ID FUT8_MOUSE Reviewed; 575 AA. AC Q9WTS2; Q543F5; Q921U1; DT 05-MAR-2002, integrated into UniProtKB/Swiss-Prot. DT 27-JUL-2011, sequence version 2. DT 27-MAR-2024, entry version 179. DE RecName: Full=Alpha-(1,6)-fucosyltransferase; DE Short=Alpha1-6FucT; DE EC=2.4.1.68; DE AltName: Full=Fucosyltransferase 8; DE AltName: Full=GDP-L-Fuc:N-acetyl-beta-D-glucosaminide alpha1,6-fucosyltransferase; DE AltName: Full=GDP-fucose--glycoprotein fucosyltransferase; DE AltName: Full=Glycoprotein 6-alpha-L-fucosyltransferase; GN Name=Fut8; 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]. RC TISSUE=Brain; RX PubMed=10902914; DOI=10.3109/10425170009033974; RA Hayashi H., Yoneda A., Asada M., Ikekita M., Imamura T.; RT "Molecular cloning of mouse alpha-1,6-fucosyltransferase and expression of RT its mRNA in the developing cerebrum."; RL DNA Seq. 11:91-96(2000). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=C57BL/6J; TISSUE=Eye, and Head; 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 [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.; RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases. RN [4] 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 [5] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-278, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Kidney, Spleen, and 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). CC -!- FUNCTION: Catalyzes the addition of fucose in alpha 1-6 linkage to the CC first GlcNAc residue, next to the peptide chains in N-glycans. CC {ECO:0000250}. CC -!- CATALYTIC ACTIVITY: CC Reaction=GDP-beta-L-fucose + N(4)-{beta-D-GlcNAc-(1->2)-alpha-D-Man- CC (1->3)-[beta-D-GlcNAc-(1->2)-alpha-D-Man-(1->6)]-beta-D-Man-(1->4)- CC beta-D-GlcNAc-(1->4)-beta-D-GlcNAc}-L-asparaginyl-[protein] = GDP + CC H(+) + N(4)-{beta-D-GlcNAc-(1->2)-alpha-D-Man-(1->3)-[beta-D-GlcNAc- CC (1->2)-alpha-D-Man-(1->6)]-beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)- CC [alpha-L-Fuc-(1->6)]-beta-D-GlcNAc}-L-asparaginyl-[protein]; CC Xref=Rhea:RHEA:12985, Rhea:RHEA-COMP:13526, Rhea:RHEA-COMP:13532, CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57273, ChEBI:CHEBI:58189, CC ChEBI:CHEBI:60651, ChEBI:CHEBI:137207; EC=2.4.1.68; CC -!- PATHWAY: Protein modification; protein glycosylation. CC -!- SUBCELLULAR LOCATION: Golgi apparatus, Golgi stack membrane CC {ECO:0000250}; Single-pass type II membrane protein {ECO:0000250}. CC Note=Membrane-bound form in trans cisternae of Golgi. {ECO:0000250}. CC -!- PTM: Tyrosine phosphorylated by PKDCC/VLK. CC {ECO:0000250|UniProtKB:Q9BYC5}. CC -!- SIMILARITY: Belongs to the glycosyltransferase 23 family. CC {ECO:0000255|PROSITE-ProRule:PRU00992}. CC -!- WEB RESOURCE: Name=Functional Glycomics Gateway - GTase; CC Note=Fucosyltransferase 8; CC URL="http://www.functionalglycomics.org/glycomics/molecule/jsp/glycoEnzyme/viewGlycoEnzyme.jsp?gbpId=gt_mou_615"; 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; AB025198; BAA76392.1; -; mRNA. DR EMBL; AK048520; BAC33357.1; -; mRNA. DR EMBL; AK051811; BAC34777.1; -; mRNA. DR EMBL; CH466526; EDL36441.1; -; Genomic_DNA. DR EMBL; CH466526; EDL36443.1; -; Genomic_DNA. DR EMBL; BC010666; AAH10666.1; -; mRNA. DR CCDS; CCDS25999.1; -. DR RefSeq; NP_001239543.1; NM_001252614.1. DR RefSeq; NP_001239544.1; NM_001252615.1. DR RefSeq; NP_001239545.1; NM_001252616.1. DR RefSeq; NP_058589.2; NM_016893.5. DR RefSeq; XP_011242446.1; XM_011244144.2. DR RefSeq; XP_011242447.1; XM_011244145.2. DR PDB; 6VLF; X-ray; 1.80 A; A/B=68-575. DR PDB; 6VLG; X-ray; 2.50 A; A/B/C/D=68-575. DR PDBsum; 6VLF; -. DR PDBsum; 6VLG; -. DR AlphaFoldDB; Q9WTS2; -. DR SMR; Q9WTS2; -. DR BioGRID; 207335; 3. DR STRING; 10090.ENSMUSP00000054530; -. DR CAZy; GT23; Glycosyltransferase Family 23. DR iPTMnet; Q9WTS2; -. DR PhosphoSitePlus; Q9WTS2; -. DR EPD; Q9WTS2; -. DR jPOST; Q9WTS2; -. DR MaxQB; Q9WTS2; -. DR PaxDb; 10090-ENSMUSP00000054530; -. DR PeptideAtlas; Q9WTS2; -. DR ProteomicsDB; 271813; -. DR Pumba; Q9WTS2; -. DR Antibodypedia; 24748; 273 antibodies from 28 providers. DR DNASU; 53618; -. DR Ensembl; ENSMUST00000062804.8; ENSMUSP00000054530.8; ENSMUSG00000021065.17. DR Ensembl; ENSMUST00000171770.10; ENSMUSP00000130845.3; ENSMUSG00000021065.17. DR Ensembl; ENSMUST00000177595.9; ENSMUSP00000136327.2; ENSMUSG00000021065.17. DR GeneID; 53618; -. DR KEGG; mmu:53618; -. DR UCSC; uc007nyy.2; mouse. DR AGR; MGI:1858901; -. DR CTD; 2530; -. DR MGI; MGI:1858901; Fut8. DR VEuPathDB; HostDB:ENSMUSG00000021065; -. DR eggNOG; KOG3705; Eukaryota. DR GeneTree; ENSGT00530000063737; -. DR HOGENOM; CLU_021940_1_0_1; -. DR InParanoid; Q9WTS2; -. DR OMA; YHDIDEY; -. DR OrthoDB; 2876062at2759; -. DR PhylomeDB; Q9WTS2; -. DR TreeFam; TF106108; -. DR BRENDA; 2.4.1.68; 3474. DR Reactome; R-MMU-975578; Reactions specific to the complex N-glycan synthesis pathway. DR UniPathway; UPA00378; -. DR BioGRID-ORCS; 53618; 4 hits in 77 CRISPR screens. DR ChiTaRS; Fut8; mouse. DR PRO; PR:Q9WTS2; -. DR Proteomes; UP000000589; Chromosome 12. DR RNAct; Q9WTS2; Protein. DR Bgee; ENSMUSG00000021065; Expressed in seminal vesicle and 260 other cell types or tissues. DR GO; GO:0032580; C:Golgi cisterna membrane; IEA:UniProtKB-SubCell. DR GO; GO:0046921; F:alpha-(1->6)-fucosyltransferase activity; IMP:MGI. DR GO; GO:0008424; F:glycoprotein 6-alpha-L-fucosyltransferase activity; ISS:UniProtKB. DR GO; GO:0016757; F:glycosyltransferase activity; ISA:MGI. DR GO; GO:0017124; F:SH3 domain binding; IEA:UniProtKB-KW. DR GO; GO:0016477; P:cell migration; IMP:MGI. DR GO; GO:0010761; P:fibroblast migration; IMP:MGI. DR GO; GO:0046368; P:GDP-L-fucose metabolic process; ISS:UniProtKB. DR GO; GO:0007229; P:integrin-mediated signaling pathway; IMP:MGI. DR GO; GO:0036071; P:N-glycan fucosylation; IMP:MGI. DR GO; GO:0006491; P:N-glycan processing; IMP:MGI. DR GO; GO:0006487; P:protein N-linked glycosylation; IBA:GO_Central. DR GO; GO:0018279; P:protein N-linked glycosylation via asparagine; ISS:UniProtKB. DR GO; GO:0043112; P:receptor metabolic process; IMP:MGI. DR GO; GO:1900407; P:regulation of cellular response to oxidative stress; IMP:MGI. DR GO; GO:0010468; P:regulation of gene expression; IMP:MGI. DR GO; GO:0007585; P:respiratory gaseous exchange by respiratory system; IMP:MGI. DR GO; GO:0007179; P:transforming growth factor beta receptor signaling pathway; IMP:MGI. DR CDD; cd11300; Fut8_like; 1. DR CDD; cd11792; SH3_Fut8; 1. DR Gene3D; 3.40.50.11350; -; 1. DR Gene3D; 1.10.287.1060; ESAT-6-like; 1. DR Gene3D; 2.30.30.40; SH3 Domains; 1. DR InterPro; IPR015827; Fut8. DR InterPro; IPR045573; Fut8_N_cat. DR InterPro; IPR035653; Fut8_SH3. DR InterPro; IPR027350; GT23_dom. DR InterPro; IPR036028; SH3-like_dom_sf. DR InterPro; IPR001452; SH3_domain. DR PANTHER; PTHR13132; ALPHA- 1,6 -FUCOSYLTRANSFERASE; 1. DR PANTHER; PTHR13132:SF29; ALPHA-(1,6)-FUCOSYLTRANSFERASE; 1. DR Pfam; PF19745; FUT8_N_cat; 1. DR Pfam; PF14604; SH3_9; 1. DR PIRSF; PIRSF000472; Alpha1_6FUT_euk; 1. DR SMART; SM00326; SH3; 1. DR SUPFAM; SSF50044; SH3-domain; 1. DR PROSITE; PS51659; GT23; 1. DR PROSITE; PS50002; SH3; 1. DR Genevisible; Q9WTS2; MM. PE 1: Evidence at protein level; KW 3D-structure; Disulfide bond; Glycosyltransferase; Golgi apparatus; KW Membrane; Phosphoprotein; Reference proteome; SH3 domain; SH3-binding; KW Signal-anchor; Transferase; Transmembrane; Transmembrane helix. FT CHAIN 1..575 FT /note="Alpha-(1,6)-fucosyltransferase" FT /id="PRO_0000080527" FT TOPO_DOM 1..9 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT TRANSMEM 10..30 FT /note="Helical; Signal-anchor for type II membrane protein" FT /evidence="ECO:0000255" FT TOPO_DOM 31..575 FT /note="Lumenal" FT /evidence="ECO:0000255" FT DOMAIN 206..493 FT /note="GT23" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00992" FT DOMAIN 502..563 FT /note="SH3" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00192" FT REGION 365..366 FT /note="Important for donor substrate binding" FT MOTIF 299..305 FT /note="SH3-binding" FT /evidence="ECO:0000255" FT MOD_RES 278 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:21183079" FT DISULFID 204..266 FT /evidence="ECO:0000250" FT DISULFID 212..230 FT /evidence="ECO:0000250" FT DISULFID 218..222 FT /evidence="ECO:0000250" FT DISULFID 465..472 FT /evidence="ECO:0000250" FT CONFLICT 40 FT /note="S -> T (in Ref. 1; BAA76392)" FT /evidence="ECO:0000305" FT CONFLICT 388 FT /note="E -> Q (in Ref. 1; BAA76392)" FT /evidence="ECO:0000305" FT CONFLICT 418 FT /note="K -> N (in Ref. 1; BAA76392)" FT /evidence="ECO:0000305" FT HELIX 110..137 FT /evidence="ECO:0007829|PDB:6VLF" FT HELIX 142..172 FT /evidence="ECO:0007829|PDB:6VLF" FT HELIX 173..175 FT /evidence="ECO:0007829|PDB:6VLF" FT HELIX 176..199 FT /evidence="ECO:0007829|PDB:6VLF" FT HELIX 204..206 FT /evidence="ECO:0007829|PDB:6VLF" FT STRAND 209..213 FT /evidence="ECO:0007829|PDB:6VLF" FT HELIX 220..237 FT /evidence="ECO:0007829|PDB:6VLF" FT STRAND 240..244 FT /evidence="ECO:0007829|PDB:6VLF" FT HELIX 255..257 FT /evidence="ECO:0007829|PDB:6VLF" FT STRAND 274..276 FT /evidence="ECO:0007829|PDB:6VLF" FT TURN 281..284 FT /evidence="ECO:0007829|PDB:6VLF" FT STRAND 287..290 FT /evidence="ECO:0007829|PDB:6VLF" FT HELIX 294..296 FT /evidence="ECO:0007829|PDB:6VLF" FT HELIX 310..317 FT /evidence="ECO:0007829|PDB:6VLF" FT HELIX 323..335 FT /evidence="ECO:0007829|PDB:6VLF" FT HELIX 340..353 FT /evidence="ECO:0007829|PDB:6VLF" FT STRAND 357..364 FT /evidence="ECO:0007829|PDB:6VLF" FT HELIX 367..369 FT /evidence="ECO:0007829|PDB:6VLG" FT TURN 371..373 FT /evidence="ECO:0007829|PDB:6VLG" FT HELIX 379..394 FT /evidence="ECO:0007829|PDB:6VLF" FT STRAND 400..409 FT /evidence="ECO:0007829|PDB:6VLF" FT HELIX 413..420 FT /evidence="ECO:0007829|PDB:6VLF" FT TURN 421..423 FT /evidence="ECO:0007829|PDB:6VLG" FT STRAND 424..427 FT /evidence="ECO:0007829|PDB:6VLF" FT HELIX 429..431 FT /evidence="ECO:0007829|PDB:6VLF" FT TURN 438..440 FT /evidence="ECO:0007829|PDB:6VLG" FT STRAND 441..443 FT /evidence="ECO:0007829|PDB:6VLG" FT HELIX 447..459 FT /evidence="ECO:0007829|PDB:6VLF" FT STRAND 460..465 FT /evidence="ECO:0007829|PDB:6VLF" FT HELIX 470..480 FT /evidence="ECO:0007829|PDB:6VLF" FT STRAND 482..484 FT /evidence="ECO:0007829|PDB:6VLF" FT STRAND 490..494 FT /evidence="ECO:0007829|PDB:6VLF" FT STRAND 506..509 FT /evidence="ECO:0007829|PDB:6VLF" FT STRAND 528..534 FT /evidence="ECO:0007829|PDB:6VLF" FT STRAND 536..544 FT /evidence="ECO:0007829|PDB:6VLF" FT TURN 545..548 FT /evidence="ECO:0007829|PDB:6VLF" FT STRAND 549..554 FT /evidence="ECO:0007829|PDB:6VLF" FT HELIX 555..557 FT /evidence="ECO:0007829|PDB:6VLF" FT STRAND 558..560 FT /evidence="ECO:0007829|PDB:6VLF" FT HELIX 571..574 FT /evidence="ECO:0007829|PDB:6VLF" SQ SEQUENCE 575 AA; 66557 MW; 226092A8959B3EB7 CRC64; MRAWTGSWRW IMLILFAWGT LLFYIGGHLV RDNDHPDHSS RELSKILAKL ERLKQQNEDL RRMAESLRIP EGPIDQGTAT GRVRVLEEQL VKAKEQIENY KKQARNGLGK DHEILRRRIE NGAKELWFFL QSELKKLKHL EGNELQRHAD EILLDLGHHE RSIMTDLYYL SQTDGAGDWR EKEAKDLTEL VQRRITYLQN PKDCSKARKL VCNINKGCGY GCQLHHVVYC FMIAYGTQRT LILESQNWRY ATGGWETVFR PVSETCTDRS GLSTGHWSGE VNDKNIQVVE LPIVDSLHPR PPYLPLAVPE DLADRLLRVH GDPAVWWVSQ FVKYLIRPQP WLEKEIEEAT KKLGFKHPVI GVHVRRTDKV GTEAAFHPIE EYMVHVEEHF QLLARRMQVD KKRVYLATDD PTLLKEAKTK YSNYEFISDN SISWSAGLHN RYTENSLRGV ILDIHFLSQA DFLVCTFSSQ VCRVAYEIMQ TLHPDASANF HSLDDIYYFG GQNAHNQIAV YPHKPRTEEE IPMEPGDIIG VAGNHWDGYS KGINRKLGKT GLYPSYKVRE KIETVKYPTY PEAEK //