Descriptions

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

Autoinhibitory domains (AIDs)

Target domain

Relief mechanism

Assay

cis-regPred

Accessory elements

No accessory elements

Autoinhibited structure

Activated structure

1 structures for Q9VUL9

Entry ID Method Resolution Chain Position Source
AF-Q9VUL9-F1 Predicted AlphaFoldDB

No variants for Q9VUL9

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for Q9VUL9

No associated diseases with Q9VUL9

1 regional properties for Q9VUL9

Type Name Position InterPro Accession
domain Fucosyltransferase, N-terminal 173 - 277 IPR031481

Functions

Description
EC Number 2.4.1.214 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

3 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.
Golgi medial cisterna The middle Golgi cisterna (or cisternae).
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.

3 GO annotations of molecular function

Name Definition
alpha-(1->3)-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->3) linkage.
fucosyltransferase activity Catalysis of the transfer of a fucosyl group to an acceptor molecule, typically another carbohydrate or a lipid.
glycoprotein 3-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->3)]-N-acetyl-beta-D-glucosaminyl}-L-asparagine + GDP + H(+).

4 GO annotations of biological process

Name Definition
fucosylation The covalent attachment of a fucosyl group to an acceptor molecule.
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.
nervous system development The process whose specific outcome is the progression of nervous tissue over time, from its formation to its mature state.
protein glycosylation A protein modification process that results in the addition of a carbohydrate or carbohydrate derivative unit to a protein amino acid, e.g. the addition of glycan chains to proteins.

2 homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
Q11131 Fut7 Alpha-(1,3)-fucosyltransferase 7 Mus musculus (Mouse) PR
Q6A1G3 fut10 Alpha-(1,3)-fucosyltransferase 10 Xenopus tropicalis (Western clawed frog) (Silurana tropicalis) PR
10 20 30 40 50 60
MRRPKISLKK YFYLTLICAL LLIFGFSLKE REIWKTLSPR SSQITTQQQQ HQHLHQLQSM
70 80 90 100 110 120
DEEHPMATSS TPPPIAATLL PEVADNLVEE PEQTVLEEEE SEADRLQEPP AEKAWFFKNG
130 140 150 160 170 180
EYYPKPAKTY SNRKARKRHA PRLLPHQDPY SDRIINQLMY VPHNYEEIKS SGKLKTILLY
190 200 210 220 230 240
NGLGPWNVKK GRDVFLKAKC PVDTCELTAN RDLASTADMI LYKDHYIPTG IRRPSNSKQV
250 260 270 280 290 300
SMLYYLECPY HTQNVKVPDA INWTATYRRD STIVAPYEKW QYYDTKVQQQ EQDINYSVNK
310 320 330 340 350 360
TKKVAWFVSN CGARNGRLQY AHELQKYIEV DIYGACGNFK CSRSTADKCF EILDNDYKFY
370 380 390 400 410 420
LAFENSNCKD YITEKFFVNA LNRRVLPIVM GARPEDYEVS APRRSYIHVD EFSSPKELAE
430 440 450 460 470 480
YLRILDHDDE LYNSYFKWKG TGEFINTYYW CRVCATLHNE EQLRKPRWYT DLNDWWRGPG
490 500
VCTTRSWRNF KARKDVISDS SDD