Q6ZNW5 (GDPP1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
GDP-D-glucose phosphorylase 1
EC=2.7.7.78

Gene names

Name:	GDPGP1
Synonyms:	C15orf58

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	385 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Specific and highly efficient GDP-D-glucose phosphorylase regulating the levels of GDP-D-glucose in cells. Ref.3
Catalytic activity	GDP-alpha-D-glucose + phosphate = alpha-D-glucose 1-phosphate + GDP. Ref.3
Subcellular location	Cytoplasm By similarity.
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.
Sequence similarities	Belongs to the GDPGP1 family.
Biophysicochemical properties	Kinetic parameters: kcat is 26 s(-1) at 31 degrees Celsius. The catalytic efficiency for GDP-D-glucose is 35-fold higher than for GDP-L-galactose. KM=2 µM for GDP-D-glucose (at 31 degrees Celsius) Ref.3 KM=12 µM for GDP-L-galactose (at 31 degrees Celsius) KM=42 µM for GDP-D-mannose (at 31 degrees Celsius) KM=2.9 mM for inorganic phosphate (at 31 degrees Celsius)

Ontologies

Keywords
Cellular component	Cytoplasm
Coding sequence diversity	Polymorphism
Ligand	Nucleotide-binding
Molecular function	Guanine-nucleotide releasing factor Hydrolase Nucleotidyltransferase Transferase
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	glucose metabolic process Inferred from mutant phenotype Ref.3. Source: UniProtKB
Cellular_component	cytoplasm Inferred from sequence or structural similarity. Source: UniProtKB
Molecular_function	GDP-D-glucose phosphorylase activity Inferred from direct assay Ref.3. Source: UniProtKB guanyl-nucleotide exchange factor activity Inferred from electronic annotation. Source: UniProtKB-KW hydrolase activity Inferred from electronic annotation. Source: UniProtKB-KW nucleotide binding Inferred from electronic annotation. Source: UniProtKB-KW nucleotidyltransferase activity Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 385	385	GDP-D-glucose phosphorylase 1		PRO_0000336750
Sites
	Active site	218	1	Tele-GMP-histidine intermediate By similarity
Natural variations
	Natural variant	37	1	M → T. Ref.1 Corresponds to variant rs7171194 [ dbSNP | Ensembl ].		VAR_043555
	Natural variant	264	1	P → T. Ref.1 Corresponds to variant rs10152994 [ dbSNP | Ensembl ].		VAR_043556
	Natural variant	307	1	T → I. Ref.1 Corresponds to variant rs10153004 [ dbSNP | Ensembl ].		VAR_043557
Experimental info
	Sequence conflict	23	1	R → G in BAC85370. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	Q6ZNW5 [UniParc]. Last modified May 18, 2010. Version 2. Checksum: 921A656C721876EC	FASTA	385	42,362
	10 20 30 40 50 60 MALPHDSNET SYLLPPNNED WGRQTIPDFV YGQKDLMAEG IQWPRNAPGI PDALPQSPFD 70 80 90 100 110 120 AALCSAWKQR VELGLFRYRL RELQTQILPG AVGFVAQLNV ERGVQRRPPQ TIKSVRQAFD 130 140 150 160 170 180 PVQFNFNKIR PGEVLFRLHR EPDLPGTLLQ EDILVVINVS PLEWGHVLLV PEPARQLPQR 190 200 210 220 230 240 LLPGALRAGI EAVLLSLHPG FRVGFNSLGG LASVNHLHLH GYYLAHRLPV EQAPSEPLDP 250 260 270 280 290 300 GGHLHLLQDL PAPGFLFYTR GPGPDLESLI SRVCRATDYL TDHEIAHNLF VTRGAPPGKT 310 320 330 340 350 360 SPSSALTGVR VILWARKSSF GIKDGEAFNV ALCELAGHLP VKTSQDFSSL TEAAAVALIQ 370 380 DCRLPPSQAE DVQAALVALM SQEEQ

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Complete sequencing and characterization of 21,243 full-length human cDNAs." Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S. Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANTS THR-37; THR-264 AND ILE-307. Tissue: Salivary gland.
[2]	"Analysis of the DNA sequence and duplication history of human chromosome 15." Zody M.C., Garber M., Sharpe T., Young S.K., Rowen L., O'Neill K., Whittaker C.A., Kamal M., Chang J.L., Cuomo C.A., Dewar K., FitzGerald M.G., Kodira C.D., Madan A., Qin S., Yang X., Abbasi N., Abouelleil A. , Arachchi H.M., Baradarani L., Birditt B., Bloom S., Bloom T., Borowsky M.L., Burke J., Butler J., Cook A., DeArellano K., DeCaprio D., Dorris L. III, Dors M., Eichler E.E., Engels R., Fahey J., Fleetwood P., Friedman C., Gearin G., Hall J.L., Hensley G., Johnson E., Jones C., Kamat A., Kaur A., Locke D.P., Madan A., Munson G., Jaffe D.B., Lui A., Macdonald P., Mauceli E., Naylor J.W., Nesbitt R., Nicol R., O'Leary S.B., Ratcliffe A., Rounsley S., She X., Sneddon K.M.B., Stewart S., Sougnez C., Stone S.M., Topham K., Vincent D., Wang S., Zimmer A.R., Birren B.W., Hood L., Lander E.S., Nusbaum C. Nature 440:671-675(2006) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[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: FUNCTION, CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY, KINETIC PARAMETERS.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AK130527 mRNA. Translation: BAC85370.1. AC091167 Genomic DNA. No translation available.
IPI	IPI00418644.
RefSeq	NP_001013679.2. NM_001013657.2.
UniGene	Hs.304673.
3D structure databases
ProteinModelPortal	Q6ZNW5.
SMR	Q6ZNW5. Positions 150-222.
ModBase	Search...
Protein-protein interaction databases
STRING	9606.ENSP00000368405.
Polymorphism databases
DMDM	296434456.
Proteomic databases
PaxDb	Q6ZNW5.
PRIDE	Q6ZNW5.
Protocols and materials databases
DNASU	390637.
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000329600; ENSP00000368405; ENSG00000183208. ENST00000558017; ENSP00000452793; ENSG00000183208.
GeneID	390637.
KEGG	hsa:390637.
UCSC	uc002bpc.3. human.
Organism-specific databases
CTD	390637.
GeneCards	GC15P090778.
HGNC	HGNC:34360. GDPGP1.
HPA	HPA048189.
neXtProt	NX_Q6ZNW5.
PharmGKB	PA162378247.
GenAtlas	Search...
Phylogenomic databases
eggNOG	NOG307761.
HOVERGEN	HBG106673.
InParanoid	Q6ZNW5.
KO	K15630.
OMA	GIQWPRN.
OrthoDB	EOG4DZ1VC.
Enzyme and pathway databases
BioCyc	MetaCyc:G66-31756-MONOMER.
Gene expression databases
ArrayExpress	Q6ZNW5.
Bgee	Q6ZNW5.
CleanEx	HS_C15orf58.
Genevestigator	Q6ZNW5.
Family and domain databases
InterPro	IPR026506. GDPGP1. [Graphical view]
PANTHER	PTHR20884:SF4. PTHR20884:SF4. 1 hit.
ProtoNet	Search...
Other
GenomeRNAi	390637.
NextBio	103948.

Entry information

Entry name

GDPP1_HUMAN

Accession

Primary (citable) accession number: Q6ZNW5

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 20, 2008
Last sequence update:	May 18, 2010
Last modified:	April 3, 2013
This is version 57 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.