FUCTA_DROME
ID FUCTA_DROME Reviewed; 503 AA.
AC Q9VUL9; Q8SYT5;
DT 02-NOV-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2001, sequence version 2.
DT 03-AUG-2022, entry version 155.
DE RecName: Full=Glycoprotein 3-alpha-L-fucosyltransferase A;
DE EC=2.4.1.214 {ECO:0000269|PubMed:11382750};
DE AltName: Full=Core alpha-(1,3)-fucosyltransferase;
GN Name=FucTA; ORFNames=CG6869;
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 [MRNA], FUNCTION, AND CATALYTIC ACTIVITY.
RC STRAIN=Canton-S;
RX PubMed=11382750; DOI=10.1074/jbc.m100573200;
RA Fabini G., Freilinger A., Altmann F., Wilson I.B.H.;
RT "Identification of core alpha1,3-fucosylated glycans and cloning of the
RT requisite fucosyltransferase cDNA from Drosophila melanogaster: Potential
RT basis of the neural anti-horseradish peroxidase epitope.";
RL J. Biol. Chem. 276:28058-28067(2001).
RN [2]
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 [3]
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Berkeley; TISSUE=Embryo;
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, AND DISRUPTION PHENOTYPE.
RX PubMed=21203496; DOI=10.1371/journal.pgen.1001254;
RA Yamamoto-Hino M., Kanie Y., Awano W., Aoki-Kinoshita K.F., Yano H.,
RA Nishihara S., Okano H., Ueda R., Kanie O., Goto S.;
RT "Identification of genes required for neural-specific glycosylation using
RT functional genomics.";
RL PLoS Genet. 6:E1001254-E1001254(2010).
CC -!- FUNCTION: Catalyzes alpha-1,3 glycosidic linkages of N-glycans
CC (PubMed:11382750). Plays a role in neuronal development by promoting
CC ventral nerve cord formation, possibly by promoting interactions
CC between migrating cells and the extracellular matrix or by promoting
CC neural activity (PubMed:21203496). {ECO:0000269|PubMed:11382750,
CC ECO:0000269|PubMed:21203496}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=GDP-beta-L-fucose + N(4)-{beta-D-GlcNAc-(1->2)-alpha-D-Man-
CC (1->3)-[beta-D-GlcNAc-(1->2)-alpha-D-Man-(1->6)]-beta-D-Man-(1->4)-
CC beta-D-GlcNAc-(1->4)-beta-D-GlcNAc}-L-asparaginyl-[protein] = GDP +
CC H(+) + N(4)-{beta-D-GlcNAc-(1->2)-alpha-D-Man-(1->3)-[beta-D-GlcNAc-
CC (1->2)-alpha-D-Man-(1->6)]-beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-
CC [(1->4)-alpha-L-Fuc]-beta-D-GlcNAc}-L-asparaginyl-[protein];
CC Xref=Rhea:RHEA:24444, Rhea:RHEA-COMP:13526, Rhea:RHEA-COMP:13529,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57273, ChEBI:CHEBI:58189,
CC ChEBI:CHEBI:60651, ChEBI:CHEBI:137182; EC=2.4.1.214;
CC Evidence={ECO:0000269|PubMed:11382750};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:24445;
CC Evidence={ECO:0000305|PubMed:11382750};
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC -!- PATHWAY: Protein modification; protein glycosylation.
CC -!- SUBCELLULAR LOCATION: Golgi apparatus, Golgi stack membrane
CC {ECO:0000250}; Single-pass type II membrane protein {ECO:0000250}.
CC Note=Membrane-bound form in trans cisternae of Golgi. {ECO:0000250}.
CC -!- DISRUPTION PHENOTYPE: Defective alpha-1,3-fucosylation activity and a
CC significantly lower longitudinal length-to-width ratio of the ventral
CC nerve cord (VNC). {ECO:0000269|PubMed:21203496}.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 10 family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAL48946.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AJ302045; CAC41641.1; -; mRNA.
DR EMBL; AE014296; AAF49657.2; -; Genomic_DNA.
DR EMBL; AY071324; AAL48946.1; ALT_FRAME; mRNA.
DR RefSeq; NP_001261872.1; NM_001274943.1.
DR RefSeq; NP_648754.2; NM_140497.3.
DR AlphaFoldDB; Q9VUL9; -.
DR BioGRID; 64975; 2.
DR DIP; DIP-23865N; -.
DR IntAct; Q9VUL9; 1.
DR STRING; 7227.FBpp0075394; -.
DR CAZy; GT10; Glycosyltransferase Family 10.
DR GlyGen; Q9VUL9; 3 sites.
DR PaxDb; Q9VUL9; -.
DR EnsemblMetazoa; FBtr0075641; FBpp0075394; FBgn0036485.
DR EnsemblMetazoa; FBtr0331831; FBpp0304215; FBgn0036485.
DR GeneID; 39653; -.
DR KEGG; dme:Dmel_CG6869; -.
DR CTD; 39653; -.
DR FlyBase; FBgn0036485; FucTA.
DR VEuPathDB; VectorBase:FBgn0036485; -.
DR eggNOG; KOG2619; Eukaryota.
DR HOGENOM; CLU_032075_6_0_1; -.
DR InParanoid; Q9VUL9; -.
DR OMA; HTQNVKV; -.
DR OrthoDB; 551308at2759; -.
DR PhylomeDB; Q9VUL9; -.
DR Reactome; R-DME-9037629; Lewis blood group biosynthesis.
DR Reactome; R-DME-975578; Reactions specific to the complex N-glycan synthesis pathway.
DR UniPathway; UPA00378; -.
DR BioGRID-ORCS; 39653; 0 hits in 3 CRISPR screens.
DR GenomeRNAi; 39653; -.
DR PRO; PR:Q9VUL9; -.
DR Proteomes; UP000000803; Chromosome 3L.
DR Bgee; FBgn0036485; Expressed in brain and 15 other tissues.
DR ExpressionAtlas; Q9VUL9; baseline and differential.
DR Genevisible; Q9VUL9; DM.
DR GO; GO:0032580; C:Golgi cisterna membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005797; C:Golgi medial cisterna; IDA:FlyBase.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0046920; F:alpha-(1->3)-fucosyltransferase activity; IDA:FlyBase.
DR GO; GO:0008417; F:fucosyltransferase activity; IDA:FlyBase.
DR GO; GO:0018392; F:glycoprotein 3-alpha-L-fucosyltransferase activity; IDA:UniProtKB.
DR GO; GO:0036065; P:fucosylation; IBA:GO_Central.
DR GO; GO:0036071; P:N-glycan fucosylation; IMP:FlyBase.
DR GO; GO:0007399; P:nervous system development; IMP:FlyBase.
DR GO; GO:0006486; P:protein glycosylation; IDA:UniProtKB.
DR Gene3D; 3.40.50.11660; -; 1.
DR InterPro; IPR031481; Glyco_tran_10_N.
DR InterPro; IPR001503; Glyco_trans_10.
DR InterPro; IPR038577; GT10-like_C_sf.
DR PANTHER; PTHR11929; PTHR11929; 1.
DR Pfam; PF17039; Glyco_tran_10_N; 1.
DR Pfam; PF00852; Glyco_transf_10; 1.
PE 1: Evidence at protein level;
KW Glycoprotein; Glycosyltransferase; Golgi apparatus; Membrane;
KW Reference proteome; Signal-anchor; Transferase; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..503
FT /note="Glycoprotein 3-alpha-L-fucosyltransferase A"
FT /id="PRO_0000221122"
FT TOPO_DOM 1..10
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 11..28
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 29..503
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT REGION 44..71
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 262
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 295
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 299
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CONFLICT 53
FT /note="H -> Y (in Ref. 1; CAC41641)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 503 AA; 59160 MW; D9DA06078E6010C2 CRC64;
MRRPKISLKK YFYLTLICAL LLIFGFSLKE REIWKTLSPR SSQITTQQQQ HQHLHQLQSM
DEEHPMATSS TPPPIAATLL PEVADNLVEE PEQTVLEEEE SEADRLQEPP AEKAWFFKNG
EYYPKPAKTY SNRKARKRHA PRLLPHQDPY SDRIINQLMY VPHNYEEIKS SGKLKTILLY
NGLGPWNVKK GRDVFLKAKC PVDTCELTAN RDLASTADMI LYKDHYIPTG IRRPSNSKQV
SMLYYLECPY HTQNVKVPDA INWTATYRRD STIVAPYEKW QYYDTKVQQQ EQDINYSVNK
TKKVAWFVSN CGARNGRLQY AHELQKYIEV DIYGACGNFK CSRSTADKCF EILDNDYKFY
LAFENSNCKD YITEKFFVNA LNRRVLPIVM GARPEDYEVS APRRSYIHVD EFSSPKELAE
YLRILDHDDE LYNSYFKWKG TGEFINTYYW CRVCATLHNE EQLRKPRWYT DLNDWWRGPG
VCTTRSWRNF KARKDVISDS SDD
