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Protein

Beta-1,3-N-acetylglucosaminyltransferase manic fringe

Gene

MFNG

Organism
Pan troglodytes (Chimpanzee)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at transcript leveli

Functioni

Glycosyltransferase involved in the elongation of O-linked ligands to activate Notch signaling. Possesses fucose-specific beta-1,3-N-acetylglucosaminyltransferase activity (By similarity).By similarity

Catalytic activityi

Transfers a beta-D-GlcNAc residue from UDP-D-GlcNAc to the fucose residue of a fucosylated protein acceptor.

Cofactori

Mn2+By similarity

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei70SubstrateBy similarity1
Binding sitei143SubstrateBy similarity1
Metal bindingi144ManganeseBy similarity1
Active sitei232By similarity1
Metal bindingi256ManganeseBy similarity1

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Developmental protein, Glycosyltransferase, Transferase

Keywords - Ligandi

Manganese, Metal-binding

Protein family/group databases

CAZyiGT31. Glycosyltransferase Family 31.

Names & Taxonomyi

Protein namesi
Recommended name:
Beta-1,3-N-acetylglucosaminyltransferase manic fringe (EC:2.4.1.222)
Alternative name(s):
O-fucosylpeptide 3-beta-N-acetylglucosaminyltransferase
Gene namesi
Name:MFNG
OrganismiPan troglodytes (Chimpanzee)
Taxonomic identifieri9598 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaePan
Proteomesi
  • UP000002277 Componenti: Unplaced

Subcellular locationi

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Topological domaini1 – 7CytoplasmicSequence analysis7
Transmembranei8 – 27Helical; Signal-anchor for type II membrane proteinSequence analysisAdd BLAST20
Topological domaini28 – 321LumenalSequence analysisAdd BLAST294

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Golgi apparatus, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00002191841 – 321Beta-1,3-N-acetylglucosaminyltransferase manic fringeAdd BLAST321

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Glycosylationi109N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi110 ↔ 121By similarity
Disulfide bondi139 ↔ 202By similarity
Glycosylationi185N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi306 ↔ 315By similarity

Keywords - PTMi

Disulfide bond, Glycoprotein

Structurei

3D structure databases

ProteinModelPortaliQ5IS64.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the glycosyltransferase 31 family.Curated

Keywords - Domaini

Signal-anchor, Transmembrane, Transmembrane helix

Phylogenomic databases

HOVERGENiHBG007986.
InParanoidiQ5IS64.
KOiK05948.

Family and domain databases

InterProiIPR017374. Fringe.
IPR003378. Fringe-like.
[Graphical view]
PfamiPF02434. Fringe. 1 hit.
[Graphical view]
PIRSFiPIRSF038073. B-acetylgalactosaminyltfrase. 1 hit.

Sequencei

Sequence statusi: Complete.

Q5IS64-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MQCRLPRGLA GALLTLLCMG LLCLRYHLNL SPQRVQETPE LRQPNPGPPE
60 70 80 90 100
LQLHDVFIAV KTTRAFHRLR LELLLDTWVS RTREQTFVFT DSPDKGLQER
110 120 130 140 150
LGSHLVVTNC SAEHSHPALS CKMAAEFDTF LASGLRWFCH VDDDNYVNPR
160 170 180 190 200
ALLQLLRAFP LAHDVYVGRP SLNRPIHASE PQPHNRTRLV QFWFATGGAG
210 220 230 240 250
FCINRRLALK MAPWASGSRF MDTSALIRLP DDCTMGYIIE CKLGGRLQPS
260 270 280 290 300
PLFHSHLETL QLLRTAQLPE QVTLSYGVFE GKLNVIKLQG PFSPEEDPSR
310 320
FRSLHCLLYP DTPWCPQLGA R
Length:321
Mass (Da):36,353
Last modified:February 15, 2005 - v1
Checksum:i62A68643836EE1DD
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY665264 mRNA. Translation: AAV74302.1.
RefSeqiNP_001012433.1. NM_001012431.1.
XP_016794235.1. XM_016938746.1.
UniGeneiPtr.6369.

Genome annotation databases

GeneIDi458811.
KEGGiptr:458811.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY665264 mRNA. Translation: AAV74302.1.
RefSeqiNP_001012433.1. NM_001012431.1.
XP_016794235.1. XM_016938746.1.
UniGeneiPtr.6369.

3D structure databases

ProteinModelPortaliQ5IS64.
ModBaseiSearch...
MobiDBiSearch...

Protein family/group databases

CAZyiGT31. Glycosyltransferase Family 31.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi458811.
KEGGiptr:458811.

Organism-specific databases

CTDi4242.

Phylogenomic databases

HOVERGENiHBG007986.
InParanoidiQ5IS64.
KOiK05948.

Family and domain databases

InterProiIPR017374. Fringe.
IPR003378. Fringe-like.
[Graphical view]
PfamiPF02434. Fringe. 1 hit.
[Graphical view]
PIRSFiPIRSF038073. B-acetylgalactosaminyltfrase. 1 hit.
ProtoNetiSearch...

Entry informationi

Entry nameiMFNG_PANTR
AccessioniPrimary (citable) accession number: Q5IS64
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 15, 2005
Last sequence update: February 15, 2005
Last modified: October 5, 2016
This is version 60 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.