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Q9Z0F8

- ADA17_MOUSE

UniProt

Q9Z0F8 - ADA17_MOUSE

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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

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. 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. negative regulation of transforming growth factor beta receptor signaling pathway Source: Ensembl
  10. Notch receptor processing Source: UniProtKB
  11. Notch signaling pathway Source: UniProtKB-KW
  12. PMA-inducible membrane protein ectodomain proteolysis Source: BHF-UCL
  13. positive regulation of cell growth Source: Ensembl
  14. positive regulation of cell proliferation Source: Ensembl
  15. positive regulation of cellular component movement Source: BHF-UCL
  16. positive regulation of chemokine production Source: Ensembl
  17. positive regulation of cyclin-dependent protein serine/threonine kinase activity involved in G1/S transition of mitotic cell cycle Source: Ensembl
  18. positive regulation of T cell chemotaxis Source: Ensembl
  19. positive regulation of transforming growth factor beta receptor signaling pathway Source: BHF-UCL
  20. proteolysis Source: UniProtKB
  21. regulation of mast cell apoptotic process Source: BHF-UCL
  22. response to drug Source: BHF-UCL
  23. response to high density lipoprotein particle Source: Ensembl
  24. response to hypoxia Source: Ensembl
  25. response to lipopolysaccharide Source: Ensembl
  26. spleen development Source: BHF-UCL
  27. T cell differentiation in thymus Source: BHF-UCL
  28. wound healing, spreading of epidermal cells Source: Ensembl
Complete GO annotation...

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
Complete GO annotation...

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

BgeeiQ9Z0F8.
CleanExiMM_ADAM17.
ExpressionAtlasiQ9Z0F8. baseline and differential.
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.
InParanoidiQ9Z0F8.
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

        10         20         30         40         50
MRRRLLILTT LVPFVLAPRP PEEAGSGSHP RLEKLDSLLS DYDILSLANI
60 70 80 90 100
QQHSIRKRDL QSATHLETLL TFSALKRHFK LYLTSSTERF SQNLRVVVVD
110 120 130 140 150
GKEESEYSVK WQNFFSGHVV GEPDSRVLAH IGDDDVTVRI NTDGAEYNVE
160 170 180 190 200
PLWRFVNDTK DKRMLVYKSE DIKDFSRLQS PKVCGYLNAD SEELLPKGLI
210 220 230 240 250
DREPSEEFVR RVKRRAEPNP LKNTCKLLVV ADHRFYKYMG RGEESTTTNY
260 270 280 290 300
LIELIDRVDD IYRNTSWDNA GFKGYGVQIE QIRILKSPQE VKPGERHFNM
310 320 330 340 350
AKSFPNEEKD AWDVKMLLEQ FSFDIAEEAS KVCLAHLFTY QDFDMGTLGL
360 370 380 390 400
AYVGSPRANS HGGVCPKAYY NPTVKKNIYL NSGLTSTKNY GKTILTKEAD
410 420 430 440 450
LVTTHELGHN FGAEHDPDGL AECAPNEDQG GKYVMYPIAV SGDHENNKMF
460 470 480 490 500
SNCSKQSIYK TIESKAQECF QERSNKVCGN SRVDEGEECD PGIMYLNNDT
510 520 530 540 550
CCNSDCTLKP GVQCSDRNSP CCKNCQFETA QKKCQEAINA TCKGVSYCTG
560 570 580 590 600
NSSECPPPGD AEDDTVCLDL GKCKAGKCIP FCKREQELES CACVDTDNSC
610 620 630 640 650
KVCCRNLSGP CVPYVDAEQK NLFLRKGKPC TVGFCDMNGK CEKRVQDVIE
660 670 680 690 700
RFWDFIDQLS INTFGKFLAD NIVGSVLVFS LIFWIPFSIL VHCVDKKLDK
710 720 730 740 750
QYESLSLFHH SNIEMLSSMD SASVRIIKPF PAPQTPGRLQ ALQPAAMMPP
760 770 780 790 800
VPAAPKLDHQ RMDTIQEDPS TDSHADDDGF EKDPFPNSST AAKSFEDLTD
810 820
HPVTRSEKAA SFKLQRQSRV DSKETEC
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.
InParanoidi Q9Z0F8.
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

Bgeei Q9Z0F8.
CleanExi MM_ADAM17.
ExpressionAtlasi Q9Z0F8. baseline and differential.
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

« Hide 'large scale' publications
  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 29, 2014
This is version 143 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