UGPA_BOVIN
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 03-AUG-2022, entry version 127.
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}.
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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.ENSBTAP00000042228; -.
DR iPTMnet; Q07130; -.
DR PaxDb; Q07130; -.
DR PeptideAtlas; Q07130; -.
DR PRIDE; Q07130; -.
DR Ensembl; ENSBTAT00000044762; ENSBTAP00000042228; ENSBTAG00000000111.
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; TNNLWAK; -.
DR OrthoDB; 503037at2759; -.
DR TreeFam; TF300567; -.
DR SABIO-RK; Q07130; -.
DR UniPathway; UPA00164; -.
DR Proteomes; UP000009136; Chromosome 11.
DR Bgee; ENSBTAG00000000111; Expressed in tongue muscle and 106 other 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; 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; 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
