P79282

PR
Gene name
FUT8
Protein name
Alpha-(1,6)-fucosyltransferase
Names
Alpha1-6FucT, Fucosyltransferase 8, GDP-L-Fuc:N-acetyl-beta-D-glucosaminide alpha1,6-fucosyltransferase, GDP-fucose--glycoprotein fucosyltransferase, Glycoprotein 6-alpha-L-fucosyltransferase
Species
Sus scrofa (Pig)
KEGG Pathway
ssc:396933
EC number
2.4.1.68: Hexosyltransferases
Protein Class

Descriptions

The autoinhibited protein was predicted that may have potential autoinhibitory elements via cis-regPred.

Autoinhibitory domains (AIDs)

9-138 (Predicted disordered autoinhibitory region) PR

Target domain

Relief mechanism

Assay

cis-regPred

Accessory elements

No accessory elements

References

Autoinhibited structure

Activated structure

1 structures for P79282

Entry ID Method Resolution Chain Position Source
AF-P79282-F1 Predicted AlphaFoldDB

No variants for P79282

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for P79282

No associated diseases with P79282

4 regional properties for P79282

Type Name Position InterPro Accession
domain SH3 domain 502 - 563 IPR001452
domain Glycosyltransferase family 23 (GT23) domain 206 - 493 IPR027350
domain Alpha-(1,6)-fucosyltransferase, SH3 domain 506 - 560 IPR035653
domain Alpha-(1,6)-fucosyltransferase, N- and catalytic domain 2 - 498 IPR045573

Functions

Description
EC Number 2.4.1.68 Hexosyltransferases
Subcellular Localization
  • Golgi apparatus, Golgi stack membrane ; Single-pass type II membrane protein
  • Membrane-bound form in trans cisternae of Golgi
PANTHER Family
PANTHER Subfamily
PANTHER Protein Class
PANTHER Pathway Category No pathway information available

2 GO annotations of cellular component

Name Definition
Golgi cisterna membrane The lipid bilayer surrounding any of the thin, flattened compartments that form the central portion of the Golgi complex.
integral component of membrane The component of a membrane consisting of the gene products and protein complexes having at least some part of their peptide sequence embedded in the hydrophobic region of the membrane.

4 GO annotations of molecular function

Name Definition
alpha-(1->6)-fucosyltransferase activity Catalysis of the transfer of an L-fucosyl group from GDP-beta-L-fucose to an acceptor molecule to form an alpha-(1->6) linkage.
glycoprotein 6-alpha-L-fucosyltransferase activity Catalysis of the reaction: N(4)-{N-acetyl-beta-D-glucosaminyl-(1->2)-alpha-D-mannosyl-(1->3)-[N-acetyl-beta-D-glucosaminyl-(1->2)-alpha-D-mannosyl-(1->6)]-beta-D-mannosyl-(1->4)-N-acetyl-beta-D-glucosaminyl-(1->4)-N-acetyl-beta-D-glucosaminyl}-L-asparagine + GDP-L-fucose = N(4)-{N-acetyl-beta-D-glucosaminyl-(1->2)-alpha-D-mannosyl-(1->3)-[N-acetyl-beta-D-glucosaminyl-(1->2)-alpha-D-mannosyl-(1->6)]-beta-D-mannosyl-(1->4)-N-acetyl-beta-D-glucosaminyl-(1->4)-[alpha-L-fucosyl-(1->6)]-N-acetyl-beta-D-glucosaminyl}asparagine + GDP + H(+).
glycosyltransferase activity Catalysis of the transfer of a glycosyl group from one compound (donor) to another (acceptor).
SH3 domain binding Binding to a SH3 domain (Src homology 3) of a protein, small protein modules containing approximately 50 amino acid residues found in a great variety of intracellular or membrane-associated proteins.

4 GO annotations of biological process

Name Definition
GDP-L-fucose metabolic process The chemical reactions and pathways involving GDP-L-fucose, a substance composed of L-fucose in glycosidic linkage with guanosine diphosphate.
N-glycan fucosylation The process of transferring a fucosyl group to an N-glycan. An N-glycan is the carbohydrate portion of an N-glycoprotein when attached to a nitrogen from asparagine or arginine side-chains.
protein N-linked glycosylation A protein glycosylation process in which a carbohydrate or carbohydrate derivative unit is added to a protein via the N4 atom of peptidyl-asparagine, the omega-N of arginine, or the N1' atom peptidyl-tryptophan.
protein N-linked glycosylation via asparagine The glycosylation of protein via the N4 atom of peptidyl-asparagine forming N4-glycosyl-L-asparagine; the most common form is N-acetylglucosaminyl asparagine; N-acetylgalactosaminyl asparagine and N4 glucosyl asparagine also occur. This modification typically occurs in extracellular peptides with an N-X-(ST) motif. Partial modification has been observed to occur with cysteine, rather than serine or threonine, in the third position; secondary structure features are important, and proline in the second or fourth positions inhibits modification.

2 homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
Q9WTS2 Fut8 Alpha-(1,6)-fucosyltransferase Mus musculus (Mouse) PR
Q6EV76 Fut8 Alpha-(1,6)-fucosyltransferase Rattus norvegicus (Rat) PR
10 20 30 40 50 60
MRPWTGSWRW IMLILFAWGT LLFYIGGHLV RDNDHSDHSS RELSKILAKL ERLKQQNEDL
70 80 90 100 110 120
RRMAESLRIP EGPIDQGPAS GRVRALEEQF MKAKEQIENY KKQTKNGPGK DHEILRRRIE
130 140 150 160 170 180
NGAKELWFFL QSELKKLKNL EGNELQRHAD EFLSDLGHHE RSIMTDLYYL SQTDGAGDWR
190 200 210 220 230 240
EKEAKDLTEL VQRRITYLQN PKDCSKAKKL VCNINKGCGY GCQLHHVVYC FMIAYGTQRT
250 260 270 280 290 300
LALESHNWRY ATGGWETVFR PVSETCTDRS GSSTGHWSGE VKDKNVQVVE LPIVDSVHPR
310 320 330 340 350 360
PPYLPLAVPE DLADRLVRVH GDPAVWWVSQ FVKYLIRPQP WLEKEIEEAT KKLGFKHPVI
370 380 390 400 410 420
GVHVRRTDKV GAEAAFHPIE EYTVHVEEDF QLLARRMQVD KKRVYLATDD PALLKEAKTK
430 440 450 460 470 480
YPSYEFISDN SISWSAGLHN RYTENSLRGV ILDIHFLSQA DFLVCTFSSQ VCRVAYEIMQ
490 500 510 520 530 540
ALHPDASANF RSLDDIYYFG GPNAHNQIAI YPHQPRTEGE IPMEPGDIIG VAGNHWDGYP
550 560 570
KGVNRKLGRT GLYPSYKVRE KIETVKYPTY PEADK