O00587 · MFNG_HUMAN
- ProteinBeta-1,3-N-acetylglucosaminyltransferase manic fringe
- GeneMFNG
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids321 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Glycosyltransferase that initiates the elongation of O-linked fucose residues attached to EGF-like repeats in the extracellular domain of Notch molecules (By similarity).
Modulates NOTCH1 activity by modifying O-fucose residues at specific EGF-like domains resulting in inhibition of NOTCH1 activation by JAG1 and enhancement of NOTCH1 activation by DLL1 via an increase in its binding to DLL1 (By similarity).
Modulates NOTCH1 activity by modifying O-fucose residues at specific EGF-like domains resulting in inhibition of NOTCH1 activation by JAG1 and enhancement of NOTCH1 activation by DLL1 via an increase in its binding to DLL1 (By similarity).
Catalytic activity
- 3-O-(alpha-L-fucosyl)-L-threonyl-[EGF-like domain protein] + UDP-N-acetyl-alpha-D-glucosamine = 3-O-(N-acetyl-beta-D-glucosaminyl-(1->3)-alpha-L-fucosyl)-L-threonyl-[EGF-like domain protein] + H+ + UDP
Cofactor
Note: Has some activity with cobalt, magnesium and calcium, but not zinc.
Features
Showing features for binding site, active site.
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | extracellular space | |
Cellular Component | Golgi membrane | |
Molecular Function | metal ion binding | |
Molecular Function | O-fucosylpeptide 3-beta-N-acetylglucosaminyltransferase activity | |
Biological Process | blastocyst formation | |
Biological Process | marginal zone B cell differentiation | |
Biological Process | pattern specification process | |
Biological Process | positive regulation of Notch signaling pathway | |
Biological Process | regulation of Notch signaling pathway |
Keywords
- Molecular function
- Ligand
Enzyme and pathway databases
Protein family/group databases
Names & Taxonomy
Protein names
- Recommended nameBeta-1,3-N-acetylglucosaminyltransferase manic fringe
- EC number
- Alternative names
Gene names
Organism names
- Organism
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Hominidae > Homo
Accessions
- Primary accessionO00587
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Golgi apparatus membrane ; Single-pass type II membrane protein
Features
Showing features for topological domain, transmembrane.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Topological domain | 1-7 | Cytoplasmic | ||||
Sequence: MQCRLPR | ||||||
Transmembrane | 8-27 | Helical; Signal-anchor for type II membrane protein | ||||
Sequence: GLAGALLTLLCMGLLCLRYH | ||||||
Topological domain | 28-321 | Lumenal | ||||
Sequence: LNLSPQRVQGTPELSQPNPGPPKLQLHDVFIAVKTTRAFHRLRLELLLDTWVSRTREQTFVFTDSPDKGLQERLGSHLVVTNCSAEHSHPALSCKMAAEFDTFLASGLRWFCHVDDDNYVNPRALLQLLRAFPLARDVYVGRPSLNRPIHASEPQPHNRTRLVQFWFATGGAGFCINRKLALKMAPWASGSRFMDTSALIRLPDDCTMGYIIECKLGGRLQPSPLFHSHLETLQLLRTAQLPEQVTLSYGVFEGKLNVIKLQGPFSPEEDPSRFRSLHCLLYPDTPWCPQLGAR |
Keywords
- Cellular component
Disease & Variants
Features
Showing features for natural variant.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Natural variant | VAR_024467 | 302 | in dbSNP:rs8192548 | |||
Sequence: R → C |
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 385 variants from UniProt as well as other sources including ClinVar and dbSNP.
Organism-specific databases
Miscellaneous
Genetic variation databases
PTM/Processing
Features
Showing features for chain, glycosylation, disulfide bond.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000219182 | 1-321 | Beta-1,3-N-acetylglucosaminyltransferase manic fringe | |||
Sequence: MQCRLPRGLAGALLTLLCMGLLCLRYHLNLSPQRVQGTPELSQPNPGPPKLQLHDVFIAVKTTRAFHRLRLELLLDTWVSRTREQTFVFTDSPDKGLQERLGSHLVVTNCSAEHSHPALSCKMAAEFDTFLASGLRWFCHVDDDNYVNPRALLQLLRAFPLARDVYVGRPSLNRPIHASEPQPHNRTRLVQFWFATGGAGFCINRKLALKMAPWASGSRFMDTSALIRLPDDCTMGYIIECKLGGRLQPSPLFHSHLETLQLLRTAQLPEQVTLSYGVFEGKLNVIKLQGPFSPEEDPSRFRSLHCLLYPDTPWCPQLGAR | ||||||
Glycosylation | 109 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Disulfide bond | 110↔121 | |||||
Sequence: CSAEHSHPALSC | ||||||
Disulfide bond | 139↔202 | |||||
Sequence: CHVDDDNYVNPRALLQLLRAFPLARDVYVGRPSLNRPIHASEPQPHNRTRLVQFWFATGGAGFC | ||||||
Glycosylation | 185 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Disulfide bond | 306↔315 | |||||
Sequence: CLLYPDTPWC |
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Structure
Sequence & Isoform
- Sequence statusComplete
This entry describes 2 isoforms produced by Alternative splicing.
O00587-1
This isoform has been chosen as the canonical sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
- Name1
- Length321
- Mass (Da)36,202
- Last updated2002-03-27 v2
- Checksum7CB847E7423DD0BC
O00587-2
- Name2
- Differences from canonical
- 86-102: TFVFTDSPDKGLQERLG → VTR
Computationally mapped potential isoform sequences
There are 6 potential isoforms mapped to this entry
Features
Showing features for sequence conflict, alternative sequence.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Sequence conflict | 85 | in Ref. 1; AAC51358 | ||||
Sequence: Q → L | ||||||
Alternative sequence | VSP_042857 | 86-102 | in isoform 2 | |||
Sequence: TFVFTDSPDKGLQERLG → VTR |
Keywords
- Coding sequence diversity
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
U94352 EMBL· GenBank· DDBJ | AAC51358.1 EMBL· GenBank· DDBJ | mRNA | ||
CR456518 EMBL· GenBank· DDBJ | CAG30404.1 EMBL· GenBank· DDBJ | mRNA | ||
AK297149 EMBL· GenBank· DDBJ | BAG59648.1 EMBL· GenBank· DDBJ | mRNA | ||
Z93096 EMBL· GenBank· DDBJ | CAB07511.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
BC094814 EMBL· GenBank· DDBJ | AAH94814.1 EMBL· GenBank· DDBJ | mRNA |