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P25723

- TLD_DROME

UniProt

P25723 - TLD_DROME

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Protein

Dorsal-ventral patterning protein tolloid

Gene
tld, CG6868
Organism
Drosophila melanogaster (Fruit fly)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at transcript leveli

Functioni

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

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi231 – 2311Zinc; catalytic By similarity
Active sitei232 – 2321 By similarity
Metal bindingi235 – 2351Zinc; catalytic By similarity
Metal bindingi241 – 2411Zinc; catalytic By similarity

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
Complete GO annotation...

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
Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 3636 Reviewed predictionAdd
BLAST
Propeptidei37 – 136100 Reviewed predictionPRO_0000028903Add
BLAST
Chaini137 – 1067931Dorsal-ventral patterning protein tolloidPRO_0000028904Add
BLAST

Amino acid modifications

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

Family & Domainsi

Domains and Repeats

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

Region

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

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi245 – 2473Cell attachment site Reviewed prediction
Motifi325 – 3273Cell attachment site Reviewed prediction

Sequence similaritiesi

Belongs to the peptidase M12A family.
Contains 5 CUB domains.
Contains 2 EGF-like domains.

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

« Hide 'large scale' publications
  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: September 3, 2014
This is version 142 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

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