GDPP1_HUMAN
ID GDPP1_HUMAN Reviewed; 385 AA.
AC Q6ZNW5;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 18-MAY-2010, sequence version 2.
DT 03-AUG-2022, entry version 110.
DE RecName: Full=GDP-D-glucose phosphorylase 1;
DE EC=2.7.7.78;
GN Name=GDPGP1; Synonyms=C15orf58;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANTS THR-37; THR-264 AND
RP ILE-307.
RC TISSUE=Salivary gland;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16572171; DOI=10.1038/nature04601;
RA Zody M.C., Garber M., Sharpe T., Young S.K., Rowen L., O'Neill K.,
RA Whittaker C.A., Kamal M., Chang J.L., Cuomo C.A., Dewar K.,
RA FitzGerald M.G., Kodira C.D., Madan A., Qin S., Yang X., Abbasi N.,
RA Abouelleil A., Arachchi H.M., Baradarani L., Birditt B., Bloom S.,
RA Bloom T., Borowsky M.L., Burke J., Butler J., Cook A., DeArellano K.,
RA DeCaprio D., Dorris L. III, Dors M., Eichler E.E., Engels R., Fahey J.,
RA Fleetwood P., Friedman C., Gearin G., Hall J.L., Hensley G., Johnson E.,
RA Jones C., Kamat A., Kaur A., Locke D.P., Madan A., Munson G., Jaffe D.B.,
RA Lui A., Macdonald P., Mauceli E., Naylor J.W., Nesbitt R., Nicol R.,
RA O'Leary S.B., Ratcliffe A., Rounsley S., She X., Sneddon K.M.B.,
RA Stewart S., Sougnez C., Stone S.M., Topham K., Vincent D., Wang S.,
RA Zimmer A.R., Birren B.W., Hood L., Lander E.S., Nusbaum C.;
RT "Analysis of the DNA sequence and duplication history of human chromosome
RT 15.";
RL Nature 440:671-675(2006).
RN [3]
RP FUNCTION, CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY, AND KINETIC
RP PARAMETERS.
RX PubMed=21507950; DOI=10.1074/jbc.m111.238774;
RA Adler L.N., Gomez T.A., Clarke S.G., Linster C.L.;
RT "A novel GDP-D-glucose phosphorylase involved in quality control of the
RT nucleoside diphosphate sugar pool in Caenorhabditis elegans and mammals.";
RL J. Biol. Chem. 286:21511-21523(2011).
CC -!- FUNCTION: Specific and highly efficient GDP-D-glucose phosphorylase
CC regulating the levels of GDP-D-glucose in cells.
CC {ECO:0000269|PubMed:21507950}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=GDP-alpha-D-glucose + phosphate = alpha-D-glucose 1-phosphate
CC + GDP + H(+); Xref=Rhea:RHEA:30387, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:58189, ChEBI:CHEBI:58601,
CC ChEBI:CHEBI:62230; EC=2.7.7.78;
CC Evidence={ECO:0000269|PubMed:21507950};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=2 uM for GDP-D-glucose (at 31 degrees Celsius)
CC {ECO:0000269|PubMed:21507950};
CC KM=12 uM for GDP-L-galactose (at 31 degrees Celsius)
CC {ECO:0000269|PubMed:21507950};
CC KM=42 uM for GDP-D-mannose (at 31 degrees Celsius)
CC {ECO:0000269|PubMed:21507950};
CC KM=2.9 mM for inorganic phosphate (at 31 degrees Celsius)
CC {ECO:0000269|PubMed:21507950};
CC Note=kcat is 26 sec(-1) at 31 degrees Celsius. The catalytic
CC efficiency for GDP-D-glucose is 35-fold higher than for GDP-L-
CC galactose.;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- MISCELLANEOUS: The orthologs in A.thaliana are GDP-L-galactose
CC phosphorylases catalyzing the first reaction of the Smirnoff-Wheeler
CC pathway, the major route to ascorbate biosynthesis in plants.
CC -!- SIMILARITY: Belongs to the GDPGP1 family. {ECO:0000305}.
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DR EMBL; AK130527; BAC85370.1; -; mRNA.
DR EMBL; AC091167; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR CCDS; CCDS32327.1; -.
DR RefSeq; NP_001013679.2; NM_001013657.2.
DR RefSeq; NP_001309740.1; NM_001322811.1.
DR AlphaFoldDB; Q6ZNW5; -.
DR BioGRID; 133642; 13.
DR STRING; 9606.ENSP00000452793; -.
DR iPTMnet; Q6ZNW5; -.
DR PhosphoSitePlus; Q6ZNW5; -.
DR BioMuta; GDPGP1; -.
DR DMDM; 296434456; -.
DR EPD; Q6ZNW5; -.
DR jPOST; Q6ZNW5; -.
DR MassIVE; Q6ZNW5; -.
DR MaxQB; Q6ZNW5; -.
DR PaxDb; Q6ZNW5; -.
DR PeptideAtlas; Q6ZNW5; -.
DR PRIDE; Q6ZNW5; -.
DR ProteomicsDB; 68049; -.
DR Antibodypedia; 28769; 55 antibodies from 13 providers.
DR DNASU; 390637; -.
DR Ensembl; ENST00000329600.8; ENSP00000368405.3; ENSG00000183208.13.
DR Ensembl; ENST00000558017.5; ENSP00000452793.1; ENSG00000183208.13.
DR Ensembl; ENST00000558291.2; ENSP00000454128.2; ENSG00000183208.13.
DR Ensembl; ENST00000559204.6; ENSP00000453822.2; ENSG00000183208.13.
DR GeneID; 390637; -.
DR KEGG; hsa:390637; -.
DR MANE-Select; ENST00000329600.8; ENSP00000368405.3; NM_001013657.3; NP_001013679.2.
DR UCSC; uc059ned.1; human.
DR CTD; 390637; -.
DR DisGeNET; 390637; -.
DR GeneCards; GDPGP1; -.
DR HGNC; HGNC:34360; GDPGP1.
DR HPA; ENSG00000183208; Low tissue specificity.
DR MIM; 619240; gene.
DR neXtProt; NX_Q6ZNW5; -.
DR OpenTargets; ENSG00000183208; -.
DR PharmGKB; PA162378247; -.
DR VEuPathDB; HostDB:ENSG00000183208; -.
DR eggNOG; KOG2720; Eukaryota.
DR GeneTree; ENSGT00390000016718; -.
DR HOGENOM; CLU_041964_2_1_1; -.
DR InParanoid; Q6ZNW5; -.
DR OMA; LEVMMTI; -.
DR OrthoDB; 1178383at2759; -.
DR PhylomeDB; Q6ZNW5; -.
DR TreeFam; TF313615; -.
DR BioCyc; MetaCyc:G66-31756-MON; -.
DR BRENDA; 2.7.7.78; 2681.
DR PathwayCommons; Q6ZNW5; -.
DR SignaLink; Q6ZNW5; -.
DR BioGRID-ORCS; 390637; 12 hits in 1077 CRISPR screens.
DR ChiTaRS; GDPGP1; human.
DR GenomeRNAi; 390637; -.
DR Pharos; Q6ZNW5; Tbio.
DR PRO; PR:Q6ZNW5; -.
DR Proteomes; UP000005640; Chromosome 15.
DR RNAct; Q6ZNW5; protein.
DR Bgee; ENSG00000183208; Expressed in mucosa of transverse colon and 103 other tissues.
DR ExpressionAtlas; Q6ZNW5; baseline and differential.
DR Genevisible; Q6ZNW5; HS.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0080048; F:GDP-D-glucose phosphorylase activity; IDA:UniProtKB.
DR GO; GO:0005085; F:guanyl-nucleotide exchange factor activity; IEA:UniProtKB-KW.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-KW.
DR GO; GO:0016779; F:nucleotidyltransferase activity; IEA:UniProtKB-KW.
DR GO; GO:0006006; P:glucose metabolic process; IMP:UniProtKB.
DR InterPro; IPR026506; GDPGP.
DR PANTHER; PTHR20884; PTHR20884; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Guanine-nucleotide releasing factor; Hydrolase;
KW Nucleotide-binding; Nucleotidyltransferase; Reference proteome;
KW Transferase.
FT CHAIN 1..385
FT /note="GDP-D-glucose phosphorylase 1"
FT /id="PRO_0000336750"
FT ACT_SITE 218
FT /note="Tele-GMP-histidine intermediate"
FT /evidence="ECO:0000250"
FT VARIANT 37
FT /note="M -> T (in dbSNP:rs7171194)"
FT /evidence="ECO:0000269|PubMed:14702039"
FT /id="VAR_043555"
FT VARIANT 264
FT /note="P -> T (in dbSNP:rs10152994)"
FT /evidence="ECO:0000269|PubMed:14702039"
FT /id="VAR_043556"
FT VARIANT 307
FT /note="T -> I (in dbSNP:rs10153004)"
FT /evidence="ECO:0000269|PubMed:14702039"
FT /id="VAR_043557"
FT CONFLICT 23
FT /note="R -> G (in Ref. 1; BAC85370)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 385 AA; 42362 MW; 921A656C721876EC CRC64;
MALPHDSNET SYLLPPNNED WGRQTIPDFV YGQKDLMAEG IQWPRNAPGI PDALPQSPFD
AALCSAWKQR VELGLFRYRL RELQTQILPG AVGFVAQLNV ERGVQRRPPQ TIKSVRQAFD
PVQFNFNKIR PGEVLFRLHR EPDLPGTLLQ EDILVVINVS PLEWGHVLLV PEPARQLPQR
LLPGALRAGI EAVLLSLHPG FRVGFNSLGG LASVNHLHLH GYYLAHRLPV EQAPSEPLDP
GGHLHLLQDL PAPGFLFYTR GPGPDLESLI SRVCRATDYL TDHEIAHNLF VTRGAPPGKT
SPSSALTGVR VILWARKSSF GIKDGEAFNV ALCELAGHLP VKTSQDFSSL TEAAAVALIQ
DCRLPPSQAE DVQAALVALM SQEEQ
