ExPASy logo ExPASy Home page Site Map Search ExPASy Contact us Swiss-Prot
Notice: This page will be replaced with beta.uniprot.org. Please send us your feedback!
Search for

UniProtKB/Swiss-Prot entry Q9VAC5


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

Note: most headings are clickable, even if they don't appear as links. They link to the user manual or other documents.
Entry information
Entry name ADA17_DROME
Primary accession number Q9VAC5
Secondary accession numbers Q868A7 Q8IMJ9 Q95RZ4
Integrated into Swiss-Prot on June 20, 2001
Sequence was last modified on October 10, 2003 (Sequence version 2)
Annotations were last modified on    April 29, 2008 (Entry version 63)
Name and origin of the protein
Protein name ADAM 17-like protease [Precursor]
Synonym EC 3.4.24.-
Gene name
Name: Tace
ORFNames: CG7908
From
Drosophila melanogaster (Fruit fly) [TaxID: 7227] 
Taxonomy Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea; Drosophilidae; Drosophila; Sophophora.
Protein existence 2: Evidence at transcript level;
References
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM A).
TISSUE=Embryo;
Wei S., Brew K.;
Submitted (JAN-2003) to the EMBL/GenBank/DDBJ databases.
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM A).
Sapir A., Tsruya R., Shilo B.-Z.;
"Asymmetric notch signaling depends on constitutive cleavage of delta.";
Submitted (JAN-2004) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=Berkeley;
DOI=10.1126/science.287.5461.2185; PubMed=10731132 [NCBI, ExPASy, EBI, Israel, Japan]
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.;
"The genome sequence of Drosophila melanogaster.";
Science 287:2185-2195(2000).
[4]
GENOME REANNOTATION, AND ALTERNATIVE SPLICING.
PubMed=12537572 [NCBI, ExPASy, EBI, Israel, Japan]
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., 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.;
"Annotation of the Drosophila melanogaster euchromatic genome: a systematic review.";
Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS A AND B).
STRAIN=Berkeley;
TISSUE=Embryo, and Head;
PubMed=12537569 [NCBI, ExPASy, EBI, Israel, Japan]
Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M., Celniker S.E.;
"A Drosophila full-length cDNA resource.";
Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002).
Comments
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
AY212802; AAO53296.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AY525768; AAS48650.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AE014297; AAN14205.2; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AE014297; AAF56986.2; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AY061030; AAL28578.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BT003184; AAO24939.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
RefSeq NP_651759.3; -.
NP_733334.1; -.
UniGene Dm.6531
3D structure databases
HSSP P78536; 1BKC. [HSSP ENTRY / PDB]
ModBase Q9VAC5.
Protein family/group databases
MEROPS M12.217; -.
Enzyme and pathway databases
BioCyc DMEL-XXX-02:DMEL-XXX-02-014082-MON; -.
Organism-specific databases
FlyBase FBgn0039734; Tace.
Gene expression databases
ArrayExpress Q9VAC5; -.
GermOnline CG7908; Drosophila melanogaster.
Family and domain databases
InterPro IPR001762; Blood-coag_inhib_Disintegrin.
IPR013032; EGF_like_reg_CS.
IPR006025; Pept_M_Zn_BS.
IPR001590; Peptidase_M12B.
Graphical view of domain structure.
Gene3D G3DSA:4.10.70.10; Blood-coag_inhib_Disintegrin; 1.
Pfam PF00200; Disintegrin; 1.
PF01421; Reprolysin; 1.
Pfam graphical view of domain structure.
ProDom PD000664; Disintegrin; 1.
[Domain structure / List of seq. sharing at least 1 domain]
SMART SM00050; DISIN; 1.
SMART graphical view of domain structure.
PROSITE PS50215; ADAM_MEPRO; 1.
PS00427; DISINTEGRIN_1; FALSE_NEG.
PS50214; DISINTEGRIN_2; 1.
PS00142; ZINC_PROTEASE; 1.
PROSITE graphical view of domain structure (profiles).
BLOCKS Q9VAC5.
Genome annotation databases
Ensembl CG7908; Drosophila melanogaster. [Contig view]
GeneID 43558; -.
KEGG dme:Dmel_CG7908; -.
NMPDR fig|7227.3.peg.15353; -.
Other
ProtoNet Q9VAC5.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Alternative splicing; Cleavage on pair of basic residues; Complete proteome; Glycoprotein; Hydrolase; Membrane; Metal-binding; Metalloprotease; Protease; Signal; Transmembrane; Zinc; Zymogen.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom   To Length Description FTId
SIGNAL   1    28  28     Potential. 
PROPEP   29   211  183     By similarity. PRO_0000029094
CHAIN   212   732  521     ADAM 17-like protease. PRO_0000029095
TOPO_DOM   212   662  451     Extracellular (Potential). 
TRANSMEM   663   683  21     Potential. 
TOPO_DOM   684   732  49     Cytoplasmic (Potential). 
DOMAIN   223   467  245     Peptidase M12B. 
DOMAIN   468   559  92     Disintegrin. 
REGION   598   662  65     Crambin-like. 
MOTIF   181   188  8     Cysteine switch (By similarity). 
COMPBIAS   560   599  40     Cys-rich. 
ACT_SITE   400   400        By similarity. 
METAL   183   183        Zinc (in inhibited form) (By similarity). 
METAL   399   399        Zinc (catalytic) (By similarity). 
METAL   403   403        Zinc (catalytic) (By similarity). 
METAL   409   409        Zinc (catalytic) (By similarity). 
CARBOHYD   100   100        N-linked (GlcNAc...) (Potential). 
CARBOHYD   263   263        N-linked (GlcNAc...) (Potential). 
CARBOHYD   492   492        N-linked (GlcNAc...) (Potential). 
CARBOHYD   604   604        N-linked (GlcNAc...) (Potential). 
DISULFID   225   328        By similarity. 
DISULFID   360   462        By similarity. 
DISULFID   416   446        By similarity. 
DISULFID   530   551        By similarity. 
DISULFID   569   578        By similarity. 
DISULFID   574   586        By similarity. 
DISULFID   588   595        By similarity. 
VAR_SEQ   1   427        Missing (in isoform B). VSP_008515
CONFLICT   208   208        R -> K (in Ref. 2; AAS48650). 
CONFLICT   428   431        MYTY -> IHT (in Ref. 2; AAS48650). 
CONFLICT   449   449        R -> A (in Ref. 2; AAS48650). 
CONFLICT   463   463        F -> L (in Ref. 5; AAL28578). 
CONFLICT   554   554        S -> F (in Ref. 2; AAS48650). 
Sequence information
Length: 732 AA [This is the length of the unprocessed precursor] Molecular weight: 83081 Da [This is the MW of the unprocessed precursor] CRC64: 0E96E7B30F973A0B [This is a checksum on the sequence]
        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 

Q9VAC5 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

BLAST logo BLAST submission on ExPASy/SIB
or at NCBI (USA)
Tools Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
PROSITE logo ScanProsite, MotifScan SWISS-MODEL Submit a homology modeling request to SWISS-MODEL
NPSA logo NPSA Sequence analysis tools

ExPASy logo ExPASy Home page Site Map Search ExPASy Contact us Swiss-Prot
 Hosted by ch flag SIB Switzerland Mirror sites: Australia  Brazil  Canada  China  Korea
Notice: This page will be replaced with beta.uniprot.org. Please send us your feedback!