Reviewed, UniProtKB/Swiss-Prot Q9VAC5 (ADA17_DROME)

Names and origin

Protein names

Recommended name:
    ADAM 17-like protease
    EC=3.4.24.-

Gene names

Name:	Tace
ORF Names:	CG7908

Organism

Drosophila melanogaster (Fruit fly) [Complete proteome]

Taxonomic identifier

7227 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Arthropoda › Hexapoda › Insecta › Pterygota › Neoptera › Endopterygota › Diptera › Brachycera › Muscomorpha › Ephydroidea › Drosophilidae › Drosophila › Sophophora

Protein attributes

Sequence length	732 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at transcript level.

General annotation (Comments)

Cofactor	Binds 1 zinc ion per subunit By similarity.
Subcellular location	Membrane; Single-pass type I membrane proteinPotential.
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.

Ontologies

Keywords
Cellular component	Membrane
Coding sequence diversity	Alternative splicing
Domain	Signal Transmembrane
Ligand	Metal-binding Zinc
Molecular function	Hydrolase Metalloprotease Protease
PTM	Cleavage on pair of basic residues Glycoprotein Zymogen
Technical term	Complete proteome
Gene Ontology (GO)
None. [Check GOA]

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:
     1-427: Missing.

Notes: No experimental confirmation available.

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view
Molecule processing
	Signal peptide	1 – 28	28	Potential
	Propeptide	29 – 211	183	By similarity
	Chain	212 – 732	521	ADAM 17-like protease
Regions
	Topological domain	212 – 662	451	Extracellular Potential
	Transmembrane	663 – 683	21	Potential
	Topological domain	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
	Compositional bias	560 – 599	40	Cys-rich
Sites
	Active site	400	1	By similarity
	Metal binding	183	1	Zinc; in inhibited form By similarity
	Metal binding	399	1	Zinc; catalytic By similarity
	Metal binding	403	1	Zinc; catalytic By similarity
	Metal binding	409	1	Zinc; catalytic By similarity
Amino acid modifications
	Glycosylation	100	1	N-linked (GlcNAc...) Potential
	Glycosylation	263	1	N-linked (GlcNAc...) Potential
	Glycosylation	492	1	N-linked (GlcNAc...) Potential
	Glycosylation	604	1	N-linked (GlcNAc...) Potential
	Disulfide bond	225 ↔ 328		By similarity
	Disulfide bond	360 ↔ 462		By similarity
	Disulfide bond	416 ↔ 446		By similarity
	Disulfide bond	530 ↔ 551		By similarity
	Disulfide bond	569 ↔ 578		By similarity
	Disulfide bond	574 ↔ 586		By similarity
	Disulfide bond	588 ↔ 595		By similarity
Natural variations
	Alternative sequence	1 – 427	427	Missing in isoform B.
Experimental info
	Sequence conflict	208	1	R → K in AAS48650. Ref.2
	Sequence conflict	428 – 431	4	MYTY → IHT in AAS48650. Ref.2
	Sequence conflict	449	1	R → A in AAS48650. Ref.2
	Sequence conflict	463	1	F → L in AAL28578. Ref.5
	Sequence conflict	554	1	S → F in AAS48650. Ref.2

Sequences

	Sequence		Length	Mass (Da)
	Isoform A [UniParc]. Last modified October 10, 2003. Version 2. Checksum: 0E96E7B30F973A0B	FASTA	732	83,081
	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
	Isoform B [UniParc]. Checksum: D1D45B94568DC83E		305	34,350
	10 20 30 40 50 60 MYTYSVSGYD VNNKKFSPCS LRSIRKVLQA KSGRCFSEPE ESFCGNLRVE GDEQCDAGLL 70 80 90 100 110 120 GTEDNDSCCD KNCKLRRNQG AMCSDKNSPC CQNCQFMASG MKCREAQYAT CEQEARCTGA 130 140 150 160 170 180 HAECPKSPAM ADGTTCQERG QCRNGKCVPY CETQGLQSCM CDIIADACKR CCRMSINETC 190 200 210 220 230 240 FPVEPPDVLP DGTPCITGFC NKGVCEKTIQ DVVERFWDII EEINVAKTLR FLKDNIVMAV 250 260 270 280 290 300 VLVTAVFWIP ISCVISYFDR KKLRHEMKLI EWSQKLDLIH PSDERRRVIH IRVPRQKISV ARACN

References

	« Hide 'large scale' referencesShow '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).
[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: 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. , 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.
[5]	"A Drosophila full-length cDNA resource." 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. Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002) [PubMed: 12537569] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS A AND B). Strain: Berkeley. Tissue: Embryo and Head.

Cross-references

Sequence databases
EMBLGenBankDDBJ	AY212802 mRNA. Translation: AAO53296.1. AY525768 mRNA. Translation: AAS48650.1. AE014297 Genomic DNA. Translation: AAN14205.2. AE014297 Genomic DNA. Translation: AAF56986.2. AY061030 mRNA. Translation: AAL28578.1. BT003184 mRNA. Translation: AAO24939.1.
RefSeq	NP_651759.3. NP_733334.1.
UniGene	Dm.6531
3D structure databases
HSSP	HSSP built from PDB template 1BKC based on UniProtKB P78536.
ModBase	Search...
Protein family/group databases
MEROPS	M12.217.
Genome annotation databases
Ensembl	CG7908. Drosophila melanogaster. [Contig view]
GeneID	43558.
KEGG	dme:Dmel_CG7908.
NMPDR	fig|7227.3.peg.15353.
Organism-specific databases
FlyBase	FBgn0039734. Tace.
Phylogenomic databases
HOGENOM	Q9VAC5.
Enzyme and pathway databases
BioCyc	DMEL-XXX-02:DMEL-XXX-02-014082-MON.
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]
Gene3D	G3DSA:4.10.70.10. Blood-coag_inhib_Disintegrin. 1 hit.
Pfam	PF00200. Disintegrin. 1 hit. PF01421. Reprolysin. 1 hit. [Graphical view]
ProDom	PD000664. Disintegrin. 1 hit. [Graphical view] [Entries sharing at least one domain]
SMART	SM00050. DISIN. 1 hit. [Graphical view]
PROSITE	PS50215. ADAM_MEPRO. 1 hit. PS00427. DISINTEGRIN_1. False negative. PS50214. DISINTEGRIN_2. 1 hit. PS00142. ZINC_PROTEASE. 1 hit. [Graphical view]
BLOCKS	Search...
Other Resources
ProtoNet	Search...

Entry information

Entry name

ADA17_DROME

Accession

Primary (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:	September 2, 2008
This is version 66 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

Drosophila annotation project