FCL_MOUSE
ID FCL_MOUSE Reviewed; 321 AA.
AC P23591;
DT 01-NOV-1991, integrated into UniProtKB/Swiss-Prot.
DT 27-MAY-2002, sequence version 3.
DT 03-AUG-2022, entry version 173.
DE RecName: Full=GDP-L-fucose synthase {ECO:0000305};
DE EC=1.1.1.271 {ECO:0000250|UniProtKB:Q13630};
DE AltName: Full=GDP-4-keto-6-deoxy-D-mannose-3,5-epimerase-4-reductase;
DE AltName: Full=Protein FX;
DE AltName: Full=Red cell NADP(H)-binding protein;
DE AltName: Full=Transplantation antigen P35B;
DE AltName: Full=Tum-P35B antigen;
GN Name=Gfus {ECO:0000312|MGI:MGI:98857};
GN Synonyms=P35b {ECO:0000303|PubMed:2108859},
GN Tsta3 {ECO:0000312|MGI:MGI:98857}, Tstap35b {ECO:0000312|MGI:MGI:98857};
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 [GENOMIC DNA / MRNA], AND VARIANT ASN-139.
RC STRAIN=DBA/2J; TISSUE=Mast cell;
RX PubMed=2108859; DOI=10.1002/j.1460-2075.1990.tb08208.x;
RA Szikora J.-P., van Pel A., Brichard V., Andre M., van Baren N., Henry P.,
RA de Plaen E., Boon T.;
RT "Structure of the gene of tum- transplantation antigen P35B: presence of a
RT point mutation in the antigenic allele.";
RL EMBO J. 9:1041-1050(1990).
RN [2]
RP SEQUENCE REVISION.
RA de Plaen E.;
RL Submitted (FEB-2001) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Testis;
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 [4]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, and Testis;
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).
CC -!- FUNCTION: Catalyzes the two-step NADP-dependent conversion of GDP-4-
CC dehydro-6-deoxy-D-mannose to GDP-fucose, involving an epimerase and a
CC reductase reaction. {ECO:0000250|UniProtKB:Q13630}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=GDP-beta-L-fucose + NADP(+) = GDP-4-dehydro-alpha-D-rhamnose +
CC H(+) + NADPH; Xref=Rhea:RHEA:18885, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:57273, ChEBI:CHEBI:57783, ChEBI:CHEBI:57964,
CC ChEBI:CHEBI:58349; EC=1.1.1.271;
CC Evidence={ECO:0000250|UniProtKB:Q13630};
CC -!- PATHWAY: Nucleotide-sugar biosynthesis; GDP-L-fucose biosynthesis via
CC de novo pathway; GDP-L-fucose from GDP-alpha-D-mannose: step 2/2.
CC {ECO:0000250|UniProtKB:Q13630}.
CC -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:Q13630}.
CC -!- MISCELLANEOUS: Mutagen treatment of P815 tumor cells produces tum-
CC variants that elicit a cytolytic T-lymphocyte response (CTL). The
CC antigenic allele differs from the normal allele by a single mutation in
CC position 139.
CC -!- SIMILARITY: Belongs to the NAD(P)-dependent epimerase/dehydratase
CC family. Fucose synthase subfamily. {ECO:0000305}.
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DR EMBL; X53620; CAB94217.1; ALT_SEQ; Genomic_DNA.
DR EMBL; X53621; CAB94217.1; JOINED; Genomic_DNA.
DR EMBL; X53622; CAB94217.1; JOINED; Genomic_DNA.
DR EMBL; X53623; CAB94217.1; JOINED; Genomic_DNA.
DR EMBL; X53624; CAB94217.1; JOINED; Genomic_DNA.
DR EMBL; X53625; CAB94217.1; JOINED; Genomic_DNA.
DR EMBL; X53626; CAB94217.1; JOINED; Genomic_DNA.
DR EMBL; X53627; CAB94217.1; JOINED; Genomic_DNA.
DR EMBL; X53628; CAB94217.1; JOINED; Genomic_DNA.
DR EMBL; M30127; AAA39673.2; -; mRNA.
DR EMBL; M30128; AAA39674.1; ALT_FRAME; Genomic_DNA.
DR EMBL; AK029632; BAC26539.1; -; mRNA.
DR CCDS; CCDS27555.1; -.
DR PIR; S12516; S12516.
DR RefSeq; NP_112478.1; NM_031201.1.
DR RefSeq; XP_006520814.1; XM_006520751.2.
DR AlphaFoldDB; P23591; -.
DR SMR; P23591; -.
DR BioGRID; 204357; 4.
DR STRING; 10090.ENSMUSP00000023231; -.
DR iPTMnet; P23591; -.
DR PhosphoSitePlus; P23591; -.
DR EPD; P23591; -.
DR jPOST; P23591; -.
DR PaxDb; P23591; -.
DR PeptideAtlas; P23591; -.
DR PRIDE; P23591; -.
DR ProteomicsDB; 270975; -.
DR Antibodypedia; 14656; 320 antibodies from 30 providers.
DR DNASU; 22122; -.
DR Ensembl; ENSMUST00000023231; ENSMUSP00000023231; ENSMUSG00000022570.
DR Ensembl; ENSMUST00000229641; ENSMUSP00000155139; ENSMUSG00000022570.
DR GeneID; 22122; -.
DR KEGG; mmu:22122; -.
DR UCSC; uc007whs.1; mouse.
DR CTD; 7264; -.
DR MGI; MGI:98857; Gfus.
DR VEuPathDB; HostDB:ENSMUSG00000022570; -.
DR eggNOG; KOG1431; Eukaryota.
DR GeneTree; ENSGT00390000004681; -.
DR HOGENOM; CLU_007383_18_2_1; -.
DR InParanoid; P23591; -.
DR OMA; IHCAGRV; -.
DR OrthoDB; 922791at2759; -.
DR PhylomeDB; P23591; -.
DR TreeFam; TF314936; -.
DR Reactome; R-MMU-6787639; GDP-fucose biosynthesis.
DR UniPathway; UPA00128; UER00191.
DR BioGRID-ORCS; 22122; 5 hits in 74 CRISPR screens.
DR PRO; PR:P23591; -.
DR Proteomes; UP000000589; Chromosome 15.
DR RNAct; P23591; protein.
DR Bgee; ENSMUSG00000022570; Expressed in paneth cell and 250 other tissues.
DR ExpressionAtlas; P23591; baseline and differential.
DR Genevisible; P23591; MM.
DR GO; GO:0050577; F:GDP-L-fucose synthase activity; ISO:MGI.
DR GO; GO:0047918; F:GDP-mannose 3,5-epimerase activity; ISO:MGI.
DR GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR GO; GO:0042351; P:'de novo' GDP-L-fucose biosynthetic process; ISO:MGI.
DR GO; GO:0019673; P:GDP-mannose metabolic process; ISO:MGI.
DR GO; GO:0010595; P:positive regulation of endothelial cell migration; ISS:UniProtKB.
DR GO; GO:1904906; P:positive regulation of endothelial cell-matrix adhesion via fibronectin; ISS:UniProtKB.
DR GO; GO:0001913; P:T cell mediated cytotoxicity; IMP:MGI.
DR CDD; cd05239; GDP_FS_SDR_e; 1.
DR HAMAP; MF_00956; GDP_fucose_synth; 1.
DR InterPro; IPR001509; Epimerase_deHydtase.
DR InterPro; IPR028614; GDP_fucose/colitose_synth.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR Pfam; PF01370; Epimerase; 1.
DR SUPFAM; SSF51735; SSF51735; 1.
PE 1: Evidence at protein level;
KW Isomerase; Multifunctional enzyme; NADP; Oxidoreductase;
KW Reference proteome; Tumor antigen.
FT CHAIN 1..321
FT /note="GDP-L-fucose synthase"
FT /id="PRO_0000174351"
FT ACT_SITE 143
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000250"
FT BINDING 14..20
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:Q13630"
FT BINDING 147
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:Q13630"
FT BINDING 170..173
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:Q13630"
FT BINDING 186
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:Q13630"
FT BINDING 194
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q13630"
FT BINDING 208
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q13630"
FT BINDING 215
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q13630"
FT BINDING 277
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q13630"
FT SITE 114
FT /note="Important for catalytic activity"
FT /evidence="ECO:0000250"
FT SITE 116
FT /note="Important for catalytic activity"
FT /evidence="ECO:0000250"
FT SITE 147
FT /note="Lowers pKa of active site Tyr"
FT /evidence="ECO:0000250"
FT VARIANT 139
FT /note="S -> N (in allele TUM-)"
FT /evidence="ECO:0000269|PubMed:2108859"
SQ SEQUENCE 321 AA; 35878 MW; 358D86D68F173531 CRC64;
MGEPHGSMRI LVTGGSGLVG RAIQKVVADG AGLPGEEWVF VSSKDADLTD AAQTQALFQK
VQPTHVIHLA AMVGGLFRNI KYNLDFWRKN VHINDNVLHS AFEVGARKVV SCLSTCIFPD
KTTYPIDETM IHNGPPHSSN FGYSYAKRMI DVQNRAYFQQ HGCTFTAVIP TNVFGPYDNF
NIEDGHVLPG LIHKVHLAKS SDSALTVWGT GKPRRQFIYS LDLARLFIWV LREYSEVEPI
ILSVGEEDEV SIKEAAEAVV EAMDFNGEVT FDSTKSDGQY KKTASNGKLR SYLPDFRFTP
FKQAVKETCT WFTDNYEQAR K
