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Protein

Exostosin-2

Gene

Ext2

Organism
Drosophila melanogaster (Fruit fly)
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. Plays a central role in diffusion of morphogens hedgehog (hh), wingless (wg) and Decapentaplegic (dpp) via its role in heparan sulfate proteoglycans (HSPGs) biosynthesis, HSPGs being required for movement of Hh, Dpp and wg morphogens.3 Publications

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 sitei489 – 4891SubstrateBy similarity
Metal bindingi539 – 5391Manganese; catalyticBy similarity
Binding sitei568 – 5681SubstrateBy similarity
Active sitei627 – 6271By similarity

GO - Molecular functioni

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

GO - Biological processi

  1. chondroitin sulfate biosynthetic process Source: FlyBase
  2. decapentaplegic signaling pathway Source: UniProtKB
  3. glycosaminoglycan biosynthetic process Source: FlyBase
  4. heparan sulfate proteoglycan biosynthetic process Source: FlyBase
  5. heparan sulfate proteoglycan biosynthetic process, polysaccharide chain biosynthetic process Source: FlyBase
  6. heparin biosynthetic process Source: FlyBase
  7. multicellular organismal development Source: UniProtKB-KW
  8. N-acetylglucosamine metabolic process Source: UniProtKB
  9. protein glycosylation Source: UniProtKB-UniPathway
  10. smoothened signaling pathway Source: UniProtKB
  11. Wnt signaling pathway Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Developmental protein, Glycosyltransferase, Transferase

Keywords - Biological processi

Wnt signaling pathway

Keywords - Ligandi

Manganese, Metal-binding

Enzyme and pathway databases

BRENDAi2.4.1.225. 1994.
ReactomeiREACT_334979. HS-GAG biosynthesis.
SignaLinkiQ9Y169.
UniPathwayiUPA00378.
UPA00756.
UPA00862.

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):
Protein sister of tout-velu
Gene namesi
Name:Ext2
Synonyms:DEXT2, sotv
ORF Names:CG33038
OrganismiDrosophila melanogaster (Fruit fly)
Taxonomic identifieri7227 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora
ProteomesiUP000000803 Componenti: Chromosome 2R

Organism-specific databases

FlyBaseiFBgn0029175. Ext2.

Subcellular locationi

Endoplasmic reticulum membrane By similarity; Single-pass type II membrane protein By similarity. Golgi apparatus membrane 1 Publication; Single-pass type II membrane protein 1 Publication
Note: Localization to the Golgi may be regulated by rti.

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 – 717671LumenalSequence AnalysisAdd
BLAST

GO - Cellular componenti

  1. endoplasmic reticulum Source: UniProtKB
  2. endoplasmic reticulum membrane Source: UniProtKB-SubCell
  3. Golgi apparatus Source: UniProtKB
  4. Golgi membrane Source: UniProtKB-SubCell
  5. integral component of membrane Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Endoplasmic reticulum, Golgi apparatus, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 717717Exostosin-2PRO_0000149665Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi91 – 911N-linked (GlcNAc...)Sequence Analysis
Glycosylationi574 – 5741N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi625 ↔ 675By similarity
Glycosylationi636 – 6361N-linked (GlcNAc...)Sequence Analysis

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

PaxDbiQ9Y169.
PRIDEiQ9Y169.

Expressioni

Tissue specificityi

In wing imaginal disk, it is ubiquitously expressed.1 Publication

Developmental stagei

Expressed both maternally and zygotically.1 Publication

Interactioni

Subunit structurei

Forms a homo/heterooligomeric complex with ttv (Probable). May interact with rti.Curated

Binary interactionsi

WithEntry#Exp.IntActNotes
ttvQ9V7303EBI-142791,EBI-166374

Protein-protein interaction databases

IntActiQ9Y169. 2 interactions.
MINTiMINT-850131.

Structurei

3D structure databases

ProteinModelPortaliQ9Y169.
SMRiQ9Y169. Positions 455-689.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni516 – 5216Substrate bindingBy similarity
Regioni537 – 5393Substrate bindingBy similarity
Regioni623 – 6275Substrate bindingBy similarity
Regioni661 – 67212Substrate bindingBy similarityAdd
BLAST

Sequence similaritiesi

Belongs to the glycosyltransferase 47 family.Curated

Keywords - Domaini

Signal-anchor, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiNOG272619.
GeneTreeiENSGT00550000074496.
InParanoidiQ9Y169.
KOiK02367.
OMAiQFGYEVW.
OrthoDBiEOG789C9T.
PhylomeDBiQ9Y169.

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.

Q9Y169-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTKIKNLLSF VTQSRAISHT NPREHILNCL TYGLLVIVAL CAGFLLWDLS
60 70 80 90 100
SSPRDGFFHG KRDSHTLILD LEHIQELAVN PEAEQRARNV NCTFWDCLNI
110 120 130 140 150
YKCEHDRLKV YIYPLQEFVD EQSDKTATTL SSEYFQILEA VLKSRYYTSN
160 170 180 190 200
PNEACLFLPS LDLLNQNVFD KHLAGAALAS LDFWDRGANH IIFNMLPGGA
210 220 230 240 250
PSYNTVLDVN TDNAIIFGGG FDSWSYRPGF DVAIPVWSPR LVRQHAHATA
260 270 280 290 300
QRKFLLVVAQ LNILPRFVRT LRELSLAHSE QLLLLGACEN LDLTMRCPLS
310 320 330 340 350
QHHKSLEYPR LLSRGKFCLL GRSLRMGQPD LVEIMSQHCI PVIAVDNYVL
360 370 380 390 400
PFEDVIDWSL ASVRIRENEL HSVMQKLKAI SSVKIVEMQK QVQWLFSKYF
410 420 430 440 450
KDLKTVTLTA LEVLESRIFP LRARSSRQWN TIDTNARSTF NPLFLPSLAP
460 470 480 490 500
KSQGFTAVIL TYDRVESLFL LIQKLAVVPS LQSILVIWNN QKKSPPHLST
510 520 530 540 550
FPSISKPLKI RQTKENKLSN RFYPYPEIET EAILTIDDDI IMLTTDELDF
560 570 580 590 600
GYEVWREFPD HIVGFPSRIH VWENVTMRWH YESEWTNQIS MVLTGAAFHH
610 620 630 640 650
KYWSHMYTHA MPGDIKDWVD EHMNCEDIAM NFLVANITNN PPIKVTPRKK
660 670 680 690 700
FKCPECTNTE MLSADLNHMR ERSACIDRFS KIYGRMPLRT VEFRADPVLF
710
RDNFPDKLKR YNDIGSL
Length:717
Mass (Da):82,726
Last modified:November 1, 1999 - v1
Checksum:iA3894493C16EF7DC
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE013599 Genomic DNA. Translation: AAF58055.2.
AF145598 mRNA. Translation: AAD38573.1.
BT003544 mRNA. Translation: AAO39548.1.
RefSeqiNP_725536.1. NM_166150.3.
UniGeneiDm.20855.

Genome annotation databases

EnsemblMetazoaiFBtr0100513; FBpp0099953; FBgn0029175.
GeneIDi3772101.
KEGGidme:Dmel_CG8433.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE013599 Genomic DNA. Translation: AAF58055.2.
AF145598 mRNA. Translation: AAD38573.1.
BT003544 mRNA. Translation: AAO39548.1.
RefSeqiNP_725536.1. NM_166150.3.
UniGeneiDm.20855.

3D structure databases

ProteinModelPortaliQ9Y169.
SMRiQ9Y169. Positions 455-689.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiQ9Y169. 2 interactions.
MINTiMINT-850131.

Protein family/group databases

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

Proteomic databases

PaxDbiQ9Y169.
PRIDEiQ9Y169.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaiFBtr0100513; FBpp0099953; FBgn0029175.
GeneIDi3772101.
KEGGidme:Dmel_CG8433.

Organism-specific databases

CTDi2132.
FlyBaseiFBgn0029175. Ext2.

Phylogenomic databases

eggNOGiNOG272619.
GeneTreeiENSGT00550000074496.
InParanoidiQ9Y169.
KOiK02367.
OMAiQFGYEVW.
OrthoDBiEOG789C9T.
PhylomeDBiQ9Y169.

Enzyme and pathway databases

UniPathwayiUPA00378.
UPA00756.
UPA00862.
BRENDAi2.4.1.225. 1994.
ReactomeiREACT_334979. HS-GAG biosynthesis.
SignaLinkiQ9Y169.

Miscellaneous databases

GenomeRNAii3772101.
NextBioi852446.
PROiQ9Y169.

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

« Hide 'large scale' publications
  1. "The genome sequence of Drosophila melanogaster."
    Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., Sutton G.G., Wortman J.R., Yandell M.D.
    , Zhang Q., Chen L.X., Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D., Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J., Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.
    Science 287:2185-2195(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: Berkeley.
  2. Cited for: GENOME REANNOTATION.
    Strain: Berkeley.
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: Berkeley.
    Tissue: Head.
  4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: Berkeley.
    Tissue: Head.
  5. "Three Drosophila EXT genes shape morphogen gradients through synthesis of heparan sulfate proteoglycans."
    Takei Y., Ozawa Y., Sato M., Watanabe A., Tabata T.
    Development 131:73-82(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, TISSUE SPECIFICITY.
  6. "Distinct and collaborative roles of Drosophila EXT family proteins in morphogen signalling and gradient formation."
    Han C., Belenkaya T.Y., Khodoun M., Tauchi M., Lin X., Lin X.
    Development 131:1563-1575(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  7. "Abrogation of heparan sulfate synthesis in Drosophila disrupts the Wingless, Hedgehog and Decapentaplegic signaling pathways."
    Bornemann D.J., Duncan J.E., Staatz W., Selleck S., Warrior R.
    Development 131:1927-1938(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, DEVELOPMENTAL STAGE.
  8. "The Drosophila GOLPH3 homolog regulates the biosynthesis of heparan sulfate proteoglycans by modulating the retrograde trafficking of exostosins."
    Chang W.L., Chang C.W., Chang Y.Y., Sung H.H., Lin M.D., Chang S.C., Chen C.H., Huang C.W., Tung K.S., Chou T.B.
    Development 140:2798-2807(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH RTI, SUBCELLULAR LOCATION.

Entry informationi

Entry nameiEXT2_DROME
AccessioniPrimary (citable) accession number: Q9Y169
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 15, 2005
Last sequence update: November 1, 1999
Last modified: April 1, 2015
This is version 107 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programDrosophila annotation project

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Drosophila
    Drosophila: entries, gene names and cross-references to FlyBase
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. 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.