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Q9Y169

- EXT2_DROME

UniProt

Q9Y169 - EXT2_DROME

Protein

Exostosin-2

Gene

Ext2

Organism
Drosophila melanogaster (Fruit fly)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 102 (01 Oct 2014)
      Sequence version 1 (01 Nov 1999)
      Previous versions | rss
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    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.

    Pathwayi

    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. N-acetylglucosaminyl-proteoglycan 4-beta-glucuronosyltransferase activity Source: UniProtKB
    5. protein binding 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

    Keywords - Molecular functioni

    Developmental protein, Glycosyltransferase, Transferase

    Keywords - Biological processi

    Wnt signaling pathway

    Enzyme and pathway databases

    ReactomeiREACT_180263. 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: 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.

    GO - Cellular componenti

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

    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
    Glycosylationi636 – 6361N-linked (GlcNAc...)Sequence Analysis

    Keywords - PTMi

    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...

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini1 – 2525CytoplasmicSequence AnalysisAdd
    BLAST
    Topological domaini47 – 717671LumenalSequence AnalysisAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei26 – 4621Helical; Signal-anchor for type II membrane proteinSequence AnalysisAdd
    BLAST

    Family & Domainsi

    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. HexNAc_Trfase_a.
    IPR029044. Nucleotide-diphossugar_trans.
    [Graphical view]
    PANTHERiPTHR11062. PTHR11062. 1 hit.
    PTHR11062: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

    MTKIKNLLSF VTQSRAISHT NPREHILNCL TYGLLVIVAL CAGFLLWDLS    50
    SSPRDGFFHG KRDSHTLILD LEHIQELAVN PEAEQRARNV NCTFWDCLNI 100
    YKCEHDRLKV YIYPLQEFVD EQSDKTATTL SSEYFQILEA VLKSRYYTSN 150
    PNEACLFLPS LDLLNQNVFD KHLAGAALAS LDFWDRGANH IIFNMLPGGA 200
    PSYNTVLDVN TDNAIIFGGG FDSWSYRPGF DVAIPVWSPR LVRQHAHATA 250
    QRKFLLVVAQ LNILPRFVRT LRELSLAHSE QLLLLGACEN LDLTMRCPLS 300
    QHHKSLEYPR LLSRGKFCLL GRSLRMGQPD LVEIMSQHCI PVIAVDNYVL 350
    PFEDVIDWSL ASVRIRENEL HSVMQKLKAI SSVKIVEMQK QVQWLFSKYF 400
    KDLKTVTLTA LEVLESRIFP LRARSSRQWN TIDTNARSTF NPLFLPSLAP 450
    KSQGFTAVIL TYDRVESLFL LIQKLAVVPS LQSILVIWNN QKKSPPHLST 500
    FPSISKPLKI RQTKENKLSN RFYPYPEIET EAILTIDDDI IMLTTDELDF 550
    GYEVWREFPD HIVGFPSRIH VWENVTMRWH YESEWTNQIS MVLTGAAFHH 600
    KYWSHMYTHA MPGDIKDWVD EHMNCEDIAM NFLVANITNN PPIKVTPRKK 650
    FKCPECTNTE MLSADLNHMR ERSACIDRFS KIYGRMPLRT VEFRADPVLF 700
    RDNFPDKLKR YNDIGSL 717
    Length:717
    Mass (Da):82,726
    Last modified:November 1, 1999 - v1
    Checksum:iA3894493C16EF7DC
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AE013599 Genomic DNA. Translation: AAF58055.2.
    AF145598 mRNA. Translation: AAD38573.1.
    BT003544 mRNA. Translation: AAO39548.1.
    RefSeqiNP_725536.1. NM_166150.2.
    NP_725537.2. NM_166151.2.
    UniGeneiDm.20855.

    Genome annotation databases

    EnsemblMetazoaiFBtr0100512; FBpp0099952; FBgn0029175.
    FBtr0100513; FBpp0099953; FBgn0029175.
    GeneIDi3772101.
    KEGGidme:Dmel_CG8433.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AE013599 Genomic DNA. Translation: AAF58055.2 .
    AF145598 mRNA. Translation: AAD38573.1 .
    BT003544 mRNA. Translation: AAO39548.1 .
    RefSeqi NP_725536.1. NM_166150.2.
    NP_725537.2. NM_166151.2.
    UniGenei Dm.20855.

    3D structure databases

    ProteinModelPortali Q9Y169.
    SMRi Q9Y169. Positions 455-689.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    IntActi Q9Y169. 2 interactions.
    MINTi MINT-850131.

    Protein family/group databases

    CAZyi GT47. Glycosyltransferase Family 47.
    GT64. Glycosyltransferase Family 64.

    Proteomic databases

    PaxDbi Q9Y169.
    PRIDEi Q9Y169.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblMetazoai FBtr0100512 ; FBpp0099952 ; FBgn0029175 .
    FBtr0100513 ; FBpp0099953 ; FBgn0029175 .
    GeneIDi 3772101.
    KEGGi dme:Dmel_CG8433.

    Organism-specific databases

    CTDi 2132.
    FlyBasei FBgn0029175. Ext2.

    Phylogenomic databases

    eggNOGi NOG272619.
    GeneTreei ENSGT00550000074496.
    InParanoidi Q9Y169.
    KOi K02367.
    OMAi QFGYEVW.
    OrthoDBi EOG789C9T.
    PhylomeDBi Q9Y169.

    Enzyme and pathway databases

    UniPathwayi UPA00378 .
    UPA00756 .
    UPA00862 .
    Reactomei REACT_180263. HS-GAG biosynthesis.
    SignaLinki Q9Y169.

    Miscellaneous databases

    GenomeRNAii 3772101.
    NextBioi 852446.
    PROi Q9Y169.

    Family and domain databases

    Gene3Di 3.90.550.10. 1 hit.
    InterProi IPR004263. Exostosin.
    IPR027673. Exostosin-2.
    IPR015338. HexNAc_Trfase_a.
    IPR029044. Nucleotide-diphossugar_trans.
    [Graphical view ]
    PANTHERi PTHR11062. PTHR11062. 1 hit.
    PTHR11062:SF6. PTHR11062:SF6. 1 hit.
    Pfami PF03016. Exostosin. 1 hit.
    PF09258. Glyco_transf_64. 1 hit.
    [Graphical view ]
    SUPFAMi SSF53448. SSF53448. 1 hit.
    ProtoNeti Search...

    Publicationsi

    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(2000) [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(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.

    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: October 1, 2014
    This is version 102 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