OFUT2_MOUSE
ID OFUT2_MOUSE Reviewed; 429 AA.
AC Q8VHI3; Q8VEM2; Q9CV66;
DT 13-AUG-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 03-AUG-2022, entry version 131.
DE RecName: Full=GDP-fucose protein O-fucosyltransferase 2;
DE EC=2.4.1.221 {ECO:0000269|PubMed:20637190};
DE AltName: Full=Peptide-O-fucosyltransferase 2;
DE Short=O-FucT-2;
DE Flags: Precursor;
GN Name=Pofut2;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Menzel O., Reymond A., Antonarakis S.E., Guipponi M.;
RT "C21orf80, a new gene from the 21q22.3 region: using RNAi to get insight
RT into the function.";
RL Submitted (DEC-2001) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-119.
RC STRAIN=C57BL/6J; TISSUE=Tongue;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [4]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Lung, Pancreas, Spleen, and
RC Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [5]
RP FUNCTION, CATALYTIC ACTIVITY, PATHWAY, DISRUPTION PHENOTYPE, AND
RP MUTAGENESIS OF GLU-396.
RX PubMed=20637190; DOI=10.1016/j.ydbio.2010.07.008;
RA Du J., Takeuchi H., Leonhard-Melief C., Shroyer K.R., Dlugosz M.,
RA Haltiwanger R.S., Holdener B.C.;
RT "O-fucosylation of thrombospondin type 1 repeats restricts epithelial to
RT mesenchymal transition (EMT) and maintains epiblast pluripotency during
RT mouse gastrulation.";
RL Dev. Biol. 346:25-38(2010).
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 (PubMed:20637190). O-fucosylates members of
CC several protein families including the ADAMTS, the thrombospondin (TSP)
CC and spondin families (PubMed:20637190). Required for the proper
CC secretion of ADAMTS family members such as ADAMTSL1 and ADAMTS13 (By
CC similarity). 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 (PubMed:20637190). {ECO:0000250|UniProtKB:Q9Y2G5,
CC ECO:0000269|PubMed:20637190}.
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:0000269|PubMed:20637190};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:63645;
CC Evidence={ECO:0000269|PubMed:20637190};
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:0000269|PubMed:20637190};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:70492;
CC Evidence={ECO:0000269|PubMed:20637190};
CC -!- PATHWAY: Protein modification; protein glycosylation.
CC {ECO:0000269|PubMed:20637190}.
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 -!- DISRUPTION PHENOTYPE: Null mice embryos die before 10.5 dpc. At the
CC onset of gastrulation at 6.5 dpc, embryos are rounder and the embryonic
CC and extra-embryonic ectoderm appears thickened and disorganized.
CC Expression of NODAL and WNT3 is significantly expanded and/or displaced
CC in the primitive streak as is BMP4 in the extra-embryonic ectoderm. By
CC 7.5 dpc, embryos are unusually dense and shorter characterized by a
CC dumb-bell appearance. There is unrestricted epithelial to mesenchymal
CC transition (EMT) producing an abundance of mesenchymal cells. SNAIL1
CC expression is expanded and E-cadherin expression decreased. There is
CC distal expansion of the proximal visceral endoderm.
CC {ECO:0000269|PubMed:20637190}.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 68 family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BC018194; Type=Frameshift; Evidence={ECO:0000305};
CC -!- WEB RESOURCE: Name=Functional Glycomics Gateway - GTase; Note=Peptide-
CC O-fucosyltransferase 2;
CC URL="http://www.functionalglycomics.org/glycomics/molecule/jsp/glycoEnzyme/viewGlycoEnzyme.jsp?gbpId=gt_mou_620";
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DR EMBL; AF455270; AAL65192.1; -; mRNA.
DR EMBL; BC018194; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; AK009301; BAB26202.1; -; mRNA.
DR CCDS; CCDS23954.1; -.
DR RefSeq; NP_084538.2; NM_030262.3.
DR AlphaFoldDB; Q8VHI3; -.
DR SMR; Q8VHI3; -.
DR BioGRID; 219781; 2.
DR STRING; 10090.ENSMUSP00000020493; -.
DR CAZy; GT68; Glycosyltransferase Family 68.
DR GlyGen; Q8VHI3; 3 sites.
DR PhosphoSitePlus; Q8VHI3; -.
DR EPD; Q8VHI3; -.
DR MaxQB; Q8VHI3; -.
DR PaxDb; Q8VHI3; -.
DR PeptideAtlas; Q8VHI3; -.
DR PRIDE; Q8VHI3; -.
DR ProteomicsDB; 294272; -.
DR Antibodypedia; 10462; 302 antibodies from 29 providers.
DR DNASU; 80294; -.
DR Ensembl; ENSMUST00000020493; ENSMUSP00000020493; ENSMUSG00000020260.
DR GeneID; 80294; -.
DR KEGG; mmu:80294; -.
DR UCSC; uc007fvj.1; mouse.
DR CTD; 23275; -.
DR MGI; MGI:1916863; Pofut2.
DR VEuPathDB; HostDB:ENSMUSG00000020260; -.
DR eggNOG; ENOG502QPS6; Eukaryota.
DR GeneTree; ENSGT00390000007989; -.
DR HOGENOM; CLU_033856_0_0_1; -.
DR InParanoid; Q8VHI3; -.
DR OMA; YILYDVN; -.
DR OrthoDB; 654070at2759; -.
DR PhylomeDB; Q8VHI3; -.
DR TreeFam; TF314337; -.
DR Reactome; R-MMU-5173214; O-glycosylation of TSR domain-containing proteins.
DR UniPathway; UPA00378; -.
DR BioGRID-ORCS; 80294; 2 hits in 73 CRISPR screens.
DR ChiTaRS; Pofut2; mouse.
DR PRO; PR:Q8VHI3; -.
DR Proteomes; UP000000589; Chromosome 10.
DR RNAct; Q8VHI3; protein.
DR Bgee; ENSMUSG00000020260; Expressed in external carotid artery and 261 other tissues.
DR ExpressionAtlas; Q8VHI3; baseline and differential.
DR Genevisible; Q8VHI3; MM.
DR GO; GO:0005783; C:endoplasmic reticulum; IEA:UniProtKB-SubCell.
DR GO; GO:0005794; C:Golgi apparatus; ISO:MGI.
DR GO; GO:0008417; F:fucosyltransferase activity; IDA:MGI.
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:0036065; P:fucosylation; IMP:MGI.
DR GO; GO:0001707; P:mesoderm formation; IMP:MGI.
DR GO; GO:1903334; P:positive regulation of protein folding; ISO:MGI.
DR GO; GO:0036066; P:protein O-linked fucosylation; ISS:UniProtKB.
DR GO; GO:0010717; P:regulation of epithelial to mesenchymal transition; IMP:MGI.
DR GO; GO:0010468; P:regulation of gene expression; IMP:MGI.
DR GO; GO:0051046; P:regulation of secretion; ISO:MGI.
DR InterPro; IPR019378; GDP-Fuc_O-FucTrfase.
DR InterPro; IPR045130; OFUT2-like.
DR PANTHER; PTHR13398; PTHR13398; 1.
DR Pfam; PF10250; O-FucT; 1.
PE 1: Evidence at protein 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_0000012155"
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="Required for enzyme activity"
FT /evidence="ECO:0000269|PubMed:20637190"
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"
FT MUTAGEN 396
FT /note="E->A: Abolishes in vitro enzyme activity."
FT /evidence="ECO:0000269|PubMed:20637190"
SQ SEQUENCE 429 AA; 49429 MW; 0E7AFF5F1CD33560 CRC64;
MAALSVVCLL LAAASWRPVS ASGEEFWPGQ SAADILSGAA SRRRYLLYDV NPPEGFNLRR
DVYIRVASLL KTLLKTEEWV LVLPPWGRLY HWQSPDIHQV RIPWSEFFDL PSLNKNIPVI
EYEQFIAESG GPFIDQVYVL QGYAEGWKEG TWEEKVDARP CIDPLLYSQD KHEYYRGWFW
GYEETRGLNV SCLSVQGSAS IVAPVLLKNT SARSVMLDRA ENLLHDHYGG REYWDTRRSM
VFAKHLRAVG DEFRSQHLNS TDAADKMAPE EDWTKMKVKL GSALGGPYLG VHLRRKDFIW
GHREDVPSLE GAVKKIRSLM KTHQLDKVFV ATDAIRKEQE ELRKLLPEMV RFEPTWEELE
LYKDGGVAII DQWICAHARF FIGTSVSTFS FRIHEEREIL GLDPKTTYNR FCGDQEKACE
QPTHWKIAY
