Reviewed, UniProtKB/Swiss-Prot O77783 (EXT2_BOVIN)

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)

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.
Sequence processing	The displayed sequence is not processed.
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
Molecular function	Glycosyltransferase Transferase
PTM	Glycoprotein
Technical term	Direct protein sequencing
Gene Ontology (GO)
Biological process	N-acetylglucosamine metabolic process Ref.1 Inferred from direct assay. Source: UniProtKB
Cellular component	Golgi membrane Inferred from electronic annotation. Source: UniProtKB-SubCell extracellular space Ref.1 Inferred from direct assay. Source: UniProtKB integral to membrane Ref.1 Non-traceable author statement. Source: UniProtKB intrinsic to endoplasmic reticulum membrane Inferred from electronic annotation. Source: InterPro
Molecular function	N-acetylglucosaminyl-proteoglycan 4-beta-glucuronosyltransferase activity Ref.1 Inferred from direct assay. Source: UniProtKB glucuronosyl-N-acetylglucosaminyl-proteoglycan 4-alpha-N-acetylglucosaminyltransferase activity Ref.1 Inferred from direct assay. 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	25	Cytoplasmic Potential
	Transmembrane	26 – 46	21	Signal-anchor for type II membrane protein Potential
	Topological domain	47 – 718	672	Lumenal Potential
Amino acid modifications
	Glycosylation	288	1	N-linked (GlcNAc...) Potential
	Glycosylation	637	1	N-linked (GlcNAc...) Potential

Sequences

	Sequence		Length	Mass (Da)
	O77783-1 [UniParc]. Last modified November 1, 1998. Version 1. Checksum: D6C18AC9C7AAD971	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

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: 9756849] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 129-147; 167-179; 485-494 AND 570-577. Tissue: Lung.

Cross-references

Sequence databases
EMBLGenBankDDBJ	AF089748 mRNA. Translation: AAC35386.1.
IPI	IPI00702531.
UniGene	Bt.5113
3D structure databases
HSSP	HSSP built from PDB template 1OMX based on UniProtKB Q9ES89.
ModBase	Search...
Protein family/group databases
CAZy	GT47. Glycosyltransferase Family 47. GT64. Glycosyltransferase Family 64.
Genome annotation databases
Ensembl	ENSBTAG00000019644. Bos taurus. [Contig view]
Phylogenomic databases
HOVERGEN	O77783.
Enzyme and pathway databases
BRENDA	2.4.1.224. 251. 2.4.1.225. 251.
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 14, 2009
This is version 57 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)