FUCM_HUMAN
ID FUCM_HUMAN Reviewed; 154 AA.
AC A2VDF0; A1L300; Q5VWY2; Q5VWY3; Q6ZPD2;
DT 15-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 15-MAY-2007, sequence version 2.
DT 03-AUG-2022, entry version 116.
DE RecName: Full=Fucose mutarotase;
DE EC=5.1.3.29 {ECO:0000269|PubMed:17602138};
GN Name=FUOM; Synonyms=C10orf125;
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] (ISOFORM 2).
RC TISSUE=Macrophage;
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=15164054; DOI=10.1038/nature02462;
RA Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L.,
RA Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K.,
RA Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L.,
RA Taylor A., Battles J., Bird C.P., Ainscough R., Almeida J.P.,
RA Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J.,
RA Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J., Brown J.Y.,
RA Burford D.C., Burrill W., Burton J., Cahill P., Camire D., Carter N.P.,
RA Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S., Corby N.,
RA Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L., Frankish A.,
RA Frankland J.A., Garner P., Garnett J., Gribble S., Griffiths C.,
RA Grocock R., Gustafson E., Hammond S., Harley J.L., Hart E., Heath P.D.,
RA Ho T.P., Hopkins B., Horne J., Howden P.J., Huckle E., Hynds C.,
RA Johnson C., Johnson D., Kana A., Kay M., Kimberley A.M., Kershaw J.K.,
RA Kokkinaki M., Laird G.K., Lawlor S., Lee H.M., Leongamornlert D.A.,
RA Laird G., Lloyd C., Lloyd D.M., Loveland J., Lovell J., McLaren S.,
RA McLay K.E., McMurray A., Mashreghi-Mohammadi M., Matthews L., Milne S.,
RA Nickerson T., Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V.,
RA Peck A.I., Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A.,
RA Ross M.T., Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M.,
RA Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W., Tracey A.,
RA Tromans A., Tsolas J., Wall M., Walsh J., Wang H., Weinstock K., West A.P.,
RA Willey D.L., Whitehead S.L., Wilming L., Wray P.W., Young L., Chen Y.,
RA Lovering R.C., Moschonas N.K., Siebert R., Fechtel K., Bentley D.,
RA Durbin R.M., Hubbard T., Doucette-Stamm L., Beck S., Smith D.R., Rogers J.;
RT "The DNA sequence and comparative analysis of human chromosome 10.";
RL Nature 429:375-381(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), AND NUCLEOTIDE SEQUENCE
RP [LARGE SCALE MRNA] OF 1-140 (ISOFORM 1).
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 95-154 (ISOFORM 1).
RG The Cancer Genome Anatomy Project (CGAP) at the National Cancer Institute;
RL Submitted (FEB-1998) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=17602138; DOI=10.1093/glycob/cwm066;
RA Park D., Ryu K.S., Choi D., Kwak J., Park C.;
RT "Characterization and role of fucose mutarotase in mammalian cells.";
RL Glycobiology 17:955-962(2007).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
CC -!- FUNCTION: Involved in the interconversion between alpha- and beta-L-
CC fucoses. L-Fucose (6-deoxy-L-galactose) exists as alpha-L-fucose
CC (29.5%) and beta-L-fucose (70.5%), the beta-form is metabolized through
CC the salvage pathway. GDP-L-fucose formed either by the de novo or
CC salvage pathways is transported into the endoplasmic reticulum, where
CC it serves as a substrate for N- and O-glycosylations by
CC fucosyltransferases. Fucosylated structures expressed on cell surfaces
CC or secreted in biological fluids are believed to play a critical role
CC in cell-cell adhesion and recognition processes.
CC {ECO:0000269|PubMed:17602138}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=alpha-L-fucose = beta-L-fucose; Xref=Rhea:RHEA:25580,
CC ChEBI:CHEBI:42548, ChEBI:CHEBI:42589; EC=5.1.3.29;
CC Evidence={ECO:0000269|PubMed:17602138};
CC -!- PATHWAY: Carbohydrate metabolism; L-fucose metabolism.
CC {ECO:0000269|PubMed:17602138}.
CC -!- SUBUNIT: Mainly homodimer, but exists also as homotetramer,
CC homooctamer, and homodecamer. The homodimeric form seems catalytically
CC inactive (By similarity). {ECO:0000250|UniProtKB:Q8R2K1}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=A2VDF0-1; Sequence=Displayed;
CC Name=2;
CC IsoId=A2VDF0-2; Sequence=VSP_025080, VSP_025081;
CC -!- SIMILARITY: Belongs to the RbsD / FucU family. {ECO:0000305}.
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DR EMBL; AK129527; BAC85178.1; -; mRNA.
DR EMBL; AL360181; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC129818; AAI29819.1; -; mRNA.
DR EMBL; BC129819; AAI29820.1; -; mRNA.
DR EMBL; AI333356; -; NOT_ANNOTATED_CDS; mRNA.
DR CCDS; CCDS44499.1; -. [A2VDF0-1]
DR CCDS; CCDS7680.1; -. [A2VDF0-2]
DR RefSeq; NP_001091953.1; NM_001098483.2. [A2VDF0-1]
DR RefSeq; NP_001288756.1; NM_001301827.1.
DR RefSeq; NP_001288757.1; NM_001301828.1.
DR RefSeq; NP_940874.2; NM_198472.2. [A2VDF0-2]
DR AlphaFoldDB; A2VDF0; -.
DR SMR; A2VDF0; -.
DR BioGRID; 129427; 19.
DR IntAct; A2VDF0; 15.
DR STRING; 9606.ENSP00000278025; -.
DR iPTMnet; A2VDF0; -.
DR PhosphoSitePlus; A2VDF0; -.
DR BioMuta; FUOM; -.
DR EPD; A2VDF0; -.
DR jPOST; A2VDF0; -.
DR MassIVE; A2VDF0; -.
DR MaxQB; A2VDF0; -.
DR PaxDb; A2VDF0; -.
DR PeptideAtlas; A2VDF0; -.
DR PRIDE; A2VDF0; -.
DR ProteomicsDB; 537; -. [A2VDF0-1]
DR ProteomicsDB; 538; -. [A2VDF0-2]
DR Antibodypedia; 48803; 85 antibodies from 16 providers.
DR DNASU; 282969; -.
DR Ensembl; ENST00000278025.9; ENSP00000278025.5; ENSG00000148803.12. [A2VDF0-1]
DR Ensembl; ENST00000368552.7; ENSP00000357540.5; ENSG00000148803.12. [A2VDF0-2]
DR GeneID; 282969; -.
DR KEGG; hsa:282969; -.
DR MANE-Select; ENST00000278025.9; ENSP00000278025.5; NM_001098483.3; NP_001091953.1.
DR UCSC; uc001lmt.3; human. [A2VDF0-1]
DR CTD; 282969; -.
DR GeneCards; FUOM; -.
DR HGNC; HGNC:24733; FUOM.
DR HPA; ENSG00000148803; Tissue enriched (liver).
DR MIM; 617725; gene.
DR neXtProt; NX_A2VDF0; -.
DR OpenTargets; ENSG00000148803; -.
DR PharmGKB; PA134972390; -.
DR VEuPathDB; HostDB:ENSG00000148803; -.
DR eggNOG; ENOG502RZR7; Eukaryota.
DR GeneTree; ENSGT00390000001197; -.
DR InParanoid; A2VDF0; -.
DR OMA; MGHGDDI; -.
DR OrthoDB; 1457717at2759; -.
DR PhylomeDB; A2VDF0; -.
DR TreeFam; TF324689; -.
DR BRENDA; 5.1.3.29; 2681.
DR PathwayCommons; A2VDF0; -.
DR Reactome; R-HSA-6787639; GDP-fucose biosynthesis.
DR SignaLink; A2VDF0; -.
DR UniPathway; UPA00956; -.
DR BioGRID-ORCS; 282969; 8 hits in 1046 CRISPR screens.
DR ChiTaRS; FUOM; human.
DR GenomeRNAi; 282969; -.
DR Pharos; A2VDF0; Tbio.
DR PRO; PR:A2VDF0; -.
DR Proteomes; UP000005640; Chromosome 10.
DR RNAct; A2VDF0; protein.
DR Bgee; ENSG00000148803; Expressed in right lobe of liver and 119 other tissues.
DR ExpressionAtlas; A2VDF0; baseline and differential.
DR Genevisible; A2VDF0; HS.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0042806; F:fucose binding; ISS:UniProtKB.
DR GO; GO:0036373; F:L-fucose mutarotase activity; ISS:UniProtKB.
DR GO; GO:0016857; F:racemase and epimerase activity, acting on carbohydrates and derivatives; ISS:UniProtKB.
DR GO; GO:0006004; P:fucose metabolic process; ISS:UniProtKB.
DR GO; GO:0036065; P:fucosylation; IBA:GO_Central.
DR Gene3D; 3.40.1650.10; -; 1.
DR InterPro; IPR023750; RbsD-like_sf.
DR InterPro; IPR007721; RbsD_FucU.
DR Pfam; PF05025; RbsD_FucU; 1.
DR SUPFAM; SSF102546; SSF102546; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Isomerase; Reference proteome.
FT CHAIN 1..154
FT /note="Fucose mutarotase"
FT /id="PRO_0000286553"
FT ACT_SITE 24
FT /note="Proton donor"
FT /evidence="ECO:0000250|UniProtKB:Q8R2K1"
FT ACT_SITE 69
FT /evidence="ECO:0000250|UniProtKB:Q8R2K1"
FT ACT_SITE 120
FT /evidence="ECO:0000250|UniProtKB:Q8R2K1"
FT BINDING 32
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q8R2K1"
FT BINDING 79
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q8R2K1"
FT BINDING 120
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q8R2K1"
FT BINDING 138
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q8R2K1"
FT BINDING 140
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q8R2K1"
FT VAR_SEQ 134
FT /note="E -> C (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:15489334"
FT /id="VSP_025080"
FT VAR_SEQ 135..154
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:15489334"
FT /id="VSP_025081"
FT CONFLICT 81
FT /note="L -> P (in Ref. 1; BAC85178)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 154 AA; 16765 MW; 96F76613566F4A6E CRC64;
MVALKGVPAL LSPELLYALA RMGHGDEIVL ADLNFPASSI CQCGPMEIRA DGLGIPQLLE
AVLKLLPLDT YVESPAAVME LVPSDKERGL QTPVWTEYES ILRRAGCVRA LAKIERFEFY
ERAKKAFAVV ATGETALYGN LILRKGVLAL NPLL
