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Q9VAC5 (ADA17_DROME) Reviewed, UniProtKB/Swiss-Prot

Last modified April 18, 2012. Version 96. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
ADAM 17-like protease
EC=3.4.24.-
Gene names
Name:Tace
ORF Names:CG7908
OrganismDrosophila melanogaster (Fruit fly)
Taxonomic identifier7227 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Arthropoda › Hexapoda › Insecta › Pterygota › Neoptera › Endopterygota › Diptera › Brachycera › Muscomorpha › Ephydroidea › Drosophilidae › Drosophila › Sophophora

Protein attributes

Sequence length732 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript level

General annotation (Comments)

Cofactor

Binds 1 zinc ion per subunit By similarity.

Subcellular location

Membrane; Single-pass type I membrane protein Potential.

Domain

The conserved cysteine present in the cysteine-switch motif binds the catalytic zinc ion, thus inhibiting the enzyme. The dissociation of the cysteine from the zinc ion upon the activation-peptide release activates the enzyme.

Sequence similarities

Contains 1 disintegrin domain.

Contains 1 peptidase M12B domain.

Sequence caution

The sequence AAO24939.1 differs from that shown. Reason: Wrong choice of frame.

Ontologies

Keywords
   Cellular componentMembrane
   Coding sequence diversityAlternative splicing
   DomainSignal
Transmembrane
Transmembrane helix
   LigandMetal-binding
Zinc
   Molecular functionHydrolase
Metalloprotease
Protease
   PTMCleavage on pair of basic residues
Disulfide bond
Glycoprotein
Zymogen
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological processproteolysis

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular componentintegral to membrane

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular functionmetalloendopeptidase activity

Inferred from electronic annotation. Source: InterPro

zinc ion binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform A (identifier: Q9VAC5-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform B (identifier: Q9VAC5-2)

The sequence of this isoform differs from the canonical sequence as follows:
     252-262: ISLIDRVHKIY → VSFLKNPRSII
     263-732: Missing.
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2828 Potential
Propeptide29 – 211183 By similarity
PRO_0000029094
Chain212 – 732521ADAM 17-like protease
PRO_0000029095

Regions

Topological domain212 – 662451Extracellular Potential
Transmembrane663 – 68321Helical; Potential
Topological domain684 – 73249Cytoplasmic Potential
Domain223 – 467245Peptidase M12B
Domain468 – 55992Disintegrin
Region598 – 66265Crambin-like
Motif181 – 1888Cysteine switch By similarity
Compositional bias560 – 59940Cys-rich

Sites

Active site4001 By similarity
Metal binding1831Zinc; in inhibited form By similarity
Metal binding3991Zinc; catalytic By similarity
Metal binding4031Zinc; catalytic By similarity
Metal binding4091Zinc; catalytic By similarity

Amino acid modifications

Glycosylation1001N-linked (GlcNAc...) Potential
Glycosylation2631N-linked (GlcNAc...) Potential
Glycosylation4921N-linked (GlcNAc...) Potential
Glycosylation6041N-linked (GlcNAc...) Potential
Disulfide bond225 ↔ 328 By similarity
Disulfide bond360 ↔ 462 By similarity
Disulfide bond416 ↔ 446 By similarity
Disulfide bond530 ↔ 551 By similarity
Disulfide bond569 ↔ 578 By similarity
Disulfide bond574 ↔ 586 By similarity
Disulfide bond588 ↔ 595 By similarity

Natural variations

Alternative sequence252 – 26211ISLIDRVHKIY → VSFLKNPRSII in isoform B.
VSP_037658
Alternative sequence263 – 732470Missing in isoform B.
VSP_037659

Experimental info

Sequence conflict2081R → K in AAS48650. Ref.2
Sequence conflict428 – 4314MYTY → IHT in AAS48650. Ref.2
Sequence conflict4491R → A in AAS48650. Ref.2
Sequence conflict4631F → L in AAL28578. Ref.5
Sequence conflict5541S → F in AAS48650. Ref.2

Sequences

Sequence LengthMass (Da)Tools
Isoform A [UniParc].

Last modified October 10, 2003. Version 2.
Checksum: 0E96E7B30F973A0B

FASTA73283,081
        10         20         30         40         50         60 
MFTKCISCCG LAIISVFFAC LFVENCAALQ KTLRHYEIFH KDDVVHRVVK RGAKHSTNPF 

        70         80         90        100        110        120 
NTIKEVEFTT LGKNFRLILH PHRDVLHSKF RAYAVDADGN ETVVHMDHDS FYSGRVFGEL 

       130        140        150        160        170        180 
ESSVRAHIED GTMTMSIHLP EETYHIEPSW RHLPEAKKDT MVAYKASDVK VHKNEAGATP 

       190        200        210        220        230        240 
KTCGYIKEGL ELEDKEHGDT LDNELHTREK RQSDQYEYTP TKTRCPLLLV ADYRFFQEMG 

       250        260        270        280        290        300 
GGNTKTTINY LISLIDRVHK IYNDTVWQDR SDQEGFKGMG FVIKKIVVHS EPTRLRGGEA 

       310        320        330        340        350        360 
HYNMIREKWD VRNLLEVFSR EYSHKDFCLA HLFTDLKFEG GILGLAYVGS PRRNSVGGIC 

       370        380        390        400        410        420 
TPEYFKNGYT LYLNSGLSSS RNHYGQRVIT READLVTAHE FGHNWGSEHD PDIPECSPSA 

       430        440        450        460        470        480 
SQGGSFLMYT YSVSGYDVNN KKFSPCSLRS IRKVLQAKSG RCFSEPEESF CGNLRVEGDE 

       490        500        510        520        530        540 
QCDAGLLGTE DNDSCCDKNC KLRRNQGAMC SDKNSPCCQN CQFMASGMKC REAQYATCEQ 

       550        560        570        580        590        600 
EARCTGAHAE CPKSPAMADG TTCQERGQCR NGKCVPYCET QGLQSCMCDI IADACKRCCR 

       610        620        630        640        650        660 
MSINETCFPV EPPDVLPDGT PCITGFCNKG VCEKTIQDVV ERFWDIIEEI NVAKTLRFLK 

       670        680        690        700        710        720 
DNIVMAVVLV TAVFWIPISC VISYFDRKKL RHEMKLIEWS QKLDLIHPSD ERRRVIHIRV 

       730 
PRQKISVARA CN

« Hide

Isoform B [UniParc].

Checksum: 1B05318322383B37
Show »

FASTA26230,041

References

« Hide 'large scale' references
[1]Wei S., Brew K.
Submitted (JAN-2003) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM A).
Tissue: Embryo.
[2]"Asymmetric notch signaling depends on constitutive cleavage of delta."
Sapir A., Tsruya R., Shilo B.-Z.
Submitted (JAN-2004) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM A).
Strain: Berkeley.
Tissue: Head.
[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: 10731132] [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: 12537572] [Abstract]
Cited for: GENOME REANNOTATION, ALTERNATIVE SPLICING.
Strain: Berkeley.
[5]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 (JAN-2003) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM A), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 2-732 (ISOFORM B).
Strain: Berkeley.
Tissue: Embryo and Head.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AY212802 mRNA. Translation: AAO53296.1.
AY525768 mRNA. Translation: AAS48650.1.
AE014297 Genomic DNA. Translation: AAN14205.3.
AE014297 Genomic DNA. Translation: AAF56986.2.
AY061030 mRNA. Translation: AAL28578.1.
BT003184 mRNA. Translation: AAO24939.1. Sequence problems.
RefSeqNP_651759.4. NM_143502.3.
NP_733334.1. NM_170455.2.
UniGeneDm.6531.

3D structure databases

ProteinModelPortalQ9VAC5.
SMRQ9VAC5. Positions 218-644.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ9VAC5.

Protein family/group databases

MEROPSM12.217.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaFBtr0085551; FBpp0084917; FBgn0039734.
GeneID43558.
KEGGdme:Dmel_CG7908.
UCSCCG7908-RA. d. melanogaster.

Organism-specific databases

CTD43558.
FlyBaseFBgn0039734. Tace.

Phylogenomic databases

eggNOGNOG269976.
GeneTreeENSGT00530000063304.
InParanoidQ9VAC5.
KOK06059.
OMAYHIEPSW.
OrthoDBEOG4Z613K.
PhylomeDBQ9VAC5.

Gene expression databases

BgeeQ9VAC5.
GermOnlineCG7908. Drosophila melanogaster.

Family and domain databases

Gene3DG3DSA:4.10.70.10. Blood-coag_inhib_Disintegrin. 1 hit.
G3DSA:3.40.390.10. G3DSA:3.40.390.10. 1 hit.
InterProIPR001762. Blood-coag_inhib_Disintegrin.
IPR024079. MetalloPept_cat_dom.
IPR001590. Peptidase_M12B.
IPR002870. Peptidase_M12B_N.
[Graphical view]
PfamPF00200. Disintegrin. 1 hit.
PF01562. Pep_M12B_propep. 1 hit.
[Graphical view]
SMARTSM00050. DISIN. 1 hit.
[Graphical view]
SUPFAMSSF57552. Disintegrin. 1 hit.
PROSITEPS50215. ADAM_MEPRO. 1 hit.
PS00427. DISINTEGRIN_1. False negative.
PS50214. DISINTEGRIN_2. 1 hit.
PS00142. ZINC_PROTEASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio834538.

Entry information

Entry nameADA17_DROME
AccessionPrimary (citable) accession number: Q9VAC5
Secondary accession number(s): Q868A7, Q8IMJ9, Q95RZ4
Entry history
Integrated into UniProtKB/Swiss-Prot: June 20, 2001
Last sequence update: October 10, 2003
Last modified: April 18, 2012
This is version 96 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programDrosophila annotation project

Relevant documents

Recent format changes

Overview of recent format changes

Peptidase families

Classification of peptidase families and list of entries

Drosophila

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

SIMILARITY comments

Index of protein domains and families

to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents