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Q9Y2G5 (OFUT2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 103. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
GDP-fucose protein O-fucosyltransferase 2

EC=2.4.1.221
Alternative name(s):
Peptide-O-fucosyltransferase 2
Short name=O-FucT-2
Gene names
Name:POFUT2
Synonyms:C21orf80, FUT13, KIAA0958
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length429 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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 1 repeats where C1 and C2 are the first and second cysteines, respectively. O-fucosylates members of several protein families including the ADAMTS family, the thrombosporin (TSP) and spondin families. The 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 By similarity. Required for the proper secretion of ADAMTS family members such as ADAMSL1 and ADAMST13. Ref.7 Ref.8 Ref.9 Ref.10 Ref.11

Catalytic activity

Transfers an alpha-L-fucosyl residue from GDP-beta-L-fucose to the serine hydroxy group of a protein acceptor. Ref.11

Enzyme regulation

Inhibited by EDTA and by Zn2+. Ref.11

Pathway

Protein modification; protein glycosylation.

Subcellular location

Endoplasmic reticulum. Golgi apparatus. Note: Mainly located in the endoplasmic reticulum. Ref.1

Tissue specificity

Isoform A is expressed in fetal liver and peripheral blood lymphocytes. Isoform B is expressed in spleen, lung, testis, bone marrow, thymus, pancreas, prostate, fetal brain, fetal liver and fetal kidney. Isoform C is expressed in brain, heart, spleen, liver, lung, stomach, testis, placenta, skin, thymus, pancreas, mammary gland, prostate, fetal brain, fetal liver and fetal heart. Ref.1

Sequence similarities

Belongs to the glycosyltransferase 68 family.

Biophysicochemical properties

Kinetic parameters:

KM=9.8 µM for GDP-fucose Ref.11

Sequence caution

The sequence BAA76802.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

The sequence CAB90496.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]
Isoform C (identifier: Q9Y2G5-3)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform A (identifier: Q9Y2G5-1)

The sequence of this isoform differs from the canonical sequence as follows:
     380-429: FFIGTSVSTF...EQPTHWKITY → CLPTSLSAES...GHFHTVCLLV
Isoform B (identifier: Q9Y2G5-2)

The sequence of this isoform differs from the canonical sequence as follows:
     379-380: RF → SS
     381-429: Missing.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2121 Potential
Chain22 – 429408GDP-fucose protein O-fucosyltransferase 2
PRO_0000012154

Regions

Region53 – 564Substrate binding
Region388 – 3892Substrate binding

Sites

Active site541Proton donor/acceptor Probable
Binding site2941Substrate
Site3961Essential for catalytic activity

Amino acid modifications

Glycosylation1891N-linked (GlcNAc...) Ref.11
Glycosylation2091N-linked (GlcNAc...) Potential
Glycosylation2591N-linked (GlcNAc...) Ref.11
Disulfide bond161 ↔ 192 Ref.11
Disulfide bond412 ↔ 419 Ref.11

Natural variations

Alternative sequence379 – 3802RF → SS in isoform B.
VSP_003833
Alternative sequence380 – 42950FFIGT…WKITY → CLPTSLSAESGSGGFQRFFC PKYSVSEQMVACVHSGHFHT VCLLV in isoform A.
VSP_003832
Alternative sequence381 – 42949Missing in isoform B.
VSP_003834

Experimental info

Mutagenesis541E → A: Abolishes enzyme activity. Ref.11
Mutagenesis921W → A: Abolishes enzyme activity. Ref.11
Mutagenesis1521W → A: Reduces enzyme activity. Ref.11
Mutagenesis2731W → A: Reduces enzyme activity. Ref.11
Mutagenesis2941R → A: Abolishes enzyme activity. Ref.11
Mutagenesis2971D → A: Reduces enzyme activity. Ref.11
Mutagenesis3951E → A: No enhanced secretion of ADASMTS13; when associated with A-396. Ref.9
Mutagenesis3961E → A: Reduces enzyme activity. No enhanced secretion of ADASMTS13; when associated with A-396. Ref.9 Ref.11

Secondary structure

........................................................... 429
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform C [UniParc].

Last modified February 15, 2005. Version 3.
Checksum: 36A4213D905AFFD1

FASTA42949,976
        10         20         30         40         50         60 
MATLSFVFLL LGAVSWPPAS ASGQEFWPGQ SAADILSGAA SRRRYLLYDV NPPEGFNLRR 

        70         80         90        100        110        120 
DVYIRIASLL KTLLKTEEWV LVLPPWGRLY HWQSPDIHQV RIPWSEFFDL PSLNKNIPVI 

       130        140        150        160        170        180 
EYEQFIAESG GPFIDQVYVL QSYAEGWKEG TWEEKVDERP CIDQLLYSQD KHEYYRGWFW 

       190        200        210        220        230        240 
GYEETRGLNV SCLSVQGSAS IVAPLLLRNT SARSVMLDRA ENLLHDHYGG KEYWDTRRSM 

       250        260        270        280        290        300 
VFARHLREVG DEFRSRHLNS TDDADRIPFQ EDWMKMKVKL GSALGGPYLG VHLRRKDFIW 

       310        320        330        340        350        360 
GHRQDVPSLE GAVRKIRSLM KTHRLDKVFV ATDAVRKEYE ELKKLLPEMV RFEPTWEELE 

       370        380        390        400        410        420 
LYKDGGVAII DQWICAHARF FIGTSVSTFS FRIHEEREIL GLDPKTTYNR FCGDQEKACE 


QPTHWKITY 

« Hide

Isoform A [UniParc].

Checksum: 60BA687F0DFB8875
Show »

FASTA42448,896
Isoform B [UniParc].

Checksum: 7D640225C9A977C0
Show »

FASTA38044,083

References

« Hide 'large scale' references
[1]"The Caenorhabditis elegans ortholog of C21orf80, a potential new protein O-fucosyltransferase, is required for normal development."
Menzel O., Vellai T., Takacs-Vellai K., Reymond A., Mueller F., Antonarakis S.E., Guipponi M.
Genomics 84:320-330(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS A; B AND C), SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
[2]"A new superfamily of protein-O-fucosyltransferases, alpha2-fucosyltransferases, and alpha6-fucosyltransferases: phylogeny and identification of conserved peptide motifs."
Martinez-Duncker I., Mollicone R., Candelier J.-J., Breton C., Oriol R.
Glycobiology 13:1C-5C(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM C).
[3]"Prediction of the coding sequences of unidentified human genes. XIII. The complete sequences of 100 new cDNA clones from brain which code for large proteins in vitro."
Nagase T., Ishikawa K., Suyama M., Kikuno R., Hirosawa M., Miyajima N., Tanaka A., Kotani H., Nomura N., Ohara O.
DNA Res. 6:63-70(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM A).
Tissue: Brain.
[4]"The full-ORF clone resource of the German cDNA consortium."
Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., Wiemann S., Schupp I.
BMC Genomics 8:399-399(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM B).
Tissue: Testis.
[5]"The DNA sequence of human chromosome 21."
Hattori M., Fujiyama A., Taylor T.D., Watanabe H., Yada T., Park H.-S., Toyoda A., Ishii K., Totoki Y., Choi D.-K., Groner Y., Soeda E., Ohki M., Takagi T., Sakaki Y., Taudien S., Blechschmidt K., Polley A. expand/collapse author list , Menzel U., Delabar J., Kumpf K., Lehmann R., Patterson D., Reichwald K., Rump A., Schillhabel M., Schudy A., Zimmermann W., Rosenthal A., Kudoh J., Shibuya K., Kawasaki K., Asakawa S., Shintani A., Sasaki T., Nagamine K., Mitsuyama S., Antonarakis S.E., Minoshima S., Shimizu N., Nordsiek G., Hornischer K., Brandt P., Scharfe M., Schoen O., Desario A., Reichelt J., Kauer G., Bloecker H., Ramser J., Beck A., Klages S., Hennig S., Riesselmann L., Dagand E., Wehrmeyer S., Borzym K., Gardiner K., Nizetic D., Francis F., Lehrach H., Reinhardt R., Yaspo M.-L.
Nature 405:311-319(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS B AND C).
Tissue: Brain.
[7]"C-mannosylation and O-fucosylation of the thrombospondin type 1 module."
Hofsteenge J., Huwiler K.G., Macek B., Hess D., Lawler J., Mosher D.F., Peter-Katalinic J.
J. Biol. Chem. 276:6485-6498(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[8]"Two distinct pathways for O-fucosylation of epidermal growth factor-like or thrombospondin type 1 repeats."
Luo Y., Nita-Lazar A., Haltiwanger R.S.
J. Biol. Chem. 281:9385-9392(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[9]"O-fucosylation is required for ADAMTS13 secretion."
Ricketts L.M., Dlugosz M., Luther K.B., Haltiwanger R.S., Majerus E.M.
J. Biol. Chem. 282:17014-17023(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, MUTAGENESIS OF GLU-395 AND GLU-396.
[10]"O-fucosylation of thrombospondin type 1 repeats in ADAMTS-like-1/punctin-1 regulates secretion: implications for the ADAMTS superfamily."
Wang L.W., Dlugosz M., Somerville R.P., Raed M., Haltiwanger R.S., Apte S.S.
J. Biol. Chem. 282:17024-17031(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[11]"Structure of human POFUT2: insights into thrombospondin type 1 repeat fold and O-fucosylation."
Chen C.I., Keusch J.J., Klein D., Hess D., Hofsteenge J., Gut H.
EMBO J. 31:3183-3197(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) OF 22-429 IN COMPLEX WITH GDP-FUCOSE, FUNCTION, CATALYTIC ACTIVITY, ENZYME REGULATION, BIOPHYSICOCHEMICAL PROPERTIES, MUTAGENESIS OF GLU-54; TRP-92; TRP-152; TRP-273; ARG-294; ASP-297 AND GLU-396, GLYCOSYLATION AT ASN-189 AND ASN-259, DISULFIDE BONDS.
+Additional computationally mapped references.

Web resources

GGDB

GlycoGene database

Functional Glycomics Gateway - GTase

Peptide-O-fucosyltransferase 2

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AJ302080 mRNA. Translation: CAC24557.1.
AJ302079 mRNA. Translation: CAC24556.1.
AY066015 mRNA. Translation: AAL47681.2.
AJ575591 mRNA. Translation: CAE01472.1.
AB023175 mRNA. Translation: BAA76802.1. Different initiation.
AL110285 mRNA. Translation: CAB53715.2.
AL163301 Genomic DNA. Translation: CAB90496.1. Different initiation.
BC011044 mRNA. Translation: AAH11044.1.
BC064623 mRNA. Translation: AAH64623.1.
RefSeqNP_056042.1. NM_015227.4.
NP_598368.2. NM_133635.4.
UniGeneHs.592164.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
4AP5X-ray3.00A/B22-429[»]
4AP6X-ray3.40A/B/C/D37-429[»]
ProteinModelPortalQ9Y2G5.
SMRQ9Y2G5. Positions 41-429.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid116876. 2 interactions.
IntActQ9Y2G5. 3 interactions.
STRING9606.ENSP00000339613.

Protein family/group databases

CAZyGT68. Glycosyltransferase Family 68.

PTM databases

PhosphoSiteQ9Y2G5.

Polymorphism databases

DMDM59803123.

Proteomic databases

PaxDbQ9Y2G5.
PRIDEQ9Y2G5.

Protocols and materials databases

DNASU23275.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000331343; ENSP00000329682; ENSG00000186866. [Q9Y2G5-1]
ENST00000334538; ENSP00000335427; ENSG00000186866. [Q9Y2G5-2]
ENST00000349485; ENSP00000339613; ENSG00000186866. [Q9Y2G5-3]
GeneID23275.
KEGGhsa:23275.
UCSCuc002zhc.3. human. [Q9Y2G5-3]
uc002zhd.3. human. [Q9Y2G5-1]

Organism-specific databases

CTD23275.
GeneCardsGC21M046683.
HGNCHGNC:14683. POFUT2.
HPAHPA044297.
MIM610249. gene.
neXtProtNX_Q9Y2G5.
PharmGKBPA25867.
HUGESearch...
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG77810.
HOVERGENHBG053367.
InParanoidQ9Y2G5.
KOK03691.
OMAICAHARF.
OrthoDBEOG76T9S1.
PhylomeDBQ9Y2G5.
TreeFamTF314337.

Enzyme and pathway databases

UniPathwayUPA00378.

Gene expression databases

ArrayExpressQ9Y2G5.
BgeeQ9Y2G5.
CleanExHS_POFUT2.
GenevestigatorQ9Y2G5.

Family and domain databases

InterProIPR019378. GDP-Fuc_O-FucTrfase.
[Graphical view]
PfamPF10250. O-FucT. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

GenomeRNAi23275.
NextBio45054.
PROQ9Y2G5.
SOURCESearch...

Entry information

Entry nameOFUT2_HUMAN
AccessionPrimary (citable) accession number: Q9Y2G5
Secondary accession number(s): Q6PJV1 expand/collapse secondary AC list , Q7Z4N0, Q8WWU6, Q9BQS4, Q9BQS5, Q9UFY3
Entry history
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: February 15, 2005
Last modified: April 16, 2014
This is version 103 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

PATHWAY comments

Index of metabolic and biosynthesis pathways

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human chromosome 21

Human chromosome 21: entries, gene names and cross-references to MIM