OFUT2_PANTR
ID OFUT2_PANTR Reviewed; 429 AA.
AC Q6EV56;
DT 15-FEB-2005, integrated into UniProtKB/Swiss-Prot.
DT 16-AUG-2004, sequence version 1.
DT 03-AUG-2022, entry version 92.
DE RecName: Full=GDP-fucose protein O-fucosyltransferase 2;
DE EC=2.4.1.221 {ECO:0000250|UniProtKB:Q9Y2G5};
DE AltName: Full=Peptide-O-fucosyltransferase 2;
DE Short=O-FucT-2;
DE Flags: Precursor;
GN Name=POFUT2; Synonyms=FUT13;
OS Pan troglodytes (Chimpanzee).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pan.
OX NCBI_TaxID=9598;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=12966037; DOI=10.1093/glycob/cwg113;
RA Martinez-Duncker I., Mollicone R., Candelier J.-J., Breton C., Oriol R.;
RT "A new superfamily of protein-O-fucosyltransferases, alpha2-
RT fucosyltransferases, and alpha6-fucosyltransferases: phylogeny and
RT identification of conserved peptide motifs.";
RL Glycobiology 13:1C-5C(2003).
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. O-fucosylates members of several protein families
CC including the ADAMTS, the thrombospondin (TSP) and spondin families.
CC Required for the proper secretion of ADAMTS family members such as
CC ADAMTSL1 and ADAMTS13 (By similarity). The O-fucosylation of TSRs is
CC also required for restricting epithelial to mesenchymal transition
CC (EMT), maintaining the correct patterning of mesoderm and localization
CC of the definite endoderm (By similarity).
CC {ECO:0000250|UniProtKB:Q8VHI3, ECO:0000250|UniProtKB:Q9Y2G5}.
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:Q9Y2G5};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:63645;
CC Evidence={ECO:0000250|UniProtKB:Q9Y2G5};
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:Q9Y2G5};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:70492;
CC Evidence={ECO:0000250|UniProtKB:Q9Y2G5};
CC -!- PATHWAY: Protein modification; protein glycosylation.
CC {ECO:0000250|UniProtKB:Q9Y2G5}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum
CC {ECO:0000250|UniProtKB:Q9Y2G5}. Golgi apparatus
CC {ECO:0000250|UniProtKB:Q9Y2G5}. Note=Mainly located in the endoplasmic
CC reticulum. {ECO:0000250|UniProtKB:Q9Y2G5}.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 68 family.
CC {ECO:0000305}.
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DR EMBL; AJ781756; CAH03731.1; -; mRNA.
DR RefSeq; NP_001008983.1; NM_001008983.1.
DR AlphaFoldDB; Q6EV56; -.
DR SMR; Q6EV56; -.
DR STRING; 9598.ENSPTRP00000024102; -.
DR CAZy; GT68; Glycosyltransferase Family 68.
DR PaxDb; Q6EV56; -.
DR GeneID; 449505; -.
DR KEGG; ptr:449505; -.
DR CTD; 23275; -.
DR eggNOG; ENOG502QPS6; Eukaryota.
DR HOGENOM; CLU_033856_0_0_1; -.
DR InParanoid; Q6EV56; -.
DR OrthoDB; 654070at2759; -.
DR TreeFam; TF314337; -.
DR UniPathway; UPA00378; -.
DR Proteomes; UP000002277; Unplaced.
DR GO; GO:0005783; C:endoplasmic reticulum; IEA:UniProtKB-SubCell.
DR GO; GO:0005794; C:Golgi apparatus; IEA:UniProtKB-SubCell.
DR GO; GO:0046922; F:peptide-O-fucosyltransferase activity; ISS:UniProtKB.
DR GO; GO:0006004; P:fucose metabolic process; IEA:UniProtKB-KW.
DR GO; GO:0036066; P:protein O-linked fucosylation; ISS: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 2: Evidence at transcript level;
KW Carbohydrate metabolism; Disulfide bond; Endoplasmic reticulum;
KW Fucose metabolism; Glycoprotein; Glycosyltransferase; Golgi apparatus;
KW Reference proteome; Signal; Transferase.
FT SIGNAL 1..21
FT /evidence="ECO:0000255"
FT CHAIN 22..429
FT /note="GDP-fucose protein O-fucosyltransferase 2"
FT /id="PRO_0000012156"
FT ACT_SITE 54
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:Q9Y2G5"
FT BINDING 53..57
FT /ligand="GDP-beta-L-fucose"
FT /ligand_id="ChEBI:CHEBI:57273"
FT /evidence="ECO:0000250|UniProtKB:Q9Y2G5"
FT BINDING 292..294
FT /ligand="GDP-beta-L-fucose"
FT /ligand_id="ChEBI:CHEBI:57273"
FT /evidence="ECO:0000250|UniProtKB:Q9Y2G5"
FT BINDING 371
FT /ligand="GDP-beta-L-fucose"
FT /ligand_id="ChEBI:CHEBI:57273"
FT /evidence="ECO:0000250|UniProtKB:Q9Y2G5"
FT BINDING 388..389
FT /ligand="GDP-beta-L-fucose"
FT /ligand_id="ChEBI:CHEBI:57273"
FT /evidence="ECO:0000250|UniProtKB:Q9Y2G5"
FT SITE 396
FT /note="Essential for catalytic activity"
FT /evidence="ECO:0000250|UniProtKB:Q9Y2G5"
FT CARBOHYD 189
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 209
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 259
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 161..192
FT /evidence="ECO:0000250|UniProtKB:Q9Y2G5"
FT DISULFID 412..419
FT /evidence="ECO:0000250|UniProtKB:Q9Y2G5"
SQ SEQUENCE 429 AA; 49847 MW; 77A3635BD4698983 CRC64;
MATLSFVFLL LGAVSWPPAS ASGQEFWPGQ SAADILSGAA SRRRYLLYDV NPPEGFNLRR
DVYIRIASLL KTLLKTEEWV LVLPPWGRLY HWQSPDIHQV RIPWSEFFDL PSLNKNIPVI
EYEQFIAESG GPFIDQVYVL QSYAEGWKEG TWEEKVDERP CIDQLLYSQD KHEYYRGWFW
GYEETRGLNV SCLSVQGSAS IVAPLLLRNT SARSVMLDRA ENLLHDHYGG KEYWDTRRSM
VFARHLREVG DEFRSRHLNS TDDADGIPFQ EDWTKMKVKL GSALGGPYLG VHLRRKDFIW
GHRQDVPSLE GAVRKIRSLM KTHRLDKVFV ATDAVRKEYE ELKKLLPEMV RFEPTWEELE
LYKDGGVAII DQWICAHARF FIGTSVSTFS FRIHEEREIL GLDPKTTYNR FCGDQEKACE
QPTHWKITY
