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   24-JAN-2024, entry version 116.
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
CC         GDP-L-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; 16.
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; 9606-ENSP00000452793; -.
DR   PeptideAtlas; Q6ZNW5; -.
DR   ProteomicsDB; 68049; -.
DR   Pumba; Q6ZNW5; -.
DR   Antibodypedia; 28769; 62 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   AGR; HGNC:34360; -.
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; 463544at2759; -.
DR   PhylomeDB; Q6ZNW5; -.
DR   TreeFam; TF313615; -.
DR   BioCyc; MetaCyc:G66-31756-MONOMER; -.
DR   BRENDA; 2.7.7.78; 2681.
DR   PathwayCommons; Q6ZNW5; -.
DR   SignaLink; Q6ZNW5; -.
DR   BioGRID-ORCS; 390637; 14 hits in 1154 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 male germ line stem cell (sensu Vertebrata) in testis and 104 other cell types or tissues.
DR   ExpressionAtlas; Q6ZNW5; baseline and differential.
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:0006006; P:glucose metabolic process; IMP:UniProtKB.
DR   InterPro; IPR026506; GDPGP.
DR   PANTHER; PTHR20884; GDP-D-GLUCOSE PHOSPHORYLASE 1; 1.
DR   PANTHER; PTHR20884:SF8; GDP-D-GLUCOSE PHOSPHORYLASE 1; 1.
DR   Genevisible; Q6ZNW5; HS.
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
//