UGPA_CRIGR
ID UGPA_CRIGR Reviewed; 508 AA.
AC O35156;
DT 15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 101.
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; Synonyms=UGP1;
OS Cricetulus griseus (Chinese hamster) (Cricetulus barabensis griseus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea;
OC Cricetidae; Cricetinae; Cricetulus.
OX NCBI_TaxID=10029;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND VARIANT ASP-116.
RC TISSUE=Fibroblast;
RX PubMed=9295324; DOI=10.1074/jbc.272.38.23784;
RA Flores-Diaz M., Alape-Giron A., Persson B., Pollesello P., Moos M.,
RA von Eichel-Streiber C., Thelestam M., Florin I.;
RT "Cellular UDP-glucose deficiency caused by a single point mutation in the
RT UDP-glucose pyrophosphorylase gene.";
RL J. Biol. Chem. 272:23784-23791(1997).
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 -!- SIMILARITY: Belongs to the UDPGP type 1 family. {ECO:0000305}.
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DR EMBL; AF004368; AAC53343.1; -; mRNA.
DR RefSeq; NP_001233687.1; NM_001246758.1.
DR AlphaFoldDB; O35156; -.
DR SMR; O35156; -.
DR STRING; 10029.NP_001233687.1; -.
DR Ensembl; ENSCGRT00001015358; ENSCGRP00001011129; ENSCGRG00001012845.
DR GeneID; 100689325; -.
DR KEGG; cge:100689325; -.
DR CTD; 7360; -.
DR eggNOG; KOG2638; Eukaryota.
DR GeneTree; ENSGT00940000153464; -.
DR OMA; TNNLWAK; -.
DR OrthoDB; 503037at2759; -.
DR UniPathway; UPA00164; -.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0042802; F:identical protein binding; IEA:Ensembl.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0003983; F:UTP:glucose-1-phosphate uridylyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0007420; P:brain development; IEA:Ensembl.
DR GO; GO:0005978; P:glycogen biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0006011; P:UDP-glucose metabolic process; IEA:Ensembl.
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 2: Evidence at transcript level;
KW Acetylation; Cytoplasm; Magnesium; Metal-binding; Nucleotidyltransferase;
KW Phosphoprotein; Transferase.
FT CHAIN 1..508
FT /note="UTP--glucose-1-phosphate uridylyltransferase"
FT /id="PRO_0000185749"
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:0000250|UniProtKB:Q16851"
FT MOD_RES 461
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q16851"
FT VARIANT 116
FT /note="G -> D (in Don Q cell line; low level of activity)"
FT /evidence="ECO:0000269|PubMed:9295324"
SQ SEQUENCE 508 AA; 56924 MW; 42C62239BE2331A8 CRC64;
MSRFVQDLSK AMSQDGASQF QEVILQELEL SVKKELEKIL TTATSHEYEH TKKDLDGFRK
LYHRFLQEKG PSVDWGKIQR PPEDSIQPYE KIKARGLPDN ISSVLNKLVV VKLNGGLGTS
MGCKGPKSLI GVRNENTFLD LTVQQIEHLN KSYNTDVPLV LMNSFNTDED TKKILQKYNH
CRVKIYTFNQ SRYPRINKES LLPVAKDVSS SGESTEAWYP PGHGDIYASF YNSGLLDTFL
EEGKEYIFVS NIDNLGATVD LYILNHLMNP PNGKRCEFVM EVTNKTRADV KGGTLTQYEG
KLRLVEIAQV PKAHVDEFKS VSKFKIFNTN NLWISLAAVK RLQEQNAIDM EIIVNPKTLD
GGLNVIQLET AVGAAIKSFE NSLGINVPRS RFLPVKTTSD LLLVMSNLYS LNAGSLTMSE
KREFPTVPLV KLGSSFTKVQ DYLRRFESIP DMLELDHLTV SGDVTFGKNV SLKGTVIIIA
NHGDRIDIPP GAVLENKIVS GNLRILDH
