Exostosin-2 - Bos taurus (Bovine)

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O77783 (EXT2_BOVIN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 3, 2013. Version 81. History...

Clusters with 100%, 90%, 50% identity |

Documents (2) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended name:
Exostosin-2
EC=2.4.1.224
EC=2.4.1.225

Alternative name(s):
Glucuronosyl-N-acetylglucosaminyl-proteoglycan/N-acetylglucosaminyl-proteoglycan 4-alpha-N-acetylglucosaminyltransferase
HS-polymerase
Short name=HS-POL
Multiple exostoses protein 2 homolog

Gene names

Name:

EXT2

Organism

Bos taurus (Bovine) [Reference proteome]

Taxonomic identifier

9913 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Laurasiatheria › Cetartiodactyla › Ruminantia › Pecora › Bovidae › Bovinae › Bos

Protein attributes

Sequence length	718 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Glycosyltransferase required for the biosynthesis of heparan-sulfate and responsible for the alternating addition of beta-1-4-linked glucuronic acid (GlcA) and alpha-1-4-linked N-acetylglucosamine (GlcNAc) units to nascent heparan sulfate chains.
Catalytic activity	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. UDP-alpha-D-glucuronate + N-acetyl-alpha-D-glucosaminyl-(1->4)-beta-D-glucuronosyl-proteoglycan = UDP + beta-D-glucuronosyl-(1->4)-N-acetyl-alpha-D-glucosaminyl-(1->4)-beta-D-glucuronosyl-proteoglycan.
Pathway	Protein modification; protein glycosylation.
Subunit structure	Forms a homo/hetero-oligomeric complex with EXT1. Interacts with GALNT5 By similarity.
Subcellular location	Endoplasmic reticulum membrane; Single-pass type II membrane protein By similarity. Golgi apparatus membrane; Single-pass type II membrane protein By similarity. Secreted. Note: The EXT1/EXT2 complex is localized in the Golgi apparatus By similarity. A soluble form is found in the serum.
Post-translational modification	The soluble form derives from the membrane form by proteolytic processing.
Sequence similarities	Belongs to the glycosyltransferase 47 family.

Ontologies

Keywords
Cellular component	Endoplasmic reticulum Golgi apparatus Membrane Secreted
Domain	Signal-anchor Transmembrane Transmembrane helix
Molecular function	Glycosyltransferase Transferase
PTM	Glycoprotein
Technical term	Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	N-acetylglucosamine metabolic process Inferred from direct assay PubMed 11256613 Ref.1. Source: UniProtKB protein glycosylation Inferred from electronic annotation. Source: UniProtKB-UniPathway
Cellular_component	Golgi membrane Inferred from electronic annotation. Source: UniProtKB-SubCell extracellular space Inferred from direct assay Ref.1. Source: BHF-UCL integral to membrane Non-traceable author statement Ref.1. Source: UniProtKB intrinsic to endoplasmic reticulum membrane Inferred from electronic annotation. Source: InterPro
Molecular_function	N-acetylglucosaminyl-proteoglycan 4-beta-glucuronosyltransferase activity Inferred from direct assay PubMed 11256613 Ref.1. Source: UniProtKB glucuronosyl-N-acetylglucosaminyl-proteoglycan 4-alpha-N-acetylglucosaminyltransferase activity Inferred from direct assay PubMed 11256613 Ref.1. Source: UniProtKB
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 718

718

Exostosin-2

PRO_0000149650

Regions

Topological domain

1 – 25

Cytoplasmic Potential

Transmembrane

26 – 46

Helical; Signal-anchor for type II membrane protein; Potential

Topological domain

47 – 718

672

Lumenal Potential

Amino acid modifications

Glycosylation

288

N-linked (GlcNAc...) Potential

Glycosylation

637

N-linked (GlcNAc...) Potential

Sequences

Sequence

Length

Mass (Da)

Tools

O77783 [UniParc].

Last modified November 1, 1998. Version 1.
Checksum: D6C18AC9C7AAD971
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FASTA

718

81,887

        10         20         30         40         50         60 
MCASVKYNIR GPALIPRMKT KHRIYYITLF SIVLLGLIAT GMFQFWPHSI ESSGDWSVEK 

        70         80         90        100        110        120 
RTGRDVPLVR LPADSPVPER GDLSCRMHTC FDVYRCGFNP KNKIKVYIYP LKKYVGEAGV 

       130        140        150        160        170        180 
PVSSTISREY NELLTAISDS DYYTDDVTRA CLFVPSIDLL NQNSLRVKET AQALAQLSRW 

       190        200        210        220        230        240 
DRGTNHLLFN MLPGGPPDYN TALDVPRDRA LLAGGGFSTW TYRQGYDVSI PVYSPLSAEV 

       250        260        270        280        290        300 
DLPEKGPGPR RYFLLSSQVA LHPEYREDLA ALQARHGEAV LVLDKCSNLS EGVPAARRRC 

       310        320        330        340        350        360 
HQQQAFDYPQ VLQEATFCMV LRGARLGQAV LSDVLRAGCV PVIIADSYVL PFSEVLDWKR 

       370        380        390        400        410        420 
ASVVVPEEKM SDVYSILQSI PRRQIEEMQR QARWFWEAYF QSIKAIALAT LQIINDRIYP 

       430        440        450        460        470        480 
YAAISYEDWN DPPAVKWGSV SNPLFLPLIP PQSQGFTAIV LTYDRVESLF RVITEVSKVP 

       490        500        510        520        530        540 
SLSKLLVVWN NQNKNPPEDS LWPKIRVPLK VVRTAENKLS NRFFPYDEIE TEAVLAIDDD 

       550        560        570        580        590        600 
IIMLTSDELQ FGYEVWREFP DRLVGYPGRL HLWDHEMNKW KYESEWTNEV SMVLTGAAFY 

       610        620        630        640        650        660 
HKYFNYLYTY KMPGDIKNWV DAHMNCEDIA MNFLVANVTG KAVIKVTPRK KFKCPECTAI 

       670        680        690        700        710 
DGLSLDQTHM VERSECINKF ASVFGTMPLK VVEHRADPVL YKDDFPEKLK SFPNIGSL

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References

[1]

"The putative tumor suppressors EXT1 and EXT2 are glycosyltransferases required for the biosynthesis of heparan sulfate."
Lind T., Tufaro F., McCormick C., Lindahl U., Lidholt K.
J. Biol. Chem. 273:26265-26268(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 129-147; 167-179; 485-494 AND 570-577.
Tissue: Lung.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AF089748 mRNA. Translation: AAC35386.1.
IPI	IPI00702531.
UniGene	Bt.5113.
3D structure databases
ProteinModelPortal	O77783.
ModBase	Search...
Protein family/group databases
CAZy	GT47. Glycosyltransferase Family 47. GT64. Glycosyltransferase Family 64.
Proteomic databases
PRIDE	O77783.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Phylogenomic databases
eggNOG	NOG272619.
HOGENOM	HOG000266990.
HOVERGEN	HBG101211.
InParanoid	O77783.
OrthoDB	EOG41VK2B.
Enzyme and pathway databases
UniPathway	UPA00378.
Family and domain databases
InterPro	IPR004263. Exostosin. IPR015338. HexNAc_Trfase_a. [Graphical view]
Pfam	PF03016. Exostosin. 1 hit. PF09258. Glyco_transf_64. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

EXT2_BOVIN

Accession

Primary (citable) accession number: O77783

Entry history

Integrated into UniProtKB/Swiss-Prot:	March 27, 2002
Last sequence update:	November 1, 1998
Last modified:	April 3, 2013
This is version 81 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Amino acid modifications

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein family/group databases

Proteomic databases

Protocols and materials databases

Phylogenomic databases

Enzyme and pathway databases

Family and domain databases

Entry information

Relevant documents