ID A0A914BQB7_PATMI Unreviewed; 444 AA.
AC A0A914BQB7;
DT 22-FEB-2023, integrated into UniProtKB/TrEMBL.
DT 22-FEB-2023, sequence version 1.
DT 28-JAN-2026, entry version 12.
DE RecName: Full=GDP-fucose protein O-fucosyltransferase 2 {ECO:0000256|ARBA:ARBA00026232};
DE EC=2.4.1.221 {ECO:0000256|ARBA:ARBA00012196};
DE AltName: Full=Peptide-O-fucosyltransferase 2 {ECO:0000256|ARBA:ARBA00033083};
OS Patiria miniata (Bat star) (Asterina miniata).
OC Eukaryota; Metazoa; Echinodermata; Eleutherozoa; Asterozoa; Asteroidea;
OC Valvatacea; Valvatida; Asterinidae; Patiria.
OX NCBI_TaxID=46514 {ECO:0000313|EnsemblMetazoa:XP_038078344.1, ECO:0000313|Proteomes:UP000887568};
RN [1] {ECO:0000313|EnsemblMetazoa:XP_038078344.1}
RP IDENTIFICATION.
RG EnsemblMetazoa;
RL Submitted (NOV-2022) to UniProtKB.
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. The O-fucosylation of TSRs is also required for
CC restricting epithelial to mesenchymal transition (EMT), maintaining the
CC correct patterning of mesoderm and localization of the definite
CC endoderm. {ECO:0000256|ARBA:ARBA00057700}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-seryl-[protein] + GDP-beta-L-fucose = 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:0000256|ARBA:ARBA00048647};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:63645;
CC Evidence={ECO:0000256|ARBA:ARBA00048647};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-threonyl-[protein] + GDP-beta-L-fucose = 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:0000256|ARBA:ARBA00047273};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:70492;
CC Evidence={ECO:0000256|ARBA:ARBA00047273};
CC -!- PATHWAY: Protein modification; protein glycosylation.
CC {ECO:0000256|ARBA:ARBA00004922}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum
CC {ECO:0000256|ARBA:ARBA00004240}. Golgi apparatus
CC {ECO:0000256|ARBA:ARBA00004555}.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 68 family.
CC {ECO:0000256|ARBA:ARBA00025803}.
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DR RefSeq; XP_038078344.1; XM_038222416.1.
DR AlphaFoldDB; A0A914BQB7; -.
DR EnsemblMetazoa; XM_038222416.1; XP_038078344.1; LOC119745805.
DR GeneID; 119745805; -.
DR CTD; 23275; -.
DR OrthoDB; 422368at2759; -.
DR Proteomes; UP000887568; Unplaced.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-ARBA.
DR GO; GO:0005794; C:Golgi apparatus; IEA:UniProtKB-SubCell.
DR GO; GO:0046922; F:peptide-O-fucosyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0006004; P:fucose metabolic process; IEA:UniProtKB-KW.
DR CDD; cd11298; O-FucT-2; 1.
DR FunFam; 3.40.50.11340:FF:000002; GDP-fucose protein O-fucosyltransferase 2; 1.
DR FunFam; 3.40.50.11350:FF:000002; GDP-fucose protein O-fucosyltransferase 2; 1.
DR Gene3D; 3.40.50.11340; -; 1.
DR Gene3D; 3.40.50.11350; -; 1.
DR InterPro; IPR019378; GDP-Fuc_O-FucTrfase.
DR InterPro; IPR045130; OFUT2-like.
DR PANTHER; PTHR13398; GDP-FUCOSE PROTEIN O-FUCOSYLTRANSFERASE 2; 1.
DR PANTHER; PTHR13398:SF0; GDP-FUCOSE PROTEIN O-FUCOSYLTRANSFERASE 2; 1.
DR Pfam; PF10250; O-FucT; 1.
PE 3: Inferred from homology;
KW Carbohydrate metabolism {ECO:0000256|ARBA:ARBA00023277};
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW Endoplasmic reticulum {ECO:0000256|ARBA:ARBA00022824};
KW Fucose metabolism {ECO:0000256|ARBA:ARBA00023253};
KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Glycosyltransferase {ECO:0000256|ARBA:ARBA00022676};
KW Golgi apparatus {ECO:0000256|ARBA:ARBA00023034};
KW Reference proteome {ECO:0000313|Proteomes:UP000887568};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT SIGNAL 1..24
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 25..444
FT /note="GDP-fucose protein O-fucosyltransferase 2"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5036712095"
SQ SEQUENCE 444 AA; 51973 MW; 018E06F5DFE804EF CRC64;
MAAHRRFVVC VVLVLCSHCL KTECSLDTEA DLSDDIVFQS GSHQTLKVGP AIPRRYLLYH
VNHGEGFNLR RDVYMRIANL VQRLQQDGDW VLVLPPWGRL YHWRTRSLEQ IRIPWATFFD
VESLNRYIPV IEFEDFIKET GQAAIDQILY LQAYKEGWTN GKWEEKIDER ECIEPPAYRL
DEAGVFRGWF WGYPDAYAKA FKCLSVQGMA RILAPVLLNN FTARSVFVDR GEKVMHDRFG
DVSYWTVRRS MRFAKHLRDI GDEFRESKLE STDEKDKTVM TDNWRDMERK PGSAIGGPYL
AAHLRREDFA RNNRKEVPTL ERAADQIKVA LKKYKLEKVF VATDAPKHEI EELRRHLQDY
QVYNYVPPKG VLENFKDGGV AIIDQWICAH ARYFIGTGVS TFSFRIHEER QILGFDTKMT
YNRFCGHSEP EDCEQPSVWK IVYH
//
