OFUT2_PLABA
ID OFUT2_PLABA Reviewed; 473 AA.
AC A0A509AKB8;
DT 25-MAY-2022, integrated into UniProtKB/Swiss-Prot.
DT 18-SEP-2019, sequence version 1.
DT 03-AUG-2022, entry version 14.
DE RecName: Full=GDP-fucose protein O-fucosyltransferase 2 {ECO:0000305};
DE EC=2.4.1.221 {ECO:0000250|UniProtKB:A5K6G1};
DE AltName: Full=Protein O-fucosyltransferase 2 {ECO:0000303|PubMed:31334132};
DE Flags: Precursor;
GN Name=POFUT2 {ECO:0000303|PubMed:31334132};
GN ORFNames=PBANKA_0810400 {ECO:0000312|EMBL:VUC55262.1};
OS Plasmodium berghei (strain Anka).
OC Eukaryota; Sar; Alveolata; Apicomplexa; Aconoidasida; Haemosporida;
OC Plasmodiidae; Plasmodium; Plasmodium (Vinckeia).
OX NCBI_TaxID=5823 {ECO:0000312|Proteomes:UP000074855};
RN [1] {ECO:0000312|Proteomes:UP000074855}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ANKA {ECO:0000312|Proteomes:UP000074855};
RX PubMed=25359557; DOI=10.1186/s12915-014-0086-0;
RA Otto T.D., Bohme U., Jackson A.P., Hunt M., Franke-Fayard B.,
RA Hoeijmakers W.A., Religa A.A., Robertson L., Sanders M., Ogun S.A.,
RA Cunningham D., Erhart A., Billker O., Khan S.M., Stunnenberg H.G.,
RA Langhorne J., Holder A.A., Waters A.P., Newbold C.I., Pain A., Berriman M.,
RA Janse C.J.;
RT "A comprehensive evaluation of rodent malaria parasite genomes and gene
RT expression.";
RL BMC Biol. 12:86-86(2014).
RN [2] {ECO:0000305}
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=31334132; DOI=10.3389/fcimb.2019.00238;
RA Sanz S., Aquilini E., Tweedell R.E., Verma G., Hamerly T., Hritzo B.,
RA Tripathi A., Machado M., Churcher T.S., Rodrigues J.A., Izquierdo L.,
RA Dinglasan R.R.;
RT "Protein O-Fucosyltransferase 2 Is Not Essential for Plasmodium berghei
RT Development.";
RL Front. Cell. Infect. Microbiol. 9:238-238(2019).
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 (By similarity). O-fucosylates sporozoite proteins
CC CSP and TRAP (By similarity). O-fucosylation regulates stability and
CC intracellular trafficking of TRAP but not of CSP (By similarity).
CC Dispensable for parasite transmission to the mosquito vector and/or
CC infection of the vertebrate host hepatocytes (PubMed:31334132).
CC {ECO:0000250|UniProtKB:A5K6G1, ECO:0000250|UniProtKB:W7K6N5,
CC ECO:0000269|PubMed:31334132}.
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:0000250|UniProtKB:A5K6G1};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:63645;
CC Evidence={ECO:0000250|UniProtKB:A5K6G1};
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:0000250|UniProtKB:A5K6G1};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:70492;
CC Evidence={ECO:0000250|UniProtKB:A5K6G1};
CC -!- PATHWAY: Protein modification; protein glycosylation.
CC {ECO:0000250|UniProtKB:A5K6G1}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum
CC {ECO:0000250|UniProtKB:W7K6N5}.
CC -!- DISRUPTION PHENOTYPE: In S.stephensi mosquito vector, number of oocysts
CC in the midgut, number of sporozoites in the salivary glands, and
CC sporozoite gliding motility are normal (PubMed:31334132). Infection of
CC mouse host is normal including invasion of hepatocytes and infection of
CC erythrocytes (PubMed:31334132). {ECO:0000269|PubMed:31334132}.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 68 family.
CC {ECO:0000305}.
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DR EMBL; LK023123; VUC55262.1; -; Genomic_DNA.
DR STRING; 5823.A0A509AKB8; -.
DR VEuPathDB; PlasmoDB:PBANKA_0810400; -.
DR OMA; YILYDVN; -.
DR UniPathway; UPA00378; -.
DR Proteomes; UP000074855; Chromosome 8.
DR GO; GO:0005783; C:endoplasmic reticulum; IEA:UniProtKB-SubCell.
DR GO; GO:0046922; F:peptide-O-fucosyltransferase activity; IEA:InterPro.
DR GO; GO:0006004; P:fucose metabolic process; IEA:UniProtKB-KW.
DR InterPro; IPR019378; GDP-Fuc_O-FucTrfase.
DR InterPro; IPR045130; OFUT2-like.
DR PANTHER; PTHR13398; PTHR13398; 1.
DR Pfam; PF10250; O-FucT; 1.
PE 3: Inferred from homology;
KW Carbohydrate metabolism; Endoplasmic reticulum; Fucose metabolism;
KW Glycosyltransferase; Reference proteome; Signal; Transferase.
FT SIGNAL 1..25
FT /evidence="ECO:0000255"
FT CHAIN 26..473
FT /note="GDP-fucose protein O-fucosyltransferase 2"
FT /evidence="ECO:0000255"
FT /id="PRO_0000455543"
FT ACT_SITE 60
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:Q9Y2G5"
FT BINDING 59..63
FT /ligand="GDP-beta-L-fucose"
FT /ligand_id="ChEBI:CHEBI:57273"
FT /evidence="ECO:0000250|UniProtKB:Q9Y2G5"
FT BINDING 283..285
FT /ligand="GDP-beta-L-fucose"
FT /ligand_id="ChEBI:CHEBI:57273"
FT /evidence="ECO:0000250|UniProtKB:Q9Y2G5"
FT BINDING 379..380
FT /ligand="GDP-beta-L-fucose"
FT /ligand_id="ChEBI:CHEBI:57273"
FT /evidence="ECO:0000250|UniProtKB:Q9Y2G5"
FT SITE 387
FT /note="Essential for catalytic activity"
FT /evidence="ECO:0000250|UniProtKB:Q9Y2G5"
SQ SEQUENCE 473 AA; 56994 MW; 7EC288E37DD00DD1 CRC64;
MKNMIYNLIS ISLYSLIIIL TDIYAKTSSL ICNKNDIYLN DKFYFLKKKK YILYDVNIGE
GFNLQKEVLY RMSLVIYQLN KRDKEYIYYL VLPPWCYLSH WSNKRHDNLQ WNIFLNMNII
KNVIPIIEFS DYKKLYGDVT DFIISFKYLL DSNAQKAKYY HVLPFDKCYI EDYKFKIVCK
NCDYKYSVTY SGNCTNIKGK NTLCYSDYIV TNYLVNYVVH KLFYIHNINS ILIKNSNVVL
VPFPNELFEN NIEDILLFNE KLIYNGNNYI KEILKNSNYI SCHLRYNDFK KITSYDVPSV
QIAILKLLYI MFMNNKEKIF ISTDEKKYVQ YIINKHFKQF KHFFYFYENK DNYHEGQVAI
IEQWICANSS TFVGNIFSRF TMHIIWERYL ITKGKEHQNI DLCGYSINNN EQLKNRYKKI
QYIYDHSSIE KLNNIYNTYS EIDKKYIITL CFGFPSHFPS NLSIYRKKYI PFA
