UGPA_MOUSE
ID UGPA_MOUSE Reviewed; 508 AA.
AC Q91ZJ5; Q8R3D2;
DT 15-FEB-2005, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 153.
DE RecName: Full=UTP--glucose-1-phosphate uridylyltransferase;
DE EC=2.7.7.9 {ECO:0000250|UniProtKB:Q16851};
DE AltName: Full=UDP-glucose pyrophosphorylase;
DE Short=UDPGP;
DE Short=UGPase;
GN Name=Ugp2;
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.
RC STRAIN=C57BL/6J;
RX PubMed=12174196; DOI=10.1186/1471-2156-3-14;
RA Fuchs S., Resch K., Thiel C., Ulbrich M., Platzer M., Jockusch H.,
RA Schmitt-John T.;
RT "Comparative transcription map of the wobbler critical region on mouse
RT chromosome 11 and the homologous region on human chromosome 2p13-14.";
RL BMC Genet. 3:14-14(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Colon;
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]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC STRAIN=FVB/N; TISSUE=Mammary tumor, and Pituitary;
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 [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-448, AND IDENTIFICATION BY
RP 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: UTP--glucose-1-phosphate uridylyltransferase catalyzing the
CC conversion of glucose-1-phosphate into UDP-glucose, a crucial precursor
CC for the production of glycogen. {ECO:0000250|UniProtKB:Q16851}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=alpha-D-glucose 1-phosphate + H(+) + UTP = diphosphate + UDP-
CC alpha-D-glucose; Xref=Rhea:RHEA:19889, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:33019, ChEBI:CHEBI:46398, ChEBI:CHEBI:58601,
CC ChEBI:CHEBI:58885; EC=2.7.7.9;
CC Evidence={ECO:0000250|UniProtKB:Q16851};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:19890;
CC Evidence={ECO:0000250|UniProtKB:Q16851};
CC -!- PATHWAY: Glycan biosynthesis; glycogen biosynthesis.
CC {ECO:0000250|UniProtKB:Q16851}.
CC -!- SUBUNIT: Homooctamer. {ECO:0000250|UniProtKB:Q16851}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q16851}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q91ZJ5-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q91ZJ5-2; Sequence=VSP_012835;
CC -!- SIMILARITY: Belongs to the UDPGP type 1 family. {ECO:0000305}.
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DR EMBL; AF424698; AAL24807.1; -; mRNA.
DR EMBL; AK033445; BAC28291.1; -; mRNA.
DR EMBL; AL772195; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL833772; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC023810; AAH23810.1; -; mRNA.
DR EMBL; BC025585; AAH25585.1; -; mRNA.
DR EMBL; BC061208; AAH61208.1; -; mRNA.
DR CCDS; CCDS24464.1; -. [Q91ZJ5-1]
DR CCDS; CCDS70148.1; -. [Q91ZJ5-2]
DR RefSeq; NP_001277563.1; NM_001290634.1. [Q91ZJ5-2]
DR RefSeq; NP_647458.1; NM_139297.6. [Q91ZJ5-1]
DR AlphaFoldDB; Q91ZJ5; -.
DR SMR; Q91ZJ5; -.
DR BioGRID; 229760; 10.
DR IntAct; Q91ZJ5; 1.
DR STRING; 10090.ENSMUSP00000099939; -.
DR iPTMnet; Q91ZJ5; -.
DR PhosphoSitePlus; Q91ZJ5; -.
DR SwissPalm; Q91ZJ5; -.
DR REPRODUCTION-2DPAGE; IPI00279474; -.
DR EPD; Q91ZJ5; -.
DR jPOST; Q91ZJ5; -.
DR MaxQB; Q91ZJ5; -.
DR PaxDb; Q91ZJ5; -.
DR PeptideAtlas; Q91ZJ5; -.
DR PRIDE; Q91ZJ5; -.
DR ProteomicsDB; 299640; -. [Q91ZJ5-1]
DR ProteomicsDB; 299641; -. [Q91ZJ5-2]
DR Antibodypedia; 30782; 213 antibodies from 24 providers.
DR DNASU; 216558; -.
DR Ensembl; ENSMUST00000060895; ENSMUSP00000056324; ENSMUSG00000001891. [Q91ZJ5-2]
DR Ensembl; ENSMUST00000102875; ENSMUSP00000099939; ENSMUSG00000001891. [Q91ZJ5-1]
DR GeneID; 216558; -.
DR KEGG; mmu:216558; -.
DR UCSC; uc007idr.4; mouse. [Q91ZJ5-1]
DR CTD; 7360; -.
DR MGI; MGI:2183447; Ugp2.
DR VEuPathDB; HostDB:ENSMUSG00000001891; -.
DR eggNOG; KOG2638; Eukaryota.
DR GeneTree; ENSGT00940000153464; -.
DR HOGENOM; CLU_023632_3_0_1; -.
DR InParanoid; Q91ZJ5; -.
DR OMA; TNNLWAK; -.
DR OrthoDB; 503037at2759; -.
DR PhylomeDB; Q91ZJ5; -.
DR TreeFam; TF300567; -.
DR Reactome; R-MMU-173599; Formation of the active cofactor, UDP-glucuronate.
DR Reactome; R-MMU-3322077; Glycogen synthesis.
DR UniPathway; UPA00164; -.
DR BioGRID-ORCS; 216558; 20 hits in 77 CRISPR screens.
DR ChiTaRS; Ugp2; mouse.
DR PRO; PR:Q91ZJ5; -.
DR Proteomes; UP000000589; Chromosome 11.
DR RNAct; Q91ZJ5; protein.
DR Bgee; ENSMUSG00000001891; Expressed in muscle of arm and 258 other tissues.
DR ExpressionAtlas; Q91ZJ5; baseline and differential.
DR Genevisible; Q91ZJ5; MM.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0005536; F:glucose binding; ISO:MGI.
DR GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0032557; F:pyrimidine ribonucleotide binding; ISO:MGI.
DR GO; GO:0003983; F:UTP:glucose-1-phosphate uridylyltransferase activity; IMP:MGI.
DR GO; GO:0007420; P:brain development; ISO:MGI.
DR GO; GO:0019255; P:glucose 1-phosphate metabolic process; ISO:MGI.
DR GO; GO:0005978; P:glycogen biosynthetic process; IMP:MGI.
DR GO; GO:0005977; P:glycogen metabolic process; IBA:GO_Central.
DR GO; GO:0006011; P:UDP-glucose metabolic process; ISO:MGI.
DR CDD; cd00897; UGPase_euk; 1.
DR Gene3D; 3.90.550.10; -; 1.
DR InterPro; IPR029044; Nucleotide-diphossugar_trans.
DR InterPro; IPR002618; UDPGP_fam.
DR InterPro; IPR016267; UDPGP_trans.
DR PANTHER; PTHR43511; PTHR43511; 1.
DR Pfam; PF01704; UDPGP; 1.
DR PIRSF; PIRSF000806; UDPGP; 1.
DR SUPFAM; SSF53448; SSF53448; 1.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; Cytoplasm; Magnesium; Metal-binding;
KW Nucleotidyltransferase; Phosphoprotein; Reference proteome; Transferase.
FT CHAIN 1..508
FT /note="UTP--glucose-1-phosphate uridylyltransferase"
FT /id="PRO_0000185753"
FT REGION 457..508
FT /note="Oligomerization"
FT /evidence="ECO:0000250"
FT REGION 502..503
FT /note="Critical for end-to-end subunit interaction"
FT /evidence="ECO:0000250"
FT ACT_SITE 396
FT /evidence="ECO:0000250"
FT BINDING 113..116
FT /ligand="UTP"
FT /ligand_id="ChEBI:CHEBI:46398"
FT /evidence="ECO:0000250|UniProtKB:Q9M9P3"
FT BINDING 115..116
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q16851"
FT BINDING 127
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 127
FT /ligand="UTP"
FT /ligand_id="ChEBI:CHEBI:46398"
FT /evidence="ECO:0000250|UniProtKB:Q9M9P3"
FT BINDING 190
FT /ligand="UTP"
FT /ligand_id="ChEBI:CHEBI:46398"
FT /evidence="ECO:0000250|UniProtKB:Q9M9P3"
FT BINDING 222
FT /ligand="UTP"
FT /ligand_id="ChEBI:CHEBI:46398"
FT /evidence="ECO:0000250|UniProtKB:Q9M9P3"
FT BINDING 223
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q16851"
FT BINDING 251..253
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q16851"
FT BINDING 253
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 253
FT /ligand="UTP"
FT /ligand_id="ChEBI:CHEBI:46398"
FT /evidence="ECO:0000250|UniProtKB:Q9M9P3"
FT BINDING 396
FT /ligand="UTP"
FT /ligand_id="ChEBI:CHEBI:46398"
FT /evidence="ECO:0000250|UniProtKB:Q9M9P3"
FT MOD_RES 13
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q16851"
FT MOD_RES 426
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q16851"
FT MOD_RES 434
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q16851"
FT MOD_RES 438
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q16851"
FT MOD_RES 448
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 461
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q16851"
FT VAR_SEQ 1..11
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_012835"
SQ SEQUENCE 508 AA; 56979 MW; 7F5FB23628D631FE CRC64;
MSRFVQDLSK AMSQDGASQF QEVILQELEL SVKKELEKIL TTAASHEFEH TKKDLDGFRK
LFHRFLQEKG PSVDWGKIQR PPEDSIQPYE KIKARGLPDN ISSVLNKLVV VKLNGGLGTS
MGCKGPKSLI GVRNENTFLD LTVQQIEHLN KTYNTDVPLV LMNSFNTDED TKKILQKYNH
CRVKIYTFNQ SRYPRINKES LLPIAKDVSY SGENTEAWYP PGHGDIYASF YNSGLLDTFI
EEGKEYIFVS NIDNLGATVD LYILNHLMNP PNGKRCEFVM EVTNKTRADV KGGTLTQYEG
KLRLVEIAQV PKAHVDEFKS VSKFKIFNTN NLWISLGAVK RLQEQNAIDM EIIVNPKTLD
GGLNVIQLET AVGAAIKSFE NSLGINVPRS RFLPVKTTSD LLLVMSNLYS LNAGSLTMSE
KREFPTVPLV KLGSSFTKVQ DYLRRFESIP DMLELDHLTV SGDVTFGKNV SLKGTVIIIA
NHGDRIDIPP GAVLENKIVS GNLRILDH
