OFUT2_PLAFO
ID OFUT2_PLAFO Reviewed; 469 AA.
AC W7K6N5;
DT 25-MAY-2022, integrated into UniProtKB/Swiss-Prot.
DT 25-MAY-2022, sequence version 2.
DT 03-AUG-2022, entry version 26.
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:28916755};
DE Flags: Precursor;
GN Name=POFUT2 {ECO:0000303|PubMed:28916755};
GN ORFNames=PFNF54_02509 {ECO:0000312|EMBL:EWC88665.1};
OS Plasmodium falciparum (isolate NF54).
OC Eukaryota; Sar; Alveolata; Apicomplexa; Aconoidasida; Haemosporida;
OC Plasmodiidae; Plasmodium; Plasmodium (Laverania).
OX NCBI_TaxID=5843 {ECO:0000312|Proteomes:UP000030673};
RN [1] {ECO:0000312|Proteomes:UP000030673}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NF54 {ECO:0000312|Proteomes:UP000030673};
RG The Broad Institute Genome Sequencing Platform;
RG The Broad Institute Genome Sequencing Center for Infectious Disease;
RA Neafsey D., Cheeseman I., Volkman S., Adams J., Walker B., Young S.K.,
RA Zeng Q., Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Alvarado L.,
RA Arachchi H.M., Berlin A.M., Chapman S.B., Dewar J., Goldberg J., Griggs A.,
RA Gujja S., Hansen M., Howarth C., Imamovic A., Larimer J., McCowan C.,
RA Murphy C., Neiman D., Pearson M., Priest M., Roberts A., Saif S., Shea T.,
RA Sisk P., Sykes S., Wortman J., Nusbaum C., Birren B.;
RT "The Genome Sequence of Plasmodium falciparum NF54.";
RL Submitted (FEB-2013) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000305}
RP FUNCTION, SUBCELLULAR LOCATION, DEVELOPMENTAL STAGE, AND DISRUPTION
RP PHENOTYPE.
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).
RN [3] {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 (PubMed:28916755).
CC Probably by regulating protein O-fucosylation, may play a role in
CC parasite transmission to the mosquito vector and/or infection of the
CC vertebrate host hepatocytes; however, POFUT2 involvement in
CC transmission/infection is controversial (PubMed:28916755,
CC PubMed:31334132). {ECO:0000250|UniProtKB:A5K6G1,
CC ECO:0000269|PubMed:28916755, 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:0000269|PubMed:28916755}.
CC -!- DEVELOPMENTAL STAGE: Expressed during parasite asexual blood stages,
CC including at the ring, trophozoite and schizont stages (at protein
CC level). {ECO:0000269|PubMed:28916755}.
CC -!- DISRUPTION PHENOTYPE: In S.stephensi mosquito vector, development into
CC ookinete is normal; however, the number of oocysts developing at the
CC basal lamina of the mosquito midgut is reduced resulting in 45-55%
CC fewer sporozoites in the mosquito salivary glands (PubMed:28916755). In
CC sporozoites, cell traversal activity, invasion of host hepatocytes and
CC gliding motility are severely reduced (PubMed:28916755). Also, TRAP,
CC but not CSP, protein levels are reduced and TRAP localization to the
CC cell membrane is impaired (PubMed:28916755). Development in host
CC erythrocytes and gametogenesis are normal (PubMed:28916755). However,
CC another study showed that in A.gambiae mosquito vector, number of
CC oocysts in the midgut, number of sporozoites in the salivary glands,
CC and sporozoite gliding motility are normal (PubMed:31334132). Also
CC invasion of host hepatocytes by sporozoites is normal
CC (PubMed:31334132). {ECO:0000269|PubMed:28916755,
CC ECO:0000269|PubMed:31334132}.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 68 family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=EWC88665.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; KE123806; EWC88665.1; ALT_SEQ; Genomic_DNA.
DR EnsemblProtists; EWC88665; EWC88665; PFNF54_02509.
DR OMA; YILYDVN; -.
DR UniPathway; UPA00378; -.
DR Proteomes; UP000030673; Unassembled WGS sequence.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:UniProtKB.
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 1: Evidence at protein level;
KW Carbohydrate metabolism; Endoplasmic reticulum; Fucose metabolism;
KW Reference proteome; Signal; Transferase.
FT SIGNAL 1..18
FT /evidence="ECO:0000255"
FT CHAIN 19..469
FT /note="GDP-fucose protein O-fucosyltransferase 2"
FT /evidence="ECO:0000255"
FT /id="PRO_0000455542"
FT ACT_SITE 57
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:Q9Y2G5"
FT BINDING 56..60
FT /ligand="GDP-beta-L-fucose"
FT /ligand_id="ChEBI:CHEBI:57273"
FT /evidence="ECO:0000250|UniProtKB:Q9Y2G5"
FT BINDING 277..279
FT /ligand="GDP-beta-L-fucose"
FT /ligand_id="ChEBI:CHEBI:57273"
FT /evidence="ECO:0000250|UniProtKB:Q9Y2G5"
FT BINDING 373..374
FT /ligand="GDP-beta-L-fucose"
FT /ligand_id="ChEBI:CHEBI:57273"
FT /evidence="ECO:0000250|UniProtKB:Q9Y2G5"
FT SITE 381
FT /note="Essential for catalytic activity"
FT /evidence="ECO:0000250|UniProtKB:Q9Y2G5"
SQ SEQUENCE 469 AA; 57003 MW; 9BFA0F3A5C75020C CRC64;
MKFIIVLLLF FFFKVIDRVI CVTPQKLICL KEDVYLGDFF FFLKRKKYIM YDVNIGEGFN
LQKEIFYRLS LVIYNLNKKD KINIYYLVLP PWCYVTHWNI RKGNNLRWEF FFNTDIMKKV
IPIIEYEEYE KLYGNYSDIM INSKYILDNY KEKSFLILPF EECNINVNRF KQFCKKCEHK
YNVLYSGYCT TINTKQSECY SYNMISNYFI TSILENLFLY NITSVLIKQS TNILVPFVNE
LYQSNLEDIL LFNNKLLSYG NNYISNILKT NHYISSHLRY TDFKYISRYN VPPIHIALLK
LLYIMFINNC RIIFIASDEK VEIQKVINKD FHQYKKHFYF YNNQNNLHEG EFSIIEQWIC
TRSYIFIGNI FSRFTMNINW ERHLINKGQI NQNIDLCSYH INDDNDQDIK NSYKKIVHIF
NHKALQKIKN IYDNYSDRDK KYINTICYNF LSHFPNNRSI YRKEYITNT
