ID   GDPP1_MOUSE             Reviewed;         386 AA.
AC   Q3TLS3; Q3UP89; Q8C3L2; Q8C3Y3; Q8CI49;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   20-MAY-2008, sequence version 2.
DT   24-JAN-2024, entry version 102.
DE   RecName: Full=GDP-D-glucose phosphorylase 1;
DE            EC=2.7.7.78;
GN   Name=Gdpgp1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Heart, Kidney, Mammary gland, and Spleen;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA   Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA   Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA   Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA   Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA   Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA   Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA   Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA   Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA   Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA   Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA   Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA   Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA   Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA   Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA   Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA   Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA   Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA   Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA   Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA   van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA   Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA   Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA   Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA   Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA   Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA   Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA   Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA   Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=FVB/N; TISSUE=Mammary tumor;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Spleen;
RX   PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA   Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA   Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT   "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL   Cell 143:1174-1189(2010).
RN   [4]
RP   TISSUE SPECIFICITY.
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. {ECO:0000250}.
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   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC   -!- TISSUE SPECIFICITY: Highly expressed in the nervous and male
CC       reproductive systems compared to kidney, liver and heart.
CC       {ECO:0000269|PubMed:21507950}.
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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAC39476.1; Type=Frameshift; Evidence={ECO:0000305};
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DR   EMBL; AK084531; BAC39213.1; -; mRNA.
DR   EMBL; AK085577; BAC39476.1; ALT_FRAME; mRNA.
DR   EMBL; AK143704; BAE25508.1; -; mRNA.
DR   EMBL; AK166345; BAE38719.1; -; mRNA.
DR   EMBL; BC037479; AAH37479.1; -; mRNA.
DR   CCDS; CCDS39995.1; -.
DR   RefSeq; NP_848867.2; NM_178752.3.
DR   AlphaFoldDB; Q3TLS3; -.
DR   BioGRID; 234734; 1.
DR   STRING; 10090.ENSMUSP00000061808; -.
DR   PhosphoSitePlus; Q3TLS3; -.
DR   EPD; Q3TLS3; -.
DR   MaxQB; Q3TLS3; -.
DR   PaxDb; 10090-ENSMUSP00000061808; -.
DR   PeptideAtlas; Q3TLS3; -.
DR   ProteomicsDB; 266789; -.
DR   Pumba; Q3TLS3; -.
DR   Ensembl; ENSMUST00000062915.9; ENSMUSP00000061808.8; ENSMUSG00000050973.12.
DR   GeneID; 269952; -.
DR   KEGG; mmu:269952; -.
DR   UCSC; uc009hzu.1; mouse.
DR   AGR; MGI:2443429; -.
DR   CTD; 390637; -.
DR   MGI; MGI:2443429; Gdpgp1.
DR   VEuPathDB; HostDB:ENSMUSG00000050973; -.
DR   eggNOG; KOG2720; Eukaryota.
DR   GeneTree; ENSGT00390000016718; -.
DR   HOGENOM; CLU_041964_2_1_1; -.
DR   InParanoid; Q3TLS3; -.
DR   OMA; GIQWPRT; -.
DR   OrthoDB; 463544at2759; -.
DR   PhylomeDB; Q3TLS3; -.
DR   TreeFam; TF313615; -.
DR   BRENDA; 2.7.7.78; 3474.
DR   BioGRID-ORCS; 269952; 0 hits in 77 CRISPR screens.
DR   ChiTaRS; Gdpgp1; mouse.
DR   PRO; PR:Q3TLS3; -.
DR   Proteomes; UP000000589; Chromosome 7.
DR   RNAct; Q3TLS3; Protein.
DR   Bgee; ENSMUSG00000050973; Expressed in primary oocyte and 132 other cell types or tissues.
DR   GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR   GO; GO:0080048; F:GDP-D-glucose phosphorylase activity; ISS: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; ISS: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; Q3TLS3; MM.
PE   1: Evidence at protein level;
KW   Cytoplasm; Guanine-nucleotide releasing factor; Hydrolase;
KW   Nucleotide-binding; Nucleotidyltransferase; Reference proteome;
KW   Transferase.
FT   CHAIN           1..386
FT                   /note="GDP-D-glucose phosphorylase 1"
FT                   /id="PRO_0000336752"
FT   ACT_SITE        219
FT                   /note="Tele-GMP-histidine intermediate"
FT                   /evidence="ECO:0000250"
FT   CONFLICT        7
FT                   /note="L -> S (in Ref. 1; BAE38719 and 2; AAH37479)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        8
FT                   /note="Q -> L (in Ref. 2; AAH37479)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        44
FT                   /note="P -> S (in Ref. 1; BAE25508)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        81
FT                   /note="E -> K (in Ref. 1; BAC39476)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        95
FT                   /note="V -> L (in Ref. 1; BAC39476)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        101
FT                   /note="E -> D (in Ref. 2; AAH37479)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   386 AA;  42515 MW;  B69E1EECF9D719A0 CRC64;
     MAVPHHLQET SYLLPPDPED WEKQGIPDFV YGQEDLVGKE VQWPRDSPSA VDTVPLSRFD
     SALRSAWRQR LELGLFRYRL EDLQTQILPG SVGFVAQLNI ERGIQRRRPQ NIRSVRQEFD
     PEQFNFNKIR PGEVLFRMQR EPKGPATPKQ EDDVLVVINV SPLEWGHVLL VPAPAQGLPQ
     RLLPGVLRVG LEAVLLSLHP GFRVGFNSLG GLASVNHLHL HCYYLAHPLP VEGAPSTPLD
     PKGCIHLLQA LPAPGFLFYT SGPGPDLEVL ISRVCRATDY LSDREIAHNL FVTRGAPPGP
     TSSTSDLSGI RVILWARKSS FGIKESGAFN VALCELAGHL PVKTSQDFSS LTEAAAVALI
     QDCLLPETQA GEVRAALVAL MAQEEL
//