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Q9Y169 (EXT2_DROME) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 98. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Exostosin-2

EC=2.4.1.224
EC=2.4.1.225
Alternative name(s):
Protein sister of tout-velu
Gene names
Name:Ext2
Synonyms:DEXT2, sotv
ORF Names:CG33038
OrganismDrosophila melanogaster (Fruit fly) [Reference proteome]
Taxonomic identifier7227 [NCBI]
Taxonomic lineageEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora

Protein attributes

Sequence length717 AA.
Sequence statusComplete.
Protein existenceEvidence 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. 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. Ref.5 Ref.6 Ref.7

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.

Glycan metabolism; heparan sulfate biosynthesis.

Glycan metabolism; heparin biosynthesis.

Subunit structure

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

Subcellular location

Endoplasmic reticulum membrane; Single-pass type II membrane protein By similarity. Golgi apparatus membrane; Single-pass type II membrane protein. Note: Localization to the Golgi may be regulated by rti. Ref.8

Tissue specificity

In wing imaginal disk, it is ubiquitously expressed. Ref.5

Developmental stage

Expressed both maternally and zygotically. Ref.7

Sequence similarities

Belongs to the glycosyltransferase 47 family.

Ontologies

Keywords
   Biological processWnt signaling pathway
   Cellular componentEndoplasmic reticulum
Golgi apparatus
Membrane
   DomainSignal-anchor
Transmembrane
Transmembrane helix
   Molecular functionDevelopmental protein
Glycosyltransferase
Transferase
   PTMGlycoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processN-acetylglucosamine metabolic process

Inferred from sequence or structural similarity. Source: UniProtKB

Wnt signaling pathway

Inferred from mutant phenotype Ref.5. Source: UniProtKB

chondroitin sulfate biosynthetic process

Inferred from mutant phenotype Ref.7. Source: FlyBase

decapentaplegic signaling pathway

Inferred from mutant phenotype Ref.5Ref.6. Source: UniProtKB

glycosaminoglycan biosynthetic process

Inferred from mutant phenotype Ref.6. Source: FlyBase

heparan sulfate proteoglycan biosynthetic process

Inferred from direct assay PubMed 16303756. Source: FlyBase

heparan sulfate proteoglycan biosynthetic process, polysaccharide chain biosynthetic process

Inferred from mutant phenotype Ref.5. Source: FlyBase

heparin biosynthetic process

Inferred from mutant phenotype Ref.7. Source: FlyBase

multicellular organismal development

Inferred from electronic annotation. Source: UniProtKB-KW

protein glycosylation

Inferred from electronic annotation. Source: UniProtKB-UniPathway

smoothened signaling pathway

Inferred from mutant phenotype Ref.5Ref.6. Source: UniProtKB

   Cellular_componentGolgi apparatus

Inferred from direct assay Ref.6. Source: UniProtKB

Golgi membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

endoplasmic reticulum

Inferred from direct assay Ref.6. Source: UniProtKB

integral component of membrane

Inferred from electronic annotation. Source: UniProtKB-KW

intrinsic component of endoplasmic reticulum membrane

Inferred from electronic annotation. Source: InterPro

   Molecular_functionN-acetylglucosaminyl-proteoglycan 4-beta-glucuronosyltransferase activity

Inferred from sequence or structural similarity. Source: UniProtKB

acetylglucosaminyltransferase activity

Non-traceable author statement PubMed 12464307. Source: FlyBase

glucuronosyl-N-acetylglucosaminyl-proteoglycan 4-alpha-N-acetylglucosaminyltransferase activity

Inferred from sequence or structural similarity. Source: UniProtKB

glucuronosyltransferase activity

Non-traceable author statement PubMed 12464307. Source: FlyBase

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

ttvQ9V7303EBI-142791,EBI-166374

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 717717Exostosin-2
PRO_0000149665

Regions

Topological domain1 – 2525Cytoplasmic Potential
Transmembrane26 – 4621Helical; Signal-anchor for type II membrane protein; Potential
Topological domain47 – 717671Lumenal Potential

Amino acid modifications

Glycosylation911N-linked (GlcNAc...) Potential
Glycosylation5741N-linked (GlcNAc...) Potential
Glycosylation6361N-linked (GlcNAc...) Potential

Sequences

Sequence LengthMass (Da)Tools
Q9Y169 [UniParc].

Last modified November 1, 1999. Version 1.
Checksum: A3894493C16EF7DC

FASTA71782,726
        10         20         30         40         50         60 
MTKIKNLLSF VTQSRAISHT NPREHILNCL TYGLLVIVAL CAGFLLWDLS SSPRDGFFHG 

        70         80         90        100        110        120 
KRDSHTLILD LEHIQELAVN PEAEQRARNV NCTFWDCLNI YKCEHDRLKV YIYPLQEFVD 

       130        140        150        160        170        180 
EQSDKTATTL SSEYFQILEA VLKSRYYTSN PNEACLFLPS LDLLNQNVFD KHLAGAALAS 

       190        200        210        220        230        240 
LDFWDRGANH IIFNMLPGGA PSYNTVLDVN TDNAIIFGGG FDSWSYRPGF DVAIPVWSPR 

       250        260        270        280        290        300 
LVRQHAHATA QRKFLLVVAQ LNILPRFVRT LRELSLAHSE QLLLLGACEN LDLTMRCPLS 

       310        320        330        340        350        360 
QHHKSLEYPR LLSRGKFCLL GRSLRMGQPD LVEIMSQHCI PVIAVDNYVL PFEDVIDWSL 

       370        380        390        400        410        420 
ASVRIRENEL HSVMQKLKAI SSVKIVEMQK QVQWLFSKYF KDLKTVTLTA LEVLESRIFP 

       430        440        450        460        470        480 
LRARSSRQWN TIDTNARSTF NPLFLPSLAP KSQGFTAVIL TYDRVESLFL LIQKLAVVPS 

       490        500        510        520        530        540 
LQSILVIWNN QKKSPPHLST FPSISKPLKI RQTKENKLSN RFYPYPEIET EAILTIDDDI 

       550        560        570        580        590        600 
IMLTTDELDF GYEVWREFPD HIVGFPSRIH VWENVTMRWH YESEWTNQIS MVLTGAAFHH 

       610        620        630        640        650        660 
KYWSHMYTHA MPGDIKDWVD EHMNCEDIAM NFLVANITNN PPIKVTPRKK FKCPECTNTE 

       670        680        690        700        710 
MLSADLNHMR ERSACIDRFS KIYGRMPLRT VEFRADPVLF RDNFPDKLKR YNDIGSL 

« Hide

References

« Hide 'large scale' references
[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. expand/collapse author list , 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(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Berkeley.
[2]"Annotation of the Drosophila melanogaster euchromatic genome: a systematic review."
Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S., Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E., Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P., Bettencourt B.R., Celniker S.E., de Grey A.D.N.J. expand/collapse author list , Drysdale R.A., Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.
Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: GENOME REANNOTATION.
Strain: Berkeley.
[3]"A Drosophila complementary DNA resource."
Rubin G.M., Hong L., Brokstein P., Evans-Holm M., Frise E., Stapleton M., Harvey D.A.
Science 287:2222-2224(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: Berkeley.
Tissue: Head.
[4]Stapleton M., Brokstein P., Hong L., Agbayani A., Carlson J.W., Champe M., Chavez C., Dorsett V., Dresnek D., Farfan D., Frise E., George R.A., Gonzalez M., Guarin H., Kronmiller B., Li P.W., Liao G., Miranda A. expand/collapse author list , Mungall C.J., Nunoo J., Pacleb J.M., Paragas V., Park S., Patel S., Phouanenavong S., Wan K.H., Yu C., Lewis S.E., Rubin G.M., Celniker S.E.
Submitted (FEB-2003) to the EMBL/GenBank/DDBJ databases
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(2004) [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(2004) [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(2004) [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(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH RTI, SUBCELLULAR LOCATION.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE013599 Genomic DNA. Translation: AAF58055.2.
AF145598 mRNA. Translation: AAD38573.1.
BT003544 mRNA. Translation: AAO39548.1.
RefSeqNP_725536.1. NM_166150.2.
NP_725537.2. NM_166151.2.
UniGeneDm.20855.

3D structure databases

ProteinModelPortalQ9Y169.
SMRQ9Y169. Positions 455-689.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

IntActQ9Y169. 2 interactions.
MINTMINT-850131.

Protein family/group databases

CAZyGT47. Glycosyltransferase Family 47.
GT64. Glycosyltransferase Family 64.

Proteomic databases

PaxDbQ9Y169.
PRIDEQ9Y169.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaFBtr0100512; FBpp0099952; FBgn0029175.
FBtr0100513; FBpp0099953; FBgn0029175.
GeneID3772101.
KEGGdme:Dmel_CG8433.

Organism-specific databases

CTD2132.
FlyBaseFBgn0029175. Ext2.

Phylogenomic databases

eggNOGNOG272619.
GeneTreeENSGT00550000074496.
InParanoidQ9Y169.
KOK02367.
OMAQFGYEVW.
OrthoDBEOG789C9T.
PhylomeDBQ9Y169.

Enzyme and pathway databases

SignaLinkQ9Y169.
UniPathwayUPA00378.
UPA00756.
UPA00862.

Family and domain databases

InterProIPR004263. Exostosin.
IPR027673. Exostosin-2.
IPR015338. HexNAc_Trfase_a.
[Graphical view]
PANTHERPTHR11062. PTHR11062. 1 hit.
PTHR11062:SF6. PTHR11062:SF6. 1 hit.
PfamPF03016. Exostosin. 1 hit.
PF09258. Glyco_transf_64. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

GenomeRNAi3772101.
NextBio852446.
PROQ9Y169.

Entry information

Entry nameEXT2_DROME
AccessionPrimary (citable) accession number: Q9Y169
Entry history
Integrated into UniProtKB/Swiss-Prot: March 15, 2005
Last sequence update: November 1, 1999
Last modified: April 16, 2014
This is version 98 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programDrosophila annotation project

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways

Drosophila

Drosophila: entries, gene names and cross-references to FlyBase