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Q9Z0F8

- ADA17_MOUSE

UniProt

Q9Z0F8 - ADA17_MOUSE

Protein

Disintegrin and metalloproteinase domain-containing protein 17

Gene

Adam17

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 142 (01 Oct 2014)
      Sequence version 3 (27 Jul 2011)
      Previous versions | rss
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    Functioni

    Cleaves the membrane-bound precursor of TNF-alpha to its mature soluble form. Responsible for the proteolytical release of soluble JAM3 from endothelial cells surface. Plays a role in the proteolytic processing of ACE2 By similarity. Responsible for the proteolytic release of several other cell-surface proteins, including p75 TNF-receptor, interleukin 1 receptor type II, p55 TNF-receptor, transforming growth factor-alpha, L-selectin, growth hormone receptor, MUC1 and the amyloid precursor protein. Acts as an activator of Notch pathway by mediating cleavage of Notch, generating the membrane-associated intermediate fragment called notch extracellular truncation (NEXT).By similarity3 Publications

    Catalytic activityi

    Narrow endopeptidase specificity. Cleaves Pro-Leu-Ala-Gln-Ala-|-Val-Arg-Ser-Ser-Ser in the membrane-bound, 26-kDa form of tumor necrosis factor alpha (TNF-alpha). Similarly cleaves other membrane-anchored, cell-surface proteins to 'shed' the extracellular domains.

    Cofactori

    Binds 1 zinc ion per subunit.By similarity

    Enzyme regulationi

    Inhibited by metalloproteinase inhibitor 3 (TIMP-3), but not by TIMP-1, TIMP-2 and TIMP-4.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi184 – 1841Zinc; in inhibited formBy similarity
    Metal bindingi405 – 4051Zinc; catalyticBy similarity
    Active sitei406 – 4061PROSITE-ProRule annotation
    Metal bindingi409 – 4091Zinc; catalyticBy similarity
    Metal bindingi415 – 4151Zinc; catalyticBy similarity

    GO - Molecular functioni

    1. metalloendopeptidase activity Source: Reactome
    2. metallopeptidase activity Source: BHF-UCL
    3. Notch binding Source: UniProtKB
    4. protein binding Source: MGI
    5. zinc ion binding Source: InterPro

    GO - Biological processi

    1. B cell differentiation Source: BHF-UCL
    2. cell adhesion mediated by integrin Source: Ensembl
    3. cell motility Source: BHF-UCL
    4. epidermal growth factor-activated receptor transactivation by G-protein coupled receptor signaling pathway Source: Ensembl
    5. epidermal growth factor receptor signaling pathway Source: Ensembl
    6. germinal center formation Source: BHF-UCL
    7. membrane protein ectodomain proteolysis Source: BHF-UCL
    8. negative regulation of interleukin-8 production Source: Ensembl
    9. Notch receptor processing Source: UniProtKB
    10. Notch signaling pathway Source: UniProtKB-KW
    11. PMA-inducible membrane protein ectodomain proteolysis Source: BHF-UCL
    12. positive regulation of cell growth Source: Ensembl
    13. positive regulation of cell proliferation Source: Ensembl
    14. positive regulation of cellular component movement Source: BHF-UCL
    15. positive regulation of chemokine production Source: Ensembl
    16. positive regulation of cyclin-dependent protein serine/threonine kinase activity involved in G1/S transition of mitotic cell cycle Source: Ensembl
    17. positive regulation of T cell chemotaxis Source: Ensembl
    18. positive regulation of transforming growth factor beta receptor signaling pathway Source: BHF-UCL
    19. proteolysis Source: UniProtKB
    20. regulation of mast cell apoptotic process Source: BHF-UCL
    21. response to drug Source: BHF-UCL
    22. response to high density lipoprotein particle Source: Ensembl
    23. response to hypoxia Source: Ensembl
    24. response to lipopolysaccharide Source: Ensembl
    25. spleen development Source: BHF-UCL
    26. T cell differentiation in thymus Source: BHF-UCL
    27. wound healing, spreading of epidermal cells Source: Ensembl

    Keywords - Molecular functioni

    Hydrolase, Metalloprotease, Protease

    Keywords - Biological processi

    Notch signaling pathway

    Keywords - Ligandi

    Metal-binding, Zinc

    Enzyme and pathway databases

    ReactomeiREACT_198574. Nuclear signaling by ERBB4.
    REACT_198614. Growth hormone receptor signaling.
    REACT_199055. Collagen degradation.
    REACT_218614. Regulated proteolysis of p75NTR.

    Protein family/group databases

    MEROPSiM12.217.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Disintegrin and metalloproteinase domain-containing protein 17 (EC:3.4.24.86)
    Short name:
    ADAM 17
    Alternative name(s):
    TNF-alpha convertase
    TNF-alpha-converting enzyme
    CD_antigen: CD156b
    Gene namesi
    Name:Adam17
    Synonyms:Tace
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 12

    Organism-specific databases

    MGIiMGI:1096335. Adam17.

    Subcellular locationi

    GO - Cellular componenti

    1. actin cytoskeleton Source: Ensembl
    2. apical plasma membrane Source: Ensembl
    3. cell-cell junction Source: Ensembl
    4. cell surface Source: Ensembl
    5. cytoplasm Source: MGI
    6. extracellular region Source: Reactome
    7. focal adhesion Source: Ensembl
    8. integral component of plasma membrane Source: Ensembl
    9. membrane raft Source: Ensembl
    10. plasma membrane Source: Reactome
    11. ruffle membrane Source: Ensembl

    Keywords - Cellular componenti

    Cell membrane, Membrane, Secreted

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 1717Sequence AnalysisAdd
    BLAST
    Propeptidei18 – 214197By similarityPRO_0000029090Add
    BLAST
    Chaini215 – 827613Disintegrin and metalloproteinase domain-containing protein 17PRO_0000029091Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi157 – 1571N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi225 ↔ 333By similarity
    Glycosylationi264 – 2641N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi365 ↔ 469By similarity
    Disulfide bondi423 ↔ 453By similarity
    Glycosylationi452 – 4521N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi498 – 4981N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi534 ↔ 555By similarity
    Glycosylationi539 – 5391N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi551 – 5511N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi573 ↔ 582By similarity
    Disulfide bondi578 ↔ 591By similarity
    Disulfide bondi593 ↔ 600By similarity
    Glycosylationi606 – 6061N-linked (GlcNAc...)Sequence Analysis
    Modified residuei735 – 7351Phosphothreonine; by MAPK14By similarity
    Modified residuei794 – 7941Phosphoserine1 Publication
    Modified residuei822 – 8221PhosphoserineBy similarity

    Post-translational modificationi

    The precursor is cleaved by a furin endopeptidase.By similarity
    Phosphorylated. Stimulation by growth factor or phorbol 12-myristate 13-acetate induces phosphorylation of Ser-822 but decreases phosphorylation of Ser-794. Phosphorylation at THR-735 by MAPK14 is required for ADAM17-mediated ectodomain shedding By similarity.By similarity

    Keywords - PTMi

    Cleavage on pair of basic residues, Disulfide bond, Glycoprotein, Phosphoprotein, Zymogen

    Proteomic databases

    MaxQBiQ9Z0F8.
    PaxDbiQ9Z0F8.
    PRIDEiQ9Z0F8.

    PTM databases

    PhosphoSiteiQ9Z0F8.

    Miscellaneous databases

    PMAP-CutDBQ505A7.

    Expressioni

    Tissue specificityi

    Ubiquitously expressed. Expressed at highest levels in heart, liver, skeletal muscle, kidney and testes. Expressed at lower levels in brain, spleen and lung.

    Gene expression databases

    ArrayExpressiQ9Z0F8.
    BgeeiQ9Z0F8.
    CleanExiMM_ADAM17.
    GenevestigatoriQ9Z0F8.

    Interactioni

    Subunit structurei

    Interacts with MAD2L1, MAPK14 and MUC1.By similarity

    Protein-protein interaction databases

    IntActiQ9Z0F8. 2 interactions.
    MINTiMINT-246289.

    Structurei

    3D structure databases

    ProteinModelPortaliQ9Z0F8.
    SMRiQ9Z0F8. Positions 220-642.
    ModBaseiSearch...
    MobiDBiSearch...

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini215 – 671457ExtracellularSequence AnalysisAdd
    BLAST
    Topological domaini693 – 827135CytoplasmicSequence AnalysisAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei672 – 69221HelicalSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini223 – 474252Peptidase M12BPROSITE-ProRule annotationAdd
    BLAST
    Domaini475 – 56389DisintegrinPROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni603 – 67169Crambin-likeAdd
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi182 – 1898Cysteine switchBy similarity
    Motifi731 – 7388SH3-bindingSequence Analysis

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi96 – 994Poly-Val
    Compositional biasi564 – 60239Cys-richAdd
    BLAST

    Domaini

    Must be membrane anchored to cleave the different substrates. The cytoplasmic domain is not required for the this activity. Only the catalytic domain is essential to shed TNF and p75 TNFR.
    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 similaritiesi

    Contains 1 disintegrin domain.PROSITE-ProRule annotation
    Contains 1 peptidase M12B domain.PROSITE-ProRule annotation

    Keywords - Domaini

    SH3-binding, Signal, Transmembrane, Transmembrane helix

    Phylogenomic databases

    eggNOGiNOG269976.
    GeneTreeiENSGT00670000097974.
    HOGENOMiHOG000033797.
    HOVERGENiHBG050457.
    KOiK06059.
    TreeFamiTF314733.

    Family and domain databases

    Gene3Di3.40.390.10. 1 hit.
    4.10.70.10. 1 hit.
    InterProiIPR001762. Blood-coag_inhib_Disintegrin.
    IPR024079. MetalloPept_cat_dom.
    IPR001590. Peptidase_M12B.
    IPR002870. Peptidase_M12B_N.
    [Graphical view]
    PfamiPF00200. Disintegrin. 1 hit.
    PF01562. Pep_M12B_propep. 1 hit.
    [Graphical view]
    SMARTiSM00050. DISIN. 1 hit.
    [Graphical view]
    SUPFAMiSSF57552. SSF57552. 1 hit.
    PROSITEiPS50215. ADAM_MEPRO. 1 hit.
    PS50214. DISINTEGRIN_2. 1 hit.
    PS00142. ZINC_PROTEASE. 1 hit.
    [Graphical view]

    Sequences (2)i

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform Long (identifier: Q9Z0F8-1) [UniParc]FASTAAdd to Basket

    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.

    « Hide

    MRRRLLILTT LVPFVLAPRP PEEAGSGSHP RLEKLDSLLS DYDILSLANI    50
    QQHSIRKRDL QSATHLETLL TFSALKRHFK LYLTSSTERF SQNLRVVVVD 100
    GKEESEYSVK WQNFFSGHVV GEPDSRVLAH IGDDDVTVRI NTDGAEYNVE 150
    PLWRFVNDTK DKRMLVYKSE DIKDFSRLQS PKVCGYLNAD SEELLPKGLI 200
    DREPSEEFVR RVKRRAEPNP LKNTCKLLVV ADHRFYKYMG RGEESTTTNY 250
    LIELIDRVDD IYRNTSWDNA GFKGYGVQIE QIRILKSPQE VKPGERHFNM 300
    AKSFPNEEKD AWDVKMLLEQ FSFDIAEEAS KVCLAHLFTY QDFDMGTLGL 350
    AYVGSPRANS HGGVCPKAYY NPTVKKNIYL NSGLTSTKNY GKTILTKEAD 400
    LVTTHELGHN FGAEHDPDGL AECAPNEDQG GKYVMYPIAV SGDHENNKMF 450
    SNCSKQSIYK TIESKAQECF QERSNKVCGN SRVDEGEECD PGIMYLNNDT 500
    CCNSDCTLKP GVQCSDRNSP CCKNCQFETA QKKCQEAINA TCKGVSYCTG 550
    NSSECPPPGD AEDDTVCLDL GKCKAGKCIP FCKREQELES CACVDTDNSC 600
    KVCCRNLSGP CVPYVDAEQK NLFLRKGKPC TVGFCDMNGK CEKRVQDVIE 650
    RFWDFIDQLS INTFGKFLAD NIVGSVLVFS LIFWIPFSIL VHCVDKKLDK 700
    QYESLSLFHH SNIEMLSSMD SASVRIIKPF PAPQTPGRLQ ALQPAAMMPP 750
    VPAAPKLDHQ RMDTIQEDPS TDSHADDDGF EKDPFPNSST AAKSFEDLTD 800
    HPVTRSEKAA SFKLQRQSRV DSKETEC 827
    Length:827
    Mass (Da):93,056
    Last modified:July 27, 2011 - v3
    Checksum:i6B434F80878197F5
    GO
    Isoform Short (identifier: Q9Z0F8-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         639-655: GKCEKRVQDVIERFWDF → CDFFSPYRANVRNEYRT
         656-827: Missing.

    Show »
    Length:655
    Mass (Da):73,884
    Checksum:i9F4B11FD8D99DDF8
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti3 – 42RR → QS in CAA07480. (PubMed:9755855)Curated
    Sequence conflicti7 – 71I → F in CAA07480. (PubMed:9755855)Curated
    Sequence conflicti28 – 281S → A in CAA07480. (PubMed:9755855)Curated
    Sequence conflicti28 – 281S → A in BAA78578. (PubMed:10375622)Curated
    Sequence conflicti113 – 1131N → D in AAC62934. (PubMed:10433800)Curated
    Sequence conflicti113 – 1131N → D in CAA07480. (PubMed:9755855)Curated
    Sequence conflicti113 – 1131N → D in BAA78578. (PubMed:10375622)Curated
    Sequence conflicti113 – 1131N → D in AAD09627. 1 PublicationCurated
    Sequence conflicti113 – 1131N → D in AAD09628. 1 PublicationCurated
    Sequence conflicti149 – 1491V → I in CAA07480. (PubMed:9755855)Curated
    Sequence conflicti149 – 1491V → I in BAA78578. (PubMed:10375622)Curated
    Sequence conflicti594 – 5941V → I in AAC62934. (PubMed:10433800)Curated
    Sequence conflicti594 – 5941V → I in AAD09627. 1 PublicationCurated
    Sequence conflicti594 – 5941V → I in AAD09628. 1 PublicationCurated
    Sequence conflicti752 – 7521P → S in CAA07480. (PubMed:9755855)Curated
    Sequence conflicti752 – 7521P → S in BAA78578. (PubMed:10375622)Curated
    Sequence conflicti775 – 7751A → V in CAA07480. (PubMed:9755855)Curated
    Sequence conflicti775 – 7751A → V in BAA78578. (PubMed:10375622)Curated

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei639 – 65517GKCEK…RFWDF → CDFFSPYRANVRNEYRT in isoform Short. 1 PublicationVSP_005479Add
    BLAST
    Alternative sequencei656 – 827172Missing in isoform Short. 1 PublicationVSP_005480Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF056359
    , AF056345, AF056346, AF056347, AF056348, AF056349, AF056350, AF056351, AF056352, AF056353, AF056354, AF056355, AF056356, AF056357, AF056358 Genomic DNA. Translation: AAC62934.1.
    AJ007365 mRNA. Translation: CAA07480.1.
    AB021709 mRNA. Translation: BAA78578.1.
    U69613 mRNA. Translation: AAD09627.1.
    U69614 mRNA. Translation: AAD09628.1.
    AK139471 mRNA. Translation: BAE24023.1.
    BC094655 mRNA. Translation: AAH94655.1.
    CCDSiCCDS25836.1. [Q9Z0F8-1]
    RefSeqiNP_001264195.1. NM_001277266.1.
    NP_001278800.1. NM_001291871.1.
    NP_033745.4. NM_009615.6. [Q9Z0F8-1]
    UniGeneiMm.27681.

    Genome annotation databases

    EnsembliENSMUST00000064536; ENSMUSP00000067953; ENSMUSG00000052593. [Q9Z0F8-1]
    ENSMUST00000145118; ENSMUSP00000136407; ENSMUSG00000052593. [Q9Z0F8-2]
    GeneIDi11491.
    KEGGimmu:11491.
    UCSCiuc007ndu.1. mouse. [Q9Z0F8-1]

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF056359
    , AF056345 , AF056346 , AF056347 , AF056348 , AF056349 , AF056350 , AF056351 , AF056352 , AF056353 , AF056354 , AF056355 , AF056356 , AF056357 , AF056358 Genomic DNA. Translation: AAC62934.1 .
    AJ007365 mRNA. Translation: CAA07480.1 .
    AB021709 mRNA. Translation: BAA78578.1 .
    U69613 mRNA. Translation: AAD09627.1 .
    U69614 mRNA. Translation: AAD09628.1 .
    AK139471 mRNA. Translation: BAE24023.1 .
    BC094655 mRNA. Translation: AAH94655.1 .
    CCDSi CCDS25836.1. [Q9Z0F8-1 ]
    RefSeqi NP_001264195.1. NM_001277266.1.
    NP_001278800.1. NM_001291871.1.
    NP_033745.4. NM_009615.6. [Q9Z0F8-1 ]
    UniGenei Mm.27681.

    3D structure databases

    ProteinModelPortali Q9Z0F8.
    SMRi Q9Z0F8. Positions 220-642.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    IntActi Q9Z0F8. 2 interactions.
    MINTi MINT-246289.

    Chemistry

    BindingDBi Q9Z0F8.
    ChEMBLi CHEMBL4379.

    Protein family/group databases

    MEROPSi M12.217.

    PTM databases

    PhosphoSitei Q9Z0F8.

    Proteomic databases

    MaxQBi Q9Z0F8.
    PaxDbi Q9Z0F8.
    PRIDEi Q9Z0F8.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000064536 ; ENSMUSP00000067953 ; ENSMUSG00000052593 . [Q9Z0F8-1 ]
    ENSMUST00000145118 ; ENSMUSP00000136407 ; ENSMUSG00000052593 . [Q9Z0F8-2 ]
    GeneIDi 11491.
    KEGGi mmu:11491.
    UCSCi uc007ndu.1. mouse. [Q9Z0F8-1 ]

    Organism-specific databases

    CTDi 6868.
    MGIi MGI:1096335. Adam17.

    Phylogenomic databases

    eggNOGi NOG269976.
    GeneTreei ENSGT00670000097974.
    HOGENOMi HOG000033797.
    HOVERGENi HBG050457.
    KOi K06059.
    TreeFami TF314733.

    Enzyme and pathway databases

    Reactomei REACT_198574. Nuclear signaling by ERBB4.
    REACT_198614. Growth hormone receptor signaling.
    REACT_199055. Collagen degradation.
    REACT_218614. Regulated proteolysis of p75NTR.

    Miscellaneous databases

    NextBioi 278866.
    PMAP-CutDB Q505A7.
    PROi Q9Z0F8.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q9Z0F8.
    Bgeei Q9Z0F8.
    CleanExi MM_ADAM17.
    Genevestigatori Q9Z0F8.

    Family and domain databases

    Gene3Di 3.40.390.10. 1 hit.
    4.10.70.10. 1 hit.
    InterProi IPR001762. Blood-coag_inhib_Disintegrin.
    IPR024079. MetalloPept_cat_dom.
    IPR001590. Peptidase_M12B.
    IPR002870. Peptidase_M12B_N.
    [Graphical view ]
    Pfami PF00200. Disintegrin. 1 hit.
    PF01562. Pep_M12B_propep. 1 hit.
    [Graphical view ]
    SMARTi SM00050. DISIN. 1 hit.
    [Graphical view ]
    SUPFAMi SSF57552. SSF57552. 1 hit.
    PROSITEi PS50215. ADAM_MEPRO. 1 hit.
    PS50214. DISINTEGRIN_2. 1 hit.
    PS00142. ZINC_PROTEASE. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Characterization of the cDNA and gene for mouse tumour necrosis factor alpha converting enzyme (TACE/ADAM17) and its location to mouse chromosome 12 and human chromosome 2p25."
      Cerretti D.P., Poindexter K., Castner B.J., Means G., Copeland N.G., Gilbert D.J., Jenkins N.A., Black R.A., Nelson N.
      Cytokine 11:541-551(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORMS LONG AND SHORT).
    2. Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM LONG).
    3. "cDNA cloning of mouse tumor necrosis factor-alpha converting enzyme (TACE) and partial analysis of its promoter."
      Mizui Y., Yamazaki K., Sagane K., Tanaka I.
      Gene 233:67-74(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM LONG).
    4. "Isolation of murine TNF-alpha converting enzyme."
      Cerretti D.P.
      Submitted (SEP-1996) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM SHORT).
    5. "The transcriptional landscape of the mammalian genome."
      Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
      , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
      Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM LONG).
      Strain: C57BL/6J.
      Tissue: Brain cortex.
    6. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
      The MGC Project Team
      Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM LONG).
      Strain: C57BL/6.
      Tissue: Brain.
    7. "Tumor necrosis factor-alpha converting enzyme (TACE) is a growth hormone binding protein (GHBP) sheddase: the metalloprotease TACE/ADAM-17 is critical for (PMA-induced) GH receptor proteolysis and GHBP generation."
      Zhang Y., Jiang J., Black R.A., Baumann G., Frank S.J.
      Endocrinology 141:4342-4348(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN PROCESSING OF GROWTH HORMONE RECEPTOR.
    8. "Functional analysis of the domain structure of tumor necrosis factor-alpha converting enzyme."
      Reddy P., Slack J.L., Davis R., Cerretti D.P., Kozlosky C.J., Blanton R.A., Shows D., Peschon J.J., Black R.A.
      J. Biol. Chem. 275:14608-14614(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    9. "A novel proteolytic cleavage involved in Notch signaling: the role of the disintegrin-metalloprotease TACE."
      Brou C., Logeat F., Gupta N., Bessia C., LeBail O., Doedens J.R., Cumano A., Roux P., Black R.A., Israel A.
      Mol. Cell 5:207-216(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    10. "The phagosomal proteome in interferon-gamma-activated macrophages."
      Trost M., English L., Lemieux S., Courcelles M., Desjardins M., Thibault P.
      Immunity 30:143-154(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-794, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

    Entry informationi

    Entry nameiADA17_MOUSE
    AccessioniPrimary (citable) accession number: Q9Z0F8
    Secondary accession number(s): O88726
    , Q505A7, Q9R1U4, Q9Z0K3
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: June 20, 2001
    Last sequence update: July 27, 2011
    Last modified: October 1, 2014
    This is version 142 of the entry and version 3 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. MGD cross-references
      Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
    2. Peptidase families
      Classification of peptidase families and list of entries
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3