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   02-SEP-2026, entry version 133.
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 also exists 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_001098483.3. [A2VDF0-1]
DR   RefSeq; NP_001288756.1; NM_001301827.2.
DR   RefSeq; NP_001288757.1; NM_001301828.2.
DR   RefSeq; NP_940874.2; NM_198472.3. [A2VDF0-2]
DR   AlphaFoldDB; A2VDF0; -.
DR   SMR; A2VDF0; -.
DR   BioGRID; 129427; 20.
DR   FunCoup; A2VDF0; 424.
DR   IntAct; A2VDF0; 17.
DR   STRING; 9606.ENSP00000278025; -.
DR   iPTMnet; A2VDF0; -.
DR   PhosphoSitePlus; A2VDF0; -.
DR   BioMuta; FUOM; -.
DR   jPOST; A2VDF0; -.
DR   MassIVE; A2VDF0; -.
DR   PaxDb; 9606-ENSP00000278025; -.
DR   PeptideAtlas; A2VDF0; -.
DR   ProteomicsDB; 537; -. [A2VDF0-1]
DR   ProteomicsDB; 538; -. [A2VDF0-2]
DR   Pumba; A2VDF0; -.
DR   Antibodypedia; 48803; 76 antibodies from 16 providers.
DR   DNASU; 282969; -.
DR   Ensembl; ENST00000278025.9; ENSP00000278025.5; ENSG00000148803.14. [A2VDF0-1]
DR   Ensembl; ENST00000368552.8; ENSP00000357540.5; ENSG00000148803.14. [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   AGR; HGNC:24733; -.
DR   ClinPGx; PA134972390; -.
DR   CTD; 282969; -.
DR   GeneCards; FUOM; -.
DR   HGNC; HGNC:24733; FUOM.
DR   HPA; ENSG00000148803; Tissue enriched (liver).
DR   MIM; 617725; gene.
DR   OpenTargets; ENSG00000148803; -.
DR   VEuPathDB; HostDB:ENSG00000148803; -.
DR   eggNOG; ENOG502RZR7; Eukaryota.
DR   GeneTree; ENSGT00390000001197; -.
DR   InParanoid; A2VDF0; -.
DR   OMA; PVWDTYT; -.
DR   OrthoDB; 10011710at2759; -.
DR   PAN-GO; A2VDF0; 3 GO annotations based on evolutionary models.
DR   PhylomeDB; A2VDF0; -.
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   Agora; ENSG00000148803; -.
DR   BioGRID-ORCS; 282969; 9 hits in 1124 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 120 other cell types or tissues.
DR   ExpressionAtlas; A2VDF0; baseline and differential.
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; EXP: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:0042352; P:GDP-L-fucose salvage; IEA:Ensembl.
DR   FunFam; 3.40.1650.10:FF:000005; Fucose mutarotase; 1.
DR   Gene3D; 3.40.1650.10; RbsD-like domain; 1.
DR   InterPro; IPR023750; RbsD-like_sf.
DR   InterPro; IPR050443; RbsD/FucU_mutarotase.
DR   InterPro; IPR007721; RbsD_FucU.
DR   PANTHER; PTHR31690; FUCOSE MUTAROTASE; 1.
DR   PANTHER; PTHR31690:SF4; FUCOSE MUTAROTASE; 1.
DR   Pfam; PF05025; RbsD_FucU; 1.
DR   SUPFAM; SSF102546; RbsD-like; 1.
PE   1: Evidence at protein level;
KW   Alternative splicing; Isomerase; Proteomics identification;
KW   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
//