FPGT_MOUSE
ID FPGT_MOUSE Reviewed; 590 AA.
AC G5E8F4; Q2TB53; Q712G7; Q8C1A2;
DT 08-JUN-2016, integrated into UniProtKB/Swiss-Prot.
DT 14-DEC-2011, sequence version 1.
DT 03-AUG-2022, entry version 68.
DE RecName: Full=Fucose-1-phosphate guanylyltransferase {ECO:0000312|MGI:MGI:1922790};
DE EC=2.7.7.30 {ECO:0000269|PubMed:14686921};
DE AltName: Full=GDP-L-fucose diphosphorylase {ECO:0000250|UniProtKB:O14772};
DE AltName: Full=GDP-L-fucose pyrophosphorylase {ECO:0000303|PubMed:14686921};
GN Name=Fpgt {ECO:0000312|MGI:MGI:1922790};
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 {ECO:0000312|Proteomes:UP000000589};
RN [1] {ECO:0000312|EMBL:CAC81971.2}
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, AND TISSUE
RP SPECIFICITY.
RC TISSUE=Kidney {ECO:0000312|EMBL:CAC81971.2};
RX PubMed=14686921; DOI=10.1046/j.1432-1033.2003.03904.x;
RA Niittymaki J., Mattila P., Roos C., Huopaniemi L., Sjoblom S., Renkonen R.;
RT "Cloning and expression of murine enzymes involved in the salvage pathway
RT of GDP-L-fucose.";
RL Eur. J. Biochem. 271:78-86(2004).
RN [2] {ECO:0000312|EMBL:BAC26043.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J {ECO:0000312|EMBL:BAC26043.1};
RC TISSUE=Skin {ECO:0000312|EMBL:BAC26043.1};
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 [3] {ECO:0000312|Proteomes:UP000000589}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [4] {ECO:0000312|EMBL:EDL11881.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases.
RN [5] {ECO:0000312|EMBL:AAI10552.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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).
CC -!- FUNCTION: Catalyzes the formation of GDP-L-fucose from GTP and L-
CC fucose-1-phosphate (PubMed:14686921). Functions as a salvage pathway to
CC reutilize L-fucose arising from the turnover of glycoproteins and
CC glycolipids (Probable). {ECO:0000269|PubMed:14686921,
CC ECO:0000305|PubMed:14686921}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=beta-L-fucose 1-phosphate + GTP + H(+) = diphosphate + GDP-
CC beta-L-fucose; Xref=Rhea:RHEA:13549, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:33019, ChEBI:CHEBI:37565, ChEBI:CHEBI:57268,
CC ChEBI:CHEBI:57273; EC=2.7.7.30;
CC Evidence={ECO:0000269|PubMed:14686921};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:13550;
CC Evidence={ECO:0000250|UniProtKB:O14772};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305|PubMed:14686921}.
CC -!- TISSUE SPECIFICITY: Expressed at highest levels in brain, moderately in
CC testis, ovary and kidney, and weakly in liver, spleen, heart and lung.
CC {ECO:0000269|PubMed:14686921}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAC26043.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AJ276067; CAC81971.2; -; mRNA.
DR EMBL; AK028640; BAC26043.1; ALT_FRAME; mRNA.
DR EMBL; AC144762; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH466532; EDL11881.1; -; Genomic_DNA.
DR EMBL; BC110551; AAI10552.1; -; mRNA.
DR EMBL; BC110552; AAI10553.1; -; mRNA.
DR CCDS; CCDS38681.1; -.
DR RefSeq; NP_083606.2; NM_029330.2.
DR AlphaFoldDB; G5E8F4; -.
DR STRING; 10090.ENSMUSP00000068939; -.
DR PhosphoSitePlus; G5E8F4; -.
DR EPD; G5E8F4; -.
DR MaxQB; G5E8F4; -.
DR PaxDb; G5E8F4; -.
DR PRIDE; G5E8F4; -.
DR ProteomicsDB; 267405; -.
DR Antibodypedia; 53161; 163 antibodies from 21 providers.
DR Ensembl; ENSMUST00000066568; ENSMUSP00000068939; ENSMUSG00000053870.
DR GeneID; 75540; -.
DR KEGG; mmu:75540; -.
DR UCSC; uc008ruu.1; mouse.
DR CTD; 8790; -.
DR MGI; MGI:1922790; Fpgt.
DR VEuPathDB; HostDB:ENSMUSG00000053870; -.
DR eggNOG; ENOG502QRKZ; Eukaryota.
DR GeneTree; ENSGT00780000122095; -.
DR HOGENOM; CLU_508637_0_0_1; -.
DR InParanoid; G5E8F4; -.
DR OMA; CFLHKPS; -.
DR OrthoDB; 324025at2759; -.
DR PhylomeDB; G5E8F4; -.
DR TreeFam; TF328750; -.
DR Reactome; R-MMU-6787639; GDP-fucose biosynthesis.
DR BioGRID-ORCS; 75540; 1 hit in 71 CRISPR screens.
DR PRO; PR:G5E8F4; -.
DR Proteomes; UP000000589; Chromosome 3.
DR RNAct; G5E8F4; protein.
DR Bgee; ENSMUSG00000053870; Expressed in animal zygote and 224 other tissues.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0047341; F:fucose-1-phosphate guanylyltransferase activity; IDA:UniProtKB.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR GO; GO:0042354; P:L-fucose metabolic process; IDA:UniProtKB.
DR InterPro; IPR012887; Fucokinase.
DR InterPro; IPR012120; Fucose-1-phosphate_GuaTrfase.
DR InterPro; IPR011004; Trimer_LpxA-like_sf.
DR Pfam; PF07959; Fucokinase; 1.
DR PIRSF; PIRSF036640; FPGT; 1.
DR SUPFAM; SSF51161; SSF51161; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; GTP-binding; Nucleotide-binding; Nucleotidyltransferase;
KW Reference proteome; Transferase.
FT CHAIN 1..590
FT /note="Fucose-1-phosphate guanylyltransferase"
FT /id="PRO_0000436384"
FT CONFLICT 231..233
FT /note="FNA -> LIS (in Ref. 1; CAC81971)"
FT /evidence="ECO:0000305"
FT CONFLICT 238
FT /note="R -> G (in Ref. 1; CAC81971)"
FT /evidence="ECO:0000305"
FT CONFLICT 241
FT /note="G -> A (in Ref. 1; CAC81971)"
FT /evidence="ECO:0000305"
FT CONFLICT 270
FT /note="H -> R (in Ref. 1; CAC81971)"
FT /evidence="ECO:0000305"
FT CONFLICT 293
FT /note="Y -> N (in Ref. 1; CAC81971)"
FT /evidence="ECO:0000305"
FT CONFLICT 297
FT /note="L -> I (in Ref. 1; CAC81971)"
FT /evidence="ECO:0000305"
FT CONFLICT 517
FT /note="C -> R (in Ref. 5; AAI10552/AAI10553)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 590 AA; 65362 MW; CBAC6708227668C9 CRC64;
MASLREATLR KLRRFSELRG KPVAAGEFWD VVAITAADEK QELAYKQQLS EKLKKRELPL
GVQYHVFPDP AGTKIGNGGS TLCSLECLES LCGDKWNSLK VLLIHSGGYS QRLPNASALG
KIFTALPLGE PIYQMLELKL AMYVDFPSNM RPGVLVTCAD DIELYSVGDS EYIAFDQPGF
TALAHPSSLA VGTTHGVFVL HSDSSLQHGD LEYRQCYQFL HKPTIENMHR FNAVHRQRSF
GQQNLSGGDT DCLPLHTEYV YTDSLFYMDH KSAKKLLDFY KSEGPLNCEI DAYGDFLQAL
GPGATAEYTR NTSHVTKEES QLLDMRQKIF HLLKGTPLNV VVLNNSRFYH IGTLQEYLLH
FTSDSALKTE LGLQSIAFSV SPSVPERSSG TACVIHSIVD SGCCVAPGSV VEYSRLGPEV
SIGENCIISS SVIAKTVVPA YSFLCSLSVK INGHLKYSTM VFGMQDNLKN SVKTLEDIKA
LQFFGVCFLS CLDIWNLKAT EKLFSGNKMN LSLWTACIFP VCSSLSESAT ASLGMLSAVR
NHSPFNLSDF NLLSIQEMLV YKDVQDMLAY REHIFLEISS NKNQSDLEKS
