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GDP-fucose protein O-fucosyltransferase 1 (EC 2.4.1.221) (Neurotic protein) (Peptide-O-fucosyltransferase 1) (O-FucT-1)

 OFUT1_DROME             Reviewed;         402 AA.
Q9V6X7; Q5BIC9; Q86SA7; Q8MSR1;
19-SEP-2002, integrated into UniProtKB/Swiss-Prot.
01-MAY-2000, sequence version 1.
05-DEC-2018, entry version 137.
RecName: Full=GDP-fucose protein O-fucosyltransferase 1;
EC=2.4.1.221;
AltName: Full=Neurotic protein;
AltName: Full=Peptide-O-fucosyltransferase 1;
Short=O-FucT-1;
Flags: Precursor;
Name=O-fut1; Synonyms=nti; ORFNames=CG12366;
Drosophila melanogaster (Fruit fly).
Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta;
Pterygota; Neoptera; Holometabola; Diptera; Brachycera; Muscomorpha;
Ephydroidea; Drosophilidae; Drosophila; Sophophora.
NCBI_TaxID=7227;
[1]
NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND DEVELOPMENTAL STAGE.
PubMed=12917292; DOI=10.1242/dev.00679;
Sasamura T., Sasaki N., Miyashita F., Nakao S., Ishikawa H., Ito M.,
Kitagawa M., Harigaya K., Spana E., Bilder D., Perrmon N., Matsuno K.;
"Neurotic, a novel maternal neurogenic gene, encodes an O-
fucosyltransferase that is essential for Notch-Delta interactions.";
Development 130:4785-4795(2003).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=Berkeley;
PubMed=10731132; DOI=10.1126/science.287.5461.2185;
Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X.,
Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D.,
Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G.,
Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D.,
Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M.,
Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S.,
Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P.,
Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I.,
Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P.,
de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M.,
Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P.,
Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W.,
Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K.,
Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J.,
Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C.,
Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A.,
Kimmel B.E., Kodira C.D., Kraft C.L., Kravitz S., Kulp D., Lai Z.,
Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X.,
Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D.,
Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A.,
Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L.,
Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M.,
Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G.,
Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H.,
Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
Spier E., Spradling A.C., Stapleton M., Strong R., Sun E.,
Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X.,
Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J.,
Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A.,
Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L.,
Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S.C., Zhu X.,
Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.;
"The genome sequence of Drosophila melanogaster.";
Science 287:2185-2195(2000).
[3]
GENOME REANNOTATION.
STRAIN=Berkeley;
PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q.,
Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M.,
Lewis S.E.;
"Annotation of the Drosophila melanogaster euchromatic genome: a
systematic review.";
Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=Berkeley; TISSUE=Embryo;
Stapleton M., Carlson J.W., Chavez C., Frise E., George R.A.,
Pacleb J.M., Park S., Wan K.H., Yu C., Rubin G.M., Celniker S.E.;
Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 11-402.
STRAIN=Berkeley; TISSUE=Embryo;
PubMed=12537569; DOI=10.1186/gb-2002-3-12-research0080;
Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M.,
George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H.,
Rubin G.M., Celniker S.E.;
"A Drosophila full-length cDNA resource.";
Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002).
[6]
HOMOLOGY.
PubMed=11524432; DOI=10.1074/jbc.M107849200;
Wang Y., Shao L., Shi S., Harris R.J., Spellman M.W., Stanley P.,
Haltiwanger R.S.;
"Modification of epidermal growth factor-like repeats with O-fucose:
molecular cloning and expression of a novel GDP-fucose protein O-
fucosyltransferase.";
J. Biol. Chem. 276:40338-40345(2001).
[7]
HOMOLOGY.
PubMed=11698403; DOI=10.1074/jbc.M107927200;
Roos C., Kolmer M., Mattila P., Renkonen R.;
"Composition of Drosophila melanogaster proteome involved in
fucosylated glycan metabolism.";
J. Biol. Chem. 277:3168-3175(2002).
[8]
FUNCTION.
PubMed=12909620; DOI=10.1074/jbc.M308687200;
Okajima T., Xu A., Irvine K.D.;
"Modulation of notch-ligand binding by protein O-fucosyltransferase 1
and fringe.";
J. Biol. Chem. 278:42340-42345(2003).
[9]
FUNCTION, AND INTERACTION WITH N.
PubMed=17329366; DOI=10.1242/dev.02811;
Sasamura T., Ishikawa H.O., Sasaki N., Higashi S., Kanai M., Nakao S.,
Ayukawa T., Aigaki T., Noda K., Miyoshi E., Taniguchi N., Matsuno K.;
"The O-fucosyltransferase O-fut1 is an extracellular component that is
essential for the constitutive endocytic trafficking of Notch in
Drosophila.";
Development 134:1347-1356(2007).
-!- FUNCTION: Catalyzes the reaction that attaches fucose through an
O-glycosidic linkage to a conserved serine or threonine residue
found in the consensus sequence C2-X(4,5)-[S/T]-C3 of EGF domains,
where C2 and C3 are the second and third conserved cysteines.
Specifically uses GDP-fucose as donor substrate and proper
disulfide pairing of the substrate EGF domains is required for
fucose transfer. Plays a crucial role in Notch signaling. Initial
fucosylation of Notch/N by POFUT1 generates a substrate for
Fringe/Fng, an acetylglucosaminyltransferase that can then extend
the fucosylation on the Notch EGF repeats. This extended
fucosylation is required for optimal ligand binding and canonical
NOTCH signaling induced by Delta/Dl or Serrate/Ser. Also required
for the transport of Notch/N to the early endosome.
{ECO:0000269|PubMed:12909620, ECO:0000269|PubMed:12917292,
ECO:0000269|PubMed:17329366}.
-!- CATALYTIC ACTIVITY:
Reaction=Transfers an alpha-L-fucosyl residue from GDP-beta-L-
fucose to the serine hydroxy group of a protein acceptor.;
EC=2.4.1.221;
-!- PATHWAY: Protein modification; protein glycosylation.
-!- SUBUNIT: Interacts with N (via its EGF domains); the interaction
is required for the endocyctic transport of N.
{ECO:0000269|PubMed:17329366}.
-!- SUBCELLULAR LOCATION: Endoplasmic reticulum {ECO:0000250}.
-!- DEVELOPMENTAL STAGE: Expressed both maternally and zygotically.
{ECO:0000269|PubMed:12917292}.
-!- SIMILARITY: Belongs to the glycosyltransferase 65 family.
{ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=AAM50020.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
-----------------------------------------------------------------------
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EMBL; AB093572; BAC55010.1; -; mRNA.
EMBL; AE013599; AAF58290.1; -; Genomic_DNA.
EMBL; BT021295; AAX33443.1; -; mRNA.
EMBL; AY118651; AAM50020.1; ALT_INIT; mRNA.
RefSeq; NP_001286406.1; NM_001299477.1.
RefSeq; NP_610931.1; NM_137087.3.
UniGene; Dm.30916; -.
ProteinModelPortal; Q9V6X7; -.
SMR; Q9V6X7; -.
BioGrid; 62315; 6.
DIP; DIP-20580N; -.
IntAct; Q9V6X7; 2.
STRING; 7227.FBpp0086649; -.
CAZy; GT65; Glycosyltransferase Family 65.
PaxDb; Q9V6X7; -.
PRIDE; Q9V6X7; -.
EnsemblMetazoa; FBtr0087520; FBpp0086649; FBgn0033901.
EnsemblMetazoa; FBtr0339959; FBpp0308981; FBgn0033901.
GeneID; 36564; -.
KEGG; dme:Dmel_CG12366; -.
CTD; 36564; -.
FlyBase; FBgn0033901; O-fut1.
eggNOG; KOG3849; Eukaryota.
eggNOG; ENOG410Y3JQ; LUCA.
GeneTree; ENSGT00390000015634; -.
InParanoid; Q9V6X7; -.
KO; K03691; -.
OMA; GQSNHFI; -.
OrthoDB; EOG091G048B; -.
PhylomeDB; Q9V6X7; -.
BRENDA; 2.4.1.221; 1994.
SignaLink; Q9V6X7; -.
UniPathway; UPA00378; -.
GenomeRNAi; 36564; -.
PRO; PR:Q9V6X7; -.
Proteomes; UP000000803; Chromosome 2R.
Bgee; FBgn0033901; Expressed in 25 organ(s), highest expression level in imaginal disc.
ExpressionAtlas; Q9V6X7; baseline and differential.
Genevisible; Q9V6X7; DM.
GO; GO:0031410; C:cytoplasmic vesicle; IDA:FlyBase.
GO; GO:0005783; C:endoplasmic reticulum; IDA:FlyBase.
GO; GO:0008417; F:fucosyltransferase activity; IDA:FlyBase.
GO; GO:0005112; F:Notch binding; IDA:FlyBase.
GO; GO:0046922; F:peptide-O-fucosyltransferase activity; IDA:FlyBase.
GO; GO:0098609; P:cell-cell adhesion; IMP:FlyBase.
GO; GO:0006897; P:endocytosis; IMP:FlyBase.
GO; GO:0006004; P:fucose metabolic process; IEA:UniProtKB-KW.
GO; GO:0045746; P:negative regulation of Notch signaling pathway; IMP:FlyBase.
GO; GO:0007219; P:Notch signaling pathway; NAS:UniProtKB.
GO; GO:0016266; P:O-glycan processing; TAS:UniProtKB.
GO; GO:0045747; P:positive regulation of Notch signaling pathway; IDA:FlyBase.
GO; GO:0030163; P:protein catabolic process; IMP:FlyBase.
GO; GO:0036066; P:protein O-linked fucosylation; IDA:FlyBase.
GO; GO:0006493; P:protein O-linked glycosylation; ISS:UniProtKB.
GO; GO:0008593; P:regulation of Notch signaling pathway; IMP:FlyBase.
GO; GO:0006355; P:regulation of transcription, DNA-templated; NAS:UniProtKB.
InterPro; IPR019378; GDP-Fuc_O-FucTrfase.
InterPro; IPR039922; POFUT1.
PANTHER; PTHR21420; PTHR21420; 1.
Pfam; PF10250; O-FucT; 1.
1: Evidence at protein level;
Carbohydrate metabolism; Complete proteome; Disulfide bond;
Endoplasmic reticulum; Fucose metabolism; Glycoprotein;
Glycosyltransferase; Notch signaling pathway; Reference proteome;
Signal; Transferase.
SIGNAL 1 23 {ECO:0000255}.
CHAIN 24 402 GDP-fucose protein O-fucosyltransferase
1.
/FTId=PRO_0000012153.
REGION 41 44 Substrate binding.
{ECO:0000250|UniProtKB:Q9H488}.
REGION 243 245 Substrate binding.
{ECO:0000250|UniProtKB:Q9H488}.
REGION 366 367 Substrate binding.
{ECO:0000250|UniProtKB:Q9H488}.
BINDING 349 349 Substrate.
{ECO:0000250|UniProtKB:Q9H488}.
CARBOHYD 60 60 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 36 38 {ECO:0000250|UniProtKB:Q9H488}.
DISULFID 122 141 {ECO:0000250|UniProtKB:Q9H488}.
DISULFID 254 284 {ECO:0000250|UniProtKB:Q9H488}.
DISULFID 269 363 {ECO:0000250|UniProtKB:Q9H488}.
CONFLICT 371 371 E -> V (in Ref. 5; AAM50020).
{ECO:0000305}.
CONFLICT 389 389 K -> E (in Ref. 1; BAC55010 and 4;
AAX33443). {ECO:0000305}.
SEQUENCE 402 AA; 46834 MW; E52FF4F86509C2E6 CRC64;
MQWLKMKLRF VNLILLLISS TCAQLGGDPN GYLTYCPCMG RFGNQADHFL GSLAFAKALN
RTLILPPWVE YRRGELRSRQ VPFNTYFEVE PLKEYHRVIT MADFMWHLAD DIWPESERVS
FCYKERYSLQ QEKNDPDKPN CHAKDGNPFG PFWDTFHIDF VRSEFYAPLH FDVHHSNEAA
KWQTKYPAES YPVLAFTGAP ASFPVQLENC KLQRYLQWSQ RYREASKDFI REQLPRGAFL
GIHLRNGIDW VRACEHVKDS QHLFASPQCL GYKNERGALY PELCMPSKEA IIRQLKRTIK
NVRQTQPDNE IKSVFVASDS NHMIGELNTA LSRMGISVHK LPEDDPYLDL AILGQSNHFI
GNCISSYSAF EKRERDVHGF PSYFWGFPKE KDRKHTNVHE EL


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