CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-018205
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 GDP-fucose protein O-fucosyltransferase 2 
Protein Synonyms/Alias
 Peptide-O-fucosyltransferase 2; O-FucT-2 
Gene Name
 Pofut2 
Gene Synonyms/Alias
  
Created Date
 July 27, 2013 
Organism
 Mus musculus (Mouse) 
NCBI Taxa ID
 10090 
Lysine Modification
Position
Peptide
Type
References
71IRVASLLKTLLKTEEacetylation[1]
171PLLYSQDKHEYYRGWacetylation[1]
417RFCGDQEKACEQPTHacetylation[1]
Reference
 [1] Quantitative acetylome analysis reveals the roles of SIRT1 in regulating diverse substrates and cellular pathways.
 Chen Y, Zhao W, Yang JS, Cheng Z, Luo H, Lu Z, Tan M, Gu W, Zhao Y.
 Mol Cell Proteomics. 2012 Oct;11(10):1048-62. [PMID: 22826441
Functional Description
 Catalyzes the reaction that attaches fucose through an O-glycosidic linkage to a conserved serine or threonine residue in the consensus sequence C1-X(2,3)-S/T-C2-X(2)-G of thrombospondin type I repeats (TSRs) where C1 and C2 are the first and second cysteines of the repeat, respectively. O-fucosylates members of several protein families including the ADAMTS superfamily and the thrombosporin (TSP) and spondin families. Required for the proper secretion of ADAMTS family members such as ADAMSL1 and ADAMST13 (By similarity). O-fucosylation of TSRs is also required for restricting epithelial to mesenchymal transition (EMT), maintaining the correct patterning of mesoderm and localization of the definite endoderm. 
Sequence Annotation
 REGION 53 56 Substrate binding (By similarity).
 REGION 388 389 Substrate binding (By similarity).
 ACT_SITE 54 54 Proton donor/acceptor (By similarity).
 BINDING 294 294 Substrate (By similarity).
 CARBOHYD 189 189 N-linked (GlcNAc...) (Potential).
 CARBOHYD 209 209 N-linked (GlcNAc...) (Potential).
 CARBOHYD 259 259 N-linked (GlcNAc...) (Potential).
 DISULFID 161 192 By similarity.
 DISULFID 412 419 By similarity.  
Keyword
 Carbohydrate metabolism; Complete proteome; Disulfide bond; Endoplasmic reticulum; Fucose metabolism; Glycoprotein; Glycosyltransferase; Golgi apparatus; Reference proteome; Signal; Transferase. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 429 AA 
Protein Sequence
MAALSVVCLL LAAASWRPVS ASGEEFWPGQ SAADILSGAA SRRRYLLYDV NPPEGFNLRR 60
DVYIRVASLL KTLLKTEEWV LVLPPWGRLY HWQSPDIHQV RIPWSEFFDL PSLNKNIPVI 120
EYEQFIAESG GPFIDQVYVL QGYAEGWKEG TWEEKVDARP CIDPLLYSQD KHEYYRGWFW 180
GYEETRGLNV SCLSVQGSAS IVAPVLLKNT SARSVMLDRA ENLLHDHYGG REYWDTRRSM 240
VFAKHLRAVG DEFRSQHLNS TDAADKMAPE EDWTKMKVKL GSALGGPYLG VHLRRKDFIW 300
GHREDVPSLE GAVKKIRSLM KTHQLDKVFV ATDAIRKEQE ELRKLLPEMV RFEPTWEELE 360
LYKDGGVAII DQWICAHARF FIGTSVSTFS FRIHEEREIL GLDPKTTYNR FCGDQEKACE 420
QPTHWKIAY 429 
Gene Ontology
 GO:0005783; C:endoplasmic reticulum; IEA:UniProtKB-SubCell.
 GO:0005794; C:Golgi apparatus; IEA:UniProtKB-SubCell.
 GO:0046922; F:peptide-O-fucosyltransferase activity; ISS:UniProtKB.
 GO:0006004; P:fucose metabolic process; IEA:UniProtKB-KW.
 GO:0001707; P:mesoderm formation; IMP:MGI.
 GO:0010717; P:regulation of epithelial to mesenchymal transition; IMP:MGI.
 GO:0010468; P:regulation of gene expression; IMP:MGI.
 GO:0051046; P:regulation of secretion; IEA:Compara. 
Interpro
 IPR019378; GDP-Fuc_O-FucTrfase. 
Pfam
 PF10250; O-FucT 
SMART
  
PROSITE
  
PRINTS