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Exostosin-2 (EC 2.4.1.224) (EC 2.4.1.225) (Glucuronosyl-N-acetylglucosaminyl-proteoglycan/N-acetylglucosaminyl-proteoglycan 4-alpha-N-acetylglucosaminyltransferase) (HS-polymerase) (HS-POL) (Multiple exostoses protein 2 homolog)

 EXT2_BOVIN              Reviewed;         718 AA.
O77783;
27-MAR-2002, integrated into UniProtKB/Swiss-Prot.
01-NOV-1998, sequence version 1.
25-OCT-2017, entry version 104.
RecName: Full=Exostosin-2;
EC=2.4.1.224;
EC=2.4.1.225;
AltName: Full=Glucuronosyl-N-acetylglucosaminyl-proteoglycan/N-acetylglucosaminyl-proteoglycan 4-alpha-N-acetylglucosaminyltransferase;
AltName: Full=HS-polymerase;
Short=HS-POL;
AltName: Full=Multiple exostoses protein 2 homolog;
Name=EXT2;
Bos taurus (Bovine).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Ruminantia;
Pecora; Bovidae; Bovinae; Bos.
NCBI_TaxID=9913;
[1]
NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 129-147; 167-179;
485-494 AND 570-577, AND SUBCELLULAR LOCATION.
TISSUE=Lung;
PubMed=9756849; DOI=10.1074/jbc.273.41.26265;
Lind T., Tufaro F., McCormick C., Lindahl U., Lidholt K.;
"The putative tumor suppressors EXT1 and EXT2 are glycosyltransferases
required for the biosynthesis of heparan sulfate.";
J. Biol. Chem. 273:26265-26268(1998).
-!- FUNCTION: Glycosyltransferase required for the biosynthesis of
heparan-sulfate. The EXT1/EXT2 complex possesses substantially
higher glycosyltransferase activity than EXT1 or EXT2 alone.
Appears to be a tumor suppressor. Required for the exosomal
release of SDCBP, CD63 and syndecan.
{ECO:0000250|UniProtKB:Q93063}.
-!- 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.
-!- CATALYTIC ACTIVITY: 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.
-!- COFACTOR:
Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
Evidence={ECO:0000250|UniProtKB:Q9ES89};
-!- PATHWAY: Protein modification; protein glycosylation.
-!- SUBUNIT: Forms a homo/hetero-oligomeric complex with EXT1.
Interacts with GALNT5. Inteacts with NDST1 (By similarity).
{ECO:0000250|UniProtKB:Q93063}.
-!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
{ECO:0000250|UniProtKB:Q93063}; Single-pass type II membrane
protein {ECO:0000250|UniProtKB:Q93063}. Golgi apparatus membrane
{ECO:0000250|UniProtKB:Q93063}; Single-pass type II membrane
protein {ECO:0000250|UniProtKB:Q93063}. Secreted
{ECO:0000269|PubMed:9756849}. Note=The EXT1/EXT2 complex is
localized in the Golgi apparatus (By similarity). A soluble form
is found in the serum (PubMed:9756849).
{ECO:0000250|UniProtKB:Q93063, ECO:0000269|PubMed:9756849}.
-!- PTM: The soluble form derives from the membrane form by
proteolytic processing.
-!- SIMILARITY: Belongs to the glycosyltransferase 47 family.
{ECO:0000305}.
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EMBL; AF089748; AAC35386.1; -; mRNA.
UniGene; Bt.5113; -.
ProteinModelPortal; O77783; -.
SMR; O77783; -.
STRING; 9913.ENSBTAP00000026177; -.
CAZy; GT47; Glycosyltransferase Family 47.
CAZy; GT64; Glycosyltransferase Family 64.
PaxDb; O77783; -.
PRIDE; O77783; -.
eggNOG; KOG1021; Eukaryota.
eggNOG; ENOG410XTFH; LUCA.
HOGENOM; HOG000266990; -.
HOVERGEN; HBG101211; -.
InParanoid; O77783; -.
BRENDA; 2.4.1.224; 908.
BRENDA; 2.4.1.225; 908.
UniPathway; UPA00378; -.
Proteomes; UP000009136; Unplaced.
GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
GO; GO:0005615; C:extracellular space; IDA:BHF-UCL.
GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
GO; GO:0016021; C:integral component of membrane; NAS:UniProtKB.
GO; GO:0008375; F:acetylglucosaminyltransferase activity; IDA:BHF-UCL.
GO; GO:0050508; F:glucuronosyl-N-acetylglucosaminyl-proteoglycan 4-alpha-N-acetylglucosaminyltransferase activity; IDA:UniProtKB.
GO; GO:0015020; F:glucuronosyltransferase activity; IDA:BHF-UCL.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0050509; F:N-acetylglucosaminyl-proteoglycan 4-beta-glucuronosyltransferase activity; IDA:UniProtKB.
GO; GO:0006024; P:glycosaminoglycan biosynthetic process; IEA:InterPro.
GO; GO:0015012; P:heparan sulfate proteoglycan biosynthetic process; IEA:InterPro.
GO; GO:0006044; P:N-acetylglucosamine metabolic process; IDA:UniProtKB.
GO; GO:0006486; P:protein glycosylation; IEA:UniProtKB-UniPathway.
Gene3D; 3.90.550.10; -; 1.
InterPro; IPR004263; Exostosin.
InterPro; IPR027673; Exostosin-2.
InterPro; IPR015338; EXT_C.
InterPro; IPR029044; Nucleotide-diphossugar_trans.
PANTHER; PTHR11062:SF128; PTHR11062:SF128; 1.
Pfam; PF03016; Exostosin; 1.
Pfam; PF09258; Glyco_transf_64; 1.
SUPFAM; SSF53448; SSF53448; 1.
1: Evidence at protein level;
Complete proteome; Direct protein sequencing; Disulfide bond;
Endoplasmic reticulum; Glycoprotein; Glycosyltransferase;
Golgi apparatus; Manganese; Membrane; Metal-binding;
Reference proteome; Secreted; Signal-anchor; Transferase;
Transmembrane; Transmembrane helix.
CHAIN 1 718 Exostosin-2.
/FTId=PRO_0000149650.
TOPO_DOM 1 25 Cytoplasmic. {ECO:0000255}.
TRANSMEM 26 46 Helical; Signal-anchor for type II
membrane protein. {ECO:0000255}.
TOPO_DOM 47 718 Lumenal. {ECO:0000255}.
REGION 517 522 Substrate binding.
{ECO:0000250|UniProtKB:Q9ES89}.
REGION 538 540 Substrate binding.
{ECO:0000250|UniProtKB:Q9ES89}.
REGION 624 628 Substrate binding.
{ECO:0000250|UniProtKB:Q9ES89}.
REGION 662 673 Substrate binding.
{ECO:0000250|UniProtKB:Q9ES89}.
ACT_SITE 628 628 {ECO:0000250|UniProtKB:Q9ES89}.
METAL 540 540 Manganese; catalytic.
{ECO:0000250|UniProtKB:Q9ES89}.
BINDING 490 490 Substrate.
{ECO:0000250|UniProtKB:Q9ES89}.
BINDING 569 569 Substrate.
{ECO:0000250|UniProtKB:Q9ES89}.
CARBOHYD 288 288 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 637 637 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 626 676 {ECO:0000250|UniProtKB:Q9ES89}.
SEQUENCE 718 AA; 81887 MW; D6C18AC9C7AAD971 CRC64;
MCASVKYNIR GPALIPRMKT KHRIYYITLF SIVLLGLIAT GMFQFWPHSI ESSGDWSVEK
RTGRDVPLVR LPADSPVPER GDLSCRMHTC FDVYRCGFNP KNKIKVYIYP LKKYVGEAGV
PVSSTISREY NELLTAISDS DYYTDDVTRA CLFVPSIDLL NQNSLRVKET AQALAQLSRW
DRGTNHLLFN MLPGGPPDYN TALDVPRDRA LLAGGGFSTW TYRQGYDVSI PVYSPLSAEV
DLPEKGPGPR RYFLLSSQVA LHPEYREDLA ALQARHGEAV LVLDKCSNLS EGVPAARRRC
HQQQAFDYPQ VLQEATFCMV LRGARLGQAV LSDVLRAGCV PVIIADSYVL PFSEVLDWKR
ASVVVPEEKM SDVYSILQSI PRRQIEEMQR QARWFWEAYF QSIKAIALAT LQIINDRIYP
YAAISYEDWN DPPAVKWGSV SNPLFLPLIP PQSQGFTAIV LTYDRVESLF RVITEVSKVP
SLSKLLVVWN NQNKNPPEDS LWPKIRVPLK VVRTAENKLS NRFFPYDEIE TEAVLAIDDD
IIMLTSDELQ FGYEVWREFP DRLVGYPGRL HLWDHEMNKW KYESEWTNEV SMVLTGAAFY
HKYFNYLYTY KMPGDIKNWV DAHMNCEDIA MNFLVANVTG KAVIKVTPRK KFKCPECTAI
DGLSLDQTHM VERSECINKF ASVFGTMPLK VVEHRADPVL YKDDFPEKLK SFPNIGSL


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