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Protein

GDP-D-glucose phosphorylase 1

Gene

Gdpgp1

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at transcript leveli

Functioni

Specific and highly efficient GDP-D-glucose phosphorylase regulating the levels of GDP-D-glucose in cells.By similarity

Catalytic activityi

GDP-alpha-D-glucose + phosphate = alpha-D-glucose 1-phosphate + GDP.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei219 – 2191Tele-GMP-histidine intermediateBy similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Guanine-nucleotide releasing factor, Hydrolase, Nucleotidyltransferase, Transferase

Keywords - Ligandi

Nucleotide-binding

Enzyme and pathway databases

BRENDAi2.7.7.78. 3474.

Names & Taxonomyi

Protein namesi
Recommended name:
GDP-D-glucose phosphorylase 1 (EC:2.7.7.78)
Gene namesi
Name:Gdpgp1
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589 Componenti: Chromosome 7

Organism-specific databases

MGIiMGI:2443429. Gdpgp1.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 386386GDP-D-glucose phosphorylase 1PRO_0000336752Add
BLAST

Proteomic databases

MaxQBiQ3TLS3.
PaxDbiQ3TLS3.
PRIDEiQ3TLS3.

Expressioni

Tissue specificityi

Highly expressed in the nervous and male reproductive systems compared to kidney, liver and heart.1 Publication

Gene expression databases

BgeeiQ3TLS3.
GenevisibleiQ3TLS3. MM.

Interactioni

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000061808.

Structurei

3D structure databases

ProteinModelPortaliQ3TLS3.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the GDPGP1 family.Curated

Phylogenomic databases

eggNOGiNOG307761.
GeneTreeiENSGT00390000016718.
HOVERGENiHBG106673.
InParanoidiQ3TLS3.
KOiK15630.
OMAiDYNDASE.
OrthoDBiEOG7M98H0.
PhylomeDBiQ3TLS3.
TreeFamiTF313615.

Family and domain databases

InterProiIPR026506. GDPGP.
[Graphical view]
PANTHERiPTHR20884. PTHR20884. 1 hit.

Sequencei

Sequence statusi: Complete.

Q3TLS3-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAVPHHLQET SYLLPPDPED WEKQGIPDFV YGQEDLVGKE VQWPRDSPSA
60 70 80 90 100
VDTVPLSRFD SALRSAWRQR LELGLFRYRL EDLQTQILPG SVGFVAQLNI
110 120 130 140 150
ERGIQRRRPQ NIRSVRQEFD PEQFNFNKIR PGEVLFRMQR EPKGPATPKQ
160 170 180 190 200
EDDVLVVINV SPLEWGHVLL VPAPAQGLPQ RLLPGVLRVG LEAVLLSLHP
210 220 230 240 250
GFRVGFNSLG GLASVNHLHL HCYYLAHPLP VEGAPSTPLD PKGCIHLLQA
260 270 280 290 300
LPAPGFLFYT SGPGPDLEVL ISRVCRATDY LSDREIAHNL FVTRGAPPGP
310 320 330 340 350
TSSTSDLSGI RVILWARKSS FGIKESGAFN VALCELAGHL PVKTSQDFSS
360 370 380
LTEAAAVALI QDCLLPETQA GEVRAALVAL MAQEEL
Length:386
Mass (Da):42,515
Last modified:May 20, 2008 - v2
Checksum:iB69E1EECF9D719A0
GO

Sequence cautioni

The sequence BAC39476.1 differs from that shown. Reason: Frameshift at positions 186, 265 and 355. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti7 – 71L → S in BAE38719 (PubMed:16141072).Curated
Sequence conflicti7 – 71L → S in AAH37479 (PubMed:15489334).Curated
Sequence conflicti8 – 81Q → L in AAH37479 (PubMed:15489334).Curated
Sequence conflicti44 – 441P → S in BAE25508 (PubMed:16141072).Curated
Sequence conflicti81 – 811E → K in BAC39476 (PubMed:16141072).Curated
Sequence conflicti95 – 951V → L in BAC39476 (PubMed:16141072).Curated
Sequence conflicti101 – 1011E → D in AAH37479 (PubMed:15489334).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK084531 mRNA. Translation: BAC39213.1.
AK085577 mRNA. Translation: BAC39476.1. Frameshift.
AK143704 mRNA. Translation: BAE25508.1.
AK166345 mRNA. Translation: BAE38719.1.
BC037479 mRNA. Translation: AAH37479.1.
CCDSiCCDS39995.1.
RefSeqiNP_848867.2. NM_178752.3.
UniGeneiMm.187733.

Genome annotation databases

EnsembliENSMUST00000062915; ENSMUSP00000061808; ENSMUSG00000050973.
GeneIDi269952.
KEGGimmu:269952.
UCSCiuc009hzu.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK084531 mRNA. Translation: BAC39213.1.
AK085577 mRNA. Translation: BAC39476.1. Frameshift.
AK143704 mRNA. Translation: BAE25508.1.
AK166345 mRNA. Translation: BAE38719.1.
BC037479 mRNA. Translation: AAH37479.1.
CCDSiCCDS39995.1.
RefSeqiNP_848867.2. NM_178752.3.
UniGeneiMm.187733.

3D structure databases

ProteinModelPortaliQ3TLS3.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000061808.

Proteomic databases

MaxQBiQ3TLS3.
PaxDbiQ3TLS3.
PRIDEiQ3TLS3.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000062915; ENSMUSP00000061808; ENSMUSG00000050973.
GeneIDi269952.
KEGGimmu:269952.
UCSCiuc009hzu.1. mouse.

Organism-specific databases

CTDi390637.
MGIiMGI:2443429. Gdpgp1.

Phylogenomic databases

eggNOGiNOG307761.
GeneTreeiENSGT00390000016718.
HOVERGENiHBG106673.
InParanoidiQ3TLS3.
KOiK15630.
OMAiDYNDASE.
OrthoDBiEOG7M98H0.
PhylomeDBiQ3TLS3.
TreeFamiTF313615.

Enzyme and pathway databases

BRENDAi2.7.7.78. 3474.

Miscellaneous databases

NextBioi393115.
PROiQ3TLS3.
SOURCEiSearch...

Gene expression databases

BgeeiQ3TLS3.
GenevisibleiQ3TLS3. MM.

Family and domain databases

InterProiIPR026506. GDPGP.
[Graphical view]
PANTHERiPTHR20884. PTHR20884. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6J.
    Tissue: Heart, Kidney, Mammary gland and Spleen.
  2. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: FVB/N.
    Tissue: Mammary tumor.
  3. "A novel GDP-D-glucose phosphorylase involved in quality control of the nucleoside diphosphate sugar pool in Caenorhabditis elegans and mammals."
    Adler L.N., Gomez T.A., Clarke S.G., Linster C.L.
    J. Biol. Chem. 286:21511-21523(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: TISSUE SPECIFICITY.

Entry informationi

Entry nameiGDPP1_MOUSE
AccessioniPrimary (citable) accession number: Q3TLS3
Secondary accession number(s): Q3UP89
, Q8C3L2, Q8C3Y3, Q8CI49
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 20, 2008
Last sequence update: May 20, 2008
Last modified: July 22, 2015
This is version 65 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Miscellaneous

The orthologs in A.thaliana are GDP-L-galactose phosphorylases catalyzing the first reaction of the Smirnoff-Wheeler pathway, the major route to ascorbate biosynthesis in plants.

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.