FUCO2_MOUSE
ID FUCO2_MOUSE Reviewed; 461 AA.
AC Q99KR8; Q8VEM3; Q9D7Z8; Q9DCL7;
DT 10-MAY-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 144.
DE RecName: Full=Plasma alpha-L-fucosidase;
DE EC=3.2.1.51;
DE AltName: Full=Alpha-L-fucoside fucohydrolase 2;
DE Short=Alpha-L-fucosidase 2;
DE Flags: Precursor;
GN Name=Fuca2;
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 [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J;
RC TISSUE=Kidney, Ovary, Stomach, Urinary bladder, and Uterus;
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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Czech II, and FVB/N; TISSUE=Mammary tumor;
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 [3]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Heart;
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: Alpha-L-fucosidase is responsible for hydrolyzing the alpha-
CC 1,6-linked fucose joined to the reducing-end N-acetylglucosamine of the
CC carbohydrate moieties of glycoproteins.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=an alpha-L-fucoside + H2O = an alcohol + L-fucose;
CC Xref=Rhea:RHEA:12288, ChEBI:CHEBI:2181, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:28349, ChEBI:CHEBI:30879; EC=3.2.1.51;
CC Evidence={ECO:0000255|PROSITE-ProRule:PRU10054};
CC -!- SUBUNIT: Homotetramer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 29 family. {ECO:0000305}.
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DR EMBL; AK002675; BAB22277.1; -; mRNA.
DR EMBL; AK008653; BAB25809.1; -; mRNA.
DR EMBL; AK030320; BAC26899.1; -; mRNA.
DR EMBL; AK035607; BAC29123.1; -; mRNA.
DR EMBL; BC004039; AAH04039.1; -; mRNA.
DR EMBL; BC018181; AAH18181.1; -; mRNA.
DR CCDS; CCDS23701.1; -.
DR RefSeq; NP_001317127.1; NM_001330198.1.
DR RefSeq; NP_080075.2; NM_025799.5.
DR RefSeq; XP_006512890.1; XM_006512827.3.
DR AlphaFoldDB; Q99KR8; -.
DR SMR; Q99KR8; -.
DR STRING; 10090.ENSMUSP00000113499; -.
DR CAZy; GH29; Glycoside Hydrolase Family 29.
DR GlyGen; Q99KR8; 3 sites.
DR PhosphoSitePlus; Q99KR8; -.
DR CPTAC; non-CPTAC-3646; -.
DR MaxQB; Q99KR8; -.
DR PaxDb; Q99KR8; -.
DR PeptideAtlas; Q99KR8; -.
DR PRIDE; Q99KR8; -.
DR ProteomicsDB; 266891; -.
DR Antibodypedia; 33149; 352 antibodies from 28 providers.
DR DNASU; 66848; -.
DR Ensembl; ENSMUST00000060212; ENSMUSP00000055519; ENSMUSG00000019810.
DR Ensembl; ENSMUST00000121465; ENSMUSP00000113499; ENSMUSG00000019810.
DR GeneID; 66848; -.
DR KEGG; mmu:66848; -.
DR UCSC; uc007ekv.1; mouse.
DR CTD; 2519; -.
DR MGI; MGI:1914098; Fuca2.
DR VEuPathDB; HostDB:ENSMUSG00000019810; -.
DR eggNOG; KOG3340; Eukaryota.
DR GeneTree; ENSGT00440000035378; -.
DR HOGENOM; CLU_002934_1_1_1; -.
DR InParanoid; Q99KR8; -.
DR OMA; WESTDKH; -.
DR OrthoDB; 929780at2759; -.
DR PhylomeDB; Q99KR8; -.
DR TreeFam; TF313034; -.
DR BRENDA; 3.2.1.51; 3474.
DR Reactome; R-MMU-381426; Regulation of Insulin-like Growth Factor (IGF) transport and uptake by Insulin-like Growth Factor Binding Proteins (IGFBPs).
DR Reactome; R-MMU-6798695; Neutrophil degranulation.
DR Reactome; R-MMU-8957275; Post-translational protein phosphorylation.
DR BioGRID-ORCS; 66848; 0 hits in 73 CRISPR screens.
DR ChiTaRS; Fuca2; mouse.
DR PRO; PR:Q99KR8; -.
DR Proteomes; UP000000589; Chromosome 10.
DR RNAct; Q99KR8; protein.
DR Bgee; ENSMUSG00000019810; Expressed in interventricular septum and 241 other tissues.
DR ExpressionAtlas; Q99KR8; baseline and differential.
DR Genevisible; Q99KR8; MM.
DR GO; GO:0005615; C:extracellular space; ISO:MGI.
DR GO; GO:0005764; C:lysosome; IBA:GO_Central.
DR GO; GO:0004560; F:alpha-L-fucosidase activity; ISO:MGI.
DR GO; GO:0006004; P:fucose metabolic process; ISO:MGI.
DR GO; GO:0016139; P:glycoside catabolic process; ISO:MGI.
DR GO; GO:2000535; P:regulation of entry of bacterium into host cell; ISO:MGI.
DR GO; GO:0009617; P:response to bacterium; ISO:MGI.
DR Gene3D; 2.60.40.1180; -; 1.
DR InterPro; IPR016286; FUC_metazoa-typ.
DR InterPro; IPR031919; Fucosidase_C.
DR InterPro; IPR000933; Glyco_hydro_29.
DR InterPro; IPR018526; Glyco_hydro_29_CS.
DR InterPro; IPR013780; Glyco_hydro_b.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR PANTHER; PTHR10030; PTHR10030; 1.
DR Pfam; PF01120; Alpha_L_fucos; 1.
DR Pfam; PF16757; Fucosidase_C; 1.
DR PIRSF; PIRSF001092; Alpha-L-fucosidase; 1.
DR PRINTS; PR00741; GLHYDRLASE29.
DR SMART; SM00812; Alpha_L_fucos; 1.
DR SUPFAM; SSF51445; SSF51445; 1.
DR PROSITE; PS00385; ALPHA_L_FUCOSIDASE; 1.
PE 1: Evidence at protein level;
KW Glycoprotein; Glycosidase; Hydrolase; Phosphoprotein; Reference proteome;
KW Secreted; Signal.
FT SIGNAL 1..25
FT /evidence="ECO:0000255"
FT CHAIN 26..461
FT /note="Plasma alpha-L-fucosidase"
FT /id="PRO_0000010313"
FT SITE 288
FT /note="May be important for catalysis"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10054"
FT MOD_RES 295
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9BTY2"
FT CARBOHYD 165
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 233
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 371
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CONFLICT 2..3
FT /note="RL -> PG (in Ref. 1; BAB25809)"
FT /evidence="ECO:0000305"
FT CONFLICT 140
FT /note="R -> H (in Ref. 2; AAH18181)"
FT /evidence="ECO:0000305"
FT CONFLICT 435
FT /note="I -> V (in Ref. 1; BAB22277)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 461 AA; 53645 MW; 1E232FE5ED6A3C1F CRC64;
MRLGFLMLLP LLLLPLLRPW GVTRALSYDP TWESLDRRPL PAWFDQAKFG IFIHWGVFSV
PSFGSEWFWW YWQKEKKPQF VDFMNNNYAP GFKYEDFVVL FTAKYFNANQ WADILQASGA
KYVVFTSKHH EGFTMWGSDR SWNWNAVDEG PKRDIVKELE VAVRNRTGLH FGLYYSLFEW
FHPLFLEDQS SSFQKQRFPV SKTLPELYEL VNRYQPEVLW SDGDGGAPDH YWNSTGFLAW
LYNESPVRKT VVTNDRWGVG SICKHGGYYT CSDRYNPGYL LPHKWENCMT IDKFSWGYRR
EAEISDYLTI EELVKKLVET VACGGNLLMN IGPTGDGTIP VIFEERLRQM GTWLKVNGEA
IYETHTWRSQ NDTVTPDVWY TSKPEKKLVY AIFLKWPISG KLFLGQPIGS LGETEVELLG
HWQPLTWTSS QPSGITVELP LLSVHQMPCK WGWTLVLSNV I
