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O35156 (UGPA_CRIGR) Reviewed, UniProtKB/Swiss-Prot

Last modified December 11, 2013. Version 65. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
UTP--glucose-1-phosphate uridylyltransferase

EC=2.7.7.9
Alternative name(s):
UDP-glucose pyrophosphorylase
Short name=UDPGP
Short name=UGPase
Gene names
Name:UGP2
Synonyms:UGP1
OrganismCricetulus griseus (Chinese hamster) (Cricetulus barabensis griseus)
Taxonomic identifier10029 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaCricetidaeCricetinaeCricetulus

Protein attributes

Sequence length508 AA.
Sequence statusComplete.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

Plays a central role as a glucosyl donor in cellular metabolic pathways.

Catalytic activity

UTP + alpha-D-glucose 1-phosphate = diphosphate + UDP-glucose.

Subunit structure

Homooctamer By similarity.

Subcellular location

Cytoplasm.

Sequence similarities

Belongs to the UDPGP type 1 family.

Ontologies

Keywords
   Cellular componentCytoplasm
   LigandMagnesium
Metal-binding
   Molecular functionNucleotidyltransferase
Transferase
   PTMAcetylation
Phosphoprotein
Gene Ontology (GO)
   Cellular_componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionUTP:glucose-1-phosphate uridylyltransferase activity

Inferred from electronic annotation. Source: UniProtKB-EC

metal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 508508UTP--glucose-1-phosphate uridylyltransferase
PRO_0000185749

Regions

Region457 – 50852Oligomerization By similarity
Region502 – 5032Critical for end-to-end subunit interaction By similarity

Sites

Active site3961 By similarity
Metal binding1271Magnesium By similarity
Metal binding2531Magnesium By similarity

Amino acid modifications

Modified residue131Phosphoserine By similarity
Modified residue4381N6-acetyllysine By similarity

Natural variations

Natural variant1161G → D in Don Q cell line; low level of activity. Ref.1

Sequences

Sequence LengthMass (Da)Tools
O35156 [UniParc].

Last modified January 23, 2007. Version 3.
Checksum: 42C62239BE2331A8

FASTA50856,924
        10         20         30         40         50         60 
MSRFVQDLSK AMSQDGASQF QEVILQELEL SVKKELEKIL TTATSHEYEH TKKDLDGFRK 

        70         80         90        100        110        120 
LYHRFLQEKG PSVDWGKIQR PPEDSIQPYE KIKARGLPDN ISSVLNKLVV VKLNGGLGTS 

       130        140        150        160        170        180 
MGCKGPKSLI GVRNENTFLD LTVQQIEHLN KSYNTDVPLV LMNSFNTDED TKKILQKYNH 

       190        200        210        220        230        240 
CRVKIYTFNQ SRYPRINKES LLPVAKDVSS SGESTEAWYP PGHGDIYASF YNSGLLDTFL 

       250        260        270        280        290        300 
EEGKEYIFVS NIDNLGATVD LYILNHLMNP PNGKRCEFVM EVTNKTRADV KGGTLTQYEG 

       310        320        330        340        350        360 
KLRLVEIAQV PKAHVDEFKS VSKFKIFNTN NLWISLAAVK RLQEQNAIDM EIIVNPKTLD 

       370        380        390        400        410        420 
GGLNVIQLET AVGAAIKSFE NSLGINVPRS RFLPVKTTSD LLLVMSNLYS LNAGSLTMSE 

       430        440        450        460        470        480 
KREFPTVPLV KLGSSFTKVQ DYLRRFESIP DMLELDHLTV SGDVTFGKNV SLKGTVIIIA 

       490        500 
NHGDRIDIPP GAVLENKIVS GNLRILDH 

« Hide

References

[1]"Cellular UDP-glucose deficiency caused by a single point mutation in the UDP-glucose pyrophosphorylase gene."
Flores-Diaz M., Alape-Giron A., Persson B., Pollesello P., Moos M., von Eichel-Streiber C., Thelestam M., Florin I.
J. Biol. Chem. 272:23784-23791(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANT ASP-116.
Tissue: Fibroblast.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF004368 mRNA. Translation: AAC53343.1.
RefSeqNP_001233687.1. NM_001246758.1.

3D structure databases

ProteinModelPortalO35156.
SMRO35156. Positions 51-508.
ModBaseSearch...
MobiDBSearch...

Proteomic databases

PRIDEO35156.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID100689325.
KEGGcge:100689325.

Organism-specific databases

CTD7360.

Phylogenomic databases

HOVERGENHBG055396.
KOK00963.

Family and domain databases

InterProIPR002618. UDPGP_trans.
IPR016267. UDPGP_trans_subgr.
[Graphical view]
PANTHERPTHR11952. PTHR11952. 1 hit.
PTHR11952:SF1. PTHR11952:SF1. 1 hit.
PfamPF01704. UDPGP. 1 hit.
[Graphical view]
PIRSFPIRSF000806. UDPGP. 1 hit.
ProtoNetSearch...

Entry information

Entry nameUGPA_CRIGR
AccessionPrimary (citable) accession number: O35156
Entry history
Integrated into UniProtKB/Swiss-Prot: July 15, 1999
Last sequence update: January 23, 2007
Last modified: December 11, 2013
This is version 65 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families