ExPASy logo ExPASy Home page Site Map Search ExPASy Contact us Swiss-Prot
Notice: This page will be replaced with www.uniprot.org. Please send us your feedback!
Search for

UniProtKB/Swiss-Prot entry Q19905


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

Note: most headings are clickable, even if they don't appear as links. They link to the user manual or other documents.
Entry information
Entry name UGDH_CAEEL
Primary accession number Q19905
Secondary accession numbers None
Integrated into Swiss-Prot on December 15, 1998
Sequence was last modified on November 1, 1996 (Sequence version 1)
Annotations were last modified on    July 22, 2008 (Entry version 59)
Name and origin of the protein
Protein name UDP-glucose 6-dehydrogenase
Synonyms UDP-Glc dehydrogenase
UDP-GlcDH
UDPGDH
EC 1.1.1.22
Squashed vulva protein 4
Gene name
Name: sqv-4
ORFNames: F29F11.1
From
Caenorhabditis elegans [TaxID: 6239] 
Taxonomy Eukaryota; Metazoa; Nematoda; Chromadorea; Rhabditida; Rhabditoidea; Rhabditidae; Peloderinae; Caenorhabditis.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [MRNA].
DOI=10.1073/pnas.172522499; PubMed=12391315 [NCBI, ExPASy, EBI, Israel, Japan]
Hwang H.Y., Horvitz H.R.;
"The Caenorhabditis elegans vulval morphogenesis gene sqv-4 encodes a UDP-glucose dehydrogenase that is temporally and spatially regulated.";
Proc. Natl. Acad. Sci. U.S.A. 99:14224-14229(2002).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=Bristol N2;
DOI=10.1126/science.282.5396.2012; PubMed=9851916 [NCBI, ExPASy, EBI, Israel, Japan]
The C. elegans sequencing consortium;
"Genome sequence of the nematode C. elegans: a platform for investigating biology.";
Science 282:2012-2018(1998).
Comments
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
AY147932; AAN39842.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
Z73974; CAA98269.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR T21550; T21550.
RefSeq NP_505730.1; -.
UniGene Cel.19769
3D structure databases
PDB
2O3J; X-ray; 1.88 A; A/B/C=1-481.[ExPASy / RCSB / EBI]
PDBsum 2O3J; -.
ModBase Q19905.
Protein-protein interaction databases
DIP DIP:24290N; -.
IntAct Q19905; -.
Organism-specific databases
WormBase WBGene00005022; sqv-4.
WormPep F29F11.1; CE05767. [WormPep / WorfDB]
Gene expression databases
ArrayExpress Q19905; -.
Ontologies
GO
GO:0042802; Molecular function: identical protein binding (inferred from physical interaction from IntAct).
GO:0009792; Biological process: embryonic development ending in birth or egg hatching (inferred from mutant phenotype from WormBase).
GO:0002009; Biological process: morphogenesis of an epithelium (inferred from mutant phenotype from WormBase).
GO:0018991; Biological process: oviposition (inferred from mutant phenotype from WormBase).
GO:0040025; Biological process: vulval development (inferred from mutant phenotype from WormBase).
QuickGo view.
Family and domain databases
InterPro IPR016040; NAD(P)-bd.
IPR017476; Nucleotide_sugar_DH.
IPR014027; UDP-Glc/GDP-Man_DHase_C.
IPR014026; UDP-Glc/GDP-Man_DHase_dimer.
IPR014028; UDP-Glc/GDP-Man_DHase_dimer-bd.
IPR001732; UDP-Glc/GDP-Man_DHase_N.
Graphical view of domain structure.
Gene3D G3DSA:3.40.50.720; NAD(P)-bd; 1.
G3DSA:3.40.50.1870; UDP-Glc/GDP-Man_DH_C; 1.
PANTHER PTHR11374; UDPG_MGDP_DH_Creg; 1.
Pfam PF00984; UDPG_MGDP_dh; 1.
PF03720; UDPG_MGDP_dh_C; 1.
PF03721; UDPG_MGDP_dh_N; 1.
Pfam graphical view of domain structure.
BLOCKS Q19905.
Genome annotation databases
Ensembl F29F11.1; Caenorhabditis elegans. [Contig view]
GeneID 179484; -.
KEGG cel:F29F11.1; -.
Other
ProtoNet Q19905.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
3D-structure; Complete proteome; NAD; Oxidoreductase.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom   To Length Description FTId
CHAIN   1   481  481     UDP-glucose 6-dehydrogenase. PRO_0000074063
NP_BIND   11    28  18     NAD (By similarity). 
REGION   169   172  4     Substrate binding (By similarity). 
ACT_SITE   283   283        Nucleophile (By similarity). 
BINDING   41    41        NAD (By similarity). 
BINDING   46    46        NAD (By similarity). 
BINDING   98    98        NAD (By similarity). 
BINDING   136   136        NAD; via amide nitrogen (By similarity). 
BINDING   172   172        NAD (By similarity). 
BINDING   227   227        Substrate (By similarity). 
BINDING   280   280        Substrate; via amide nitrogen (By similarity). 
BINDING   286   286        NAD (By similarity). 
BINDING   346   346        Substrate (By similarity). 
BINDING   353   353        NAD (By similarity). 
STRAND   11    15  5      
HELIX   21    31  11      
STRAND   35    40  6      
HELIX   44    50  7      
STRAND   52    54  3      
HELIX   62    69  8      
TURN   71    73  3      
STRAND   74    78  5      
HELIX   80    86  7      
STRAND   88    92  5      
TURN   103   107  5      
HELIX   112   124  13      
STRAND   129   133  5      
HELIX   141   152  12      
STRAND   161   165  5      
HELIX   175   180  6      
STRAND   185   189  5      
HELIX   193   207  15      
HELIX   212   214  3      
STRAND   215   219  5      
HELIX   220   251  32      
HELIX   255   263  9      
TURN   266   268  3      
STRAND   270   272  3      
STRAND   281   283  3      
HELIX   284   297  14      
HELIX   301   328  28      
TURN   329   331  3      
STRAND   337   341  5      
STRAND   344   346  3      
HELIX   356   366  11      
STRAND   370   374  5      
STRAND   376   378  3      
HELIX   380   390  11      
HELIX   393   399  7      
STRAND   400   405  6      
HELIX   406   410  5      
STRAND   414   418  5      
HELIX   423   425  3      
HELIX   430   436  7      
STRAND   442   448  7      
HELIX   452   458  7      
STRAND   461   464  4      
Sequence information
Length: 481 AA [This is the length of the unprocessed precursor] Molecular weight: 52755 Da [This is the MW of the unprocessed precursor] CRC64: 4E789DC5D6679531 [This is a checksum on the sequence]
        10         20         30         40         50         60 
MTDQVFGKVS KVVCVGAGYV GGPTCAMIAH KCPHITVTVV DMNTAKIAEW NSDKLPIYEP 

        70         80         90        100        110        120 
GLDEIVFAAR GRNLFFSSDI PKAIAEADLI FISVNTPTKM YGRGKGMAPD LKYVESVSRT 

       130        140        150        160        170        180 
IAQYAGGPKI VVEKSTVPVK AAESIGCILR EAQKNNENLK FQVLSNPEFL AEGTAMKDLA 

       190        200        210        220        230        240 
NPDRVLIGGE SSPEGLQAVA ELVRIYENWV PRNRIITTNT WSSELSKLVA NAFLAQRISS 

       250        260        270        280        290        300 
INSISAVCEA TGAEISEVAH AVGYDTRIGS KFLQASVGFG GSCFQKDVLS LVYLCESLNL 

       310        320        330        340        350        360 
PQVADYWQGV ININNWQRRR FADKIIAELF NTVTDKKIAI FGFAFKKNTG DTRESSAIHV 

       370        380        390        400        410        420 
IKHLMEEHAK LSVYDPKVQK SQMLNDLASV TSAQDVERLI TVESDPYAAA RGAHAIVVLT 

       430        440        450        460        470        480 
EWDEFVELNY SQIHNDMQHP AAIFDGRLIL DQKALREIGF RTFAIGTSPD QAYNLFGTAG 


Y 

Q19905 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

BLAST logo BLAST submission on ExPASy/SIB
or at NCBI (USA)
Tools Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
PROSITE logo ScanProsite, MotifScan SWISS-MODEL Submit a homology modeling request to SWISS-MODEL
NPSA logo NPSA Sequence analysis tools

ExPASy logo ExPASy Home page Site Map Search ExPASy Contact us Swiss-Prot
 Hosted by kr flag YPRC Korea Mirror sites: Australia  Brazil  Canada  China  Switzerland
Notice: This page will be replaced with www.uniprot.org. Please send us your feedback!