ID B2RV73_MOUSE Unreviewed; 429 AA. AC B2RV73; DT 01-JUL-2008, integrated into UniProtKB/TrEMBL. DT 01-JUL-2008, sequence version 1. DT 24-JAN-2024, entry version 111. DE RecName: Full=GDP-fucose protein O-fucosyltransferase 2 {ECO:0000256|ARBA:ARBA00026232}; DE EC=2.4.1.221 {ECO:0000256|ARBA:ARBA00012196}; DE AltName: Full=Peptide-O-fucosyltransferase 2 {ECO:0000256|ARBA:ARBA00033083}; GN Name=Pofut2 {ECO:0000313|EMBL:AAI47078.1, GN ECO:0000313|MGI:MGI:1916863}; 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 {ECO:0000313|EMBL:AAI47078.1}; RN [1] {ECO:0000313|EMBL:AAI47078.1} RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Brain {ECO:0000313|EMBL:AAI47078.1}; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RA Gerhard D.S., Wagner L., Feingold E.A., Shenmen C.M., Grouse L.H., RA Schuler G., Klein S.L., Old S., Rasooly R., Good P., Guyer M., Peck A.M., RA Derge J.G., Lipman D., Collins F.S., Jang W., Sherry S., Feolo M., RA Misquitta L., Lee E., Rotmistrovsky K., Greenhut S.F., Schaefer C.F., RA Buetow K., Bonner T.I., Haussler D., Kent J., Kiekhaus M., Furey T., RA Brent M., Prange C., Schreiber K., Shapiro N., Bhat N.K., Hopkins R.F., RA Hsie F., Driscoll T., Soares M.B., Casavant T.L., Scheetz T.E., RA Brown-stein M.J., Usdin T.B., Toshiyuki S., Carninci P., Piao Y., RA Dudekula D.B., Ko M.S., Kawakami K., Suzuki Y., Sugano S., Gruber C.E., RA Smith M.R., Simmons B., Moore T., Waterman R., Johnson S.L., Ruan Y., RA Wei C.L., Mathavan S., Gunaratne P.H., Wu J., Garcia A.M., Hulyk S.W., RA Fuh E., Yuan Y., Sneed A., Kowis C., Hodgson A., Muzny D.M., McPherson J., RA Gibbs R.A., Fahey J., Helton E., Ketteman M., Madan A., Rodrigues S., RA Sanchez A., Whiting M., Madari A., Young A.C., Wetherby K.D., Granite S.J., RA Kwong P.N., Brinkley C.P., Pearson R.L., Bouffard G.G., Blakesly R.W., RA Green E.D., Dickson M.C., Rodriguez A.C., Grimwood J., Schmutz J., RA Myers R.M., Butterfield Y.S., Griffith M., Griffith O.L., Krzywinski M.I., RA Liao N., Morin R., Morrin R., Palmquist D., Petrescu A.S., Skalska U., RA Smailus D.E., Stott J.M., Schnerch A., Schein J.E., Jones S.J., Holt R.A., RA Baross A., Marra M.A., Clifton S., Makowski K.A., Bosak S., Malek J.; 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 [2] {ECO:0007829|PubMed:21183079} RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. 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). 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:0000256|ARBA:ARBA00033615}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:63645; CC Evidence={ECO:0000256|ARBA:ARBA00033615}; 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:0000256|ARBA:ARBA00033628}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:70492; CC Evidence={ECO:0000256|ARBA:ARBA00033628}; CC -!- PATHWAY: Protein modification; protein glycosylation. CC {ECO:0000256|ARBA:ARBA00004922}. CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum CC {ECO:0000256|ARBA:ARBA00004240}. CC -!- SIMILARITY: Belongs to the glycosyltransferase 68 family. CC {ECO:0000256|ARBA:ARBA00025803}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; BC147077; AAI47078.1; -; mRNA. DR EMBL; BC147078; AAI47079.1; -; mRNA. DR RefSeq; NP_084538.2; NM_030262.3. DR AlphaFoldDB; B2RV73; -. DR SMR; B2RV73; -. DR CAZy; GT68; Glycosyltransferase Family 68. DR PeptideAtlas; B2RV73; -. DR Antibodypedia; 10462; 336 antibodies from 29 providers. DR DNASU; 80294; -. DR GeneID; 80294; -. DR KEGG; mmu:80294; -. DR AGR; MGI:1916863; -. DR CTD; 23275; -. DR MGI; MGI:1916863; Pofut2. DR VEuPathDB; HostDB:ENSMUSG00000020260; -. DR HOGENOM; CLU_033856_0_0_1; -. DR OMA; YILYDVN; -. DR OrthoDB; 197532at2759; -. DR UniPathway; UPA00378; -. DR BioGRID-ORCS; 80294; 3 hits in 78 CRISPR screens. DR ChiTaRS; Pofut2; mouse. DR ExpressionAtlas; B2RV73; baseline and differential. DR GO; GO:0005783; C:endoplasmic reticulum; IEA:UniProtKB-SubCell. DR GO; GO:0005794; C:Golgi apparatus; IEA:Ensembl. DR GO; GO:0046922; F:peptide-O-fucosyltransferase activity; IEA:UniProtKB-EC. DR GO; GO:0006004; P:fucose metabolic process; IEA:UniProtKB-KW. DR GO; GO:1903334; P:positive regulation of protein folding; IEA:Ensembl. DR GO; GO:0051046; P:regulation of secretion; IEA:Ensembl. 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. PE 1: Evidence at protein level; KW Carbohydrate metabolism {ECO:0000256|ARBA:ARBA00023277}; KW Endoplasmic reticulum {ECO:0000256|ARBA:ARBA00022824}; KW Fucose metabolism {ECO:0000256|ARBA:ARBA00023253}; KW Glycosyltransferase {ECO:0000313|EMBL:AAI47078.1}; KW Signal {ECO:0000256|SAM:SignalP}; KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:AAI47078.1}. FT SIGNAL 1..21 FT /evidence="ECO:0000256|SAM:SignalP" FT CHAIN 22..429 FT /note="GDP-fucose protein O-fucosyltransferase 2" FT /evidence="ECO:0000256|SAM:SignalP" FT /id="PRO_5014298366" 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 //