FPGT_HUMAN
ID FPGT_HUMAN Reviewed; 607 AA.
AC O14772; A0A0A0MRP2; A6NMH3; B4DRX2; B4E2Y7; E9PNQ2; Q8N5J7;
DT 10-JAN-2003, integrated into UniProtKB/Swiss-Prot.
DT 25-APR-2018, sequence version 3.
DT 03-AUG-2022, entry version 157.
DE RecName: Full=Fucose-1-phosphate guanylyltransferase {ECO:0000305};
DE EC=2.7.7.30 {ECO:0000269|PubMed:9804772};
DE AltName: Full=GDP-L-fucose diphosphorylase;
DE AltName: Full=GDP-L-fucose pyrophosphorylase;
GN Name=FPGT {ECO:0000312|HGNC:HGNC:3825}; Synonyms=GFPP;
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 [GENOMIC DNA / MRNA] (ISOFORM 2), FUNCTION, CATALYTIC
RP ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=9804772; DOI=10.1074/jbc.273.46.30165;
RA Pastuszak I., Ketchum C., Hermanson G., Sjoberg E.J., Drake R.,
RA Elbein A.D.;
RT "GDP-L-fucose pyrophosphorylase: purification, cDNA cloning, and properties
RT of the enzyme.";
RL J. Biol. Chem. 273:30165-30174(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 5 AND 6).
RC TISSUE=Tongue, and Uterus;
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16710414; DOI=10.1038/nature04727;
RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A.,
RA Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C.,
RA Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.,
RA Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C.,
RA Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W.,
RA Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J.,
RA Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J.,
RA Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y.,
RA Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J.,
RA Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S.,
RA Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K.,
RA Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R.,
RA Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M.,
RA Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S.,
RA Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J.,
RA Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W.,
RA McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S.,
RA Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M.,
RA White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H.,
RA Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E.,
RA Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G.,
RA Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.;
RT "The DNA sequence and biological annotation of human chromosome 1.";
RL Nature 441:315-321(2006).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 7-607 (ISOFORM 2).
RC TISSUE=Colon, and Kidney;
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:9804772). Functions as a salvage pathway to
CC reutilize L-fucose arising from the turnover of glycoproteins and
CC glycolipids (PubMed:9804772). {ECO:0000269|PubMed:9804772}.
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:9804772};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:13550;
CC Evidence={ECO:0000305|PubMed:9804772};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC pH dependence:
CC Optimum pH is 6.8 to 7.8. {ECO:0000305|PubMed:9804772};
CC -!- SUBCELLULAR LOCATION: Cytoplasm.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=6;
CC Name=2;
CC IsoId=O14772-1; Sequence=Displayed;
CC Name=1;
CC IsoId=Q59H18-1; Sequence=External;
CC Name=3;
CC IsoId=Q59H18-3; Sequence=External;
CC Name=4;
CC IsoId=Q59H18-4; Sequence=External;
CC Name=5;
CC IsoId=O14772-2; Sequence=VSP_059541, VSP_059543;
CC Name=6;
CC IsoId=O14772-3; Sequence=VSP_059541, VSP_059542;
CC -!- TISSUE SPECIFICITY: Expressed in many tissues.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAC73005.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=AAC82511.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=AAH32308.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAG65299.1; Type=Erroneous translation; Note=Wrong choice of CDS.; Evidence={ECO:0000305};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AF017445; AAC73005.1; ALT_INIT; mRNA.
DR EMBL; AF017446; AAC82511.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AK299468; BAG61434.1; -; mRNA.
DR EMBL; AK304490; BAG65299.1; ALT_SEQ; mRNA.
DR EMBL; AC098692; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC032308; AAH32308.1; ALT_INIT; mRNA.
DR RefSeq; NP_001186257.2; NM_001199328.2. [O14772-2]
DR RefSeq; NP_001186258.2; NM_001199329.2. [O14772-3]
DR RefSeq; NP_003829.3; NM_003838.4.
DR AlphaFoldDB; O14772; -.
DR BioGRID; 114318; 4.
DR STRING; 9606.ENSP00000359935; -.
DR iPTMnet; O14772; -.
DR PhosphoSitePlus; O14772; -.
DR BioMuta; FPGT; -.
DR EPD; O14772; -.
DR jPOST; O14772; -.
DR MassIVE; O14772; -.
DR MaxQB; O14772; -.
DR PaxDb; O14772; -.
DR PeptideAtlas; O14772; -.
DR PRIDE; O14772; -.
DR ProteomicsDB; 1539; -.
DR ProteomicsDB; 22483; -.
DR ProteomicsDB; 48223; -. [O14772-1]
DR Antibodypedia; 53161; 163 antibodies from 21 providers.
DR DNASU; 8790; -.
DR Ensembl; ENST00000370894.9; ENSP00000359931.4; ENSG00000254685.8. [O14772-3]
DR Ensembl; ENST00000534056.5; ENSP00000432819.1; ENSG00000254685.8. [O14772-2]
DR GeneID; 8790; -.
DR KEGG; hsa:8790; -.
DR UCSC; uc001dgb.4; human.
DR UCSC; uc057hpq.1; human. [O14772-1]
DR CTD; 8790; -.
DR DisGeNET; 8790; -.
DR GeneCards; FPGT; -.
DR HGNC; HGNC:3825; FPGT.
DR HPA; ENSG00000254685; Low tissue specificity.
DR MIM; 603609; gene.
DR neXtProt; NX_O14772; -.
DR OpenTargets; ENSG00000254685; -.
DR PharmGKB; PA28243; -.
DR VEuPathDB; HostDB:ENSG00000254685; -.
DR eggNOG; ENOG502QRKZ; Eukaryota.
DR GeneTree; ENSGT00780000122095; -.
DR HOGENOM; CLU_1577964_0_0_1; -.
DR InParanoid; O14772; -.
DR OMA; CFLHKPS; -.
DR PhylomeDB; O14772; -.
DR TreeFam; TF328750; -.
DR BRENDA; 2.7.7.30; 2681.
DR PathwayCommons; O14772; -.
DR Reactome; R-HSA-6787639; GDP-fucose biosynthesis.
DR BioGRID-ORCS; 8790; 5 hits in 906 CRISPR screens.
DR GeneWiki; FPGT; -.
DR GenomeRNAi; 8790; -.
DR Pharos; O14772; Tbio.
DR Proteomes; UP000005640; Chromosome 1.
DR RNAct; O14772; protein.
DR Bgee; ENSG00000254685; Expressed in monocyte and 165 other tissues.
DR ExpressionAtlas; O14772; baseline and differential.
DR Genevisible; O14772; HS.
DR GO; GO:0005737; C:cytoplasm; TAS:ProtInc.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0003824; F:catalytic activity; TAS:ProtInc.
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:0006004; P:fucose metabolic process; TAS:ProtInc.
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 Alternative splicing; Cytoplasm; GTP-binding; Nucleotide-binding;
KW Nucleotidyltransferase; Reference proteome; Transferase.
FT CHAIN 1..607
FT /note="Fucose-1-phosphate guanylyltransferase"
FT /id="PRO_0000087327"
FT REGION 1..21
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 1..13
FT /note="Missing (in isoform 5 and isoform 6)"
FT /evidence="ECO:0000305"
FT /id="VSP_059541"
FT VAR_SEQ 128..607
FT /note="GGYSQRLPNASALGKIFTALPLGNPIYQMLELKLAMYIDFPLNMNPGILVTC
FT ADDIELYSIGEFEFIRFDKPGFTALAHPSSLTIGTTHGVFVLDPFDDLKHRDLEYRSCH
FT RFLHKPSIEKMYQFNAVCRPGNFCQQDFAGGDIADLKLDSDYVYTDSLFYMDHKSAKML
FT LAFYEKIGTLSCEIDAYGDFLQALGPGATVEYTRNTSNVIKEESELVEMRQRIFHLLKG
FT TSLNVVVLNNSKFYHIGTTEEYLFYFTSDNSLKSELGLQSITFSIFPDIPECSGKTSCI
FT IQSILDSRCSVAPGSVVEYSRLGPDVSVGENCIISGSYILTKAALPAHSFVCSLSLKMN
FT RCLKYATMAFGVQDNLKKSVKTLSDIKLLQFFGVCFLSCLDVWNLKVTEELFSGNKTCL
FT SLWTARIFPVCSSLSDSVITSLKMLNAVKNKSAFSLNSYKLLSIEEMLIYKDVEDMITY
FT REQIFLEISLKSSLM -> VSFQIYQNALAKHPVSFKAYWIQDVLWHLAQLWSIPDWGL
FT MFQLGKTALLVVLTS (in isoform 6)"
FT /evidence="ECO:0000305"
FT /id="VSP_059542"
FT VAR_SEQ 150..403
FT /note="Missing (in isoform 5)"
FT /evidence="ECO:0000305"
FT /id="VSP_059543"
FT VARIANT 461
FT /note="P -> L (in dbSNP:rs55882158)"
FT /id="VAR_061650"
FT CONFLICT 57
FT /note="A -> T (in Ref. 2; BAG61434)"
FT /evidence="ECO:0000305"
FT CONFLICT 335
FT /note="N -> H (in Ref. 1; AAC73005)"
FT /evidence="ECO:0000305"
FT CONFLICT 562
FT /note="K -> R (in Ref. 2; BAG61434)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 607 AA; 68010 MW; 5175BB73A69255F1 CRC64;
MRAVRRGLRE GGAMAAARDP PEVSLREATQ RKLRRFSELR GKLVARGEFW DIVAITAADE
KQELAYNQQL SEKLKRKELP LGVQYHVFVD PAGAKIGNGG STLCALQCLE KLYGDKWNSF
TILLIHSGGY SQRLPNASAL GKIFTALPLG NPIYQMLELK LAMYIDFPLN MNPGILVTCA
DDIELYSIGE FEFIRFDKPG FTALAHPSSL TIGTTHGVFV LDPFDDLKHR DLEYRSCHRF
LHKPSIEKMY QFNAVCRPGN FCQQDFAGGD IADLKLDSDY VYTDSLFYMD HKSAKMLLAF
YEKIGTLSCE IDAYGDFLQA LGPGATVEYT RNTSNVIKEE SELVEMRQRI FHLLKGTSLN
VVVLNNSKFY HIGTTEEYLF YFTSDNSLKS ELGLQSITFS IFPDIPECSG KTSCIIQSIL
DSRCSVAPGS VVEYSRLGPD VSVGENCIIS GSYILTKAAL PAHSFVCSLS LKMNRCLKYA
TMAFGVQDNL KKSVKTLSDI KLLQFFGVCF LSCLDVWNLK VTEELFSGNK TCLSLWTARI
FPVCSSLSDS VITSLKMLNA VKNKSAFSLN SYKLLSIEEM LIYKDVEDMI TYREQIFLEI
SLKSSLM
