8VDL4; -.
DR UniPathway; UPA00109; -.
DR BioGRID-ORCS; 72141; 2 hits in 72 CRISPR screens.
DR ChiTaRS; Adpgk; mouse.
DR PRO; PR:Q8VDL4; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; Q8VDL4; protein.
DR GO; GO:0005783; C:endoplasmic reticulum; ISO:MGI.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0043843; F:ADP-specific glucokinase activity; IDA:MGI.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0005975; P:carbohydrate metabolic process; IBA:GO_Central.
DR GO; GO:0006006; P:glucose metabolic process; IDA:MGI.
DR GO; GO:0006096; P:glycolytic process; IEA:UniProtKB-UniPathway.
DR Gene3D; 3.40.1190.20; -; 1.
DR InterPro; IPR007666; ADP_PFK/GK.
DR InterPro; IPR029056; Ribokinase-like.
DR PANTHER; PTHR21208; PTHR21208; 1.
DR Pfam; PF04587; ADP_PFK_GK; 1.
DR SUPFAM; SSF53613; SSF53613; 1.
DR PROSITE; PS51255; ADPK; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Glycolysis; Kinase; Magnesium;
KW Metal-binding; Reference proteome; Secreted; Signal; Transferase.
FT SIGNAL 1..22
FT /evidence="ECO:0000255"
FT CHAIN 23..496
FT /note="ADP-dependent glucokinase"
FT /id="PRO_0000184777"
FT DOMAIN 52..496
FT /note="ADPK"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00584"
FT ACT_SITE 481
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00584"
FT BINDING 297
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00584"
FT BINDING 328
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00584"
FT BINDING 481
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00584"
FT VAR_SEQ 154..159
FT /note="HYVGGN -> VCPTHQ (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_013555"
FT VAR_SEQ 160..496
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_013556"
FT VAR_SEQ 313
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_013557"
FT CONFLICT 318
FT /note="A -> T (in Ref. 1; BAB27619)"
FT /evidence="ECO:0000305"
FT CONFLICT 341
FT /note="S -> A (in Ref. 1; BAB27619)"
FT /evidence="ECO:0000305"
FT CONFLICT 373
FT /note="A -> S (in Ref. 2; AAH21526)"
FT /evidence="ECO:0000305"
FT HELIX 53..64
FT /evidence="ECO:0007829|PDB:5CCF"
FT STRAND 73..79
FT /evidence="ECO:0007829|PDB:5CCF"
FT STRAND 82..88
FT /evidence="ECO:0007829|PDB:5CCF"
FT HELIX 89..95
FT /evidence="ECO:0007829|PDB:5CCF"
FT STRAND 107..109
FT /evidence="ECO:0007829|PDB:5CCF"
FT HELIX 112..125
FT /evidence="ECO:0007829|PDB:5CCF"
FT STRAND 129..133
FT /evidence="ECO:0007829|PDB:5CCF"
FT HELIX 136..148
FT /evidence="ECO:0007829|PDB:5CCF"
FT STRAND 153..158
FT /evidence="ECO:0007829|PDB:5CCF"
FT HELIX 159..168
FT /evidence="ECO:0007829|PDB:5CCF"
FT STRAND 173..177
FT /evidence="ECO:0007829|PDB:5CCF"
FT HELIX 183..188
FT /evidence="ECO:0007829|PDB:5CCF"
FT HELIX 197..199
FT /evidence="ECO:0007829|PDB:5CCF"
FT STRAND 206..212
FT /evidence="ECO:0007829|PDB:5CCF"
FT STRAND 227..232
FT /evidence="ECO:0007829|PDB:5CCF"
FT HELIX 235..238
FT /evidence="ECO:0007829|PDB:5CCF"
FT TURN 239..242
FT /evidence="ECO:0007829|PDB:5CCF"
FT HELIX 243..253
FT /evidence="ECO:0007829|PDB:5CCF"
FT STRAND 256..260
FT /evidence="ECO:0007829|PDB:5CCF"
FT HELIX 263..266
FT /evidence="ECO:0007829|PDB:5CCF"
FT HELIX 271..287
FT /evidence="ECO:0007829|PDB:5CCF"
FT STRAND 294..297
FT /evidence="ECO:0007829|PDB:5CCF"
FT HELIX 304..313
FT /evidence="ECO:0007829|PDB:5CCF"
FT HELIX 316..318
FT /evidence="ECO:0007829|PDB:5CCF"
FT STRAND 320..324
FT /evidence="ECO:0007829|PDB:5CCF"
FT HELIX 326..335
FT /evidence="ECO:0007829|PDB:5CCF"
FT TURN 339..342
FT /evidence="ECO:0007829|PDB:5CCF"
FT HELIX 352..366
FT /evidence="ECO:0007829|PDB:5CCF"
FT TURN 370..372
FT /evidence="ECO:0007829|PDB:5CCF"
FT STRAND 378..382
FT /evidence="ECO:0007829|PDB:5CCF"
FT STRAND 384..392
FT /evidence="ECO:0007829|PDB:5CCF"
FT STRAND 395..397
FT /evidence="ECO:0007829|PDB:5CCF"
FT HELIX 399..415
FT /evidence="ECO:0007829|PDB:5CCF"
FT STRAND 424..427
FT /evidence="ECO:0007829|PDB:5CCF"
FT STRAND 431..435
FT /evidence="ECO:0007829|PDB:5CCF"
FT TURN 437..440
FT /evidence="ECO:0007829|PDB:5CCF"
FT STRAND 443..445
FT /evidence="ECO:0007829|PDB:5CCF"
FT STRAND 453..456
FT /evidence="ECO:0007829|PDB:5CCF"
FT STRAND 458..466
FT /evidence="ECO:0007829|PDB:5CCF"
FT STRAND 468..472
FT /evidence="ECO:0007829|PDB:5CCF"
FT HELIX 479..489
FT /evidence="ECO:0007829|PDB:5CCF"
SQ SEQUENCE 496 AA; 53902 MW; CAFCB41D50131A54 CRC64;
MALWRGSACA GFLALAVGCV FLLEPELPGT ALRSLWSSLR LGPAPVPVGP LSPESRLAAA
WDALIAQPAR RWRRVAVGVN ACVDVVISGV KLLQALGLSP GSGKDHAILH SRSDLEEAFL
YFMGKGAAAE RFFSDKETFH DIAQAASEFP GAQHYVGGNA ALIGQRFAAN TDLKVLLCGP
IGPKLHELLD DNVFVPPESL QEEDEFHLIL EYLAGEEWGP FKAPHANRFI FSHDLSNGAM
NMLEVFVSSL EEFQPDLVVL SGLHMMEGQS KELQRKRLLE VVTAISDIPT GIPVHLELAS
MTNRELMSSI VHQQVFPAVA SLGLNEQELL FLSQSASGPH SSLSSWDGVP DVGMVSDILF
WILKEHGRSE NRASDLTRIH FHTLVYHILA TVDGHWANQL AAVAAGARVA GTQACATETI
DTNRVSLRAP QEFTTSHLES GSRIVLNPDK PVVEWHREGI TFHFTPVLVC KDPVRTVGLG
DAISAEGLFY SEARPD
