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GDP-fucose protein O-fucosyltransferase 2 (EC 2.4.1.221) (Peptide-O-fucosyltransferase 2) (O-FucT-2)

 OFUT2_HUMAN             Reviewed;         429 AA.
Q9Y2G5; Q6PJV1; Q7Z4N0; Q8WWU6; Q9BQS4; Q9BQS5; Q9UFY3;
30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
15-FEB-2005, sequence version 3.
25-OCT-2017, entry version 129.
RecName: Full=GDP-fucose protein O-fucosyltransferase 2;
EC=2.4.1.221;
AltName: Full=Peptide-O-fucosyltransferase 2;
Short=O-FucT-2;
Flags: Precursor;
Name=POFUT2; Synonyms=C21orf80, FUT13, KIAA0958;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS A; B AND C), SUBCELLULAR
LOCATION, AND TISSUE SPECIFICITY.
PubMed=15233996; DOI=10.1016/j.ygeno.2004.04.002;
Menzel O., Vellai T., Takacs-Vellai K., Reymond A., Mueller F.,
Antonarakis S.E., Guipponi M.;
"The Caenorhabditis elegans ortholog of C21orf80, a potential new
protein O-fucosyltransferase, is required for normal development.";
Genomics 84:320-330(2004).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM C).
PubMed=12966037; DOI=10.1093/glycob/cwg113;
Martinez-Duncker I., Mollicone R., Candelier J.-J., Breton C.,
Oriol R.;
"A new superfamily of protein-O-fucosyltransferases, alpha2-
fucosyltransferases, and alpha6-fucosyltransferases: phylogeny and
identification of conserved peptide motifs.";
Glycobiology 13:1C-5C(2003).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM A).
TISSUE=Brain;
PubMed=10231032; DOI=10.1093/dnares/6.1.63;
Nagase T., Ishikawa K., Suyama M., Kikuno R., Hirosawa M.,
Miyajima N., Tanaka A., Kotani H., Nomura N., Ohara O.;
"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.";
DNA Res. 6:63-70(1999).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM B).
TISSUE=Testis;
PubMed=17974005; DOI=10.1186/1471-2164-8-399;
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.;
"The full-ORF clone resource of the German cDNA consortium.";
BMC Genomics 8:399-399(2007).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=10830953; DOI=10.1038/35012518;
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., 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.;
"The DNA sequence of human chromosome 21.";
Nature 405:311-319(2000).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS B AND C).
TISSUE=Brain;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[7]
FUNCTION.
PubMed=11067851; DOI=10.1074/jbc.M008073200;
Hofsteenge J., Huwiler K.G., Macek B., Hess D., Lawler J.,
Mosher D.F., Peter-Katalinic J.;
"C-mannosylation and O-fucosylation of the thrombospondin type 1
module.";
J. Biol. Chem. 276:6485-6498(2001).
[8]
FUNCTION.
PubMed=16464858; DOI=10.1074/jbc.M511974200;
Luo Y., Nita-Lazar A., Haltiwanger R.S.;
"Two distinct pathways for O-fucosylation of epidermal growth factor-
like or thrombospondin type 1 repeats.";
J. Biol. Chem. 281:9385-9392(2006).
[9]
FUNCTION, AND MUTAGENESIS OF GLU-395 AND GLU-396.
PubMed=17395589; DOI=10.1074/jbc.M700317200;
Ricketts L.M., Dlugosz M., Luther K.B., Haltiwanger R.S.,
Majerus E.M.;
"O-fucosylation is required for ADAMTS13 secretion.";
J. Biol. Chem. 282:17014-17023(2007).
[10]
FUNCTION.
PubMed=17395588; DOI=10.1074/jbc.M701065200;
Wang L.W., Dlugosz M., Somerville R.P., Raed M., Haltiwanger R.S.,
Apte S.S.;
"O-fucosylation of thrombospondin type 1 repeats in ADAMTS-like-
1/punctin-1 regulates secretion: implications for the ADAMTS
superfamily.";
J. Biol. Chem. 282:17024-17031(2007).
[11]
CLEAVAGE OF SIGNAL PEPTIDE [LARGE SCALE ANALYSIS] AFTER ALA-21, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=25944712; DOI=10.1002/pmic.201400617;
Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M.,
Ayoub D., Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
"N-terminome analysis of the human mitochondrial proteome.";
Proteomics 15:2519-2524(2015).
[12]
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, AND DISULFIDE BONDS.
PubMed=22588082; DOI=10.1038/emboj.2012.143;
Chen C.I., Keusch J.J., Klein D., Hess D., Hofsteenge J., Gut H.;
"Structure of human POFUT2: insights into thrombospondin type 1 repeat
fold and O-fucosylation.";
EMBO J. 31:3183-3197(2012).
-!- 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.
{ECO:0000250, ECO:0000269|PubMed:11067851,
ECO:0000269|PubMed:16464858, ECO:0000269|PubMed:17395588,
ECO:0000269|PubMed:17395589, ECO:0000269|PubMed:22588082}.
-!- CATALYTIC ACTIVITY: Transfers an alpha-L-fucosyl residue from GDP-
beta-L-fucose to the serine hydroxy group of a protein acceptor.
{ECO:0000269|PubMed:22588082}.
-!- ENZYME REGULATION: Inhibited by EDTA and by Zn(2+).
{ECO:0000269|PubMed:22588082}.
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Kinetic parameters:
KM=9.8 uM for GDP-fucose {ECO:0000269|PubMed:22588082};
-!- PATHWAY: Protein modification; protein glycosylation.
-!- SUBCELLULAR LOCATION: Endoplasmic reticulum
{ECO:0000269|PubMed:15233996}. Golgi apparatus
{ECO:0000269|PubMed:15233996}. Note=Mainly located in the
endoplasmic reticulum.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=3;
Name=C;
IsoId=Q9Y2G5-3; Sequence=Displayed;
Name=A;
IsoId=Q9Y2G5-1; Sequence=VSP_003832;
Name=B;
IsoId=Q9Y2G5-2; Sequence=VSP_003833, VSP_003834;
-!- 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. {ECO:0000269|PubMed:15233996}.
-!- SIMILARITY: Belongs to the glycosyltransferase 68 family.
{ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=BAA76802.1; Type=Erroneous initiation; Note=Translation N-terminally shortened.; Evidence={ECO:0000305};
Sequence=CAB90496.1; Type=Erroneous initiation; Note=Translation N-terminally shortened.; Evidence={ECO:0000305};
-!- WEB RESOURCE: Name=Functional Glycomics Gateway - GTase;
Note=Peptide-O-fucosyltransferase 2;
URL="http://www.functionalglycomics.org/glycomics/molecule/jsp/glycoEnzyme/viewGlycoEnzyme.jsp?gbpId=gt_hum_610";
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EMBL; AJ302080; CAC24557.1; -; mRNA.
EMBL; AJ302079; CAC24556.1; -; mRNA.
EMBL; AY066015; AAL47681.2; -; mRNA.
EMBL; AJ575591; CAE01472.1; -; mRNA.
EMBL; AB023175; BAA76802.1; ALT_INIT; mRNA.
EMBL; AL110285; CAB53715.2; -; mRNA.
EMBL; AL163301; CAB90496.1; ALT_INIT; Genomic_DNA.
EMBL; BC011044; AAH11044.1; -; mRNA.
EMBL; BC064623; AAH64623.1; -; mRNA.
CCDS; CCDS13719.1; -. [Q9Y2G5-3]
CCDS; CCDS13721.1; -. [Q9Y2G5-1]
RefSeq; NP_056042.1; NM_015227.4. [Q9Y2G5-1]
RefSeq; NP_598368.2; NM_133635.4. [Q9Y2G5-3]
UniGene; Hs.592164; -.
PDB; 4AP5; X-ray; 3.00 A; A/B=22-429.
PDB; 4AP6; X-ray; 3.40 A; A/B/C/D=37-429.
PDBsum; 4AP5; -.
PDBsum; 4AP6; -.
ProteinModelPortal; Q9Y2G5; -.
SMR; Q9Y2G5; -.
BioGrid; 116876; 1.
IntAct; Q9Y2G5; 4.
STRING; 9606.ENSP00000339613; -.
CAZy; GT68; Glycosyltransferase Family 68.
iPTMnet; Q9Y2G5; -.
PhosphoSitePlus; Q9Y2G5; -.
BioMuta; POFUT2; -.
DMDM; 59803123; -.
EPD; Q9Y2G5; -.
MaxQB; Q9Y2G5; -.
PaxDb; Q9Y2G5; -.
PeptideAtlas; Q9Y2G5; -.
PRIDE; Q9Y2G5; -.
DNASU; 23275; -.
Ensembl; ENST00000331343; ENSP00000329682; ENSG00000186866. [Q9Y2G5-1]
Ensembl; ENST00000334538; ENSP00000335427; ENSG00000186866. [Q9Y2G5-2]
Ensembl; ENST00000349485; ENSP00000339613; ENSG00000186866. [Q9Y2G5-3]
GeneID; 23275; -.
KEGG; hsa:23275; -.
UCSC; uc002zhb.4; human. [Q9Y2G5-3]
CTD; 23275; -.
DisGeNET; 23275; -.
EuPathDB; HostDB:ENSG00000186866.16; -.
GeneCards; POFUT2; -.
HGNC; HGNC:14683; POFUT2.
HPA; HPA044297; -.
MIM; 610249; gene.
neXtProt; NX_Q9Y2G5; -.
OpenTargets; ENSG00000186866; -.
PharmGKB; PA25867; -.
eggNOG; ENOG410IFPR; Eukaryota.
eggNOG; ENOG410Y78N; LUCA.
GeneTree; ENSGT00390000007989; -.
HOVERGEN; HBG053367; -.
InParanoid; Q9Y2G5; -.
KO; K03691; -.
OMA; YILYDVN; -.
OrthoDB; EOG091G13P1; -.
PhylomeDB; Q9Y2G5; -.
TreeFam; TF314337; -.
BRENDA; 2.4.1.221; 2681.
Reactome; R-HSA-5173214; O-glycosylation of TSR domain-containing proteins.
UniPathway; UPA00378; -.
GenomeRNAi; 23275; -.
PRO; PR:Q9Y2G5; -.
Proteomes; UP000005640; Chromosome 21.
Bgee; ENSG00000186866; -.
CleanEx; HS_POFUT2; -.
ExpressionAtlas; Q9Y2G5; baseline and differential.
Genevisible; Q9Y2G5; HS.
GO; GO:0005789; C:endoplasmic reticulum membrane; TAS:Reactome.
GO; GO:0005794; C:Golgi apparatus; IDA:UniProtKB.
GO; GO:0046922; F:peptide-O-fucosyltransferase activity; IDA:UniProtKB.
GO; GO:0006004; P:fucose metabolic process; IEA:UniProtKB-KW.
GO; GO:0001707; P:mesoderm formation; IEA:Ensembl.
GO; GO:0036066; P:protein O-linked fucosylation; IDA:UniProtKB.
GO; GO:0010717; P:regulation of epithelial to mesenchymal transition; IEA:Ensembl.
GO; GO:0010468; P:regulation of gene expression; IEA:Ensembl.
GO; GO:0051046; P:regulation of secretion; IDA:UniProtKB.
InterPro; IPR019378; GDP-Fuc_O-FucTrfase.
Pfam; PF10250; O-FucT; 1.
1: Evidence at protein level;
3D-structure; Alternative splicing; Carbohydrate metabolism;
Complete proteome; Disulfide bond; Endoplasmic reticulum;
Fucose metabolism; Glycoprotein; Glycosyltransferase; Golgi apparatus;
Reference proteome; Signal; Transferase.
SIGNAL 1 21 {ECO:0000244|PubMed:25944712,
ECO:0000255}.
CHAIN 22 429 GDP-fucose protein O-fucosyltransferase
2.
/FTId=PRO_0000012154.
REGION 53 57 Substrate binding.
{ECO:0000244|PDB:4AP6}.
REGION 292 294 Substrate binding.
{ECO:0000244|PDB:4AP6}.
REGION 388 389 Substrate binding.
{ECO:0000244|PDB:4AP6}.
ACT_SITE 54 54 Proton donor/acceptor. {ECO:0000305}.
BINDING 371 371 Substrate. {ECO:0000244|PDB:4AP6}.
SITE 396 396 Essential for catalytic activity.
CARBOHYD 189 189 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:22588082}.
CARBOHYD 209 209 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 259 259 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:22588082}.
DISULFID 161 192 {ECO:0000269|PubMed:22588082}.
DISULFID 412 419 {ECO:0000269|PubMed:22588082}.
VAR_SEQ 379 380 RF -> SS (in isoform B).
{ECO:0000303|PubMed:15233996,
ECO:0000303|PubMed:15489334,
ECO:0000303|PubMed:17974005}.
/FTId=VSP_003833.
VAR_SEQ 380 429 FFIGTSVSTFSFRIHEEREILGLDPKTTYNRFCGDQEKACE
QPTHWKITY -> CLPTSLSAESGSGGFQRFFCPKYSVSEQ
MVACVHSGHFHTVCLLV (in isoform A).
{ECO:0000303|PubMed:10231032,
ECO:0000303|PubMed:15233996}.
/FTId=VSP_003832.
VAR_SEQ 381 429 Missing (in isoform B).
{ECO:0000303|PubMed:15233996,
ECO:0000303|PubMed:15489334,
ECO:0000303|PubMed:17974005}.
/FTId=VSP_003834.
MUTAGEN 54 54 E->A: Abolishes enzyme activity.
{ECO:0000269|PubMed:22588082}.
MUTAGEN 92 92 W->A: Abolishes enzyme activity.
{ECO:0000269|PubMed:22588082}.
MUTAGEN 152 152 W->A: Reduces enzyme activity.
{ECO:0000269|PubMed:22588082}.
MUTAGEN 273 273 W->A: Reduces enzyme activity.
{ECO:0000269|PubMed:22588082}.
MUTAGEN 294 294 R->A: Abolishes enzyme activity.
{ECO:0000269|PubMed:22588082}.
MUTAGEN 297 297 D->A: Reduces enzyme activity.
{ECO:0000269|PubMed:22588082}.
MUTAGEN 395 395 E->A: No enhanced secretion of ADASMTS13;
when associated with A-396.
{ECO:0000269|PubMed:17395589}.
MUTAGEN 396 396 E->A: Reduces enzyme activity. No
enhanced secretion of ADASMTS13; when
associated with A-396.
{ECO:0000269|PubMed:17395589,
ECO:0000269|PubMed:22588082}.
STRAND 44 48 {ECO:0000244|PDB:4AP5}.
HELIX 56 74 {ECO:0000244|PDB:4AP5}.
STRAND 79 83 {ECO:0000244|PDB:4AP5}.
HELIX 91 93 {ECO:0000244|PDB:4AP5}.
HELIX 104 106 {ECO:0000244|PDB:4AP5}.
HELIX 110 114 {ECO:0000244|PDB:4AP5}.
STRAND 119 121 {ECO:0000244|PDB:4AP5}.
HELIX 122 128 {ECO:0000244|PDB:4AP5}.
STRAND 129 141 {ECO:0000244|PDB:4AP5}.
STRAND 156 159 {ECO:0000244|PDB:4AP5}.
HELIX 179 181 {ECO:0000244|PDB:4AP5}.
STRAND 186 195 {ECO:0000244|PDB:4AP5}.
HELIX 199 202 {ECO:0000244|PDB:4AP5}.
HELIX 203 208 {ECO:0000244|PDB:4AP5}.
STRAND 213 219 {ECO:0000244|PDB:4AP5}.
HELIX 220 222 {ECO:0000244|PDB:4AP5}.
HELIX 231 238 {ECO:0000244|PDB:4AP5}.
HELIX 244 258 {ECO:0000244|PDB:4AP5}.
TURN 262 266 {ECO:0000244|PDB:4AP5}.
HELIX 273 275 {ECO:0000244|PDB:4AP5}.
STRAND 286 293 {ECO:0000244|PDB:4AP5}.
TURN 296 302 {ECO:0000244|PDB:4AP5}.
STRAND 304 306 {ECO:0000244|PDB:4AP5}.
HELIX 309 323 {ECO:0000244|PDB:4AP5}.
STRAND 328 332 {ECO:0000244|PDB:4AP5}.
HELIX 336 345 {ECO:0000244|PDB:4AP5}.
STRAND 349 351 {ECO:0000244|PDB:4AP6}.
HELIX 356 376 {ECO:0000244|PDB:4AP5}.
STRAND 378 383 {ECO:0000244|PDB:4AP5}.
HELIX 388 400 {ECO:0000244|PDB:4AP5}.
HELIX 404 406 {ECO:0000244|PDB:4AP5}.
SEQUENCE 429 AA; 49976 MW; 36A4213D905AFFD1 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 TDDADRIPFQ EDWMKMKVKL GSALGGPYLG VHLRRKDFIW
GHRQDVPSLE GAVRKIRSLM KTHRLDKVFV ATDAVRKEYE ELKKLLPEMV RFEPTWEELE
LYKDGGVAII DQWICAHARF FIGTSVSTFS FRIHEEREIL GLDPKTTYNR FCGDQEKACE
QPTHWKITY


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Tel 01 43 25 01 50

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GENTAUR GmbH
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Tel (408) 780-0908,
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Genprice Inc, Invoices and accounting
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GENTAUR Poland Sp. z o.o.


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