FUT2_MOUSE
ID FUT2_MOUSE Reviewed; 347 AA.
AC Q9JL27; O70504;
DT 06-JUN-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 147.
DE RecName: Full=Galactoside alpha-(1,2)-fucosyltransferase 2 {ECO:0000305};
DE AltName: Full=Alpha(1,2)FT 2;
DE AltName: Full=Fucosyltransferase 2;
DE AltName: Full=GDP-L-fucose:beta-D-galactoside 2-alpha-L-fucosyltransferase 2;
DE AltName: Full=GDP-fucose: beta-galactoside alpha1,2-fucosyltransferase {ECO:0000303|PubMed:11018479};
DE Short=MFUT-II {ECO:0000303|PubMed:11018479};
DE AltName: Full=Secretory blood group protein 2;
DE AltName: Full=Type 1 galactoside alpha-(1,2)-fucosyltransferase FUT2 {ECO:0000305};
DE EC=2.4.1.69 {ECO:0000269|PubMed:11323419};
DE AltName: Full=Type 2 galactoside alpha-(1,2)-fucosyltransferase FUT2 {ECO:0000305};
DE EC=2.4.1.344 {ECO:0000269|PubMed:11323419};
GN Name=Fut2 {ECO:0000312|MGI:MGI:109374}; Synonyms=Sec2;
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], CATALYTIC ACTIVITY, AND FUNCTION.
RC STRAIN=ICR; TISSUE=Gastrointestinal tract;
RX PubMed=11018479; DOI=10.1016/s1388-1981(00)00103-7;
RA Lin B., Hayashi Y., Saito M., Sakakibara Y., Yanagisawa M., Iwamori M.;
RT "GDP-fucose: beta-galactoside alpha1,2-fucosyltransferase, MFUT-II, and not
RT MFUT-I or -III, is induced in a restricted region of the digestive tract of
RT germ-free mice by host-microbe interactions and cycloheximide.";
RL Biochim. Biophys. Acta 1487:275-285(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY, TISSUE
RP SPECIFICITY, AND DEVELOPMENTAL STAGE.
RC STRAIN=129/Ola;
RX PubMed=11323419; DOI=10.1074/jbc.m100735200;
RA Domino S.E., Zhang L., Lowe J.B.;
RT "Molecular cloning, genomic mapping, and expression of two secretor blood
RT group alpha (1,2)fucosyltransferase genes differentially regulated in mouse
RT uterine epithelium and gastrointestinal tract.";
RL J. Biol. Chem. 276:23748-23756(2001).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Colon;
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 CATALYTIC ACTIVITY, FUNCTION, TISSUE SPECIFICITY, BIOPHYSICOCHEMICAL
RP PROPERTIES, AND INDUCTION.
RX PubMed=11368156; DOI=10.1006/abbi.2001.2303;
RA Lin B., Saito M., Sakakibara Y., Hayashi Y., Yanagisawa M., Iwamori M.;
RT "Characterization of three members of murine alpha1,2-fucosyltransferases:
RT change in the expression of the Se gene in the intestine of mice after
RT administration of microbes.";
RL Arch. Biochem. Biophys. 388:207-215(2001).
RN [5]
RP DISRUPTION PHENOTYPE, AND FUNCTION.
RX PubMed=11713270; DOI=10.1128/mcb.21.24.8336-8345.2001;
RA Domino S.E., Zhang L., Gillespie P.J., Saunders T.L., Lowe J.B.;
RT "Deficiency of reproductive tract alpha(1,2)fucosylated glycans and normal
RT fertility in mice with targeted deletions of the FUT1 or FUT2
RT alpha(1,2)fucosyltransferase locus.";
RL Mol. Cell. Biol. 21:8336-8345(2001).
RN [6]
RP CATALYTIC ACTIVITY, FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, TISSUE
RP SPECIFICITY, AND INDUCTION.
RX PubMed=14967068; DOI=10.1042/bj20031668;
RA Iwamori M., Domino S.E.;
RT "Tissue-specific loss of fucosylated glycolipids in mice with targeted
RT deletion of alpha(1,2)fucosyltransferase genes.";
RL Biochem. J. 380:75-81(2004).
RN [7]
RP FUNCTION.
RX PubMed=19706747; DOI=10.1093/glycob/cwp131;
RA Magalhaes A., Gomes J., Ismail M.N., Haslam S.M., Mendes N., Osorio H.,
RA David L., Le Pendu J., Haas R., Dell A., Boren T., Reis C.A.;
RT "Fut2-null mice display an altered glycosylation profile and impaired BabA-
RT mediated Helicobacter pylori adhesion to gastric mucosa.";
RL Glycobiology 19:1525-1536(2009).
RN [8]
RP INDUCTION.
RX PubMed=24284406; DOI=10.3390/ijms141123188;
RA Wang C.M., Hu S.G., Ru Y.F., Yao G.X., Ma W.B., Gu Y.H., Chu C., Wang S.L.,
RA Zhou Z.M., Liu Q., Zhou Y.C., Zhang Y.L.;
RT "Different effects of androgen on the expression of Fut1, Fut2, Fut4 and
RT Fut9 in male mouse reproductive tract.";
RL Int. J. Mol. Sci. 14:23188-23202(2013).
RN [9]
RP FUNCTION.
RX PubMed=27161092; DOI=10.1038/srep25575;
RA Magalhaes A., Rossez Y., Robbe-Masselot C., Maes E., Gomes J.,
RA Shevtsova A., Bugaytsova J., Boren T., Reis C.A.;
RT "Muc5ac gastric mucin glycosylation is shaped by FUT2 activity and
RT functionally impacts Helicobacter pylori binding.";
RL Sci. Rep. 6:25575-25575(2016).
CC -!- FUNCTION: Catalyzes the transfer of L-fucose, from a guanosine
CC diphosphate-beta-L-fucose, to the terminal galactose on both O- and N-
CC linked glycans chains of cell surface glycoproteins and glycolipids and
CC the resulting epitope regulates several processes such as cell-cell
CC interaction including host-microbe interaction, cell surface expression
CC and cell proliferation (PubMed:11018479, PubMed:11368156,
CC PubMed:14967068, PubMed:11323419, PubMed:27161092, PubMed:19706747).
CC Preferentially fucosylates gangliosides GA1 and GM1 in the antrum,
CC cecum and colon and in the female reproductive organs (PubMed:11713270,
CC PubMed:14967068). Fucosylated host glycoproteins or glycolipids mediate
CC interaction with intestinal microbiota influencing its composition
CC (PubMed:27161092, PubMed:19706747). Creates a soluble precursor
CC oligosaccharide FuC-alpha ((1,2)Galbeta-) called the H antigen which is
CC an essential substrate for the final step in the soluble ABO blood
CC group antigen synthesis pathway (PubMed:11323419).
CC {ECO:0000269|PubMed:11018479, ECO:0000269|PubMed:11323419,
CC ECO:0000269|PubMed:11368156, ECO:0000269|PubMed:11713270,
CC ECO:0000269|PubMed:14967068, ECO:0000269|PubMed:19706747,
CC ECO:0000269|PubMed:27161092}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a beta-D-galactosyl-(1->3)-N-acetyl-beta-D-glucosaminyl
CC derivative + GDP-beta-L-fucose = an alpha-L-Fuc-(1->2)-beta-D-Gal-
CC (1->3)-beta-D-GlcNAc derivative + GDP + H(+); Xref=Rhea:RHEA:50664,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57273, ChEBI:CHEBI:58189,
CC ChEBI:CHEBI:133506, ChEBI:CHEBI:133509; EC=2.4.1.69;
CC Evidence={ECO:0000269|PubMed:11323419};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:50665;
CC Evidence={ECO:0000305|PubMed:11323419};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a beta-D-galactosyl-(1->4)-N-acetyl-beta-D-glucosaminyl
CC derivative + GDP-beta-L-fucose = an alpha-L-Fuc-(1->2)-beta-D-Gal-
CC (1->4)-beta-D-GlcNAc derivative + GDP + H(+); Xref=Rhea:RHEA:50668,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57273, ChEBI:CHEBI:58189,
CC ChEBI:CHEBI:133507, ChEBI:CHEBI:133510; EC=2.4.1.344;
CC Evidence={ECO:0000269|PubMed:11323419};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:50669;
CC Evidence={ECO:0000305|PubMed:11323419};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a neolactoside nLc4Cer + GDP-beta-L-fucose = a neolactoside
CC IV(2)-alpha-Fuc-nLc4Cer + GDP + H(+); Xref=Rhea:RHEA:48800,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57273, ChEBI:CHEBI:58189,
CC ChEBI:CHEBI:90376, ChEBI:CHEBI:90803;
CC Evidence={ECO:0000269|PubMed:11368156, ECO:0000269|PubMed:14967068};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:48801;
CC Evidence={ECO:0000305|PubMed:11368156, ECO:0000305|PubMed:14967068};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a neolactoside nLc4Cer(d18:1(4E)) + GDP-beta-L-fucose = a
CC neolactoside IV(2)-alpha-Fuc-nLc4Cer(d18:1(4E)) + GDP + H(+);
CC Xref=Rhea:RHEA:48304, ChEBI:CHEBI:15378, ChEBI:CHEBI:17006,
CC ChEBI:CHEBI:28691, ChEBI:CHEBI:57273, ChEBI:CHEBI:58189;
CC Evidence={ECO:0000269|PubMed:11368156, ECO:0000269|PubMed:14967068};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:48305;
CC Evidence={ECO:0000305|PubMed:11368156, ECO:0000305|PubMed:14967068};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ganglioside GM1 + GDP-beta-L-fucose = ganglioside Fuc-GM1 +
CC GDP + H(+); Xref=Rhea:RHEA:48292, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:57273, ChEBI:CHEBI:58189, ChEBI:CHEBI:82639,
CC ChEBI:CHEBI:90189; Evidence={ECO:0000269|PubMed:11368156};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:48293;
CC Evidence={ECO:0000269|PubMed:14967068};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ganglioside GA1 + GDP-beta-L-fucose = ganglioside Fuc-GA1 +
CC GDP + H(+); Xref=Rhea:RHEA:48320, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:57273, ChEBI:CHEBI:58189, ChEBI:CHEBI:88069,
CC ChEBI:CHEBI:90262; Evidence={ECO:0000269|PubMed:11018479,
CC ECO:0000269|PubMed:11368156, ECO:0000269|PubMed:14967068};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:48321;
CC Evidence={ECO:0000269|PubMed:14967068};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=GDP-beta-L-fucose + Lc4Cer = alpha-L-fucosyl-(1->2)-beta-D-
CC galactosyl-(1->3)-N-acetyl-beta-D-glucosaminyl-(1->3)-beta-D-
CC galactosyl-(1->4)-beta-D-glucosyl-(1<->1')-ceramide + GDP + H(+);
CC Xref=Rhea:RHEA:48792, ChEBI:CHEBI:15378, ChEBI:CHEBI:57273,
CC ChEBI:CHEBI:58189, ChEBI:CHEBI:90800, ChEBI:CHEBI:90802;
CC Evidence={ECO:0000269|PubMed:11368156, ECO:0000269|PubMed:14967068};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:48793;
CC Evidence={ECO:0000305|PubMed:11368156, ECO:0000305|PubMed:14967068};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a beta-D-Gal-(1->3)-beta-D-GlcNAc-(1->3)-beta-D-Gal-(1->4)-
CC beta-D-Glc-(1<->1')-Cer(d18:1(4E)) + GDP-beta-L-fucose = alpha-L-
CC fucosyl-(1->2)- beta-D-galactosyl-(1->3)-N-acetyl-beta-D-
CC glucosaminyl-(1->3)-beta-D-galactosyl-(1->4)-beta-D-glucosyl-
CC (1<->1')-N-acylsphing-4-enine + GDP + H(+); Xref=Rhea:RHEA:32175,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:17292, ChEBI:CHEBI:28743,
CC ChEBI:CHEBI:57273, ChEBI:CHEBI:58189; EC=2.4.1.69;
CC Evidence={ECO:0000269|PubMed:11368156, ECO:0000269|PubMed:14967068};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:32176;
CC Evidence={ECO:0000305|PubMed:11368156, ECO:0000305|PubMed:14967068};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ganglioside GD1b + GDP-beta-L-fucose = ganglioside Fuc-GD1b +
CC GDP + H(+); Xref=Rhea:RHEA:48324, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:57273, ChEBI:CHEBI:58189, ChEBI:CHEBI:82939,
CC ChEBI:CHEBI:90265; Evidence={ECO:0000269|PubMed:11368156};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:48325;
CC Evidence={ECO:0000305|PubMed:11368156, ECO:0000305|PubMed:14967068};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ganglioside GM1 (d18:1(4E)) + GDP-beta-L-fucose =
CC gangliosideFuc-GM1 (d18:1(4E)) + GDP + H(+); Xref=Rhea:RHEA:42040,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57273, ChEBI:CHEBI:58189,
CC ChEBI:CHEBI:77709, ChEBI:CHEBI:78607;
CC Evidence={ECO:0000250|UniProtKB:Q10984};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:42041;
CC Evidence={ECO:0000250|UniProtKB:Q10984};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=GDP-beta-L-fucose + globoside GalGb4Cer (d18:1(4E)) = GDP +
CC globoside Globo-H (d18:1(4E)) + H(+); Xref=Rhea:RHEA:42044,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57273, ChEBI:CHEBI:58189,
CC ChEBI:CHEBI:62571, ChEBI:CHEBI:62649;
CC Evidence={ECO:0000250|UniProtKB:Q10984};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:42045;
CC Evidence={ECO:0000250|UniProtKB:Q10984};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a lactoside III(4)-a-Fuc-Lc4Cer + GDP-beta-L-fucose = a
CC lactoside IV(2),III(4)-a-[Fuc]2-Lc4Cer + GDP + H(+);
CC Xref=Rhea:RHEA:62616, ChEBI:CHEBI:15378, ChEBI:CHEBI:57273,
CC ChEBI:CHEBI:58189, ChEBI:CHEBI:90811, ChEBI:CHEBI:142612;
CC Evidence={ECO:0000269|PubMed:11368156};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:62617;
CC Evidence={ECO:0000305|PubMed:11368156};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=beta-D-galactosyl-(1->3)-N-acetyl-D-galactosamine + GDP-beta-
CC L-fucose = alpha-L-fucosyl-(1->2)-beta-D-galactosyl-(1->3)-N-acetyl-
CC D-galactosamine + GDP + H(+); Xref=Rhea:RHEA:62964,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57273, ChEBI:CHEBI:58189,
CC ChEBI:CHEBI:84728, ChEBI:CHEBI:546807;
CC Evidence={ECO:0000250|UniProtKB:Q28113};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:62965;
CC Evidence={ECO:0000250|UniProtKB:Q28113};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=10.2 mM for phenyl-beta-D-galactoside
CC {ECO:0000269|PubMed:11323419};
CC KM=54.73 mM for phenyl-beta-D-galactoside
CC {ECO:0000269|PubMed:11368156};
CC KM=36.46 mM for lactose {ECO:0000269|PubMed:11368156};
CC KM=50 uM for ganglioside GA1 {ECO:0000269|PubMed:14967068};
CC KM=500 uM for ganglioside GM1a {ECO:0000269|PubMed:14967068};
CC KM=166 uM for nLc4Cer {ECO:0000269|PubMed:14967068};
CC KM=95 uM for Lc4Cer {ECO:0000269|PubMed:14967068};
CC -!- PATHWAY: Protein modification; protein glycosylation.
CC {ECO:0000269|PubMed:11323419}.
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 -!- TISSUE SPECIFICITY: Expressed in stomach, colon, ovary and uterus,
CC specifically in luminal uterine epithelium (PubMed:11323419,
CC PubMed:11368156). Expressed in various tissues including heart, liver,
CC kidney, testis, epididymis, small intestine,and cecum
CC (PubMed:11368156). Expressed in duodenum, jejunum and ileum
CC (PubMed:14967068). {ECO:0000269|PubMed:11323419,
CC ECO:0000269|PubMed:11368156, ECO:0000269|PubMed:14967068}.
CC -!- DEVELOPMENTAL STAGE: Detected at highest levels in proestrus and
CC estrus, with 10- to 12-fold increases over early diestrus.
CC {ECO:0000269|PubMed:11323419}.
CC -!- INDUCTION: Induced after microbes administration in the intestinal
CC epithelia, particularly in the duodenal and jejunal epithelia
CC (PubMed:11368156, PubMed:14967068). Down-regulated by androgen in the
CC caput epididymis (PubMed:24284406). {ECO:0000269|PubMed:11368156,
CC ECO:0000269|PubMed:14967068, ECO:0000269|PubMed:24284406}.
CC -!- DISRUPTION PHENOTYPE: Homozygous knockout mice for FUT2 are fertiles
CC and develop normally and exhibit no gross phenotypic abnormalities.
CC {ECO:0000269|PubMed:11713270}.
CC -!- MISCELLANEOUS: In mouse, there are three genes (Fut1, Fut2 and Sec1)
CC which encode galactoside 2-L-fucosyltransferase.
CC {ECO:0000269|PubMed:11323419}.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 11 family.
CC {ECO:0000305}.
CC -!- WEB RESOURCE: Name=Functional Glycomics Gateway - GTase;
CC Note=Fucosyltransferase 2;
CC URL="http://www.functionalglycomics.org/glycomics/molecule/jsp/glycoEnzyme/viewGlycoEnzyme.jsp?gbpId=gt_mou_612";
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DR EMBL; AF064792; AAC16887.1; -; mRNA.
DR EMBL; AF214656; AAF45146.1; -; Genomic_DNA.
DR EMBL; AK033520; BAC28338.1; -; mRNA.
DR CCDS; CCDS21258.1; -.
DR RefSeq; NP_001258922.1; NM_001271993.1.
DR RefSeq; NP_061364.2; NM_018876.4.
DR RefSeq; XP_011249097.1; XM_011250795.1.
DR AlphaFoldDB; Q9JL27; -.
DR STRING; 10090.ENSMUSP00000063719; -.
DR SwissLipids; SLP:000001426; -.
DR CAZy; GT11; Glycosyltransferase Family 11.
DR GlyGen; Q9JL27; 4 sites.
DR PhosphoSitePlus; Q9JL27; -.
DR MaxQB; Q9JL27; -.
DR PaxDb; Q9JL27; -.
DR PRIDE; Q9JL27; -.
DR ProteomicsDB; 271614; -.
DR Antibodypedia; 2644; 153 antibodies from 30 providers.
DR DNASU; 14344; -.
DR Ensembl; ENSMUST00000069800; ENSMUSP00000063719; ENSMUSG00000055978.
DR GeneID; 14344; -.
DR KEGG; mmu:14344; -.
DR UCSC; uc009gwn.2; mouse.
DR CTD; 2524; -.
DR MGI; MGI:109374; Fut2.
DR VEuPathDB; HostDB:ENSMUSG00000055978; -.
DR eggNOG; ENOG502S316; Eukaryota.
DR GeneTree; ENSGT00390000001450; -.
DR HOGENOM; CLU_043399_0_1_1; -.
DR InParanoid; Q9JL27; -.
DR OMA; KGMWTIN; -.
DR OrthoDB; 1006406at2759; -.
DR PhylomeDB; Q9JL27; -.
DR TreeFam; TF315810; -.
DR BRENDA; 2.4.1.344; 3474.
DR BRENDA; 2.4.1.69; 3474.
DR Reactome; R-MMU-9033807; ABO blood group biosynthesis.
DR Reactome; R-MMU-9037629; Lewis blood group biosynthesis.
DR SABIO-RK; Q9JL27; -.
DR UniPathway; UPA00378; -.
DR BioGRID-ORCS; 14344; 1 hit in 76 CRISPR screens.
DR PRO; PR:Q9JL27; -.
DR Proteomes; UP000000589; Chromosome 7.
DR RNAct; Q9JL27; protein.
DR Bgee; ENSMUSG00000055978; Expressed in lip and 68 other tissues.
DR ExpressionAtlas; Q9JL27; baseline and differential.
DR Genevisible; Q9JL27; 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:0031127; F:alpha-(1,2)-fucosyltransferase activity; IDA:UniProtKB.
DR GO; GO:0008417; F:fucosyltransferase activity; IDA:MGI.
DR GO; GO:0008107; F:galactoside 2-alpha-L-fucosyltransferase activity; IDA:MGI.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR GO; GO:0036065; P:fucosylation; IDA:UniProtKB.
DR GO; GO:0006664; P:glycolipid metabolic process; IMP:UniProtKB.
DR GO; GO:0006486; P:protein glycosylation; IDA:MGI.
DR GO; GO:0030155; P:regulation of cell adhesion; ISS:UniProtKB.
DR GO; GO:0001936; P:regulation of endothelial cell proliferation; ISS:UniProtKB.
DR InterPro; IPR002516; Glyco_trans_11.
DR PANTHER; PTHR11927; PTHR11927; 1.
DR Pfam; PF01531; Glyco_transf_11; 1.
PE 1: Evidence at protein level;
KW Glycoprotein; Glycosyltransferase; Golgi apparatus; Lipid metabolism;
KW Membrane; Reference proteome; Signal-anchor; Transferase; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..347
FT /note="Galactoside alpha-(1,2)-fucosyltransferase 2"
FT /id="PRO_0000149109"
FT TOPO_DOM 1..5
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 6..26
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 27..347
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT CARBOHYD 192
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 258
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 286
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 312
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CONFLICT 31
FT /note="R -> Q (in Ref. 1; AAC16887)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 347 AA; 39243 MW; DD5F441046CC8E79 CRC64;
MASAQVPFSF PLAHFLIFVF VTSTIIHLQQ RIVKLQTLSE KELQAVQMSS PNAARTDMQQ
SAKLQGIFTI NSIGRLGNQM GEYATLFALA RMNGRLAFIP ESMHNALAPI FRISLPVLHS
DTARRIPWQN YHLNDWMEER YRHIPGQYVR FTGYPCSWTF YHHLRPEILK EFTLHDHVRE
EAQAFLRGLR VNGSQPSTFV GVHVRRGDYV HVMPKVWKGV VADRGYLEKA LDRFRARYSS
PVFVVTSNGM AWCRENINTS LGDVVFAGNG IEGSPAKDFA LLTQCNHTIM TIGTFGIWAA
YLAGGDTIYL ANYTLPDSPF LKIFKPAAAF LPEWMGIPAD LSPLLKH
