FGGY_MOUSE
ID FGGY_MOUSE Reviewed; 552 AA.
AC A2AJL3; Q8BUF2; Q8K0F0; Q9D7H0;
DT 18-MAR-2008, integrated into UniProtKB/Swiss-Prot.
DT 20-FEB-2007, sequence version 1.
DT 03-AUG-2022, entry version 112.
DE RecName: Full=FGGY carbohydrate kinase domain-containing protein;
DE AltName: Full=D-ribulokinase FGGY {ECO:0000250|UniProtKB:Q96C11};
DE EC=2.7.1.47 {ECO:0000250|UniProtKB:Q96C11};
GN Name=Fggy;
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] (ISOFORM 2), AND NUCLEOTIDE SEQUENCE
RP [LARGE SCALE MRNA] OF 246-552 (ISOFORM 1).
RC STRAIN=C57BL/6J; TISSUE=Kidney, and Tongue;
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] (ISOFORM 2).
RC STRAIN=FVB/N; TISSUE=Liver;
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 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC 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).
CC -!- FUNCTION: Catalyzes ATP-dependent phosphorylation of D-ribulose at C-5
CC to form D-ribulose 5-phosphate. Postulated to function in a metabolite
CC repair mechanism by preventing toxic accumulation of free D-ribulose
CC formed by non-specific phosphatase activities. Alternatively, may play
CC a role in regulating D-ribulose 5-phosphate recycling in the pentose
CC phosphate pathway. Can phosphorylate ribitol with low efficiency.
CC {ECO:0000250|UniProtKB:Q96C11}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + D-ribulose = ADP + D-ribulose 5-phosphate + H(+);
CC Xref=Rhea:RHEA:17601, ChEBI:CHEBI:15378, ChEBI:CHEBI:17173,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:58121, ChEBI:CHEBI:456216;
CC EC=2.7.1.47; Evidence={ECO:0000250|UniProtKB:Q96C11};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:17602;
CC Evidence={ECO:0000250|UniProtKB:Q96C11};
CC -!- PATHWAY: Carbohydrate metabolism; pentose and glucuronate
CC interconversion. {ECO:0000250|UniProtKB:Q96C11}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=A2AJL3-1; Sequence=Displayed;
CC Name=2;
CC IsoId=A2AJL3-2; Sequence=VSP_032660, VSP_032661;
CC -!- SIMILARITY: Belongs to the FGGY kinase family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB26167.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=BAC39466.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AK009249; BAB26167.1; ALT_INIT; mRNA.
DR EMBL; AK085534; BAC39466.1; ALT_FRAME; mRNA.
DR EMBL; AL772131; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL844609; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL928634; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BX005293; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC031708; AAH31708.1; -; mRNA.
DR CCDS; CCDS18365.1; -. [A2AJL3-2]
DR CCDS; CCDS51233.1; -. [A2AJL3-1]
DR RefSeq; NP_001106883.1; NM_001113412.1. [A2AJL3-1]
DR RefSeq; NP_083623.1; NM_029347.2. [A2AJL3-2]
DR RefSeq; XP_006503524.1; XM_006503461.3. [A2AJL3-1]
DR RefSeq; XP_006503539.1; XM_006503476.1.
DR AlphaFoldDB; A2AJL3; -.
DR SMR; A2AJL3; -.
DR STRING; 10090.ENSMUSP00000078216; -.
DR iPTMnet; A2AJL3; -.
DR PhosphoSitePlus; A2AJL3; -.
DR SwissPalm; A2AJL3; -.
DR EPD; A2AJL3; -.
DR jPOST; A2AJL3; -.
DR MaxQB; A2AJL3; -.
DR PaxDb; A2AJL3; -.
DR PeptideAtlas; A2AJL3; -.
DR PRIDE; A2AJL3; -.
DR ProteomicsDB; 271585; -. [A2AJL3-1]
DR ProteomicsDB; 271586; -. [A2AJL3-2]
DR Antibodypedia; 33269; 122 antibodies from 22 providers.
DR DNASU; 75578; -.
DR Ensembl; ENSMUST00000043335; ENSMUSP00000043460; ENSMUSG00000028573. [A2AJL3-2]
DR Ensembl; ENSMUST00000079223; ENSMUSP00000078216; ENSMUSG00000028573. [A2AJL3-1]
DR GeneID; 75578; -.
DR KEGG; mmu:75578; -.
DR UCSC; uc008tsx.2; mouse. [A2AJL3-2]
DR UCSC; uc008tsy.2; mouse. [A2AJL3-1]
DR CTD; 55277; -.
DR MGI; MGI:1922828; Fggy.
DR VEuPathDB; HostDB:ENSMUSG00000028573; -.
DR eggNOG; KOG2517; Eukaryota.
DR GeneTree; ENSGT01000000214434; -.
DR HOGENOM; CLU_009281_10_2_1; -.
DR InParanoid; A2AJL3; -.
DR OMA; GHKAMWH; -.
DR OrthoDB; 1252682at2759; -.
DR PhylomeDB; A2AJL3; -.
DR TreeFam; TF300904; -.
DR UniPathway; UPA00246; -.
DR BioGRID-ORCS; 75578; 2 hits in 74 CRISPR screens.
DR ChiTaRS; Fggy; mouse.
DR PRO; PR:A2AJL3; -.
DR Proteomes; UP000000589; Chromosome 4.
DR RNAct; A2AJL3; protein.
DR Bgee; ENSMUSG00000028573; Expressed in right kidney and 175 other tissues.
DR ExpressionAtlas; A2AJL3; baseline and differential.
DR Genevisible; A2AJL3; MM.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0019150; F:D-ribulokinase activity; ISO:MGI.
DR GO; GO:0046835; P:carbohydrate phosphorylation; ISO:MGI.
DR GO; GO:0070050; P:neuron cellular homeostasis; ISO:MGI.
DR GO; GO:0019321; P:pentose metabolic process; ISO:MGI.
DR CDD; cd07782; FGGY_YpCarbK_like; 1.
DR InterPro; IPR043129; ATPase_NBD.
DR InterPro; IPR000577; Carb_kinase_FGGY.
DR InterPro; IPR018485; Carb_kinase_FGGY_C.
DR InterPro; IPR018484; Carb_kinase_FGGY_N.
DR InterPro; IPR006003; FGGY_RbtK-like.
DR Pfam; PF02782; FGGY_C; 1.
DR Pfam; PF00370; FGGY_N; 1.
DR PIRSF; PIRSF000538; GlpK; 1.
DR SUPFAM; SSF53067; SSF53067; 2.
DR TIGRFAMs; TIGR01315; 5C_CHO_kinase; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Kinase; Reference proteome; Transferase.
FT CHAIN 1..552
FT /note="FGGY carbohydrate kinase domain-containing protein"
FT /id="PRO_0000326453"
FT VAR_SEQ 360..387
FT /note="CQSIYAYLNSHLDLIKKAQPVGFLTVDL -> NLQKHHGIHGDTPGIAKYEL
FT EVTSSKAF (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:16141072"
FT /id="VSP_032660"
FT VAR_SEQ 388..552
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:16141072"
FT /id="VSP_032661"
FT CONFLICT 280
FT /note="T -> A (in Ref. 1; BAC39466)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 552 AA; 60336 MW; F9EF93D1D013E1B3 CRC64;
MMSGRDQEPS RYYVGIDVGT GSVRAALVDQ RGLLLAFAEQ PIKKWEPQFN HHEQSSEDIW
AACCLVTKEV VQGIDAHRIR GLGFDATCSL VVLDKEFHPL PVNHEGDSSR NVIMWLDHRA
VSQVHRINET KHRVLQYVGG VMSVEMQAPK LLWLKENLRE ICWDKAGHFF DLPDFLSWKA
TGVTARSLCS LVCKWTYSAE KGWDDSFWKM IGLEDLIDDN YSKIGNLVLL PGAALGIGLT
PEAARELGLP SGIAVAASLI DAHAGGLGVI GADVRGHGLT CEGQPVTSRL AVICGTSSCH
MGISKDPVFV PGVWGPYYSA MVPGFWLNEG GQSVTGKLID HMVQGHPAFP ELQAKATARC
QSIYAYLNSH LDLIKKAQPV GFLTVDLHVW PDFHGNRSPL ADLTLKGMVT GLTLSQDLDD
LAILYLATVQ AIAFGTRFII ETMEAAGHSL STLFLCGGLS KNPLFVQMHA DITGMPVVLS
QEVESVLVGA AILGACASGD FTSVQEAMAR MSKVGKVVFP EHADKKYYDK KYQVFLRMVE
HQKEYSAIMN GS
