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

 OFUT1_CRIGR             Reviewed;         392 AA.
P83337; G3HE95;
13-SEP-2004, integrated into UniProtKB/Swiss-Prot.
09-JAN-2013, sequence version 2.
16-JAN-2019, entry version 60.
RecName: Full=GDP-fucose protein O-fucosyltransferase 1;
EC=2.4.1.221 {ECO:0000269|PubMed:8358148, ECO:0000269|PubMed:9525914};
AltName: Full=Peptide-O-fucosyltransferase 1;
Short=O-FucT-1;
Name=POFUT1;
Cricetulus griseus (Chinese hamster) (Cricetulus barabensis griseus).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Cricetidae; Cricetinae; Cricetulus.
NCBI_TaxID=10029;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=21804562; DOI=10.1038/nbt.1932;
Xu X., Nagarajan H., Lewis N.E., Pan S., Cai Z., Liu X., Chen W.,
Xie M., Wang W., Hammond S., Andersen M.R., Neff N., Passarelli B.,
Koh W., Fan H.C., Wang J., Gui Y., Lee K.H., Betenbaugh M.J.,
Quake S.R., Famili I., Palsson B.O., Wang J.;
"The genomic sequence of the Chinese hamster ovary (CHO)-K1 cell
line.";
Nat. Biotechnol. 29:735-741(2011).
[2] {ECO:0000305}
PROTEIN SEQUENCE OF 28-88.
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).
[3] {ECO:0000305}
ACTIVITY REGULATION, SUBSTRATE SPECIFICITY, AND CATALYTIC ACTIVITY.
PubMed=8358148; DOI=10.1093/glycob/3.3.219;
Harris R.J., Spellman M.W.;
"O-linked fucose and other post-translational modifications unique to
EGF modules.";
Glycobiology 3:219-224(1993).
[4] {ECO:0000305}
FUNCTION.
PubMed=9023546; DOI=10.1093/glycob/6.8.837;
Wang Y., Lee G.F., Kelley R.F., Spellman M.W.;
"Identification of a GDP-L-fucose:polypeptide fucosyltransferase and
enzymatic addition of O-linked fucose to EGF domains.";
Glycobiology 6:837-842(1996).
[5] {ECO:0000305}
BIOPHYSICOCHEMICAL PROPERTIES, SUBSTRATE SPECIFICITY, GLYCOSYLATION,
AND STRUCTURE OF CARBOHYDRATES.
PubMed=9525914; DOI=10.1074/jbc.273.14.8112;
Wang Y., Spellman M.W.;
"Purification and characterization of a GDP-fucose:polypeptide
fucosyltransferase from Chinese hamster ovary cells.";
J. Biol. Chem. 273:8112-8118(1998).
-!- 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 by POFUT1 generates a substrate for
FRINGE/RFNG, 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 DELTA1 or JAGGED1 (By similarity).
Fucosylates AGRN and determines its ability to cluster
acetylcholine receptors (AChRs) (By similarity). {ECO:0000250,
ECO:0000269|PubMed:9023546}.
-!- 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; Evidence={ECO:0000269|PubMed:8358148,
ECO:0000269|PubMed:9023546, ECO:0000269|PubMed:9525914};
-!- ACTIVITY REGULATION: Activated by manganese and, to a lesser
extent, by other divalent metals such as cobalt and calcium.
Inhibited by copper, ferric and zinc ions.
{ECO:0000269|PubMed:8358148}.
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Kinetic parameters:
KM=11 uM for His(6)-F7-EGF-1 {ECO:0000269|PubMed:9525914};
KM=15 uM for F7-EGF-1 {ECO:0000269|PubMed:9525914};
Vmax=2.5 umol/min/mg enzyme {ECO:0000269|PubMed:9525914};
Vmax=2.4 umol/min/mg enzyme {ECO:0000269|PubMed:9525914};
pH dependence:
Optimum pH is 5.5-8.0. {ECO:0000269|PubMed:9525914};
-!- PATHWAY: Protein modification; protein glycosylation.
-!- SUBCELLULAR LOCATION: Endoplasmic reticulum
{ECO:0000250|UniProtKB:Q6EV70}.
-!- PTM: N-glycosylated. Contains high mannose-type carbohydrates.
{ECO:0000269|PubMed:9525914}.
-!- SIMILARITY: Belongs to the glycosyltransferase 65 family.
{ECO:0000305}.
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EMBL; JH000311; EGW00282.1; -; Genomic_DNA.
RefSeq; XP_003502364.1; XM_003502316.2.
SMR; P83337; -.
PRIDE; P83337; -.
Ensembl; ENSCGRT00000018370; ENSCGRP00000018105; ENSCGRG00000013168.
Ensembl; ENSCGRT00001015791; ENSCGRP00001011559; ENSCGRG00001013152.
GeneID; 100753417; -.
KEGG; cge:100753417; -.
CTD; 23509; -.
InParanoid; P83337; -.
KO; K03691; -.
OrthoDB; 1127619at2759; -.
UniPathway; UPA00378; -.
Proteomes; UP000001075; Unassembled WGS sequence.
GO; GO:0005789; C:endoplasmic reticulum membrane; TAS:Reactome.
GO; GO:0046922; F:peptide-O-fucosyltransferase activity; IDA:UniProtKB.
GO; GO:0016740; F:transferase activity; IDA:UniProtKB.
GO; GO:0016757; F:transferase activity, transferring glycosyl groups; IDA:UniProtKB.
GO; GO:0001525; P:angiogenesis; IEA:Ensembl.
GO; GO:0006004; P:fucose metabolic process; IEA:UniProtKB-KW.
GO; GO:0007507; P:heart development; IEA:Ensembl.
GO; GO:0007399; P:nervous system development; IEA:Ensembl.
GO; GO:0007219; P:Notch signaling pathway; IEA:UniProtKB-KW.
GO; GO:0006486; P:protein glycosylation; IDA:UniProtKB.
GO; GO:0008593; P:regulation of Notch signaling pathway; ISS:UniProtKB.
GO; GO:0001756; P:somitogenesis; IEA:Ensembl.
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; Direct protein sequencing;
Disulfide bond; Endoplasmic reticulum; Fucose metabolism;
Glycoprotein; Glycosyltransferase; Notch signaling pathway;
Reference proteome; Transferase.
CHAIN 1 392 GDP-fucose protein O-fucosyltransferase
1.
/FTId=PRO_0000220935.
REGION 47 50 Substrate binding.
{ECO:0000250|UniProtKB:Q9H488}.
REGION 242 244 Substrate binding.
{ECO:0000250|UniProtKB:Q9H488}.
REGION 361 362 Substrate binding.
{ECO:0000250|UniProtKB:Q9H488}.
MOTIF 389 392 Prevents secretion from ER.
{ECO:0000255}.
BINDING 344 344 Substrate.
{ECO:0000250|UniProtKB:Q9H488}.
CARBOHYD 66 66 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 164 164 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 42 44 {ECO:0000250|UniProtKB:Q9H488}.
DISULFID 130 144 {ECO:0000250|UniProtKB:Q9H488}.
DISULFID 253 287 {ECO:0000250|UniProtKB:Q9H488}.
DISULFID 271 358 {ECO:0000250|UniProtKB:Q9H488}.
CONFLICT 66 66 N -> V (in Ref. 2; AA sequence).
{ECO:0000305}.
SEQUENCE 392 AA; 44669 MW; 45E1421CBA0880C4 CRC64;
MGAAAWAPPH LLLRVSLLLL LLLPLRGRLA GSWDLAGYLL YCPCMGRFGN QADHFLGSLA
FAKLLNRTLA VPPWIEYQHH KPPFTNLHVS YQKYFKLEPL QAYHRVISLE EFMEKLAPIH
WPPEKRVAYC FEVAAQRSPD KKTCPMKEGN PFGPFWDQFH VSFNKSELFT GISFSASYKE
QWIQRFPPEE HPVLALPGAP AQFPVLEEHR ALQKYMVWSD EMVKTGEAQI STHLIRPYVG
IHLRIGSDWK NACAMLKDGT AGSHFMASPQ CVGYSRSTAT PLTMTMCLPD LNEIQRAVKL
WVRALNARSI YIATDSESYV PEIQQLFKEK VKVVSLKPEV AQVDLYILGQ ADHFIGNCVS
SFTAFVKRER DLHGRQSSFF GMDRPSQPRD EF


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