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P25723 (TLD_DROME) Reviewed, UniProtKB/Swiss-Prot

Last modified March 19, 2014. Version 138. 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·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Dorsal-ventral patterning protein tolloid

EC=3.4.24.-
Gene names
Name:tld
ORF Names:CG6868
OrganismDrosophila melanogaster (Fruit fly) [Reference proteome]
Taxonomic identifier7227 [NCBI]
Taxonomic lineageEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora

Protein attributes

Sequence length1067 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

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

Miscellaneous

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

Sequence similarities

Belongs to the peptidase M12A family.

Contains 5 CUB domains.

Contains 2 EGF-like domains.

Sequence caution

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

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

Ontologies

Keywords
   DomainEGF-like domain
Repeat
Signal
   LigandCalcium
Metal-binding
Zinc
   Molecular functionDevelopmental protein
Hydrolase
Metalloprotease
Protease
   PTMCleavage on pair of basic residues
Disulfide bond
Glycoprotein
Zymogen
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processamnioserosa formation

Non-traceable author statement PubMed 11532914. Source: FlyBase

imaginal disc-derived wing vein morphogenesis

Inferred from mutant phenotype PubMed 15872004. Source: FlyBase

maternal specification of dorsal/ventral axis, oocyte, soma encoded

Inferred from mutant phenotype PubMed 16781701. Source: FlyBase

negative regulation of gene expression

Inferred from direct assay PubMed 16780828. Source: FlyBase

positive regulation of BMP signaling pathway

Traceable author statement PubMed 11290316. Source: FlyBase

protein processing

Inferred from direct assay PubMed 17119021. Source: FlyBase

proteolysis

Non-traceable author statement PubMed 9712300. Source: FlyBase

regulation of transforming growth factor beta receptor signaling pathway

Traceable author statement PubMed 11700289. Source: FlyBase

terminal region determination

Inferred from genetic interaction PubMed 1905816. Source: FlyBase

torso signaling pathway

Inferred from genetic interaction PubMed 1905816. Source: FlyBase

   Cellular_componentextracellular region

Non-traceable author statement PubMed 9712300. Source: FlyBase

   Molecular_functioncalcium ion binding

Inferred from electronic annotation. Source: InterPro

metalloendopeptidase activity

Non-traceable author statement PubMed 11290316PubMed 11700289. Source: FlyBase

zinc ion binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 3636 Potential
Propeptide37 – 136100 Potential
PRO_0000028903
Chain137 – 1067931Dorsal-ventral patterning protein tolloid
PRO_0000028904

Regions

Domain340 – 477138CUB 1
Domain478 – 591114CUB 2
Domain591 – 63141EGF-like 1; calcium-binding Potential
Domain634 – 753120CUB 3
Domain753 – 79341EGF-like 2; calcium-binding Potential
Domain797 – 909113CUB 4
Domain910 – 1026117CUB 5
Region137 – 339203Metalloprotease
Motif245 – 2473Cell attachment site Potential
Motif325 – 3273Cell attachment site Potential

Sites

Active site2321 By similarity
Metal binding2311Zinc; catalytic By similarity
Metal binding2351Zinc; catalytic By similarity
Metal binding2411Zinc; catalytic By similarity

Amino acid modifications

Glycosylation1761N-linked (GlcNAc...) Potential
Glycosylation4411N-linked (GlcNAc...) Potential
Glycosylation5431N-linked (GlcNAc...) Potential
Glycosylation6441N-linked (GlcNAc...) Potential
Glycosylation6771N-linked (GlcNAc...) Potential
Glycosylation7911N-linked (GlcNAc...) Potential
Glycosylation8641N-linked (GlcNAc...) Potential
Glycosylation9181N-linked (GlcNAc...) Potential
Disulfide bond340 ↔ 390 By similarity
Disulfide bond417 ↔ 439 By similarity
Disulfide bond478 ↔ 505 By similarity
Disulfide bond532 ↔ 554 By similarity
Disulfide bond595 ↔ 606 By similarity
Disulfide bond602 ↔ 615 By similarity
Disulfide bond617 ↔ 630 By similarity
Disulfide bond634 ↔ 662 By similarity
Disulfide bond693 ↔ 716 By similarity
Disulfide bond757 ↔ 768 By similarity
Disulfide bond764 ↔ 777 By similarity
Disulfide bond779 ↔ 792 By similarity
Disulfide bond797 ↔ 823 By similarity
Disulfide bond850 ↔ 872 By similarity
Disulfide bond910 ↔ 940 By similarity
Disulfide bond967 ↔ 989 By similarity

Sequences

Sequence LengthMass (Da)Tools
P25723 [UniParc].

Last modified August 16, 2004. Version 2.
Checksum: 6375871E9F2B54C2

FASTA1,067121,780
        10         20         30         40         50         60 
MKGMRLMPMK MKAKLVVLSV GALWMMMFFL VDYAEGRRLS QLPESECDFD FKEQPEDFFG 

        70         80         90        100        110        120 
ILDSSLVPPK EPKDDIYQLK TTRQHSGRRR KQSHKSQNKA ALRLPPPFLW TDDAVDVLQH 

       130        140        150        160        170        180 
SHSPTLNGQP IQRRRRAVTV RKERTWDYGV IPYEIDTIFS GAHKALFKQA MRHWENFTCI 

       190        200        210        220        230        240 
KFVERDPNLH ANYIYFTVKN CGCCSFLGKN GNGRQPISIG RNCEKFGIII HELGHTIGFH 

       250        260        270        280        290        300 
HEHARGDRDK HIVINKGNIM RGQEYNFDVL SPEEVDLPLL PYDLNSIMHY AKNSFSKSPY 

       310        320        330        340        350        360 
LDTITPIGIP PGTHLELGQR KRLSRGDIVQ ANLLYKCASC GRTYQQNSGH IVSPHFIYSG 

       370        380        390        400        410        420 
NGVLSEFEGS GDAGEDPSAE SEFDASLTNC EWRITATNGE KVILHLQQLH LMSSDDCTQD 

       430        440        450        460        470        480 
YLEIRDGYWH KSPLVRRICG NVSGEVITTQ TSRMLLNYVN RNAAKGYRGF KARFEVVCGG 

       490        500        510        520        530        540 
DLKLTKDQSI DSPNYPMDYM PDKECVWRIT APDNHQVALK FQSFELEKHD GCAYDFVEIR 

       550        560        570        580        590        600 
DGNHSDSRLI GRFCGDKLPP NIKTRSNQMY IRFVSDSSVQ KLGFSAALML DVDECKFTDH 

       610        620        630        640        650        660 
GCQHLCINTL GSYQCGCRAG YELQANGKTC EDACGGVVDA TKSNGSLYSP SYPDVYPNSK 

       670        680        690        700        710        720 
QCVWEVVAPP NHAVFLNFSH FDLEGTRFHY TKCNYDYLII YSKMRDNRLK KIGIYCGHEL 

       730        740        750        760        770        780 
PPVVNSEQSI LRLEFYSDRT VQRSGFVAKF VIDVDECSMN NGGCQHRCRN TFGSYQCSCR 

       790        800        810        820        830        840 
NGYTLAENGH NCTETRCKFE ITTSYGVLQS PNYPEDYPRN IYCYWHFQTV LGHRIQLTFH 

       850        860        870        880        890        900 
DFEVESHQEC IYDYVAIYDG RSENSSTLGI YCGGREPYAV IASTNEMFMV LATDAGLQRK 

       910        920        930        940        950        960 
GFKATFVSEC GGYLRATNHS QTFYSHPRYG SRPYKRNMYC DWRIQADPES SVKIRFLHFE 

       970        980        990       1000       1010       1020 
IEYSERCDYD YLEITEEGYS MNTIHGRFCG KHKPPIIISN SDTLLLRFQT DESNSLRGFA 

      1030       1040       1050       1060 
ISFMAVDPPE DSVGEDFDAV TPFPGYLKSM YSSETGSDHL LPPSRLI 

« Hide

References

« Hide 'large scale' references
[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. 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.
[4]"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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M76976 mRNA. Translation: AAA28491.1. Different initiation.
U04239 Unassigned DNA. Translation: AAC46482.1. Different initiation.
AE014297 Genomic DNA. Translation: AAF56329.2.
PIRA39288.
RefSeqNP_524487.2. NM_079763.3.
UniGeneDm.18982.

3D structure databases

ProteinModelPortalP25723.
SMRP25723. Positions 103-1065.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid67870. 4 interactions.
DIPDIP-22889N.
IntActP25723. 1 interaction.
MINTMINT-1022959.

Protein family/group databases

MEROPSM12.010.

Proteomic databases

PaxDbP25723.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaFBtr0084691; FBpp0084070; FBgn0003719.
GeneID42945.
KEGGdme:Dmel_CG6868.
UCSCCG6868-RA. d. melanogaster.

Organism-specific databases

CTD42945.
FlyBaseFBgn0003719. tld.

Phylogenomic databases

eggNOGNOG87014.
GeneTreeENSGT00740000115257.
InParanoidP25723.
KOK13045.
OMADGRSENS.
OrthoDBEOG7N8ZTV.
PhylomeDBP25723.

Gene expression databases

BgeeP25723.

Family and domain databases

Gene3D2.60.120.290. 5 hits.
3.40.390.10. 1 hit.
InterProIPR015446. 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]
PfamPF01400. Astacin. 1 hit.
PF00431. CUB. 5 hits.
PF07645. EGF_CA. 1 hit.
[Graphical view]
PIRSFPIRSF001199. BMP_1/tolloid-like. 1 hit.
PRINTSPR00480. ASTACIN.
SMARTSM00042. CUB. 5 hits.
SM00179. EGF_CA. 2 hits.
SM00235. ZnMc. 1 hit.
[Graphical view]
SUPFAMSSF49854. SSF49854. 6 hits.
PROSITEPS00010. 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]
ProtoNetSearch...

Other

GenomeRNAi42945.
NextBio831452.

Entry information

Entry nameTLD_DROME
AccessionPrimary (citable) accession number: P25723
Secondary accession number(s): Q9VC46
Entry history
Integrated into UniProtKB/Swiss-Prot: May 1, 1992
Last sequence update: August 16, 2004
Last modified: March 19, 2014
This is version 138 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programDrosophila annotation project

Relevant documents

SIMILARITY comments

Index of protein domains and families

Peptidase families

Classification of peptidase families and list of entries

Drosophila

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