FUT7_MOUSE
ID FUT7_MOUSE Reviewed; 389 AA.
AC Q11131; Q0VGH5;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 158.
DE RecName: Full=Alpha-(1,3)-fucosyltransferase 7 {ECO:0000305};
DE EC=2.4.1.- {ECO:0000269|PubMed:11485743, ECO:0000269|PubMed:8626519, ECO:0000269|PubMed:8752218};
DE AltName: Full=Fucosyltransferase 7;
DE AltName: Full=Fucosyltransferase VII {ECO:0000250|UniProtKB:Q11130};
DE Short=Fuc-TVII {ECO:0000250|UniProtKB:Q11130};
DE Short=FucT-VII;
DE AltName: Full=Galactoside 3-L-fucosyltransferase;
GN Name=Fut7 {ECO:0000312|MGI:MGI:107692};
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 [GENOMIC DNA] (ISOFORMS 1 AND 2), TISSUE SPECIFICITY,
RP CATALYTIC ACTIVITY, AND FUNCTION.
RC STRAIN=NIH Swiss;
RX PubMed=8626519; DOI=10.1074/jbc.271.14.8250;
RA Smith P.L., Gersten K.M., Petryniak B., Kelly R.J., Rogers C., Natsuka Y.,
RA Alford J.A. III, Scheidegger E.P., Natsuka S., Lowe J.B.;
RT "Expression of the alpha(1,3)fucosyltransferase Fuc-TVII in lymphoid
RT aggregate high endothelial venules correlates with expression of L-selectin
RT ligands.";
RL J. Biol. Chem. 271:8250-8259(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
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 FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=8752218; DOI=10.1016/s0092-8674(00)80137-3;
RA Maly P., Thall A., Petryniak B., Rogers C.E., Smith P.L., Marks R.M.,
RA Kelly R.J., Gersten K.M., Cheng G., Saunders T.L., Camper S.A.,
RA Camphausen R.T., Sullivan F.X., Isogai Y., Hindsgaul O., von Andrian U.H.,
RA Lowe J.B.;
RT "The alpha(1,3)fucosyltransferase Fuc-TVII controls leukocyte trafficking
RT through an essential role in L-, E-, and P-selectin ligand biosynthesis.";
RL Cell 86:643-653(1996).
RN [4]
RP FUNCTION.
RX PubMed=10894166; DOI=10.1016/s1074-7613(00)80217-4;
RA Weninger W., Ulfman L.H., Cheng G., Souchkova N., Quackenbush E.J.,
RA Lowe J.B., von Andrian U.H.;
RT "Specialized contributions by alpha(1,3)-fucosyltransferase-IV and FucT-VII
RT during leukocyte rolling in dermal microvessels.";
RL Immunity 12:665-676(2000).
RN [5]
RP FUNCTION.
RX PubMed=10882744; DOI=10.1074/jbc.m005449200;
RA Huang M.C., Zoellner O., Moll T., Maly P., Thall A.D., Lowe J.B.,
RA Vestweber D.;
RT "P-selectin glycoprotein ligand-1 and E-selectin ligand-1 are
RT differentially modified by fucosyltransferases Fuc-TIV and Fuc-TVII in
RT mouse neutrophils.";
RL J. Biol. Chem. 275:31353-31360(2000).
RN [6]
RP FUNCTION, CATALYTIC ACTIVITY, AND PATHWAY.
RX PubMed=11485743; DOI=10.1016/s1074-7613(01)00166-2;
RA Homeister J.W., Thall A.D., Petryniak B., Maly P., Rogers C.E., Smith P.L.,
RA Kelly R.J., Gersten K.M., Askari S.W., Cheng G., Smithson G., Marks R.M.,
RA Misra A.K., Hindsgaul O., von Andrian U.H., Lowe J.B.;
RT "The alpha(1,3)fucosyltransferases FucT-IV and FucT-VII exert collaborative
RT control over selectin-dependent leukocyte recruitment and lymphocyte
RT homing.";
RL Immunity 15:115-126(2001).
RN [7]
RP FUNCTION.
RX PubMed=11535629; DOI=10.1084/jem.194.5.601;
RA Smithson G., Rogers C.E., Smith P.L., Scheidegger E.P., Petryniak B.,
RA Myers J.T., Kim D.S., Homeister J.W., Lowe J.B.;
RT "Fuc-TVII is required for T helper 1 and T cytotoxic 1 lymphocyte selectin
RT ligand expression and recruitment in inflammation, and together with Fuc-
RT TIV regulates naive T cell trafficking to lymph nodes.";
RL J. Exp. Med. 194:601-614(2001).
RN [8]
RP FUNCTION.
RX PubMed=12359718; DOI=10.1074/jbc.m208283200;
RA Huang M.C., Laskowska A., Vestweber D., Wild M.K.;
RT "The alpha (1,3)-fucosyltransferase Fuc-TIV, but not Fuc-TVII, generates
RT sialyl Lewis X-like epitopes preferentially on glycolipids.";
RL J. Biol. Chem. 277:47786-47795(2002).
RN [9]
RP FUNCTION.
RX PubMed=15843584; DOI=10.4049/jimmunol.174.9.5805;
RA Piccio L., Rossi B., Colantonio L., Grenningloh R., Gho A., Ottoboni L.,
RA Homeister J.W., Scarpini E., Martinello M., Laudanna C., D'Ambrosio D.,
RA Lowe J.B., Constantin G.;
RT "Efficient recruitment of lymphocytes in inflamed brain venules requires
RT expression of cutaneous lymphocyte antigen and fucosyltransferase-VII.";
RL J. Immunol. 174:5805-5813(2005).
CC -!- FUNCTION: Catalyzes the transfer of L-fucose, from a guanosine
CC diphosphate-beta-L-fucose, to the N-acetyl glucosamine (GlcNAc) of a
CC distal alpha2,3 sialylated lactosamine unit of a glycoprotein or a
CC glycolipid-linked sialopolylactosamines chain through an alpha-1,3
CC glycosidic linkage and participates in the final fucosylation step in
CC the biosynthesis of the sialyl Lewis X (sLe(x)), a carbohydrate
CC involved in cell and matrix adhesion during leukocyte trafficking and
CC fertilization (PubMed:8752218, PubMed:8626519, PubMed:15843584,
CC PubMed:10882744, PubMed:11535629, PubMed:12359718, PubMed:11485743). In
CC vitro, also synthesizes sialyl-dimeric-Lex structures, from VIM-2
CC structures and both di-fucosylated and trifucosylated structures from
CC mono-fucosylated precursors (By similarity). However does not catalyze
CC alpha 1-3 fucosylation when an internal alpha 1-3 fucosylation is
CC present in polylactosamine chain and the fucosylation rate of the
CC internal GlcNAc residues is reduced once fucose has been added to the
CC distal GlcNAc (By similarity). Also catalyzes the transfer of a fucose
CC from GDP-beta-fucose to the 6-sulfated a(2,3)sialylated substrate to
CC produce 6-sulfo sLex mediating significant L-selectin-dependent cell
CC adhesion (PubMed:8752218, PubMed:10894166). Through sialyl-Lewis(x)
CC biosynthesis, can control SELE- and SELP-mediated cell adhesion with
CC leukocytes and allows leukocytes tethering and rolling along the
CC endothelial tissue thereby enabling the leukocytes to accumulate at a
CC site of inflammation (PubMed:15843584, PubMed:8752218, PubMed:10882744,
CC PubMed:11535629). May enhance embryo implantation through sialyl Lewis
CC X (sLeX)-mediated adhesion of embryo cells to endometrium (By
CC similarity). May affect insulin signaling by up-regulating the
CC phosphorylation and expression of some signaling molecules involved in
CC the insulin-signaling pathway through SLe(x) which is present on the
CC glycans of the INSRR alpha subunit (By similarity).
CC {ECO:0000250|UniProtKB:Q11130, ECO:0000269|PubMed:10882744,
CC ECO:0000269|PubMed:10894166, ECO:0000269|PubMed:11535629,
CC ECO:0000269|PubMed:12359718, ECO:0000269|PubMed:15843584,
CC ECO:0000269|PubMed:8626519, ECO:0000269|PubMed:8752218}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=an N-acetyl-alpha-neuraminyl-(2->3)-beta-D-galactosyl-(1->4)-
CC N-acetyl-beta-D-glucosaminyl derivative + GDP-beta-L-fucose = an
CC alpha-Neu5Ac-(2->3)-beta-D-Gal-(1->4)-[alpha-L-Fuc-(1->3)]-beta-D-
CC GlcNAc derivative + GDP + H(+); Xref=Rhea:RHEA:56076,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57273, ChEBI:CHEBI:58189,
CC ChEBI:CHEBI:136545, ChEBI:CHEBI:139509;
CC Evidence={ECO:0000269|PubMed:11485743, ECO:0000269|PubMed:8626519,
CC ECO:0000269|PubMed:8752218};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:56077;
CC Evidence={ECO:0000305|PubMed:11485743, ECO:0000305|PubMed:8626519,
CC ECO:0000305|PubMed:8752218};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=an alpha-Neu5Ac-(2->3)-beta-D-Gal-(1->4)-beta-D-GlcNAc6S
CC derivative + GDP-beta-L-fucose = an alpha-Neu5Ac-(2->3)-beta-D-Gal-
CC (1->4)-[alpha-L-Fuc-(1->3)]-beta-D-GlcNAc6S derivative + GDP + H(+);
CC Xref=Rhea:RHEA:62004, ChEBI:CHEBI:15378, ChEBI:CHEBI:57273,
CC ChEBI:CHEBI:58189, ChEBI:CHEBI:145344, ChEBI:CHEBI:145345;
CC Evidence={ECO:0000269|PubMed:11485743, ECO:0000269|PubMed:8752218};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:62005;
CC Evidence={ECO:0000305|PubMed:11485743, ECO:0000305|PubMed:8752218};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a neolactoside IV(3)-alpha-NeuAc-nLc4Cer + GDP-beta-L-fucose =
CC GDP + H(+) + N-acetyl-alpha-neuraminosyl-(2->3)-beta-D-galactosyl-
CC (1->4)-[alpha-L-fucosyl-(1->3)]-N-acetyl-beta-D-glucosaminyl-(1->3)-
CC beta-D-galactosyl-(1->4)-beta-D-glucosyl-(1<->1')-ceramide;
CC Xref=Rhea:RHEA:48392, ChEBI:CHEBI:15378, ChEBI:CHEBI:57273,
CC ChEBI:CHEBI:58189, ChEBI:CHEBI:90390, ChEBI:CHEBI:90392;
CC Evidence={ECO:0000250|UniProtKB:Q11130};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:48393;
CC Evidence={ECO:0000250|UniProtKB:Q11130};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=GDP-beta-L-fucose + N-acetyl-alpha-neuraminosyl-(2->3)-beta-D-
CC galactosyl-(1->4)-N-acetyl-beta-D-glucosaminyl-(1->3)-beta-D-
CC galactosyl-(1->4)-N-acetyl-beta-D-glucosaminyl-(1->3)-beta-D-
CC galactosyl-(1->4)-beta-D-glucosyl-(1<->1')-ceramide = GDP + H(+) + N-
CC acetyl-alpha-neuraminosyl-(2->3)-beta-D-galactosyl-(1->4)-[alpha-L-
CC fucosyl-(1->3)]-N-acetyl-beta-D-glucosaminyl-(1->3)-beta-D-
CC galactosyl-(1->4)-N-acetyl-beta-D-glucosaminyl-(1->3)-beta-D-
CC galactosyl-(1->4)-beta-D-glucosyl-(1<->1')-ceramide;
CC Xref=Rhea:RHEA:48356, ChEBI:CHEBI:15378, ChEBI:CHEBI:57273,
CC ChEBI:CHEBI:58189, ChEBI:CHEBI:90336, ChEBI:CHEBI:90339;
CC Evidence={ECO:0000250|UniProtKB:Q11130};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:48357;
CC Evidence={ECO:0000250|UniProtKB:Q11130};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=an alpha-Neu5Ac-(2->3)-beta-D-Gal-(1->4)-beta-D-GlcNAc-(1->3)-
CC beta-D-Gal-(1->4)-[alpha-L-Fuc-(1->3)]-beta-D-GlcNAc derivative +
CC GDP-beta-L-fucose = an alpha-Neu5Ac-(2->3)-beta-D-Gal-(1->4)-[alpha-
CC L-Fuc-(1->3)]-beta-D-GlcNAc-(1->3)-beta-D-Gal-(1->4)-[alpha-L-Fuc-
CC (1->3)]-beta-D-GlcNAc derivative + GDP + H(+); Xref=Rhea:RHEA:52864,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57273, ChEBI:CHEBI:58189,
CC ChEBI:CHEBI:145342, ChEBI:CHEBI:145343;
CC Evidence={ECO:0000250|UniProtKB:Q11130};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:52865;
CC Evidence={ECO:0000250|UniProtKB:Q11130};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=alpha-Neu5Ac-(2->3)-beta-D-Gal-(1->4)-beta-D-GlcNAc-(1->3)-
CC beta-D-Gal-(1->4)-D-Glc + GDP-beta-L-fucose = alpha-Neu5Ac-(2->3)-
CC beta-D-Gal-(1->4)-[alpha-L-Fuc-(1->3)]-beta-D-GlcNAc-(1->3)-beta-D-
CC Gal-(1->4)-D-Glc + GDP + H(+); Xref=Rhea:RHEA:62008,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57273, ChEBI:CHEBI:58189,
CC ChEBI:CHEBI:145346, ChEBI:CHEBI:145347;
CC Evidence={ECO:0000250|UniProtKB:Q11130};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:62009;
CC Evidence={ECO:0000250|UniProtKB:Q11130};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=alpha-Neu5Ac-(2->3)-beta-D-Gal-(1->4)-beta-D-GlcNAc-(1->3)-
CC beta-D-Gal-(1->4)-[alpha-L-Fuc-(1->3)]-beta-D-GlcNAc-(1->3)-beta-D-
CC Gal-(1->4)-beta-D-GlcNAc + GDP-beta-L-fucose = alpha-Neu5Ac-(2->3)-
CC beta-D-Gal-(1->4)-[alpha-L-Fuc-(1->3)]-beta-D-GlcNAc-(1->3)-beta-D-
CC Gal-(1->4)-[alpha-L-Fuc-(1->3)]-beta-D-GlcNAc-(1->3)-beta-D-Gal-
CC (1->4)-beta-D-GlcNAc + GDP + H(+); Xref=Rhea:RHEA:62060,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57273, ChEBI:CHEBI:58189,
CC ChEBI:CHEBI:145400, ChEBI:CHEBI:145401;
CC Evidence={ECO:0000250|UniProtKB:Q11130};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:62061;
CC Evidence={ECO:0000250|UniProtKB:Q11130};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=alpha-Neu5Ac-(2->3)-beta-D-Gal-(1->4)-beta-D-GlcNAc-(1->3)-
CC beta-D-Gal-(1->4)-beta-D-GlcNAc-(1->3)-beta-D-Gal-(1->4)-beta-D-
CC GlcNAc + GDP-beta-L-fucose = alpha-Neu5Ac-(2->3)-beta-D-Gal-(1->4)-
CC [alpha-L-Fuc-(1->3)]-beta-D-GlcNAc-(1->3)-beta-D-Gal-(1->4)-beta-D-
CC GlcNAc-(1->3)-beta-D-Gal-(1->4)-beta-D-GlcNAc + GDP + H(+);
CC Xref=Rhea:RHEA:62056, ChEBI:CHEBI:15378, ChEBI:CHEBI:57273,
CC ChEBI:CHEBI:58189, ChEBI:CHEBI:145398, ChEBI:CHEBI:145399;
CC Evidence={ECO:0000250|UniProtKB:Q11130};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:62057;
CC Evidence={ECO:0000250|UniProtKB:Q11130};
CC -!- ACTIVITY REGULATION: Inhibited by NaCl. Inhibited by GDP in a
CC concentration dependent manner, with an IC(50) value of 93 uM. Also
CC inhibited by GMP and GTP. Inhibited by N-ethylmaleimide. Activated by
CC poly(ethylene glycol) by enhancing the thermal stability of FUT7.
CC Activated by Mn2+, Ca2+, and Mg2+. Both panosialin A and B inhibit
CC activity with IC(50) values of 4.8 and 5.3 ug/ml, respectively.
CC Inhibited by gallic acid (GA) and (-)-epigallocatechin gallate (EGCG)
CC in a time-dependent and irreversible manner with IC(50) values of 60
CC and 700 nM, respectively. {ECO:0000250|UniProtKB:Q11130}.
CC -!- PATHWAY: Protein modification; protein glycosylation.
CC {ECO:0000269|PubMed:11485743}.
CC -!- SUBCELLULAR LOCATION: Golgi apparatus, Golgi stack membrane; Single-
CC pass type II membrane protein. Note=Membrane-bound form in trans
CC cisternae of Golgi.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q11131-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q11131-2; Sequence=VSP_001781;
CC -!- TISSUE SPECIFICITY: Highly expressed in lung and bone marrow and to a
CC much lesser extent in spleen, salivary gland and skeletal muscle.
CC {ECO:0000269|PubMed:8626519}.
CC -!- PTM: N-glycosylated. {ECO:0000250|UniProtKB:Q11130}.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 10 family.
CC {ECO:0000305}.
CC -!- WEB RESOURCE: Name=Functional Glycomics Gateway - GTase;
CC Note=Fucosyltransferase 7;
CC URL="http://www.functionalglycomics.org/glycomics/molecule/jsp/glycoEnzyme/viewGlycoEnzyme.jsp?gbpId=gt_mou_614";
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DR EMBL; U45980; AAC52484.1; -; Genomic_DNA.
DR EMBL; U45980; AAC52485.1; -; Genomic_DNA.
DR EMBL; BC105670; AAI05671.1; -; mRNA.
DR CCDS; CCDS15772.1; -. [Q11131-2]
DR CCDS; CCDS50530.1; -. [Q11131-1]
DR RefSeq; NP_001170837.1; NM_001177366.1. [Q11131-1]
DR RefSeq; NP_001170838.1; NM_001177367.1. [Q11131-2]
DR RefSeq; NP_001276382.1; NM_001289453.1. [Q11131-2]
DR RefSeq; NP_001276383.1; NM_001289454.1. [Q11131-2]
DR RefSeq; NP_001276384.1; NM_001289455.1. [Q11131-2]
DR RefSeq; NP_001276385.1; NM_001289456.1. [Q11131-2]
DR RefSeq; NP_038552.1; NM_013524.3. [Q11131-2]
DR RefSeq; XP_006497767.1; XM_006497704.1. [Q11131-1]
DR AlphaFoldDB; Q11131; -.
DR STRING; 10090.ENSMUSP00000109917; -.
DR CAZy; GT10; Glycosyltransferase Family 10.
DR GlyGen; Q11131; 2 sites.
DR iPTMnet; Q11131; -.
DR PhosphoSitePlus; Q11131; -.
DR PaxDb; Q11131; -.
DR PRIDE; Q11131; -.
DR ProteomicsDB; 271651; -. [Q11131-1]
DR ProteomicsDB; 271652; -. [Q11131-2]
DR Antibodypedia; 32341; 157 antibodies from 26 providers.
DR DNASU; 14347; -.
DR Ensembl; ENSMUST00000041654; ENSMUSP00000039985; ENSMUSG00000036587. [Q11131-2]
DR Ensembl; ENSMUST00000100320; ENSMUSP00000097895; ENSMUSG00000036587. [Q11131-1]
DR Ensembl; ENSMUST00000114278; ENSMUSP00000109917; ENSMUSG00000036587. [Q11131-2]
DR GeneID; 14347; -.
DR KEGG; mmu:14347; -.
DR UCSC; uc012bry.1; mouse. [Q11131-1]
DR CTD; 2529; -.
DR MGI; MGI:107692; Fut7.
DR VEuPathDB; HostDB:ENSMUSG00000036587; -.
DR eggNOG; KOG2619; Eukaryota.
DR GeneTree; ENSGT00940000161618; -.
DR HOGENOM; CLU_032075_4_1_1; -.
DR InParanoid; Q11131; -.
DR OMA; SDTCTRY; -.
DR OrthoDB; 551308at2759; -.
DR PhylomeDB; Q11131; -.
DR TreeFam; TF316348; -.
DR BRENDA; 2.4.1.152; 3474.
DR Reactome; R-MMU-9037629; Lewis blood group biosynthesis.
DR UniPathway; UPA00378; -.
DR BioGRID-ORCS; 14347; 2 hits in 74 CRISPR screens.
DR PRO; PR:Q11131; -.
DR Proteomes; UP000000589; Chromosome 2.
DR RNAct; Q11131; protein.
DR Bgee; ENSMUSG00000036587; Expressed in granulocyte and 24 other tissues.
DR ExpressionAtlas; Q11131; baseline and differential.
DR Genevisible; Q11131; MM.
DR GO; GO:0005794; C:Golgi apparatus; ISO:MGI.
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:0005802; C:trans-Golgi network; ISO:MGI.
DR GO; GO:0017083; F:4-galactosyl-N-acetylglucosaminide 3-alpha-L-fucosyltransferase activity; ISS:UniProtKB.
DR GO; GO:0046920; F:alpha-(1->3)-fucosyltransferase activity; IDA:UniProtKB.
DR GO; GO:0008417; F:fucosyltransferase activity; ISS:UniProtKB.
DR GO; GO:0002361; P:CD4-positive, CD25-positive, alpha-beta regulatory T cell differentiation; IMP:MGI.
DR GO; GO:0006672; P:ceramide metabolic process; ISO:MGI.
DR GO; GO:0007566; P:embryo implantation; ISS:UniProtKB.
DR GO; GO:0036065; P:fucosylation; IBA:GO_Central.
DR GO; GO:0006954; P:inflammatory response; ISS:UniProtKB.
DR GO; GO:0002522; P:leukocyte migration involved in immune response; IMP:MGI.
DR GO; GO:0002523; P:leukocyte migration involved in inflammatory response; IMP:UniProtKB.
DR GO; GO:0097022; P:lymphocyte migration into lymph node; IMP:UniProtKB.
DR GO; GO:0097021; P:lymphocyte migration into lymphoid organs; IMP:UniProtKB.
DR GO; GO:0045785; P:positive regulation of cell adhesion; ISS:UniProtKB.
DR GO; GO:0022409; P:positive regulation of cell-cell adhesion; ISS:UniProtKB.
DR GO; GO:1904996; P:positive regulation of leukocyte adhesion to vascular endothelial cell; ISS:UniProtKB.
DR GO; GO:1903238; P:positive regulation of leukocyte tethering or rolling; IMP:UniProtKB.
DR GO; GO:1902624; P:positive regulation of neutrophil migration; IMP:UniProtKB.
DR GO; GO:0006486; P:protein glycosylation; ISS:UniProtKB.
DR GO; GO:0060353; P:regulation of cell adhesion molecule production; ISO:MGI.
DR GO; GO:0022407; P:regulation of cell-cell adhesion; ISS:UniProtKB.
DR GO; GO:0046626; P:regulation of insulin receptor signaling pathway; ISS:UniProtKB.
DR GO; GO:1904994; P:regulation of leukocyte adhesion to vascular endothelial cell; IMP:UniProtKB.
DR GO; GO:1903037; P:regulation of leukocyte cell-cell adhesion; ISO:MGI.
DR GO; GO:1903236; P:regulation of leukocyte tethering or rolling; ISO:MGI.
DR GO; GO:2000389; P:regulation of neutrophil extravasation; IMP:UniProtKB.
DR GO; GO:0001807; P:regulation of type IV hypersensitivity; IMP:UniProtKB.
DR GO; GO:0072678; P:T cell migration; IMP:MGI.
DR Gene3D; 3.40.50.11660; -; 1.
DR InterPro; IPR031481; Glyco_tran_10_N.
DR InterPro; IPR001503; Glyco_trans_10.
DR InterPro; IPR038577; GT10-like_C_sf.
DR PANTHER; PTHR11929; PTHR11929; 1.
DR Pfam; PF17039; Glyco_tran_10_N; 1.
DR Pfam; PF00852; Glyco_transf_10; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Disulfide bond; Glycoprotein; Glycosyltransferase;
KW Golgi apparatus; Membrane; Reference proteome; Signal-anchor; Transferase;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..389
FT /note="Alpha-(1,3)-fucosyltransferase 7"
FT /id="PRO_0000221114"
FT TOPO_DOM 1..55
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 56..78
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 79..389
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT CARBOHYD 128
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 338
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 115..123
FT /evidence="ECO:0000250|UniProtKB:Q11130"
FT DISULFID 258..261
FT /evidence="ECO:0000250|UniProtKB:Q11130"
FT DISULFID 365..368
FT /evidence="ECO:0000250|UniProtKB:Q11130"
FT VAR_SEQ 1..51
FT /note="MPTPCPPACLSTPGTHRLLPFPDWKAPSWESRKEATCNSSSPGPWAEPTVQ
FT -> MNCI (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_001781"
SQ SEQUENCE 389 AA; 44495 MW; 118FC6B2378B99C6 CRC64;
MPTPCPPACL STPGTHRLLP FPDWKAPSWE SRKEATCNSS SPGPWAEPTV QGYHPTRRLR
AWGGLAGGAT FMVIWFFWLW GSAPGSAPVP QSTLTILIWH WPFTNRPPEL PGDTCTRYGM
ASCRLSANRS LLASADAVVF HHRELQTRQS LLPLDQRPHG QPWVWASMES PSNTHGLHRF
RGIFNWVLSY RRDSDIFVPY GRLEPLSGPT SPLPAKSRMA AWVISNFQER QQRAKLYRQL
APHLQVDVFG RASGRPLCAN CLLPTLARYR FYLAFENSQH RDYITEKFWR NALAAGAVPV
ALGPPRATYE AFVPPDAFVH VDDFSSAREL AVFLVSMNES RYRGFFAWRD RLRVRLLGDW
RERFCTICAR YPYLPRSQVY EDLESWFQA
