OFUT2_DROME
ID OFUT2_DROME Reviewed; 490 AA.
AC Q9W589; Q7K729; Q9U985;
DT 30-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 129.
DE RecName: Full=GDP-fucose protein O-fucosyltransferase 2 {ECO:0000305};
DE EC=2.4.1.221 {ECO:0000269|PubMed:16464857};
DE AltName: Full=Peptide-O-fucosyltransferase 2 {ECO:0000303|PubMed:16464857};
DE Short=O-FucT-2;
DE Flags: Precursor;
GN Name=O-fut2 {ECO:0000303|PubMed:16464857, ECO:0000312|FlyBase:FBgn0027791};
GN ORFNames=CG14789 {ECO:0000312|FlyBase:FBgn0027791};
OS Drosophila melanogaster (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7227;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley;
RX PubMed=10731132; DOI=10.1126/science.287.5461.2185;
RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., Brandon R.C.,
RA Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C.,
RA Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A.,
RA An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A.,
RA Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V.,
RA Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J.,
RA Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E.,
RA Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B.,
RA Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I.,
RA Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C.,
RA Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S.,
RA Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M.,
RA Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D.,
RA Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F.,
RA Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D.,
RA Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A.,
RA Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C.,
RA McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C.,
RA Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L.,
RA Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R.,
RA Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V.,
RA Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F.,
RA Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R.,
RA Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y.,
RA Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T.,
RA Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S.,
RA Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W.,
RA Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M.,
RA Venter J.C.;
RT "The genome sequence of Drosophila melanogaster.";
RL Science 287:2185-2195(2000).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=Berkeley;
RX PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M.,
RA Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.;
RT "Annotation of the Drosophila melanogaster euchromatic genome: a systematic
RT review.";
RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Oregon-R;
RX PubMed=10731137; DOI=10.1126/science.287.5461.2220;
RA Benos P.V., Gatt M.K., Ashburner M., Murphy L., Harris D., Barrell B.G.,
RA Ferraz C., Vidal S., Brun C., Demailles J., Cadieu E., Dreano S., Gloux S.,
RA Lelaure V., Mottier S., Galibert F., Borkova D., Minana B., Kafatos F.C.,
RA Louis C., Siden-Kiamos I., Bolshakov S., Papagiannakis G., Spanos L.,
RA Cox S., Madueno E., de Pablos B., Modolell J., Peter A., Schoettler P.,
RA Werner M., Mourkioti F., Beinert N., Dowe G., Schaefer U., Jaeckle H.,
RA Bucheton A., Callister D.M., Campbell L.A., Darlamitsou A., Henderson N.S.,
RA McMillan P.J., Salles C., Tait E.A., Valenti P., Saunders R.D.C.,
RA Glover D.M.;
RT "From sequence to chromosome: the tip of the X chromosome of D.
RT melanogaster.";
RL Science 287:2220-2222(2000).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Berkeley; TISSUE=Head;
RX PubMed=12537569; DOI=10.1186/gb-2002-3-12-research0080;
RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A.,
RA Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M.,
RA Celniker S.E.;
RT "A Drosophila full-length cDNA resource.";
RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002).
RN [5]
RP FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION, PATHWAY, SUBCELLULAR
RP LOCATION, AND MUTAGENESIS OF GLU-442 AND GLU-443.
RX PubMed=16464857; DOI=10.1074/jbc.m511975200;
RA Luo Y., Koles K., Vorndam W., Haltiwanger R.S., Panin V.M.;
RT "Protein O-fucosyltransferase 2 adds O-fucose to thrombospondin type 1
RT repeats.";
RL J. Biol. Chem. 281:9393-9399(2006).
CC -!- FUNCTION: Catalyzes the reaction that attaches fucose through an O-
CC glycosidic linkage to a conserved serine or threonine residue in the
CC consensus sequence C1-X-X-S/T-C2 of thrombospondin type I repeats
CC (TSRs) where C1 and C2 are the first and second cysteines of the
CC repeat, respectively. O-fucosylates members of several protein families
CC including the ADAMTS, the thrombospondin (TSP) and spondin families.
CC {ECO:0000269|PubMed:16464857}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=GDP-beta-L-fucose + L-seryl-[protein] = 3-O-(alpha-L-fucosyl)-
CC L-seryl-[protein] + GDP + H(+); Xref=Rhea:RHEA:63644, Rhea:RHEA-
CC COMP:9863, Rhea:RHEA-COMP:17914, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:29999, ChEBI:CHEBI:57273, ChEBI:CHEBI:58189,
CC ChEBI:CHEBI:189632; EC=2.4.1.221;
CC Evidence={ECO:0000269|PubMed:16464857};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:63645;
CC Evidence={ECO:0000269|PubMed:16464857};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=GDP-beta-L-fucose + L-threonyl-[protein] = 3-O-(alpha-L-
CC fucosyl)-L-threonyl-[protein] + GDP + H(+); Xref=Rhea:RHEA:70491,
CC Rhea:RHEA-COMP:11060, Rhea:RHEA-COMP:17915, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:30013, ChEBI:CHEBI:57273, ChEBI:CHEBI:58189,
CC ChEBI:CHEBI:189631; EC=2.4.1.221;
CC Evidence={ECO:0000269|PubMed:16464857};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:70492;
CC Evidence={ECO:0000269|PubMed:16464857};
CC -!- ACTIVITY REGULATION: Does not require divalent metal ions for optimal
CC activity. {ECO:0000269|PubMed:16464857}.
CC -!- PATHWAY: Protein modification; protein glycosylation.
CC {ECO:0000269|PubMed:16464857}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum
CC {ECO:0000269|PubMed:16464857}. Golgi apparatus
CC {ECO:0000269|PubMed:16464857}. Note=Mainly located in the endoplasmic
CC reticulum. {ECO:0000269|PubMed:16464857}.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 68 family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAB53644.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AE014298; AAF45629.1; -; Genomic_DNA.
DR EMBL; AL031027; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL035632; CAB53644.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AY047568; AAK77300.1; -; mRNA.
DR RefSeq; NP_569916.1; NM_130560.4.
DR AlphaFoldDB; Q9W589; -.
DR SMR; Q9W589; -.
DR BioGRID; 57655; 1.
DR IntAct; Q9W589; 5.
DR STRING; 7227.FBpp0070283; -.
DR CAZy; GT68; Glycosyltransferase Family 68.
DR GlyGen; Q9W589; 3 sites.
DR PaxDb; Q9W589; -.
DR PRIDE; Q9W589; -.
DR DNASU; 31098; -.
DR EnsemblMetazoa; FBtr0070296; FBpp0070283; FBgn0027791.
DR GeneID; 31098; -.
DR KEGG; dme:Dmel_CG14789; -.
DR CTD; 31098; -.
DR FlyBase; FBgn0027791; O-fut2.
DR VEuPathDB; VectorBase:FBgn0027791; -.
DR eggNOG; ENOG502QPS6; Eukaryota.
DR GeneTree; ENSGT00390000007989; -.
DR HOGENOM; CLU_033856_0_0_1; -.
DR InParanoid; Q9W589; -.
DR OMA; YILYDVN; -.
DR OrthoDB; 654070at2759; -.
DR PhylomeDB; Q9W589; -.
DR Reactome; R-DME-5173214; O-glycosylation of TSR domain-containing proteins.
DR SignaLink; Q9W589; -.
DR UniPathway; UPA00378; -.
DR BioGRID-ORCS; 31098; 0 hits in 1 CRISPR screen.
DR GenomeRNAi; 31098; -.
DR PRO; PR:Q9W589; -.
DR Proteomes; UP000000803; Chromosome X.
DR Bgee; FBgn0027791; Expressed in embryonic/larval hemocyte (Drosophila) and 23 other tissues.
DR Genevisible; Q9W589; DM.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:UniProtKB.
DR GO; GO:0005794; C:Golgi apparatus; IDA:UniProtKB.
DR GO; GO:0046922; F:peptide-O-fucosyltransferase activity; IDA:UniProtKB.
DR GO; GO:0006004; P:fucose metabolic process; IEA:UniProtKB-KW.
DR GO; GO:0016266; P:O-glycan processing; IDA:UniProtKB.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; NAS:UniProtKB.
DR InterPro; IPR019378; GDP-Fuc_O-FucTrfase.
DR InterPro; IPR045130; OFUT2-like.
DR PANTHER; PTHR13398; PTHR13398; 1.
DR Pfam; PF10250; O-FucT; 1.
PE 1: Evidence at protein level;
KW Carbohydrate metabolism; Disulfide bond; Endoplasmic reticulum;
KW Fucose metabolism; Glycoprotein; Glycosyltransferase; Golgi apparatus;
KW Reference proteome; Signal; Transferase.
FT SIGNAL 1..25
FT /evidence="ECO:0000255"
FT CHAIN 26..490
FT /note="GDP-fucose protein O-fucosyltransferase 2"
FT /id="PRO_0000236806"
FT ACT_SITE 82
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:Q9Y2G5"
FT BINDING 81..85
FT /ligand="GDP-beta-L-fucose"
FT /ligand_id="ChEBI:CHEBI:57273"
FT /evidence="ECO:0000250|UniProtKB:Q9Y2G5"
FT BINDING 336..338
FT /ligand="GDP-beta-L-fucose"
FT /ligand_id="ChEBI:CHEBI:57273"
FT /evidence="ECO:0000250|UniProtKB:Q9Y2G5"
FT BINDING 418
FT /ligand="GDP-beta-L-fucose"
FT /ligand_id="ChEBI:CHEBI:57273"
FT /evidence="ECO:0000250|UniProtKB:Q9Y2G5"
FT BINDING 435..436
FT /ligand="GDP-beta-L-fucose"
FT /ligand_id="ChEBI:CHEBI:57273"
FT /evidence="ECO:0000250|UniProtKB:Q9Y2G5"
FT SITE 443
FT /note="Essential for catalytic activity"
FT /evidence="ECO:0000250|UniProtKB:Q9Y2G5"
FT CARBOHYD 29
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 79
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 368
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 203..226
FT /evidence="ECO:0000250|UniProtKB:Q9Y2G5"
FT DISULFID 459..466
FT /evidence="ECO:0000250|UniProtKB:Q9Y2G5"
FT MUTAGEN 442
FT /note="E->A: Abolishes enzyme activity but no effect on
FT protein folding nor secretion; when associated with A-443."
FT /evidence="ECO:0000269|PubMed:16464857"
FT MUTAGEN 443
FT /note="E->A: Abolishes enzyme activity but no effect on
FT protein folding nor secretion; when associated with A-442."
FT /evidence="ECO:0000269|PubMed:16464857"
SQ SEQUENCE 490 AA; 56021 MW; 54038E7CDD020768 CRC64;
MRGSWPRLGF PALLLLLHLL TGSDAAVRNG TAKREIGDSR GSSGTCVKGF LQEILPLPAT
CPPEVLGMRG AVYILYDVNI SEGFNLRRDV YIRMAVFVRR LQRRRRFRHV RLVLPPWPRL
YHWHSQGLQQ SGLPWSHFFD LASLRRYAPV LDYEEFLAEQ RLFGNPGAPL VHVGHAFRLQ
HYEVMLEQGI FRDKFERVTD KPCSEGSLSG GPLLQQAELR VGRFHCVRFQ GSAGLLEKLL
REAIDEDTAG PEDVDDMRTY ALLSAETVLH DHWGDEHFWQ ARRSMRFARR LEQVAADFRR
QALDTTDASA GVQRPAMWEL ERPKRNAKGG DYLCAHLRRG DFVRSRDATT PTLKAAAQQV
KQLLRGFNMT TVFLATDATP YELMELKELF YRFRLVHFAP ESNVQRRELK DGGVAVVDQL
VCAYARYFVG TYESTFTYRI YEEREILGFT QASTFNTFCK ALGGSCSRNA VWPIVWADGD
SDSEEDSDPY
