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   24-JAN-2024, entry version 138.
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;
CC       Note=Peptide-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   GlyCosmos; Q8VHI3; 3 sites, No reported glycans.
DR   GlyGen; Q8VHI3; 3 sites.
DR   PhosphoSitePlus; Q8VHI3; -.
DR   EPD; Q8VHI3; -.
DR   MaxQB; Q8VHI3; -.
DR   PaxDb; 10090-ENSMUSP00000020493; -.
DR   PeptideAtlas; Q8VHI3; -.
DR   ProteomicsDB; 294272; -.
DR   Pumba; Q8VHI3; -.
DR   Antibodypedia; 10462; 336 antibodies from 29 providers.
DR   DNASU; 80294; -.
DR   Ensembl; ENSMUST00000020493.9; ENSMUSP00000020493.8; ENSMUSG00000020260.10.
DR   GeneID; 80294; -.
DR   KEGG; mmu:80294; -.
DR   UCSC; uc007fvj.1; mouse.
DR   AGR; MGI:1916863; -.
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; 197532at2759; -.
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; 3 hits in 78 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 264 other cell types or tissues.
DR   ExpressionAtlas; Q8VHI3; baseline and differential.
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   CDD; cd11298; O-FucT-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.
DR   Genevisible; Q8VHI3; MM.
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
//