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Protein

Exostosin-1

Gene

EXT1

Organism
Cricetulus griseus (Chinese hamster) (Cricetulus barabensis griseus)
Status
Reviewed-Annotation score: -Experimental evidence at protein leveli

Functioni

Glycosyltransferase required for the biosynthesis of heparan-sulfate. The EXT1/EXT2 complex possesses substantially higher glycosyltransferase activity than EXT1 or EXT2 alone. Required for the exosomal release of SDCBP, CD63 and syndecan (By similarity).By similarity

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 similarityNote: Manganese. Divalent cations.By similarity

Pathwayi: protein glycosylation

This protein is involved in the pathway protein glycosylation, which is part of Protein modification.
View all proteins of this organism that are known to be involved in the pathway protein glycosylation and in Protein modification.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei518SubstrateBy similarity1
Metal bindingi567Manganese; catalyticBy similarity1
Binding sitei595SubstrateBy similarity1
Active sitei654By similarity1

GO - Molecular functioni

GO - Biological processi

Keywordsi

Molecular functionGlycosyltransferase, Transferase
LigandManganese, Metal-binding

Enzyme and pathway databases

UniPathwayi
UPA00378

Protein family/group databases

CAZyiGT47 Glycosyltransferase Family 47
GT64 Glycosyltransferase Family 64

Names & Taxonomyi

Protein namesi
Recommended name:
Exostosin-1 (EC:2.4.1.224, EC:2.4.1.225)
Alternative name(s):
Heparan sulfate copolymerase
Multiple exostoses protein 1 homolog
Gene namesi
Name:EXT1
OrganismiCricetulus griseus (Chinese hamster) (Cricetulus barabensis griseus)
Taxonomic identifieri10029 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaCricetidaeCricetinaeCricetulus

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Topological domaini1 – 5CytoplasmicSequence analysis5
Transmembranei6 – 26Helical; Signal-anchor for type II membrane proteinSequence analysisAdd BLAST21
Topological domaini27 – 746LumenalSequence analysisAdd BLAST720

Keywords - Cellular componenti

Endoplasmic reticulum, Golgi apparatus, Membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi268G → E: Reduced GlcA transferase activity. 1
Mutagenesisi298C → Y: Reduced GlcA transferase activity. 1
Mutagenesisi341R → K: Reduced GlcA transferase activity. 1
Mutagenesisi344S → F: Reduced GlcA transferase activity. 1
Mutagenesisi346R → K: Reduced GlcA transferase activity. 1
Mutagenesisi349E → K: Reduced GlcA transferase activity. 1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001496471 – 746Exostosin-1Add BLAST746

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Glycosylationi89N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi330N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi652 ↔ 704By similarity

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

PRIDEiQ9JK82

Interactioni

Subunit structurei

Forms a homo/hetero-oligomeric complex with EXT2.By similarity

GO - Molecular functioni

Structurei

3D structure databases

ProteinModelPortaliQ9JK82
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni544 – 549Substrate bindingBy similarity6
Regioni565 – 567Substrate bindingBy similarity3
Regioni650 – 654Substrate bindingBy similarity5
Regioni688 – 701Substrate bindingBy similarityAdd BLAST14

Sequence similaritiesi

Belongs to the glycosyltransferase 47 family.Curated

Keywords - Domaini

Signal-anchor, Transmembrane, Transmembrane helix

Phylogenomic databases

HOVERGENiHBG003459
KOiK02366

Family and domain databases

Gene3Di3.90.550.10, 1 hit
InterProiView protein in InterPro
IPR004263 Exostosin
IPR027670 Exostosin-1
IPR015338 EXT_C
IPR029044 Nucleotide-diphossugar_trans
PANTHERiPTHR11062 PTHR11062, 1 hit
PTHR11062:SF97 PTHR11062:SF97, 1 hit
PfamiView protein in Pfam
PF03016 Exostosin, 1 hit
PF09258 Glyco_transf_64, 1 hit
SUPFAMiSSF53448 SSF53448, 1 hit

Sequencei

Sequence statusi: Complete.

Q9JK82-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MQAKKRYFIL LSAGSCLALL FYFGGVQFRA SRSHSRREEH SGRNGLHQPS
60 70 80 90 100
PDHFWPRFAD ALHPFFPWDQ LENEDSGVHV SPRQKRDANS SVYKGKKCRM
110 120 130 140 150
ESCFDFALCK KNGFKVYVYP QQKGEKIAES YQNILAAIEG SRFYTSDPSQ
160 170 180 190 200
ACLFVLSLDT LDRDQLSPQY VHNLRSKVQS LHLWNNGRNH LIFNLYSGTW
210 220 230 240 250
PDYTEDVGFD IGQAMLAKAS ISTENFRPNF DVSIPLFSKD HPRTGGERGF
260 270 280 290 300
LKFNTIPPLR KYMLVFKGKR YLTGIGSDTR NALYHVHNGE DVLLLTTCKH
310 320 330 340 350
GKDWQKHKDS RCDRDNTEYE KYDYREMLHN ATFCLVPRGR RLGSFRFLEA
360 370 380 390 400
LQAACVPVML SNGWELPFSE VINWNQAAVI GDERLLLQIP STIRSIHQDK
410 420 430 440 450
ILALRQQTQF LWEAYFSSVE KIVLTTLEII QDRIFKHISR NSLIWNKHPG
460 470 480 490 500
GLFVLPQYSS YLGDFPYYYA NLGLKPPSKF TAVIHAVTPL VSQSQPVLKL
510 520 530 540 550
LVAAAKSQYC AQIIVLWNCD KPLPAKHRWP ATAVPVIVIE GESKVMSSRF
560 570 580 590 600
LPYDNIITDA VLSLDEDTVL STTEVDFAFT VWQSFPERIV GYPARSHFWD
610 620 630 640 650
NSKERWGYTS KWTNDYSMVL TGAAIYHKYY HYLYTHYLPA SLKNMVDQLA
660 670 680 690 700
NCEDILMNFL VSAVTKLPPI KVTQKKQYKE TMMGQTSRAS RWADPDHFAQ
710 720 730 740
RQSCMNTFAS WFGYMPLIHS QMRLDPVLFK DQVSILRKKY RDIERL
Length:746
Mass (Da):86,189
Last modified:October 1, 2000 - v1
Checksum:iC3697B4A421DA4F2
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF252858 mRNA Translation: AAF71276.1
RefSeqiNP_001233696.1, NM_001246767.1

Genome annotation databases

GeneIDi100689334
KEGGicge:100689334

Similar proteinsi

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF252858 mRNA Translation: AAF71276.1
RefSeqiNP_001233696.1, NM_001246767.1

3D structure databases

ProteinModelPortaliQ9JK82
ModBaseiSearch...
MobiDBiSearch...

Protein family/group databases

CAZyiGT47 Glycosyltransferase Family 47
GT64 Glycosyltransferase Family 64

Proteomic databases

PRIDEiQ9JK82

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi100689334
KEGGicge:100689334

Organism-specific databases

CTDi2131

Phylogenomic databases

HOVERGENiHBG003459
KOiK02366

Enzyme and pathway databases

UniPathwayi
UPA00378

Family and domain databases

Gene3Di3.90.550.10, 1 hit
InterProiView protein in InterPro
IPR004263 Exostosin
IPR027670 Exostosin-1
IPR015338 EXT_C
IPR029044 Nucleotide-diphossugar_trans
PANTHERiPTHR11062 PTHR11062, 1 hit
PTHR11062:SF97 PTHR11062:SF97, 1 hit
PfamiView protein in Pfam
PF03016 Exostosin, 1 hit
PF09258 Glyco_transf_64, 1 hit
SUPFAMiSSF53448 SSF53448, 1 hit
ProtoNetiSearch...

Entry informationi

Entry nameiEXT1_CRIGR
AccessioniPrimary (citable) accession number: Q9JK82
Entry historyiIntegrated into UniProtKB/Swiss-Prot: March 27, 2002
Last sequence update: October 1, 2000
Last modified: October 10, 2018
This is version 82 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Documents

  1. SIMILARITY comments
    Index of protein domains and families
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health

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