Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

P25723

- TLD_DROME

UniProt

P25723 - TLD_DROME

Protein

Dorsal-ventral patterning protein tolloid

Gene

tld

Organism
Drosophila melanogaster (Fruit fly)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at transcript leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 143 (01 Oct 2014)
      Sequence version 2 (16 Aug 2004)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    Functioni

    Required for normal dorsal development. TLD may interact physically with DPP-C protein.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi231 – 2311Zinc; catalyticPROSITE-ProRule annotation
    Active sitei232 – 2321PROSITE-ProRule annotation
    Metal bindingi235 – 2351Zinc; catalyticPROSITE-ProRule annotation
    Metal bindingi241 – 2411Zinc; catalyticPROSITE-ProRule annotation

    GO - Molecular functioni

    1. calcium ion binding Source: InterPro
    2. metalloendopeptidase activity Source: FlyBase
    3. zinc ion binding Source: InterPro

    GO - Biological processi

    1. amnioserosa formation Source: FlyBase
    2. embryonic pattern specification Source: FlyBase
    3. imaginal disc-derived wing vein morphogenesis Source: FlyBase
    4. maternal specification of dorsal/ventral axis, oocyte, soma encoded Source: FlyBase
    5. negative regulation of gene expression Source: FlyBase
    6. positive regulation of BMP signaling pathway Source: FlyBase
    7. protein processing Source: FlyBase
    8. proteolysis Source: FlyBase
    9. regulation of transforming growth factor beta receptor signaling pathway Source: FlyBase
    10. terminal region determination Source: FlyBase
    11. torso signaling pathway Source: FlyBase

    Keywords - Molecular functioni

    Developmental protein, Hydrolase, Metalloprotease, Protease

    Keywords - Ligandi

    Calcium, Metal-binding, Zinc

    Enzyme and pathway databases

    ReactomeiREACT_180755. Collagen biosynthesis and modifying enzymes.
    REACT_184283. Degradation of the extracellular matrix.
    REACT_224951. Anchoring fibril formation.

    Protein family/group databases

    MEROPSiM12.010.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Dorsal-ventral patterning protein tolloid (EC:3.4.24.-)
    Gene namesi
    Name:tld
    ORF Names:CG6868
    OrganismiDrosophila melanogaster (Fruit fly)
    Taxonomic identifieri7227 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora
    ProteomesiUP000000803: Chromosome 3R

    Organism-specific databases

    FlyBaseiFBgn0003719. tld.

    Subcellular locationi

    GO - Cellular componenti

    1. extracellular region Source: FlyBase

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 3636Sequence AnalysisAdd
    BLAST
    Propeptidei37 – 136100Sequence AnalysisPRO_0000028903Add
    BLAST
    Chaini137 – 1067931Dorsal-ventral patterning protein tolloidPRO_0000028904Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi176 – 1761N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi340 ↔ 390By similarity
    Disulfide bondi417 ↔ 439By similarity
    Glycosylationi441 – 4411N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi478 ↔ 505By similarity
    Disulfide bondi532 ↔ 554By similarity
    Glycosylationi543 – 5431N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi595 ↔ 606By similarity
    Disulfide bondi602 ↔ 615By similarity
    Disulfide bondi617 ↔ 630By similarity
    Disulfide bondi634 ↔ 662By similarity
    Glycosylationi644 – 6441N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi677 – 6771N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi693 ↔ 716By similarity
    Disulfide bondi757 ↔ 768By similarity
    Disulfide bondi764 ↔ 777By similarity
    Disulfide bondi779 ↔ 792By similarity
    Glycosylationi791 – 7911N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi797 ↔ 823By similarity
    Disulfide bondi850 ↔ 872By similarity
    Glycosylationi864 – 8641N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi910 ↔ 940By similarity
    Glycosylationi918 – 9181N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi967 ↔ 989By similarity

    Keywords - PTMi

    Cleavage on pair of basic residues, Disulfide bond, Glycoprotein, Zymogen

    Proteomic databases

    PaxDbiP25723.

    Expressioni

    Gene expression databases

    BgeeiP25723.

    Interactioni

    Protein-protein interaction databases

    BioGridi67870. 4 interactions.
    DIPiDIP-22889N.
    IntActiP25723. 1 interaction.
    MINTiMINT-1022959.

    Structurei

    3D structure databases

    ProteinModelPortaliP25723.
    SMRiP25723. Positions 137-1065.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini340 – 477138CUB 1PROSITE-ProRule annotationAdd
    BLAST
    Domaini478 – 591114CUB 2PROSITE-ProRule annotationAdd
    BLAST
    Domaini591 – 63141EGF-like 1; calcium-bindingPROSITE-ProRule annotationAdd
    BLAST
    Domaini634 – 753120CUB 3PROSITE-ProRule annotationAdd
    BLAST
    Domaini753 – 79341EGF-like 2; calcium-bindingPROSITE-ProRule annotationAdd
    BLAST
    Domaini797 – 909113CUB 4PROSITE-ProRule annotationAdd
    BLAST
    Domaini910 – 1026117CUB 5PROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni137 – 339203MetalloproteaseAdd
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi245 – 2473Cell attachment siteSequence Analysis
    Motifi325 – 3273Cell attachment siteSequence Analysis

    Sequence similaritiesi

    Belongs to the peptidase M12A family.Curated
    Contains 5 CUB domains.PROSITE-ProRule annotation
    Contains 2 EGF-like domains.PROSITE-ProRule annotation

    Keywords - Domaini

    EGF-like domain, Repeat, Signal

    Phylogenomic databases

    eggNOGiNOG87014.
    GeneTreeiENSGT00750000117289.
    InParanoidiP25723.
    KOiK13045.
    OMAiDGRSENS.
    OrthoDBiEOG7N8ZTV.
    PhylomeDBiP25723.

    Family and domain databases

    Gene3Di2.60.120.290. 5 hits.
    3.40.390.10. 1 hit.
    InterProiIPR015446. BMP_1/tolloid-like.
    IPR000859. CUB_dom.
    IPR000742. EG-like_dom.
    IPR001881. EGF-like_Ca-bd_dom.
    IPR013032. EGF-like_CS.
    IPR000152. EGF-type_Asp/Asn_hydroxyl_site.
    IPR018097. EGF_Ca-bd_CS.
    IPR024079. MetalloPept_cat_dom.
    IPR001506. Peptidase_M12A.
    IPR006026. Peptidase_Metallo.
    [Graphical view]
    PfamiPF01400. Astacin. 1 hit.
    PF00431. CUB. 5 hits.
    PF07645. EGF_CA. 1 hit.
    [Graphical view]
    PIRSFiPIRSF001199. BMP_1/tolloid-like. 1 hit.
    PRINTSiPR00480. ASTACIN.
    SMARTiSM00042. CUB. 5 hits.
    SM00179. EGF_CA. 2 hits.
    SM00235. ZnMc. 1 hit.
    [Graphical view]
    SUPFAMiSSF49854. SSF49854. 6 hits.
    PROSITEiPS00010. ASX_HYDROXYL. 2 hits.
    PS01180. CUB. 5 hits.
    PS01186. EGF_2. 2 hits.
    PS50026. EGF_3. 2 hits.
    PS01187. EGF_CA. 2 hits.
    PS00142. ZINC_PROTEASE. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    P25723-1 [UniParc]FASTAAdd to Basket

    « Hide

    MKGMRLMPMK MKAKLVVLSV GALWMMMFFL VDYAEGRRLS QLPESECDFD     50
    FKEQPEDFFG ILDSSLVPPK EPKDDIYQLK TTRQHSGRRR KQSHKSQNKA 100
    ALRLPPPFLW TDDAVDVLQH SHSPTLNGQP IQRRRRAVTV RKERTWDYGV 150
    IPYEIDTIFS GAHKALFKQA MRHWENFTCI KFVERDPNLH ANYIYFTVKN 200
    CGCCSFLGKN GNGRQPISIG RNCEKFGIII HELGHTIGFH HEHARGDRDK 250
    HIVINKGNIM RGQEYNFDVL SPEEVDLPLL PYDLNSIMHY AKNSFSKSPY 300
    LDTITPIGIP PGTHLELGQR KRLSRGDIVQ ANLLYKCASC GRTYQQNSGH 350
    IVSPHFIYSG NGVLSEFEGS GDAGEDPSAE SEFDASLTNC EWRITATNGE 400
    KVILHLQQLH LMSSDDCTQD YLEIRDGYWH KSPLVRRICG NVSGEVITTQ 450
    TSRMLLNYVN RNAAKGYRGF KARFEVVCGG DLKLTKDQSI DSPNYPMDYM 500
    PDKECVWRIT APDNHQVALK FQSFELEKHD GCAYDFVEIR DGNHSDSRLI 550
    GRFCGDKLPP NIKTRSNQMY IRFVSDSSVQ KLGFSAALML DVDECKFTDH 600
    GCQHLCINTL GSYQCGCRAG YELQANGKTC EDACGGVVDA TKSNGSLYSP 650
    SYPDVYPNSK QCVWEVVAPP NHAVFLNFSH FDLEGTRFHY TKCNYDYLII 700
    YSKMRDNRLK KIGIYCGHEL PPVVNSEQSI LRLEFYSDRT VQRSGFVAKF 750
    VIDVDECSMN NGGCQHRCRN TFGSYQCSCR NGYTLAENGH NCTETRCKFE 800
    ITTSYGVLQS PNYPEDYPRN IYCYWHFQTV LGHRIQLTFH DFEVESHQEC 850
    IYDYVAIYDG RSENSSTLGI YCGGREPYAV IASTNEMFMV LATDAGLQRK 900
    GFKATFVSEC GGYLRATNHS QTFYSHPRYG SRPYKRNMYC DWRIQADPES 950
    SVKIRFLHFE IEYSERCDYD YLEITEEGYS MNTIHGRFCG KHKPPIIISN 1000
    SDTLLLRFQT DESNSLRGFA ISFMAVDPPE DSVGEDFDAV TPFPGYLKSM 1050
    YSSETGSDHL LPPSRLI 1067
    Length:1,067
    Mass (Da):121,780
    Last modified:August 16, 2004 - v2
    Checksum:i6375871E9F2B54C2
    GO

    Sequence cautioni

    The sequence AAA28491.1 differs from that shown. Reason: Erroneous initiation.
    The sequence AAC46482.1 differs from that shown. Reason: Erroneous initiation.

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M76976 mRNA. Translation: AAA28491.1. Different initiation.
    U04239 Unassigned DNA. Translation: AAC46482.1. Different initiation.
    AE014297 Genomic DNA. Translation: AAF56329.2.
    PIRiA39288.
    RefSeqiNP_524487.2. NM_079763.3.
    UniGeneiDm.18982.

    Genome annotation databases

    EnsemblMetazoaiFBtr0084691; FBpp0084070; FBgn0003719.
    GeneIDi42945.
    KEGGidme:Dmel_CG6868.
    UCSCiCG6868-RA. d. melanogaster.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M76976 mRNA. Translation: AAA28491.1 . Different initiation.
    U04239 Unassigned DNA. Translation: AAC46482.1 . Different initiation.
    AE014297 Genomic DNA. Translation: AAF56329.2 .
    PIRi A39288.
    RefSeqi NP_524487.2. NM_079763.3.
    UniGenei Dm.18982.

    3D structure databases

    ProteinModelPortali P25723.
    SMRi P25723. Positions 137-1065.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 67870. 4 interactions.
    DIPi DIP-22889N.
    IntActi P25723. 1 interaction.
    MINTi MINT-1022959.

    Protein family/group databases

    MEROPSi M12.010.

    Proteomic databases

    PaxDbi P25723.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblMetazoai FBtr0084691 ; FBpp0084070 ; FBgn0003719 .
    GeneIDi 42945.
    KEGGi dme:Dmel_CG6868.
    UCSCi CG6868-RA. d. melanogaster.

    Organism-specific databases

    CTDi 42945.
    FlyBasei FBgn0003719. tld.

    Phylogenomic databases

    eggNOGi NOG87014.
    GeneTreei ENSGT00750000117289.
    InParanoidi P25723.
    KOi K13045.
    OMAi DGRSENS.
    OrthoDBi EOG7N8ZTV.
    PhylomeDBi P25723.

    Enzyme and pathway databases

    Reactomei REACT_180755. Collagen biosynthesis and modifying enzymes.
    REACT_184283. Degradation of the extracellular matrix.
    REACT_224951. Anchoring fibril formation.

    Miscellaneous databases

    GenomeRNAii 42945.
    NextBioi 831452.

    Gene expression databases

    Bgeei P25723.

    Family and domain databases

    Gene3Di 2.60.120.290. 5 hits.
    3.40.390.10. 1 hit.
    InterProi IPR015446. BMP_1/tolloid-like.
    IPR000859. CUB_dom.
    IPR000742. EG-like_dom.
    IPR001881. EGF-like_Ca-bd_dom.
    IPR013032. EGF-like_CS.
    IPR000152. EGF-type_Asp/Asn_hydroxyl_site.
    IPR018097. EGF_Ca-bd_CS.
    IPR024079. MetalloPept_cat_dom.
    IPR001506. Peptidase_M12A.
    IPR006026. Peptidase_Metallo.
    [Graphical view ]
    Pfami PF01400. Astacin. 1 hit.
    PF00431. CUB. 5 hits.
    PF07645. EGF_CA. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF001199. BMP_1/tolloid-like. 1 hit.
    PRINTSi PR00480. ASTACIN.
    SMARTi SM00042. CUB. 5 hits.
    SM00179. EGF_CA. 2 hits.
    SM00235. ZnMc. 1 hit.
    [Graphical view ]
    SUPFAMi SSF49854. SSF49854. 6 hits.
    PROSITEi PS00010. ASX_HYDROXYL. 2 hits.
    PS01180. CUB. 5 hits.
    PS01186. EGF_2. 2 hits.
    PS50026. EGF_3. 2 hits.
    PS01187. EGF_CA. 2 hits.
    PS00142. ZINC_PROTEASE. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "The Drosophila dorsal-ventral patterning gene tolloid is related to human bone morphogenetic protein 1."
      Shimell M.J., Ferguson E.L., Childs S.R., O'Connor M.B.
      Cell 67:469-481(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Strain: Canton-S.
    2. "Mutational analysis of the Drosophila tolloid gene, a human BMP-1 homolog."
      Finelli A.L., Bossie C.A., Xie T., Padgett R.W.
      Development 120:861-870(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE.
    3. "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.
    4. Cited for: GENOME REANNOTATION.
      Strain: Berkeley.

    Entry informationi

    Entry nameiTLD_DROME
    AccessioniPrimary (citable) accession number: P25723
    Secondary accession number(s): Q9VC46
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: May 1, 1992
    Last sequence update: August 16, 2004
    Last modified: October 1, 2014
    This is version 143 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programDrosophila annotation project

    Miscellaneousi

    Miscellaneous

    Mutations in TLD lead to a partial transformation of dorsal ectoderm into ventral ectoderm.

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. Drosophila
      Drosophila: entries, gene names and cross-references to FlyBase
    2. Peptidase families
      Classification of peptidase families and list of entries
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3