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Protein

Exostosin-2

Gene

EXT2

Organism
Bos taurus (Bovine)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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 activityi

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.

Cofactori

Mn2+By similarity

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei490 – 4901SubstrateBy similarity
Metal bindingi540 – 5401Manganese; catalyticBy similarity
Binding sitei569 – 5691SubstrateBy similarity
Active sitei628 – 6281By similarity

GO - Molecular functioni

  1. acetylglucosaminyltransferase activity Source: BHF-UCL
  2. glucuronosyl-N-acetylglucosaminyl-proteoglycan 4-alpha-N-acetylglucosaminyltransferase activity Source: UniProtKB
  3. glucuronosyltransferase activity Source: BHF-UCL
  4. metal ion binding Source: UniProtKB-KW
  5. N-acetylglucosaminyl-proteoglycan 4-beta-glucuronosyltransferase activity Source: UniProtKB

GO - Biological processi

  1. glycosaminoglycan biosynthetic process Source: InterPro
  2. heparan sulfate proteoglycan biosynthetic process Source: InterPro
  3. N-acetylglucosamine metabolic process Source: UniProtKB
  4. protein glycosylation Source: UniProtKB-UniPathway
Complete GO annotation...

Keywords - Molecular functioni

Glycosyltransferase, Transferase

Keywords - Ligandi

Manganese, Metal-binding

Enzyme and pathway databases

BRENDAi2.4.1.224. 908.
2.4.1.225. 908.
UniPathwayiUPA00378.

Protein family/group databases

CAZyiGT47. Glycosyltransferase Family 47.
GT64. Glycosyltransferase Family 64.

Names & Taxonomyi

Protein namesi
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 namesi
Name:EXT2
OrganismiBos taurus (Bovine)
Taxonomic identifieri9913 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos
ProteomesiUP000009136 Componenti: Unplaced

Subcellular locationi

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

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 2525CytoplasmicSequence AnalysisAdd
BLAST
Transmembranei26 – 4621Helical; Signal-anchor for type II membrane proteinSequence AnalysisAdd
BLAST
Topological domaini47 – 718672LumenalSequence AnalysisAdd
BLAST

GO - Cellular componenti

  1. endoplasmic reticulum membrane Source: UniProtKB-SubCell
  2. extracellular space Source: BHF-UCL
  3. Golgi membrane Source: UniProtKB-SubCell
  4. integral component of membrane Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Endoplasmic reticulum, Golgi apparatus, Membrane, Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 718718Exostosin-2PRO_0000149650Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi288 – 2881N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi626 ↔ 676By similarity
Glycosylationi637 – 6371N-linked (GlcNAc...)Sequence Analysis

Post-translational modificationi

The soluble form derives from the membrane form by proteolytic processing.

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

PRIDEiO77783.

Interactioni

Subunit structurei

Forms a homo/hetero-oligomeric complex with EXT1. Interacts with GALNT5 (By similarity).By similarity

Structurei

3D structure databases

ProteinModelPortaliO77783.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni517 – 5226Substrate bindingBy similarity
Regioni538 – 5403Substrate bindingBy similarity
Regioni624 – 6285Substrate bindingBy similarity
Regioni662 – 67312Substrate bindingBy similarityAdd
BLAST

Sequence similaritiesi

Belongs to the glycosyltransferase 47 family.Curated

Keywords - Domaini

Signal-anchor, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiNOG272619.
HOGENOMiHOG000266990.
HOVERGENiHBG101211.
InParanoidiO77783.

Family and domain databases

Gene3Di3.90.550.10. 1 hit.
InterProiIPR004263. Exostosin.
IPR027673. Exostosin-2.
IPR015338. EXT_C.
IPR029044. Nucleotide-diphossugar_trans.
[Graphical view]
PANTHERiPTHR11062:SF6. PTHR11062:SF6. 1 hit.
PfamiPF03016. Exostosin. 1 hit.
PF09258. Glyco_transf_64. 1 hit.
[Graphical view]
SUPFAMiSSF53448. SSF53448. 1 hit.

Sequencei

Sequence statusi: Complete.

O77783-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MCASVKYNIR GPALIPRMKT KHRIYYITLF SIVLLGLIAT GMFQFWPHSI
60 70 80 90 100
ESSGDWSVEK RTGRDVPLVR LPADSPVPER GDLSCRMHTC FDVYRCGFNP
110 120 130 140 150
KNKIKVYIYP LKKYVGEAGV PVSSTISREY NELLTAISDS DYYTDDVTRA
160 170 180 190 200
CLFVPSIDLL NQNSLRVKET AQALAQLSRW DRGTNHLLFN MLPGGPPDYN
210 220 230 240 250
TALDVPRDRA LLAGGGFSTW TYRQGYDVSI PVYSPLSAEV DLPEKGPGPR
260 270 280 290 300
RYFLLSSQVA LHPEYREDLA ALQARHGEAV LVLDKCSNLS EGVPAARRRC
310 320 330 340 350
HQQQAFDYPQ VLQEATFCMV LRGARLGQAV LSDVLRAGCV PVIIADSYVL
360 370 380 390 400
PFSEVLDWKR ASVVVPEEKM SDVYSILQSI PRRQIEEMQR QARWFWEAYF
410 420 430 440 450
QSIKAIALAT LQIINDRIYP YAAISYEDWN DPPAVKWGSV SNPLFLPLIP
460 470 480 490 500
PQSQGFTAIV LTYDRVESLF RVITEVSKVP SLSKLLVVWN NQNKNPPEDS
510 520 530 540 550
LWPKIRVPLK VVRTAENKLS NRFFPYDEIE TEAVLAIDDD IIMLTSDELQ
560 570 580 590 600
FGYEVWREFP DRLVGYPGRL HLWDHEMNKW KYESEWTNEV SMVLTGAAFY
610 620 630 640 650
HKYFNYLYTY KMPGDIKNWV DAHMNCEDIA MNFLVANVTG KAVIKVTPRK
660 670 680 690 700
KFKCPECTAI DGLSLDQTHM VERSECINKF ASVFGTMPLK VVEHRADPVL
710
YKDDFPEKLK SFPNIGSL
Length:718
Mass (Da):81,887
Last modified:November 1, 1998 - v1
Checksum:iD6C18AC9C7AAD971
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF089748 mRNA. Translation: AAC35386.1.
UniGeneiBt.5113.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF089748 mRNA. Translation: AAC35386.1.
UniGeneiBt.5113.

3D structure databases

ProteinModelPortaliO77783.
ModBaseiSearch...
MobiDBiSearch...

Protein family/group databases

CAZyiGT47. Glycosyltransferase Family 47.
GT64. Glycosyltransferase Family 64.

Proteomic databases

PRIDEiO77783.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Phylogenomic databases

eggNOGiNOG272619.
HOGENOMiHOG000266990.
HOVERGENiHBG101211.
InParanoidiO77783.

Enzyme and pathway databases

UniPathwayiUPA00378.
BRENDAi2.4.1.224. 908.
2.4.1.225. 908.

Family and domain databases

Gene3Di3.90.550.10. 1 hit.
InterProiIPR004263. Exostosin.
IPR027673. Exostosin-2.
IPR015338. EXT_C.
IPR029044. Nucleotide-diphossugar_trans.
[Graphical view]
PANTHERiPTHR11062:SF6. PTHR11062:SF6. 1 hit.
PfamiPF03016. Exostosin. 1 hit.
PF09258. Glyco_transf_64. 1 hit.
[Graphical view]
SUPFAMiSSF53448. SSF53448. 1 hit.
ProtoNetiSearch...

Publicationsi

  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(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 129-147; 167-179; 485-494 AND 570-577.
    Tissue: Lung.

Entry informationi

Entry nameiEXT2_BOVIN
AccessioniPrimary (citable) accession number: O77783
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 27, 2002
Last sequence update: November 1, 1998
Last modified: April 1, 2015
This is version 96 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, Direct protein sequencing, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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 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.