ID UGPA_BOVIN Reviewed; 508 AA. AC Q07130; Q17QU0; DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2007, sequence version 2. DT 27-MAR-2024, entry version 135. 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 Bos taurus (Bovine). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae; OC Bovinae; Bos. OX NCBI_TaxID=9913; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA], AND PARTIAL PROTEIN SEQUENCE. RC STRAIN=Danshaku-Imo; TISSUE=Liver; RX PubMed=8407878; DOI=10.1093/oxfordjournals.jbchem.a124141; RA Konishi Y., Tanizawa K., Muroya S., Fukui T.; RT "Molecular cloning, nucleotide sequencing, and affinity labeling of bovine RT liver UDP-glucose pyrophosphorylase."; RL J. Biochem. 114:61-68(1993). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=Hereford; TISSUE=Thalamus; RG NIH - Mammalian Gene Collection (MGC) project; RL Submitted (JUN-2006) to the EMBL/GenBank/DDBJ databases. 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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; L14019; AAA30801.1; -; mRNA. DR EMBL; BC118181; AAI18182.1; -; mRNA. DR PIR; JX0277; JX0277. DR RefSeq; NP_776637.1; NM_174212.2. DR AlphaFoldDB; Q07130; -. DR SMR; Q07130; -. DR STRING; 9913.ENSBTAP00000073301; -. DR iPTMnet; Q07130; -. DR PaxDb; 9913-ENSBTAP00000042228; -. DR PeptideAtlas; Q07130; -. DR Ensembl; ENSBTAT00000044762.4; ENSBTAP00000042228.3; ENSBTAG00000000111.6. DR GeneID; 281565; -. DR KEGG; bta:281565; -. DR CTD; 7360; -. DR VEuPathDB; HostDB:ENSBTAG00000000111; -. DR VGNC; VGNC:36651; UGP2. DR eggNOG; KOG2638; Eukaryota. DR GeneTree; ENSGT00940000153464; -. DR HOGENOM; CLU_023632_3_0_1; -. DR InParanoid; Q07130; -. DR OMA; KEYCFLS; -. DR OrthoDB; 45684at2759; -. DR TreeFam; TF300567; -. DR Reactome; R-BTA-173599; Formation of the active cofactor, UDP-glucuronate. DR Reactome; R-BTA-3322077; Glycogen synthesis. DR SABIO-RK; Q07130; -. DR UniPathway; UPA00164; -. DR Proteomes; UP000009136; Chromosome 11. DR Bgee; ENSBTAG00000000111; Expressed in tongue muscle and 106 other cell types or tissues. DR ExpressionAtlas; Q07130; baseline and differential. DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0003983; F:UTP:glucose-1-phosphate uridylyltransferase activity; IBA:GO_Central. DR GO; GO:0005978; P:glycogen biosynthetic process; IEA:UniProtKB-UniPathway. DR GO; GO:0005977; P:glycogen metabolic process; IBA:GO_Central. DR GO; GO:0006011; P:UDP-glucose metabolic process; IBA:GO_Central. DR CDD; cd00897; UGPase_euk; 1. DR Gene3D; 2.160.10.10; Hexapeptide repeat proteins; 1. DR InterPro; IPR029044; Nucleotide-diphossugar_trans. DR InterPro; IPR002618; UDPGP_fam. DR InterPro; IPR016267; UDPGP_trans. DR PANTHER; PTHR43511; -; 1. DR PANTHER; PTHR43511:SF4; UTP--GLUCOSE-1-PHOSPHATE URIDYLYLTRANSFERASE; 1. DR Pfam; PF01704; UDPGP; 1. DR PIRSF; PIRSF000806; UDPGP; 1. DR SUPFAM; SSF53448; Nucleotide-diphospho-sugar transferases; 1. PE 1: Evidence at protein level; KW Acetylation; Cytoplasm; Direct protein sequencing; Magnesium; KW Metal-binding; Nucleotidyltransferase; Phosphoprotein; Reference proteome; KW Transferase. FT CHAIN 1..508 FT /note="UTP--glucose-1-phosphate uridylyltransferase" FT /id="PRO_0000185751" 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 2 FT /note="Blocked amino end (Ser)" 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" SQ SEQUENCE 508 AA; 56903 MW; A264DD254E6ED934 CRC64; MSRFVQDLSK AMSQDGASQF QEVIRQELEL SVKKELEKIL TTAPSHEFEH TKKDLDGFRK LFHRFLQEKG PSVDWGKIQR PPEDSIQPYE KIKARGLPDN VSSVLNKLVV VKLNGGLGTS MGCKGPKSLI GVRNENTFLD LTVQQIEHLN KTYDTDVPLV LMNSFNTDED TKKILQKYNH CRVKIYTFNQ SRYPRINKES LLPVAKNVSY SGENTEAWYP PGHGDIYASF YNSGLLDTFI GEGKEYIFVS NIDNLGATVD LYILNHLMNP PNGKPCEFVM EVTNKTRADV KGGTLTQYEG KLRLVEIAQV PKAHVDEFKS VSKFKIFNTN NLWISLAAVK RLQEQNAIDM EIIVNPKTLD GGLNVIQLET AVGAAIKSFE NSLGINVPRS RFLPVKTTSD LLLVMSNLYS LNAGSLTMSE KREFPTVPLV KLGSSFTKVQ DYLRRFESIP DMLELDHLTV SGDVTFGKNV SLKGTVIIIA NHGDRIDIPP GAVLENKIVS GNLRILDH //