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Q9Z0F8 (ADA17_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 137. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | 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

Names and origin

Protein namesRecommended name:
Disintegrin and metalloproteinase domain-containing protein 17

Short name=ADAM 17
EC=3.4.24.86
Alternative name(s):
TNF-alpha convertase
TNF-alpha-converting enzyme
CD_antigen=CD156b
Gene names
Name:Adam17
Synonyms:Tace
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length827 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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 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). Ref.7 Ref.8 Ref.9

Catalytic activity

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.

Cofactor

Binds 1 zinc ion per subunit By similarity.

Enzyme regulation

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

Subunit structure

Interacts with MAD2L1, MAPK14 and MUC1 By similarity.

Subcellular location

Isoform Long: Cell membrane; Single-pass type I membrane protein.

Isoform Short: Secreted.

Tissue specificity

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

Domain

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.

Post-translational modification

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.

Sequence similarities

Contains 1 disintegrin domain.

Contains 1 peptidase M12B domain.

Ontologies

Keywords
   Biological processNotch signaling pathway
   Cellular componentCell membrane
Membrane
Secreted
   Coding sequence diversityAlternative splicing
   DomainSH3-binding
Signal
Transmembrane
Transmembrane helix
   LigandMetal-binding
Zinc
   Molecular functionHydrolase
Metalloprotease
Protease
   PTMCleavage on pair of basic residues
Disulfide bond
Glycoprotein
Phosphoprotein
Zymogen
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processB cell differentiation

Inferred from mutant phenotype PubMed 17371977. Source: BHF-UCL

Notch receptor processing

Inferred from sequence or structural similarity. Source: UniProtKB

Notch signaling pathway

Inferred from electronic annotation. Source: UniProtKB-KW

PMA-inducible membrane protein ectodomain proteolysis

Inferred from direct assay PubMed 15691827. Source: BHF-UCL

T cell differentiation in thymus

Inferred from mutant phenotype PubMed 17371977. Source: BHF-UCL

cell adhesion mediated by integrin

Inferred from electronic annotation. Source: Ensembl

cell motility

Inferred from mutant phenotype PubMed 18625725. Source: BHF-UCL

epidermal growth factor receptor signaling pathway

Inferred from electronic annotation. Source: Ensembl

epidermal growth factor-activated receptor transactivation by G-protein coupled receptor signaling pathway

Inferred from electronic annotation. Source: Ensembl

germinal center formation

Inferred from mutant phenotype PubMed 17371977. Source: BHF-UCL

membrane protein ectodomain proteolysis

Inferred from mutant phenotype PubMed 9034190. Source: BHF-UCL

negative regulation of interleukin-8 production

Inferred from electronic annotation. Source: Ensembl

positive regulation of T cell chemotaxis

Inferred from electronic annotation. Source: Ensembl

positive regulation of cell growth

Inferred from electronic annotation. Source: Ensembl

positive regulation of cell proliferation

Inferred from electronic annotation. Source: Ensembl

positive regulation of cellular component movement

Inferred from mutant phenotype PubMed 18625725. Source: BHF-UCL

positive regulation of chemokine production

Inferred from electronic annotation. Source: Ensembl

positive regulation of cyclin-dependent protein serine/threonine kinase activity involved in G1/S transition of mitotic cell cycle

Inferred from electronic annotation. Source: Ensembl

positive regulation of transforming growth factor beta receptor signaling pathway

Inferred from mutant phenotype PubMed 18625725. Source: BHF-UCL

regulation of mast cell apoptotic process

Inferred from mutant phenotype PubMed 14625290. Source: BHF-UCL

response to drug

Inferred from mutant phenotype PubMed 16179345. Source: BHF-UCL

response to high density lipoprotein particle

Inferred from electronic annotation. Source: Ensembl

response to hypoxia

Inferred from electronic annotation. Source: Ensembl

response to lipopolysaccharide

Inferred from electronic annotation. Source: Ensembl

spleen development

Inferred from mutant phenotype PubMed 17371977. Source: BHF-UCL

wound healing, spreading of epidermal cells

Inferred from electronic annotation. Source: Ensembl

   Cellular_componentactin cytoskeleton

Inferred from electronic annotation. Source: Ensembl

apical plasma membrane

Inferred from electronic annotation. Source: Ensembl

cell surface

Inferred from electronic annotation. Source: Ensembl

cell-cell junction

Inferred from electronic annotation. Source: Ensembl

cytoplasm

Inferred from direct assay PubMed 15739225. Source: MGI

extracellular region

Traceable author statement. Source: Reactome

focal adhesion

Inferred from electronic annotation. Source: Ensembl

integral component of plasma membrane

Inferred from electronic annotation. Source: Ensembl

membrane raft

Inferred from electronic annotation. Source: Ensembl

plasma membrane

Traceable author statement. Source: Reactome

ruffle membrane

Inferred from electronic annotation. Source: Ensembl

   Molecular_functionNotch binding

Inferred from sequence or structural similarity. Source: UniProtKB

metalloendopeptidase activity

Traceable author statement. Source: Reactome

metallopeptidase activity

Inferred from direct assay PubMed 14761956. Source: BHF-UCL

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 Long (identifier: Q9Z0F8-1)

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 Short (identifier: Q9Z0F8-2)

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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 1717 Potential
Propeptide18 – 214197 By similarity
PRO_0000029090
Chain215 – 827613Disintegrin and metalloproteinase domain-containing protein 17
PRO_0000029091

Regions

Topological domain215 – 671457Extracellular Potential
Transmembrane672 – 69221Helical; Potential
Topological domain693 – 827135Cytoplasmic Potential
Domain223 – 474252Peptidase M12B
Domain475 – 56389Disintegrin
Region603 – 67169Crambin-like
Motif182 – 1898Cysteine switch By similarity
Motif731 – 7388SH3-binding Potential
Compositional bias96 – 994Poly-Val
Compositional bias564 – 60239Cys-rich

Sites

Active site4061 By similarity
Metal binding1841Zinc; in inhibited form By similarity
Metal binding4051Zinc; catalytic By similarity
Metal binding4091Zinc; catalytic By similarity
Metal binding4151Zinc; catalytic By similarity

Amino acid modifications

Modified residue7351Phosphothreonine; by MAPK14 By similarity
Modified residue7941Phosphoserine Ref.10
Modified residue8221Phosphoserine By similarity
Glycosylation1571N-linked (GlcNAc...) Potential
Glycosylation2641N-linked (GlcNAc...) Potential
Glycosylation4521N-linked (GlcNAc...) Potential
Glycosylation4981N-linked (GlcNAc...) Potential
Glycosylation5391N-linked (GlcNAc...) Potential
Glycosylation5511N-linked (GlcNAc...) Potential
Glycosylation6061N-linked (GlcNAc...) Potential
Disulfide bond225 ↔ 333 By similarity
Disulfide bond365 ↔ 469 By similarity
Disulfide bond423 ↔ 453 By similarity
Disulfide bond534 ↔ 555 By similarity
Disulfide bond573 ↔ 582 By similarity
Disulfide bond578 ↔ 591 By similarity
Disulfide bond593 ↔ 600 By similarity

Natural variations

Alternative sequence639 – 65517GKCEK…RFWDF → CDFFSPYRANVRNEYRT in isoform Short.
VSP_005479
Alternative sequence656 – 827172Missing in isoform Short.
VSP_005480

Experimental info

Sequence conflict3 – 42RR → QS in CAA07480. Ref.2
Sequence conflict71I → F in CAA07480. Ref.2
Sequence conflict281S → A in CAA07480. Ref.2
Sequence conflict281S → A in BAA78578. Ref.3
Sequence conflict1131N → D in AAC62934. Ref.1
Sequence conflict1131N → D in CAA07480. Ref.2
Sequence conflict1131N → D in BAA78578. Ref.3
Sequence conflict1131N → D in AAD09627. Ref.4
Sequence conflict1131N → D in AAD09628. Ref.4
Sequence conflict1491V → I in CAA07480. Ref.2
Sequence conflict1491V → I in BAA78578. Ref.3
Sequence conflict5941V → I in AAC62934. Ref.1
Sequence conflict5941V → I in AAD09627. Ref.4
Sequence conflict5941V → I in AAD09628. Ref.4
Sequence conflict7521P → S in CAA07480. Ref.2
Sequence conflict7521P → S in BAA78578. Ref.3
Sequence conflict7751A → V in CAA07480. Ref.2
Sequence conflict7751A → V in BAA78578. Ref.3

Sequences

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

Last modified July 27, 2011. Version 3.
Checksum: 6B434F80878197F5

FASTA82793,056
        10         20         30         40         50         60 
MRRRLLILTT LVPFVLAPRP PEEAGSGSHP RLEKLDSLLS DYDILSLANI QQHSIRKRDL 

        70         80         90        100        110        120 
QSATHLETLL TFSALKRHFK LYLTSSTERF SQNLRVVVVD GKEESEYSVK WQNFFSGHVV 

       130        140        150        160        170        180 
GEPDSRVLAH IGDDDVTVRI NTDGAEYNVE PLWRFVNDTK DKRMLVYKSE DIKDFSRLQS 

       190        200        210        220        230        240 
PKVCGYLNAD SEELLPKGLI DREPSEEFVR RVKRRAEPNP LKNTCKLLVV ADHRFYKYMG 

       250        260        270        280        290        300 
RGEESTTTNY LIELIDRVDD IYRNTSWDNA GFKGYGVQIE QIRILKSPQE VKPGERHFNM 

       310        320        330        340        350        360 
AKSFPNEEKD AWDVKMLLEQ FSFDIAEEAS KVCLAHLFTY QDFDMGTLGL AYVGSPRANS 

       370        380        390        400        410        420 
HGGVCPKAYY NPTVKKNIYL NSGLTSTKNY GKTILTKEAD LVTTHELGHN FGAEHDPDGL 

       430        440        450        460        470        480 
AECAPNEDQG GKYVMYPIAV SGDHENNKMF SNCSKQSIYK TIESKAQECF QERSNKVCGN 

       490        500        510        520        530        540 
SRVDEGEECD PGIMYLNNDT CCNSDCTLKP GVQCSDRNSP CCKNCQFETA QKKCQEAINA 

       550        560        570        580        590        600 
TCKGVSYCTG NSSECPPPGD AEDDTVCLDL GKCKAGKCIP FCKREQELES CACVDTDNSC 

       610        620        630        640        650        660 
KVCCRNLSGP CVPYVDAEQK NLFLRKGKPC TVGFCDMNGK CEKRVQDVIE RFWDFIDQLS 

       670        680        690        700        710        720 
INTFGKFLAD NIVGSVLVFS LIFWIPFSIL VHCVDKKLDK QYESLSLFHH SNIEMLSSMD 

       730        740        750        760        770        780 
SASVRIIKPF PAPQTPGRLQ ALQPAAMMPP VPAAPKLDHQ RMDTIQEDPS TDSHADDDGF 

       790        800        810        820 
EKDPFPNSST AAKSFEDLTD HPVTRSEKAA SFKLQRQSRV DSKETEC 

« Hide

Isoform Short [UniParc].

Checksum: 9F4B11FD8D99DDF8
Show »

FASTA65573,884

References

« Hide 'large scale' references
[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]"TNF-alpha converting enzyme (TACE) is inhibited by TIMP-3."
Amour A., Slocombe P.M., Webster A., Butler M., Knight C.G., Smith B.J., Stephens P.E., Shelley C., Hutton M., Knauper V., Docherty A.J., Murphy G.
FEBS Lett. 435:39-44(1998) [PubMed] [Europe PMC] [Abstract]
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. expand/collapse author list , 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].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF056359 expand/collapse EMBL AC list , 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.
RefSeqNP_001264195.1. NM_001277266.1.
NP_033745.4. NM_009615.6.
UniGeneMm.27681.

3D structure databases

ProteinModelPortalQ9Z0F8.
SMRQ9Z0F8. Positions 220-646.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

IntActQ9Z0F8. 2 interactions.
MINTMINT-246289.

Chemistry

BindingDBQ9Z0F8.
ChEMBLCHEMBL4379.

Protein family/group databases

MEROPSM12.217.

PTM databases

PhosphoSiteQ9Z0F8.

Proteomic databases

PaxDbQ9Z0F8.
PRIDEQ9Z0F8.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000064536; ENSMUSP00000067953; ENSMUSG00000052593. [Q9Z0F8-1]
ENSMUST00000145118; ENSMUSP00000136407; ENSMUSG00000052593. [Q9Z0F8-2]
GeneID11491.
KEGGmmu:11491.
UCSCuc007ndu.1. mouse. [Q9Z0F8-1]

Organism-specific databases

CTD6868.
MGIMGI:1096335. Adam17.

Phylogenomic databases

eggNOGNOG269976.
GeneTreeENSGT00670000097974.
HOGENOMHOG000033797.
HOVERGENHBG050457.
KOK06059.
TreeFamTF314733.

Enzyme and pathway databases

ReactomeREACT_188257. Signal Transduction.
REACT_189085. Disease.
REACT_98458. Immune System.

Gene expression databases

ArrayExpressQ9Z0F8.
BgeeQ9Z0F8.
CleanExMM_ADAM17.
GenevestigatorQ9Z0F8.

Family and domain databases

Gene3D3.40.390.10. 1 hit.
4.10.70.10. 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. SSF57552. 1 hit.
PROSITEPS50215. ADAM_MEPRO. 1 hit.
PS50214. DISINTEGRIN_2. 1 hit.
PS00142. ZINC_PROTEASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio278866.
PMAP-CutDBQ505A7.
PROQ9Z0F8.
SOURCESearch...

Entry information

Entry nameADA17_MOUSE
AccessionPrimary (citable) accession number: Q9Z0F8
Secondary accession number(s): O88726 expand/collapse secondary AC list , Q505A7, Q9R1U4, Q9Z0K3
Entry history
Integrated into UniProtKB/Swiss-Prot: June 20, 2001
Last sequence update: July 27, 2011
Last modified: April 16, 2014
This is version 137 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Peptidase families

Classification of peptidase families and list of entries

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot