OFUT2_PLAVS
ID OFUT2_PLAVS Reviewed; 481 AA.
AC A5K6G1;
DT 25-MAY-2022, integrated into UniProtKB/Swiss-Prot.
DT 10-JUL-2007, sequence version 1.
DT 03-AUG-2022, entry version 55.
DE RecName: Full=GDP-fucose protein O-fucosyltransferase 2 {ECO:0000305};
DE EC=2.4.1.221 {ECO:0000269|PubMed:28916755};
DE AltName: Full=Protein O-fucosyltransferase 2 {ECO:0000303|PubMed:28916755};
DE Flags: Precursor;
GN Name=POFUT2 {ECO:0000303|PubMed:28916755};
GN ORFNames=PVX_098900 {ECO:0000312|EMBL:EDL44902.1};
OS Plasmodium vivax (strain Salvador I).
OC Eukaryota; Sar; Alveolata; Apicomplexa; Aconoidasida; Haemosporida;
OC Plasmodiidae; Plasmodium; Plasmodium (Plasmodium).
OX NCBI_TaxID=126793 {ECO:0000312|Proteomes:UP000008333};
RN [1] {ECO:0000312|Proteomes:UP000008333}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Salvador I {ECO:0000312|Proteomes:UP000008333};
RX PubMed=18843361; DOI=10.1038/nature07327;
RA Carlton J.M., Adams J.H., Silva J.C., Bidwell S.L., Lorenzi H., Caler E.,
RA Crabtree J., Angiuoli S.V., Merino E.F., Amedeo P., Cheng Q.,
RA Coulson R.M.R., Crabb B.S., del Portillo H.A., Essien K., Feldblyum T.V.,
RA Fernandez-Becerra C., Gilson P.R., Gueye A.H., Guo X., Kang'a S.,
RA Kooij T.W.A., Korsinczky M., Meyer E.V.-S., Nene V., Paulsen I., White O.,
RA Ralph S.A., Ren Q., Sargeant T.J., Salzberg S.L., Stoeckert C.J.,
RA Sullivan S.A., Yamamoto M.M., Hoffman S.L., Wortman J.R., Gardner M.J.,
RA Galinski M.R., Barnwell J.W., Fraser-Liggett C.M.;
RT "Comparative genomics of the neglected human malaria parasite Plasmodium
RT vivax.";
RL Nature 455:757-763(2008).
RN [2] {ECO:0000305}
RP FUNCTION, CATALYTIC ACTIVITY, AND PATHWAY.
RX PubMed=28916755; DOI=10.1038/s41467-017-00571-y;
RA Lopaticki S., Yang A.S.P., John A., Scott N.E., Lingford J.P.,
RA O'Neill M.T., Erickson S.M., McKenzie N.C., Jennison C., Whitehead L.W.,
RA Douglas D.N., Kneteman N.M., Goddard-Borger E.D., Boddey J.A.;
RT "Protein O-fucosylation in Plasmodium falciparum ensures efficient
RT infection of mosquito and vertebrate hosts.";
RL Nat. Commun. 8:561-561(2017).
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 (PubMed:28916755). O-fucosylates sporozoite
CC proteins CSP and TRAP (PubMed:28916755). O-fucosylation regulates
CC stability and intracellular trafficking of TRAP but not of CSP (By
CC similarity). Probably by regulating protein O-fucosylation, may play a
CC role in parasite transmission to the mosquito vector and/or infection
CC of the vertebrate host hepatocytes; however, POFUT2 involvement in
CC transmission/infection is controversial (By similarity).
CC {ECO:0000250|UniProtKB:W7K6N5, ECO:0000269|PubMed:28916755}.
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:28916755};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:63645;
CC Evidence={ECO:0000269|PubMed:28916755};
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:28916755};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:70492;
CC Evidence={ECO:0000269|PubMed:28916755};
CC -!- PATHWAY: Protein modification; protein glycosylation.
CC {ECO:0000269|PubMed:28916755}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum
CC {ECO:0000250|UniProtKB:W7K6N5}.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 68 family.
CC {ECO:0000305}.
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DR EMBL; AAKM01000007; EDL44902.1; -; Genomic_DNA.
DR RefSeq; XP_001614629.1; XM_001614579.1.
DR STRING; 126793.A5K6G1; -.
DR EnsemblProtists; EDL44902; EDL44902; PVX_098900.
DR GeneID; 5473920; -.
DR KEGG; pvx:PVX_098900; -.
DR VEuPathDB; PlasmoDB:PVX_098900; -.
DR InParanoid; A5K6G1; -.
DR OMA; YILYDVN; -.
DR PhylomeDB; A5K6G1; -.
DR UniPathway; UPA00378; -.
DR Proteomes; UP000008333; Chromosome 7.
DR Proteomes; UP000008333; Unassembled WGS sequence.
DR GO; GO:0005783; C:endoplasmic reticulum; IEA:UniProtKB-SubCell.
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:0036066; P:protein O-linked fucosylation; IDA: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; Endoplasmic reticulum; Fucose metabolism;
KW Reference proteome; Signal; Transferase.
FT SIGNAL 1..22
FT /evidence="ECO:0000255"
FT CHAIN 23..481
FT /note="GDP-fucose protein O-fucosyltransferase 2"
FT /evidence="ECO:0000255"
FT /id="PRO_5002685082"
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 287..289
FT /ligand="GDP-beta-L-fucose"
FT /ligand_id="ChEBI:CHEBI:57273"
FT /evidence="ECO:0000250|UniProtKB:Q9Y2G5"
FT BINDING 365
FT /ligand="GDP-beta-L-fucose"
FT /ligand_id="ChEBI:CHEBI:57273"
FT /evidence="ECO:0000250|UniProtKB:Q9Y2G5"
FT BINDING 382..383
FT /ligand="GDP-beta-L-fucose"
FT /ligand_id="ChEBI:CHEBI:57273"
FT /evidence="ECO:0000250|UniProtKB:Q9Y2G5"
FT SITE 390
FT /note="Essential for catalytic activity"
FT /evidence="ECO:0000250|UniProtKB:Q9Y2G5"
SQ SEQUENCE 481 AA; 56766 MW; AB9FF9B3AAB6213B CRC64;
MKGRAHIWVA LLLACLPPRF RNLDKDVSSP VCRTDDVYTG DAFYPFKKKK YVLYDVHIGE
GFNLQKEVLY RVALAVYYLN QEERTHVHYL VLPPWCYVTH WGRERTNARI KWSIFFNLKA
LQNVIPVMEY AEYEGQFGPH TDYILSYRHI IGEWPKRGDK KSFQVLKLDK CQVKGYKLKK
NLRKNCDHKY SVEYSGKCTN VKGKKMECLE FFFITSHFVS STLLDIFQYD ADSVLIKHGS
NILVAFMNEL VDANLEDVLP YSEDLINEGD QFVEKNFKSS KNYISCHLRY TDFRKISTYD
VSPVGISLLK LLYIMFLRKS TLIFVSTDEK KEVKKVIDSQ FPQFKHFFFF YENEKLHTGQ
VAIVDQWICA RSGTFVGNIF SRFSMHIKWE RSLIGKGGPD HNLDLCGYSI STNHELRKKY
SDVQDAHLDE EALQKLRPLY MRLSQKDRDF LRTICYDFAH YYPQNVSIYR RGERREEGRL
M
