Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

O01705 (EXT2_CAEEL) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 98. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Exostosin-2

EC=2.4.1.223
EC=2.4.1.224
Alternative name(s):
Glucuronyl-galactosyl-proteoglycan/Glucuronosyl-N-acetylglucosaminyl-proteoglycan 4-alpha-N-acetylglucosaminyltransferase
Multiple exostoses homolog 2
Gene names
Name:rib-2
ORF Names:K01G5.6
OrganismCaenorhabditis elegans [Reference proteome]
Taxonomic identifier6239 [NCBI]
Taxonomic lineageEukaryotaMetazoaEcdysozoaNematodaChromadoreaRhabditidaRhabditoideaRhabditidaePeloderinaeCaenorhabditis

Protein attributes

Sequence length814 AA.
Sequence statusComplete.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

Probable alpha1,4-N-acetylglucosaminyltransferase required for the biosynthesis of heparan-sulfate By similarity.

Catalytic activity

UDP-N-acetyl-D-glucosamine + beta-D-glucuronosyl-(1->3)-beta-D-galactosyl-(1->3)-beta-D-galactosyl-(1->4)-beta-D-xylosyl-proteoglycan = UDP + alpha-N-acetyl-D-glucosaminyl-(1->4)-beta-D-glucuronosyl-(1->3)-beta-D-galactosyl-(1->3)-beta-D-galactosyl-(1->4)-beta-D-xylosyl-proteoglycan.

UDP-N-acetyl-D-glucosamine + beta-D-glucuronosyl-(1->4)-N-acetyl-alpha-D-glucosaminyl-proteoglycan = UDP + N-acetyl-alpha-D-glucosaminyl-(1->4)-beta-D-glucuronosyl-(1->4)-N-acetyl-alpha-D-glucosaminyl-proteoglycan.

Pathway

Glycan metabolism; heparan sulfate biosynthesis.

Subcellular location

Endoplasmic reticulum membrane; Single-pass type II membrane protein By similarity.

Sequence similarities

Belongs to the glycosyltransferase 47 family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 814814Exostosin-2
PRO_0000149663

Regions

Topological domain1 – 1414Cytoplasmic Potential
Transmembrane15 – 3521Helical; Signal-anchor for type II membrane protein; Potential
Topological domain36 – 814779Lumenal Potential

Amino acid modifications

Glycosylation361N-linked (GlcNAc...) Potential
Glycosylation2271N-linked (GlcNAc...) Potential
Glycosylation2971N-linked (GlcNAc...) Potential
Glycosylation3221N-linked (GlcNAc...) Potential
Glycosylation4541N-linked (GlcNAc...) Potential
Glycosylation4921N-linked (GlcNAc...) Potential
Glycosylation6851N-linked (GlcNAc...) Potential

Experimental info

Sequence conflict6041T → S in AAC47510. Ref.1

Sequences

Sequence LengthMass (Da)Tools
O01705 [UniParc].

Last modified March 27, 2002. Version 2.
Checksum: 38FA58C5EB17DB16

FASTA81494,197
        10         20         30         40         50         60 
MAIKLNGSSR SFVPSLRVSA FLIFIFFVIT YIIIYNVSFS EPSWITQDAL KQNIENLDDY 

        70         80         90        100        110        120 
DASCSGYSIG RILREQKRIL ASVRLELTES QVKIEEIRTV QEELQRLIPQ KQLELSALEG 

       130        140        150        160        170        180 
EIEAAQRQLE ELRETQNVKV FLPFSPLQIP RELEQPSQIS PNQLDDIIDY SRCSISSFMP 

       190        200        210        220        230        240 
VYVDIITSGQ SEKEWLNVFQ EVIPNLVETP DKACIKIHIS NGIASPNTTF NSILFNVGSP 

       250        260        270        280        290        300 
IINFQSKSIH VQASKIRSFD FPVDVNHIAV EKVDLTPLLP FQRENLISLI VDNTELNFSA 

       310        320        330        340        350        360 
FSSLSAEPSR RPIVIVKCSQ ENCSLERRRQ LIGSSTFCFL LPSEMFFQDF LSSLQLGCIP 

       370        380        390        400        410        420 
IILSNSQLLP FQDLIDWRRA TYRLPLARLP EAHFIVQSFE ISDIIEMRRV GRLFYETYLA 

       430        440        450        460        470        480 
DRHLLARSLL AALRYKLQIP TREVRRNQAI PLFNSSFTAP KGSVVNVQAN FDDEYLLGPL 

       490        500        510        520        530        540 
ESRVESTSYA YNFTEFQLYS YDFWNIIMSP HYTKEFLVNA AELPTEAEFF EDTKIGFRPI 

       550        560        570        580        590        600 
EPGSGAEFSK ALGGNRQREQ FTVVLLTYER DAVLTGALER LHQLPYLNKI IVVWNNVNRD 

       610        620        630        640        650        660 
PPDTWPSLHI PVEFIRVAEN NLNNRFVPWD RIETEAVLSL DDDIDLMQQE IILAFRVWRE 

       670        680        690        700        710        720 
NRDRIVGFPA RHHARYGDSM FYNSNHTCQM SMILTGAAFI HKNYLTAYTY EMPAEIREHV 

       730        740        750        760        770        780 
NSIKNCEDIA MNYLVSHLTR KPPIKTTSRW TLKCPTCTES LYKEGTHFEK RHECMRLFTK 

       790        800        810 
IYGYNPLKFS QFRADSILFK TRLPQNHQKC FKYV 

« Hide

References

« Hide 'large scale' references
[1]"The structure of the human multiple exostoses 2 gene and characterization of homologs in mouse and Caenorhabditis elegans."
Clines G.A., Ashley J.A., Shah S., Lovett M.
Genome Res. 7:359-367(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]"rib-2, a Caenorhabditis elegans homolog of the human tumor suppressor EXT genes encodes a novel alpha1,4-N-acetylglucosaminyltransferase involved in the biosynthetic initiation and elongation of heparan sulfate."
Kitagawa H., Egusa N., Tamura J., Kusche-Gullberg M., Lindahl U., Sugahara K.
J. Biol. Chem. 276:4834-4838(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[3]"Genome sequence of the nematode C. elegans: a platform for investigating biology."
The C. elegans sequencing consortium
Science 282:2012-2018(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Bristol N2.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U94835 mRNA. Translation: AAC47510.1.
AB077851 mRNA. Translation: BAB83878.1.
Z92803 Genomic DNA. Translation: CAB07245.1.
PIRT23200.
RefSeqNP_499368.1. NM_066967.6.
UniGeneCel.17904.

3D structure databases

ProteinModelPortalO01705.
SMRO01705. Positions 559-790.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING6239.K01G5.6.

Protein family/group databases

CAZyGT47. Glycosyltransferase Family 47.
GT64. Glycosyltransferase Family 64.

Proteomic databases

PRIDEO01705.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaK01G5.6; K01G5.6; K01G5.6.
GeneID176502.
KEGGcel:CELE_K01G5.6.
UCSCK01G5.6. c. elegans.

Organism-specific databases

CTD176502.
WormBaseK01G5.6; CE16196; WBGene00004361; rib-2.

Phylogenomic databases

eggNOGNOG243446.
GeneTreeENSGT00550000074496.
HOGENOMHOG000007975.
InParanoidO01705.
KOK02370.
OMAWDRIETE.
OrthoDBEOG7PZRWK.

Enzyme and pathway databases

UniPathwayUPA00756.

Family and domain databases

InterProIPR027674. EXO3/EXOL3.
IPR004263. Exostosin.
IPR015338. HexNAc_Trfase_a.
[Graphical view]
PANTHERPTHR11062. PTHR11062. 1 hit.
PTHR11062:SF5. PTHR11062:SF5. 1 hit.
PfamPF03016. Exostosin. 1 hit.
PF09258. Glyco_transf_64. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio892848.
PROO01705.

Entry information

Entry nameEXT2_CAEEL
AccessionPrimary (citable) accession number: O01705
Secondary accession number(s): O17920
Entry history
Integrated into UniProtKB/Swiss-Prot: July 15, 1998
Last sequence update: March 27, 2002
Last modified: February 19, 2014
This is version 98 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programCaenorhabditis annotation project

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways

Caenorhabditis elegans

Caenorhabditis elegans: entries, gene names and cross-references to WormBase