FUCM_MOUSE
ID FUCM_MOUSE Reviewed; 153 AA.
AC Q8R2K1; Q3TQB6; Q76K68; Q8C566; Q8C8P5;
DT 15-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 1.
DT 03-AUG-2022, entry version 115.
DE RecName: Full=Fucose mutarotase;
DE EC=5.1.3.29 {ECO:0000269|PubMed:17602138, ECO:0000269|PubMed:19524593};
GN Name=Fuom; Synonyms=Le51;
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 [MRNA] (ISOFORM 3).
RC STRAIN=BALB/cJ; TISSUE=Liver;
RX PubMed=15052633; DOI=10.1002/bit.20024;
RA Nakashima N., Tamura T.;
RT "A novel system for expressing recombinant proteins over a wide temperature
RT range from 4 to 35 degrees C.";
RL Biotechnol. Bioeng. 86:136-148(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 4), AND NUCLEOTIDE
RP SEQUENCE [LARGE SCALE MRNA] OF 17-153 (ISOFORM 5).
RC STRAIN=C57BL/6J; TISSUE=Bone, Cerebellum, and Retina;
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]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=C57BL/6J; TISSUE=Mammary gland;
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 FUNCTION, CATALYTIC ACTIVITY, AND TISSUE SPECIFICITY.
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 [5]
RP X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 1-149 IN COMPLEX WITH L-FUCOSE,
RP SUBUNIT, SUBSTRATE-BINDING SITES, ACTIVE SITE, CATALYTIC ACTIVITY, AND
RP FUNCTION.
RX PubMed=19524593; DOI=10.1016/j.jmb.2009.06.022;
RA Lee K.H., Ryu K.S., Kim M.S., Suh H.Y., Ku B., Song Y.L., Ko S., Lee W.,
RA Oh B.H.;
RT "Crystal structures and enzyme mechanisms of a dual fucose
RT mutarotase/ribose pyranase.";
RL J. Mol. Biol. 391:178-191(2009).
RN [6]
RP DISRUPTION PHENOTYPE.
RX PubMed=20609214; DOI=10.1186/1471-2156-11-62;
RA Park D., Choi D., Lee J., Lim D.S., Park C.;
RT "Male-like sexual behavior of female mouse lacking fucose mutarotase.";
RL BMC Genet. 11:62-62(2010).
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, ECO:0000269|PubMed:19524593};
CC -!- PATHWAY: Carbohydrate metabolism; L-fucose metabolism.
CC {ECO:0000269|PubMed:17602138, ECO:0000269|PubMed:19524593}.
CC -!- SUBUNIT: Mainly homodimer, but exists also as homotetramer,
CC homooctamer, and homodecamer. The homodimeric form seems catalytically
CC inactive. {ECO:0000269|PubMed:19524593}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=5;
CC Name=1;
CC IsoId=Q8R2K1-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8R2K1-2; Sequence=VSP_025085;
CC Name=3;
CC IsoId=Q8R2K1-3; Sequence=VSP_025082;
CC Name=4;
CC IsoId=Q8R2K1-4; Sequence=VSP_025083;
CC Name=5;
CC IsoId=Q8R2K1-5; Sequence=VSP_025084;
CC -!- TISSUE SPECIFICITY: Widely expressed in various tissues and cell lines,
CC including kidney, liver, and pancreas, marginally in muscle and testis.
CC {ECO:0000269|PubMed:17602138}.
CC -!- DISRUPTION PHENOTYPE: Deficient female mice show reduced sexual
CC receptivity, as measured by lordosis quotient and masculinized sexual
CC behaviors in female mice. Display a reduced number of tyrosine
CC hydroxylase-positive neurons in the anteroventral periventricular
CC nucleus, a sexually dimorphic feature in rats and mice. Embryos at 16.5
CC dpc have reduced alpha-feto-protein levels and reduced fucosylation of
CC alpha-feto-protein. {ECO:0000269|PubMed:20609214}.
CC -!- SIMILARITY: Belongs to the RbsD / FucU family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAE37468.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AB094480; BAD11304.1; -; mRNA.
DR EMBL; AK044731; BAC32055.1; -; mRNA.
DR EMBL; AK079410; BAC37637.1; -; mRNA.
DR EMBL; AK163708; BAE37468.1; ALT_INIT; mRNA.
DR EMBL; BC028662; AAH28662.1; -; mRNA.
DR CCDS; CCDS40173.1; -. [Q8R2K1-1]
DR RefSeq; NP_001273146.1; NM_001286217.1.
DR RefSeq; NP_001273147.1; NM_001286218.1.
DR RefSeq; NP_081204.2; NM_026928.3. [Q8R2K1-1]
DR PDB; 2WCU; X-ray; 1.90 A; A/B=1-149.
DR PDBsum; 2WCU; -.
DR AlphaFoldDB; Q8R2K1; -.
DR SMR; Q8R2K1; -.
DR STRING; 10090.ENSMUSP00000026539; -.
DR iPTMnet; Q8R2K1; -.
DR PhosphoSitePlus; Q8R2K1; -.
DR EPD; Q8R2K1; -.
DR jPOST; Q8R2K1; -.
DR MaxQB; Q8R2K1; -.
DR PaxDb; Q8R2K1; -.
DR PeptideAtlas; Q8R2K1; -.
DR PRIDE; Q8R2K1; -.
DR ProteomicsDB; 266886; -. [Q8R2K1-1]
DR ProteomicsDB; 266887; -. [Q8R2K1-2]
DR ProteomicsDB; 266888; -. [Q8R2K1-3]
DR ProteomicsDB; 266889; -. [Q8R2K1-4]
DR ProteomicsDB; 266890; -. [Q8R2K1-5]
DR Antibodypedia; 48803; 85 antibodies from 16 providers.
DR DNASU; 69064; -.
DR Ensembl; ENSMUST00000026539; ENSMUSP00000026539; ENSMUSG00000025466. [Q8R2K1-1]
DR Ensembl; ENSMUST00000121115; ENSMUSP00000112970; ENSMUSG00000025466. [Q8R2K1-4]
DR Ensembl; ENSMUST00000148716; ENSMUSP00000120353; ENSMUSG00000025466. [Q8R2K1-2]
DR GeneID; 69064; -.
DR KEGG; mmu:69064; -.
DR UCSC; uc009kgu.2; mouse. [Q8R2K1-1]
DR UCSC; uc009kgw.2; mouse. [Q8R2K1-4]
DR CTD; 282969; -.
DR MGI; MGI:1916314; Fuom.
DR VEuPathDB; HostDB:ENSMUSG00000025466; -.
DR eggNOG; ENOG502RZR7; Eukaryota.
DR GeneTree; ENSGT00390000001197; -.
DR HOGENOM; CLU_120075_2_0_1; -.
DR InParanoid; Q8R2K1; -.
DR OMA; MGHGDDI; -.
DR OrthoDB; 1457717at2759; -.
DR PhylomeDB; Q8R2K1; -.
DR TreeFam; TF324689; -.
DR BRENDA; 5.1.3.29; 3474.
DR BRENDA; 5.4.99.62; 3474.
DR Reactome; R-MMU-6787639; GDP-fucose biosynthesis.
DR UniPathway; UPA00956; -.
DR BioGRID-ORCS; 69064; 0 hits in 72 CRISPR screens.
DR ChiTaRS; Fuom; mouse.
DR EvolutionaryTrace; Q8R2K1; -.
DR PRO; PR:Q8R2K1; -.
DR Proteomes; UP000000589; Chromosome 7.
DR RNAct; Q8R2K1; protein.
DR Bgee; ENSMUSG00000025466; Expressed in interventricular septum and 225 other tissues.
DR ExpressionAtlas; Q8R2K1; baseline and differential.
DR Genevisible; Q8R2K1; MM.
DR GO; GO:0042806; F:fucose binding; IDA:UniProtKB.
DR GO; GO:0036373; F:L-fucose mutarotase activity; IDA:UniProtKB.
DR GO; GO:0016857; F:racemase and epimerase activity, acting on carbohydrates and derivatives; IDA:UniProtKB.
DR GO; GO:0060180; P:female mating behavior; IMP:MGI.
DR GO; GO:0006004; P:fucose metabolic process; IDA:UniProtKB.
DR GO; GO:0036065; P:fucosylation; IMP:MGI.
DR GO; GO:0045665; P:negative regulation of neuron differentiation; IMP:MGI.
DR GO; GO:0030182; P:neuron differentiation; IMP:MGI.
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 3D-structure; Alternative splicing; Isomerase; Reference proteome.
FT CHAIN 1..153
FT /note="Fucose mutarotase"
FT /id="PRO_0000286554"
FT ACT_SITE 24
FT /note="Proton donor"
FT /evidence="ECO:0000269|PubMed:19524593"
FT ACT_SITE 69
FT /evidence="ECO:0000269|PubMed:19524593"
FT ACT_SITE 120
FT /evidence="ECO:0000269|PubMed:19524593"
FT BINDING 32
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:19524593"
FT BINDING 79
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:19524593"
FT BINDING 120
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:19524593"
FT BINDING 138
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:19524593"
FT BINDING 140
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:19524593"
FT VAR_SEQ 1..24
FT /note="MVALKGIPKVLSPELLFALARMGH -> MSISGIVILSAVLSIKINMLILTK
FT TSCRIRHEASCRIRHE (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15052633"
FT /id="VSP_025082"
FT VAR_SEQ 109..153
FT /note="KTLMKLERFEFYERAKKAFAVVATGEMALYGNIILKKGTLDLGPS -> VSA
FT APTMGRSVSWHLGSEG (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_025083"
FT VAR_SEQ 109..153
FT /note="KTLMKLERFEFYERAKKAFAVVATGEMALYGNIILKKGTLDLGPS -> AQT
FT EKRYKRYPLSLDP (in isoform 5)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_025084"
FT VAR_SEQ 134..153
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_025085"
FT HELIX 13..21
FT /evidence="ECO:0007829|PDB:2WCU"
FT STRAND 27..31
FT /evidence="ECO:0007829|PDB:2WCU"
FT HELIX 37..40
FT /evidence="ECO:0007829|PDB:2WCU"
FT HELIX 41..43
FT /evidence="ECO:0007829|PDB:2WCU"
FT STRAND 46..50
FT /evidence="ECO:0007829|PDB:2WCU"
FT HELIX 55..65
FT /evidence="ECO:0007829|PDB:2WCU"
FT STRAND 70..73
FT /evidence="ECO:0007829|PDB:2WCU"
FT STRAND 75..79
FT /evidence="ECO:0007829|PDB:2WCU"
FT HELIX 83..87
FT /evidence="ECO:0007829|PDB:2WCU"
FT HELIX 94..104
FT /evidence="ECO:0007829|PDB:2WCU"
FT STRAND 112..114
FT /evidence="ECO:0007829|PDB:2WCU"
FT HELIX 116..124
FT /evidence="ECO:0007829|PDB:2WCU"
FT STRAND 126..132
FT /evidence="ECO:0007829|PDB:2WCU"
FT STRAND 141..145
FT /evidence="ECO:0007829|PDB:2WCU"
SQ SEQUENCE 153 AA; 16805 MW; 4CDCC14F54D59C66 CRC64;
MVALKGIPKV LSPELLFALA RMGHGDEIVL ADANFPTSSI CQCGPVEIRA DGLDIPQLLE
AVLRLLPLDT YVESPAAVMD LVPSDKEKGL QTPIWKRYES LLLEADCKKT LMKLERFEFY
ERAKKAFAVV ATGEMALYGN IILKKGTLDL GPS
