FUT8_MOUSE
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 03-AUG-2022, entry version 170.
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-GlcNAcl-(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";
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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; Q9WTS2; -.
DR PeptideAtlas; Q9WTS2; -.
DR PRIDE; Q9WTS2; -.
DR ProteomicsDB; 271813; -.
DR Antibodypedia; 24748; 251 antibodies from 28 providers.
DR DNASU; 53618; -.
DR Ensembl; ENSMUST00000062804; ENSMUSP00000054530; ENSMUSG00000021065.
DR Ensembl; ENSMUST00000171770; ENSMUSP00000130845; ENSMUSG00000021065.
DR Ensembl; ENSMUST00000177595; ENSMUSP00000136327; ENSMUSG00000021065.
DR GeneID; 53618; -.
DR KEGG; mmu:53618; -.
DR UCSC; uc007nyy.2; mouse.
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; GGQNPHN; -.
DR OrthoDB; 1290594at2759; -.
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; 3 hits in 72 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 256 other tissues.
DR Genevisible; Q9WTS2; MM.
DR GO; GO:0032580; C:Golgi cisterna membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
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; cd11792; SH3_Fut8; 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 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; SSF50044; 1.
DR PROSITE; PS51659; GT23; 1.
DR PROSITE; PS50002; SH3; 1.
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
