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Disintegrin and metalloproteinase domain-containing protein 17 (ADAM 17) (EC 3.4.24.86) (Snake venom-like protease) (TNF-alpha convertase) (TNF-alpha-converting enzyme) (CD antigen CD156b)

 ADA17_HUMAN             Reviewed;         824 AA.
P78536; O60226;
20-JUN-2001, integrated into UniProtKB/Swiss-Prot.
01-MAY-1997, sequence version 1.
22-NOV-2017, entry version 203.
RecName: Full=Disintegrin and metalloproteinase domain-containing protein 17;
Short=ADAM 17;
EC=3.4.24.86 {ECO:0000269|PubMed:12441351, ECO:0000269|PubMed:20592283, ECO:0000269|PubMed:24227843};
AltName: Full=Snake venom-like protease;
AltName: Full=TNF-alpha convertase;
AltName: Full=TNF-alpha-converting enzyme;
AltName: CD_antigen=CD156b;
Flags: Precursor;
Name=ADAM17; Synonyms=CSVP, TACE;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM A), AND PARTIAL PROTEIN SEQUENCE.
TISSUE=Leukocyte, and Monocyte;
PubMed=9034191; DOI=10.1038/385733a0;
Moss M.L., Jin S.-L.C., Milla M.E., Burkhart W., Carter H.L.,
Chen W.-J., Clay W.C., Didsbury J.R., Hassler D., Hoffman C.R.,
Kost T.A., Lambert M.H., Leesnitzer M.A., McCauley P., McGeehan G.,
Mitchell J., Moyer M., Pahel G., Rocque W., Overton L.K., Schoenen F.,
Seaton T., Su J.-L., Warner J., Willard D., Becherer J.D.;
"Cloning of a disintegrin metalloproteinase that processes precursor
tumour-necrosis factor-alpha.";
Nature 385:733-736(1997).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS A AND B).
PubMed=9034190; DOI=10.1038/385729a0;
Black R.A., Rauch C.T., Kozlosky C.J., Peschon J.J., Slack J.L.,
Wolfson M.F., Castner B.J., Stocking K.L., Reddy P., Srinivasan S.,
Nelson N., Bioani N., Schooley K.A., Gerhart M., Davis R.,
Fitzner J.N., Johnson R.S., Paxton R.J., March C.J., Cerretti D.P.;
"A metalloproteinase disintegrin that releases tumour-necrosis factor-
alpha from cells.";
Nature 385:729-733(1997).
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM A).
TISSUE=Cartilage;
PubMed=9574564;
Patel I.R., Attur M.G., Patel R.N., Stuchin S.A., Abagyan R.A.,
Abramson S.B., Amin A.R.;
"TNF-alpha convertase enzyme from human arthritis-affected cartilage:
isolation of cDNA by differential display, expression of the active
enzyme, and regulation of TNF-alpha.";
J. Immunol. 160:4570-4579(1998).
[4]
PHOSPHORYLATION AT THR-735.
PubMed=12058067; DOI=10.1091/mbc.01-11-0561;
Diaz-Rodriguez E., Montero J.C., Esparis-Ogando A., Yuste L.,
Pandiella A.;
"Extracellular signal-regulated kinase phosphorylates tumor necrosis
factor alpha-converting enzyme at threonine 735: a potential role in
regulated shedding.";
Mol. Biol. Cell 13:2031-2044(2002).
[5]
FUNCTION, CATALYTIC ACTIVITY, AND INTERACTION WITH MUC1.
PubMed=12441351; DOI=10.1074/jbc.M208326200;
Thathiah A., Blobel C.P., Carson D.D.;
"Tumor necrosis factor-alpha converting enzyme/ADAM 17 mediates MUC1
shedding.";
J. Biol. Chem. 278:3386-3394(2003).
[6]
PHOSPHORYLATION AT SER-819.
PubMed=12621058; DOI=10.1074/jbc.M300331200;
Fan H., Turck C.W., Derynck R.;
"Characterization of growth factor-induced serine phosphorylation of
tumor necrosis factor-alpha converting enzyme and of an alternatively
translated polypeptide.";
J. Biol. Chem. 278:18617-18627(2003).
[7]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-791, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,
Mann M.;
"Global, in vivo, and site-specific phosphorylation dynamics in
signaling networks.";
Cell 127:635-648(2006).
[8]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-791, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18669648; DOI=10.1073/pnas.0805139105;
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
Elledge S.J., Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
[9]
ROLE IN PROTEOLYTICAL RELEASE OF JAM3.
PubMed=20592283; DOI=10.4049/jimmunol.1000556;
Rabquer B.J., Amin M.A., Teegala N., Shaheen M.K., Tsou P.S.,
Ruth J.H., Lesch C.A., Imhof B.A., Koch A.E.;
"Junctional adhesion molecule-C is a soluble mediator of
angiogenesis.";
J. Immunol. 185:1777-1785(2010).
[10]
PHOSPHORYLATION AT THR-735, AND INTERACTION WITH MAPK14.
PubMed=20188673; DOI=10.1016/j.molcel.2010.01.034;
Xu P., Derynck R.;
"Direct activation of TACE-mediated ectodomain shedding by p38 MAP
kinase regulates EGF receptor-dependent cell proliferation.";
Mol. Cell 37:551-566(2010).
[11]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-791, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=20068231; DOI=10.1126/scisignal.2000475;
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
Mann M.;
"Quantitative phosphoproteomics reveals widespread full
phosphorylation site occupancy during mitosis.";
Sci. Signal. 3:RA3-RA3(2010).
[12]
INVOLVEMENT IN NISBD1.
PubMed=22010916; DOI=10.1056/NEJMoa1100721;
Blaydon D.C., Biancheri P., Di W.L., Plagnol V., Cabral R.M.,
Brooke M.A., van Heel D.A., Ruschendorf F., Toynbee M., Walne A.,
O'Toole E.A., Martin J.E., Lindley K., Vulliamy T., Abrams D.J.,
MacDonald T.T., Harper J.I., Kelsell D.P.;
"Inflammatory skin and bowel disease linked to ADAM17 deletion.";
N. Engl. J. Med. 365:1502-1508(2011).
[13]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-791, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21406692; DOI=10.1126/scisignal.2001570;
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
Blagoev B.;
"System-wide temporal characterization of the proteome and
phosphoproteome of human embryonic stem cell differentiation.";
Sci. Signal. 4:RS3-RS3(2011).
[14]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-761 AND SER-791, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[15]
FUNCTION.
PubMed=24226769; DOI=10.1038/nature12723;
Boskovski M.T., Yuan S., Pedersen N.B., Goth C.K., Makova S.,
Clausen H., Brueckner M., Khokha M.K.;
"The heterotaxy gene GALNT11 glycosylates Notch to orchestrate cilia
type and laterality.";
Nature 504:456-459(2013).
[16]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-791, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[17]
FUNCTION, AND CATALYTIC ACTIVITY.
PubMed=24227843; DOI=10.1128/JVI.02202-13;
Heurich A., Hofmann-Winkler H., Gierer S., Liepold T., Jahn O.,
Poehlmann S.;
"TMPRSS2 and ADAM17 cleave ACE2 differentially and only proteolysis by
TMPRSS2 augments entry driven by the severe acute respiratory syndrome
coronavirus spike protein.";
J. Virol. 88:1293-1307(2014).
[18]
X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 219-473 IN COMPLEX WITH ZINC,
COFACTOR, ACTIVE SITE, AND DISULFIDE BONDS.
PubMed=9520379; DOI=10.1073/pnas.95.7.3408;
Maskos K., Fernandez-Catalan C., Huber R., Bourenkov G.P.,
Bartunik H., Ellestad G.A., Reddy P., Wolfson M.F., Rauch C.T.,
Castner B.J., Davis R., Clarke H.R.G., Petersen M., Fitzner J.N.,
Cerretti D.P., March C.J., Paxton R.J., Black R.A., Bode W.;
"Crystal structure of the catalytic domain of human tumor necrosis
factor-alpha-converting enzyme.";
Proc. Natl. Acad. Sci. U.S.A. 95:3408-3412(1998).
-!- 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. 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). Plays a role in the
proteolytic processing of ACE2. {ECO:0000269|PubMed:12441351,
ECO:0000269|PubMed:20592283, ECO:0000269|PubMed:24226769,
ECO:0000269|PubMed:24227843}.
-!- 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. {ECO:0000269|PubMed:12441351,
ECO:0000269|PubMed:20592283, ECO:0000269|PubMed:24227843}.
-!- COFACTOR:
Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
Evidence={ECO:0000269|PubMed:9520379};
Note=Binds 1 zinc ion per subunit. {ECO:0000269|PubMed:9520379};
-!- SUBUNIT: Interacts with MAD2L1, MAPK14 and MUC1.
{ECO:0000269|PubMed:12441351, ECO:0000269|PubMed:20188673}.
-!- INTERACTION:
Q12959:DLG1; NbExp=7; IntAct=EBI-78188, EBI-357481;
Q13257:MAD2L1; NbExp=3; IntAct=EBI-78188, EBI-78203;
Q80WQ6:Rhbdf2 (xeno); NbExp=2; IntAct=EBI-78188, EBI-647271;
-!- SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane
protein.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=A;
IsoId=P78536-1; Sequence=Displayed;
Name=B;
IsoId=P78536-2; Sequence=VSP_005478;
Note=No experimental confirmation available.;
-!- TISSUE SPECIFICITY: Ubiquitously expressed. Expressed at highest
levels in adult heart, placenta, skeletal muscle, pancreas,
spleen, thymus, prostate, testes, ovary and small intestine, and
in fetal brain, lung, liver and kidney.
-!- INDUCTION: In arthritis-affected cartilage.
-!- 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 (By similarity). {ECO:0000250}.
-!- 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.
-!- PTM: The precursor is cleaved by a furin endopeptidase.
{ECO:0000250}.
-!- PTM: Phosphorylated. Stimulation by growth factor or phorbol 12-
myristate 13-acetate induces phosphorylation of Ser-819 but
decreases phosphorylation of Ser-791. Phosphorylation at THR-735
by MAPK14 is required for ADAM17-mediated ectodomain shedding.
{ECO:0000269|PubMed:12058067, ECO:0000269|PubMed:12621058,
ECO:0000269|PubMed:20188673}.
-!- DISEASE: Inflammatory skin and bowel disease, neonatal, 1 (NISBD1)
[MIM:614328]: A disorder characterized by inflammatory features
with neonatal onset, involving the skin, hair, and gut. The skin
lesions involve perioral and perianal erythema, psoriasiform
erythroderma, with flares of erythema, scaling, and widespread
pustules. Gastrointestinal symptoms include malabsorptive diarrhea
that is exacerbated by intercurrent gastrointestinal infections.
The hair is short or broken, and the eyelashes and eyebrows are
wiry and disorganized. {ECO:0000269|PubMed:22010916}. Note=The
disease is caused by mutations affecting the gene represented in
this entry.
-!- WEB RESOURCE: Name=Wikipedia; Note=Tumor necrosis factor alpha-
converting enzyme entry;
URL="https://en.wikipedia.org/wiki/Tumor_Necrosis_Factor_Alpha_Converting_Enzyme";
-!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology
and Haematology;
URL="http://atlasgeneticsoncology.org/Genes/ADAM17ID572ch2p25.html";
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EMBL; U86755; AAB51586.1; -; mRNA.
EMBL; U69611; AAB51514.1; -; mRNA.
EMBL; U69612; AAB53014.1; -; mRNA.
EMBL; U92649; AAC39721.1; -; mRNA.
CCDS; CCDS1665.1; -. [P78536-1]
RefSeq; NP_003174.3; NM_003183.5. [P78536-1]
UniGene; Hs.404914; -.
UniGene; Hs.570189; -.
UniGene; Hs.744980; -.
PDB; 1BKC; X-ray; 2.00 A; A/C/E/I=219-474.
PDB; 1ZXC; X-ray; 2.28 A; A/B=215-477.
PDB; 2A8H; X-ray; 2.30 A; A/B=215-477.
PDB; 2DDF; X-ray; 1.70 A; A/B=218-474.
PDB; 2FV5; X-ray; 2.10 A; A/B=216-475.
PDB; 2FV9; X-ray; 2.02 A; A/B=218-475.
PDB; 2I47; X-ray; 1.90 A; A/B/C/D=212-492.
PDB; 2M2F; NMR; -; A=581-642.
PDB; 2OI0; X-ray; 2.00 A; A=216-477.
PDB; 3B92; X-ray; 2.00 A; A=216-474.
PDB; 3CKI; X-ray; 2.30 A; A=219-474.
PDB; 3E8R; X-ray; 1.90 A; A/B=215-477.
PDB; 3EDZ; X-ray; 1.90 A; A/B=215-477.
PDB; 3EWJ; X-ray; 1.80 A; A/B=215-477.
PDB; 3G42; X-ray; 2.10 A; A/B/C/D=212-492.
PDB; 3KMC; X-ray; 1.80 A; A/B=215-476.
PDB; 3KME; X-ray; 1.85 A; A/B=215-476.
PDB; 3L0T; X-ray; 1.92 A; A/B=215-476.
PDB; 3L0V; X-ray; 1.75 A; A/B=215-476.
PDB; 3LE9; X-ray; 1.85 A; A/B=215-476.
PDB; 3LEA; X-ray; 2.00 A; A/B=215-476.
PDB; 3LGP; X-ray; 1.90 A; A/B=215-476.
PDB; 3O64; X-ray; 1.88 A; A/B=215-476.
PDBsum; 1BKC; -.
PDBsum; 1ZXC; -.
PDBsum; 2A8H; -.
PDBsum; 2DDF; -.
PDBsum; 2FV5; -.
PDBsum; 2FV9; -.
PDBsum; 2I47; -.
PDBsum; 2M2F; -.
PDBsum; 2OI0; -.
PDBsum; 3B92; -.
PDBsum; 3CKI; -.
PDBsum; 3E8R; -.
PDBsum; 3EDZ; -.
PDBsum; 3EWJ; -.
PDBsum; 3G42; -.
PDBsum; 3KMC; -.
PDBsum; 3KME; -.
PDBsum; 3L0T; -.
PDBsum; 3L0V; -.
PDBsum; 3LE9; -.
PDBsum; 3LEA; -.
PDBsum; 3LGP; -.
PDBsum; 3O64; -.
ProteinModelPortal; P78536; -.
SMR; P78536; -.
BioGrid; 112731; 21.
DIP; DIP-31044N; -.
IntAct; P78536; 12.
MINT; MINT-108290; -.
STRING; 9606.ENSP00000309968; -.
BindingDB; P78536; -.
ChEMBL; CHEMBL3706; -.
DrugBank; DB07145; (2R)-N-HYDROXY-2-[(3S)-3-METHYL-3-{4-[(2-METHYLQUINOLIN-4-YL)METHOXY]PHENYL}-2-OXOPYRROLIDIN-1-YL]PROPANAMIDE.
DrugBank; DB06943; (3S)-1-{[4-(but-2-yn-1-yloxy)phenyl]sulfonyl}pyrrolidine-3-thiol.
DrugBank; DB07079; 3-{[4-(but-2-yn-1-yloxy)phenyl]sulfonyl}propane-1-thiol.
DrugBank; DB07233; N-{[4-(but-2-yn-1-yloxy)phenyl]sulfonyl}-5-methyl-D-tryptophan.
GuidetoPHARMACOLOGY; 1662; -.
MEROPS; M12.217; -.
TCDB; 8.A.77.1.2; the sheddase (sheddase) family.
iPTMnet; P78536; -.
PhosphoSitePlus; P78536; -.
SwissPalm; P78536; -.
BioMuta; ADAM17; -.
DMDM; 14423632; -.
EPD; P78536; -.
MaxQB; P78536; -.
PaxDb; P78536; -.
PeptideAtlas; P78536; -.
PRIDE; P78536; -.
DNASU; 6868; -.
Ensembl; ENST00000310823; ENSP00000309968; ENSG00000151694. [P78536-1]
GeneID; 6868; -.
KEGG; hsa:6868; -.
UCSC; uc002qzu.5; human. [P78536-1]
CTD; 6868; -.
DisGeNET; 6868; -.
EuPathDB; HostDB:ENSG00000151694.12; -.
GeneCards; ADAM17; -.
HGNC; HGNC:195; ADAM17.
HPA; CAB025906; -.
HPA; HPA010738; -.
HPA; HPA051575; -.
MalaCards; ADAM17; -.
MIM; 603639; gene.
MIM; 614328; phenotype.
neXtProt; NX_P78536; -.
OpenTargets; ENSG00000151694; -.
Orphanet; 294023; Neonatal inflammatory skin and bowel disease.
PharmGKB; PA24512; -.
eggNOG; KOG3658; Eukaryota.
eggNOG; ENOG410XQWB; LUCA.
GeneTree; ENSGT00670000097974; -.
HOGENOM; HOG000033797; -.
HOVERGEN; HBG050457; -.
InParanoid; P78536; -.
KO; K06059; -.
OMA; DGTPCIQ; -.
OrthoDB; EOG091G03AL; -.
PhylomeDB; P78536; -.
TreeFam; TF314733; -.
BRENDA; 3.4.24.86; 2681.
Reactome; R-HSA-1251985; Nuclear signaling by ERBB4.
Reactome; R-HSA-1442490; Collagen degradation.
Reactome; R-HSA-177929; Signaling by EGFR.
Reactome; R-HSA-193692; Regulated proteolysis of p75NTR.
Reactome; R-HSA-2122948; Activated NOTCH1 Transmits Signal to the Nucleus.
Reactome; R-HSA-2644606; Constitutive Signaling by NOTCH1 PEST Domain Mutants.
Reactome; R-HSA-2660826; Constitutive Signaling by NOTCH1 t(7;9)(NOTCH1:M1580_K2555) Translocation Mutant.
Reactome; R-HSA-2691232; Constitutive Signaling by NOTCH1 HD Domain Mutants.
Reactome; R-HSA-2894862; Constitutive Signaling by NOTCH1 HD+PEST Domain Mutants.
Reactome; R-HSA-5362798; Release of Hh-Np from the secreting cell.
Reactome; R-HSA-75893; TNF signaling.
Reactome; R-HSA-982772; Growth hormone receptor signaling.
SignaLink; P78536; -.
SIGNOR; P78536; -.
ChiTaRS; ADAM17; human.
EvolutionaryTrace; P78536; -.
GeneWiki; ADAM17; -.
GenomeRNAi; 6868; -.
PRO; PR:P78536; -.
Proteomes; UP000005640; Chromosome 2.
Bgee; ENSG00000151694; -.
CleanEx; HS_ADAM17; -.
ExpressionAtlas; P78536; baseline and differential.
Genevisible; P78536; HS.
GO; GO:0015629; C:actin cytoskeleton; IDA:BHF-UCL.
GO; GO:0016324; C:apical plasma membrane; IDA:BHF-UCL.
GO; GO:0009986; C:cell surface; IDA:BHF-UCL.
GO; GO:0005737; C:cytoplasm; IDA:BHF-UCL.
GO; GO:0005829; C:cytosol; IDA:HPA.
GO; GO:0005887; C:integral component of plasma membrane; IDA:BHF-UCL.
GO; GO:0016020; C:membrane; IDA:UniProtKB.
GO; GO:0045121; C:membrane raft; IDA:BHF-UCL.
GO; GO:0005886; C:plasma membrane; TAS:Reactome.
GO; GO:0005178; F:integrin binding; IPI:BHF-UCL.
GO; GO:0005138; F:interleukin-6 receptor binding; IPI:BHF-UCL.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0004222; F:metalloendopeptidase activity; IDA:UniProtKB.
GO; GO:0008237; F:metallopeptidase activity; IDA:BHF-UCL.
GO; GO:0005112; F:Notch binding; IDA:UniProtKB.
GO; GO:0030165; F:PDZ domain binding; IPI:BHF-UCL.
GO; GO:0017124; F:SH3 domain binding; IEA:UniProtKB-KW.
GO; GO:0030183; P:B cell differentiation; ISS:BHF-UCL.
GO; GO:0007155; P:cell adhesion; IDA:BHF-UCL.
GO; GO:0033627; P:cell adhesion mediated by integrin; IDA:BHF-UCL.
GO; GO:0048870; P:cell motility; ISS:BHF-UCL.
GO; GO:0050830; P:defense response to Gram-positive bacterium; IMP:BHF-UCL.
GO; GO:0007173; P:epidermal growth factor receptor signaling pathway; IDA:BHF-UCL.
GO; GO:0035625; P:epidermal growth factor-activated receptor transactivation by G-protein coupled receptor signaling pathway; IMP:BHF-UCL.
GO; GO:0002467; P:germinal center formation; ISS:BHF-UCL.
GO; GO:0006509; P:membrane protein ectodomain proteolysis; IDA:BHF-UCL.
GO; GO:0031293; P:membrane protein intracellular domain proteolysis; TAS:Reactome.
GO; GO:0030512; P:negative regulation of transforming growth factor beta receptor signaling pathway; IMP:UniProtKB.
GO; GO:0002446; P:neutrophil mediated immunity; IC:BHF-UCL.
GO; GO:0007220; P:Notch receptor processing; IDA:UniProtKB.
GO; GO:0007219; P:Notch signaling pathway; IEA:UniProtKB-KW.
GO; GO:0051088; P:PMA-inducible membrane protein ectodomain proteolysis; IDA:BHF-UCL.
GO; GO:0030307; P:positive regulation of cell growth; IMP:BHF-UCL.
GO; GO:0030335; P:positive regulation of cell migration; IMP:BHF-UCL.
GO; GO:0008284; P:positive regulation of cell proliferation; IMP:BHF-UCL.
GO; GO:0051272; P:positive regulation of cellular component movement; ISS:BHF-UCL.
GO; GO:0032722; P:positive regulation of chemokine production; IMP:BHF-UCL.
GO; GO:0031659; P:positive regulation of cyclin-dependent protein serine/threonine kinase activity involved in G1/S transition of mitotic cell cycle; IDA:BHF-UCL.
GO; GO:0045741; P:positive regulation of epidermal growth factor-activated receptor activity; IDA:BHF-UCL.
GO; GO:0002690; P:positive regulation of leukocyte chemotaxis; IC:BHF-UCL.
GO; GO:0001934; P:positive regulation of protein phosphorylation; IMP:BHF-UCL.
GO; GO:0010820; P:positive regulation of T cell chemotaxis; IMP:BHF-UCL.
GO; GO:0030511; P:positive regulation of transforming growth factor beta receptor signaling pathway; ISS:BHF-UCL.
GO; GO:0006508; P:proteolysis; IDA:UniProtKB.
GO; GO:0033025; P:regulation of mast cell apoptotic process; ISS:BHF-UCL.
GO; GO:0042493; P:response to drug; ISS:BHF-UCL.
GO; GO:0055099; P:response to high density lipoprotein particle; IDA:BHF-UCL.
GO; GO:0001666; P:response to hypoxia; IDA:BHF-UCL.
GO; GO:0032496; P:response to lipopolysaccharide; IDA:BHF-UCL.
GO; GO:0048536; P:spleen development; ISS:BHF-UCL.
GO; GO:0033077; P:T cell differentiation in thymus; ISS:BHF-UCL.
GO; GO:0033209; P:tumor necrosis factor-mediated signaling pathway; TAS:Reactome.
GO; GO:0035313; P:wound healing, spreading of epidermal cells; IEP:BHF-UCL.
CDD; cd14246; ADAM17_MPD; 1.
CDD; cd04270; ZnMc_TACE_like; 1.
Gene3D; 3.40.390.10; -; 1.
Gene3D; 4.10.70.10; -; 1.
InterPro; IPR034025; ADAM10_ADAM17.
InterPro; IPR032029; ADAM17_MPD.
InterPro; IPR001762; Disintegrin_dom.
InterPro; IPR036436; Disintegrin_dom_sf.
InterPro; IPR024079; MetalloPept_cat_dom_sf.
InterPro; IPR001590; Peptidase_M12B.
InterPro; IPR002870; Peptidase_M12B_N.
Pfam; PF16698; ADAM17_MPD; 1.
Pfam; PF00200; Disintegrin; 1.
Pfam; PF01562; Pep_M12B_propep; 1.
SMART; SM00050; DISIN; 1.
SUPFAM; SSF57552; SSF57552; 1.
PROSITE; PS50215; ADAM_MEPRO; 1.
PROSITE; PS50214; DISINTEGRIN_2; 1.
PROSITE; PS00142; ZINC_PROTEASE; 1.
1: Evidence at protein level;
3D-structure; Alternative splicing;
Cleavage on pair of basic residues; Complete proteome;
Direct protein sequencing; Disulfide bond; Glycoprotein; Hydrolase;
Membrane; Metal-binding; Metalloprotease; Notch signaling pathway;
Phosphoprotein; Polymorphism; Protease; Reference proteome;
SH3-binding; Signal; Transmembrane; Transmembrane helix; Zinc;
Zymogen.
SIGNAL 1 17 {ECO:0000250|UniProtKB:Q9Z1K9}.
PROPEP 18 214 {ECO:0000269|PubMed:9034191}.
/FTId=PRO_0000029088.
CHAIN 215 824 Disintegrin and metalloproteinase domain-
containing protein 17.
/FTId=PRO_0000029089.
TOPO_DOM 215 671 Extracellular. {ECO:0000255}.
TRANSMEM 672 692 Helical. {ECO:0000255}.
TOPO_DOM 693 824 Cytoplasmic. {ECO:0000255}.
DOMAIN 223 474 Peptidase M12B. {ECO:0000255|PROSITE-
ProRule:PRU00276}.
DOMAIN 475 563 Disintegrin. {ECO:0000255|PROSITE-
ProRule:PRU00068}.
REGION 603 671 Crambin-like.
MOTIF 182 189 Cysteine switch. {ECO:0000250}.
MOTIF 731 738 SH3-binding. {ECO:0000255}.
MOTIF 741 748 SH3-binding. {ECO:0000255}.
COMPBIAS 96 99 Poly-Val.
COMPBIAS 564 602 Cys-rich.
ACT_SITE 406 406 {ECO:0000255|PROSITE-ProRule:PRU00276,
ECO:0000255|PROSITE-ProRule:PRU10095,
ECO:0000269|PubMed:9520379}.
METAL 184 184 Zinc; in inhibited form. {ECO:0000250}.
METAL 405 405 Zinc; catalytic.
{ECO:0000269|PubMed:9520379}.
METAL 409 409 Zinc; catalytic.
{ECO:0000269|PubMed:9520379}.
METAL 415 415 Zinc; catalytic.
{ECO:0000269|PubMed:9520379}.
MOD_RES 735 735 Phosphothreonine; by MAPK14.
{ECO:0000269|PubMed:12058067,
ECO:0000269|PubMed:20188673}.
MOD_RES 761 761 Phosphothreonine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 767 767 Phosphoserine.
{ECO:0000250|UniProtKB:Q9Z1K9}.
MOD_RES 791 791 Phosphoserine.
{ECO:0000244|PubMed:17081983,
ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163,
ECO:0000244|PubMed:24275569}.
MOD_RES 819 819 Phosphoserine.
{ECO:0000269|PubMed:12621058}.
CARBOHYD 103 103 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 157 157 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 174 174 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 264 264 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 452 452 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 498 498 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 539 539 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 551 551 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 594 594 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 225 333 {ECO:0000269|PubMed:9520379}.
DISULFID 365 469 {ECO:0000269|PubMed:9520379}.
DISULFID 423 453 {ECO:0000269|PubMed:9520379}.
DISULFID 534 555 {ECO:0000250}.
DISULFID 573 582 {ECO:0000250}.
DISULFID 578 591 {ECO:0000250}.
DISULFID 593 600 {ECO:0000250}.
VAR_SEQ 695 824 Missing (in isoform B).
{ECO:0000303|PubMed:9034190}.
/FTId=VSP_005478.
VARIANT 162 162 K -> E (in dbSNP:rs34431503).
/FTId=VAR_051586.
VARIANT 202 202 R -> G (in dbSNP:rs2230818).
/FTId=VAR_051587.
CONFLICT 109 109 V -> A (in Ref. 3; AAC39721).
{ECO:0000305}.
CONFLICT 563 563 D -> N (in Ref. 3; AAC39721).
{ECO:0000305}.
CONFLICT 801 801 T -> A (in Ref. 3; AAC39721).
{ECO:0000305}.
CONFLICT 818 818 D -> N (in Ref. 3; AAC39721).
{ECO:0000305}.
HELIX 220 222 {ECO:0000244|PDB:3L0V}.
STRAND 224 231 {ECO:0000244|PDB:2DDF}.
HELIX 233 238 {ECO:0000244|PDB:2DDF}.
TURN 239 242 {ECO:0000244|PDB:3EDZ}.
HELIX 244 263 {ECO:0000244|PDB:2DDF}.
STRAND 269 271 {ECO:0000244|PDB:2DDF}.
STRAND 276 284 {ECO:0000244|PDB:2DDF}.
STRAND 300 302 {ECO:0000244|PDB:2DDF}.
STRAND 309 311 {ECO:0000244|PDB:2DDF}.
HELIX 314 324 {ECO:0000244|PDB:2DDF}.
HELIX 326 329 {ECO:0000244|PDB:2DDF}.
STRAND 332 339 {ECO:0000244|PDB:2DDF}.
HELIX 344 346 {ECO:0000244|PDB:2DDF}.
STRAND 349 354 {ECO:0000244|PDB:2DDF}.
STRAND 355 357 {ECO:0000244|PDB:3O64}.
STRAND 363 365 {ECO:0000244|PDB:3O64}.
STRAND 368 371 {ECO:0000244|PDB:2DDF}.
TURN 372 375 {ECO:0000244|PDB:2DDF}.
STRAND 376 379 {ECO:0000244|PDB:2DDF}.
STRAND 382 389 {ECO:0000244|PDB:2DDF}.
HELIX 396 410 {ECO:0000244|PDB:2DDF}.
STRAND 418 420 {ECO:0000244|PDB:3CKI}.
TURN 421 423 {ECO:0000244|PDB:2DDF}.
HELIX 427 429 {ECO:0000244|PDB:2DDF}.
STRAND 436 438 {ECO:0000244|PDB:3CKI}.
STRAND 442 444 {ECO:0000244|PDB:3LGP}.
TURN 445 448 {ECO:0000244|PDB:2DDF}.
HELIX 452 469 {ECO:0000244|PDB:2DDF}.
HELIX 583 586 {ECO:0000244|PDB:2M2F}.
STRAND 589 591 {ECO:0000244|PDB:2M2F}.
HELIX 597 600 {ECO:0000244|PDB:2M2F}.
STRAND 603 605 {ECO:0000244|PDB:2M2F}.
STRAND 611 613 {ECO:0000244|PDB:2M2F}.
STRAND 631 636 {ECO:0000244|PDB:2M2F}.
TURN 637 639 {ECO:0000244|PDB:2M2F}.
SEQUENCE 824 AA; 93021 MW; 5B1032F6B88A837F CRC64;
MRQSLLFLTS VVPFVLAPRP PDDPGFGPHQ RLEKLDSLLS DYDILSLSNI QQHSVRKRDL
QTSTHVETLL TFSALKRHFK LYLTSSTERF SQNFKVVVVD GKNESEYTVK WQDFFTGHVV
GEPDSRVLAH IRDDDVIIRI NTDGAEYNIE PLWRFVNDTK DKRMLVYKSE DIKNVSRLQS
PKVCGYLKVD NEELLPKGLV DREPPEELVH RVKRRADPDP MKNTCKLLVV ADHRFYRYMG
RGEESTTTNY LIELIDRVDD IYRNTSWDNA GFKGYGIQIE QIRILKSPQE VKPGEKHYNM
AKSYPNEEKD AWDVKMLLEQ FSFDIAEEAS KVCLAHLFTY QDFDMGTLGL AYVGSPRANS
HGGVCPKAYY SPVGKKNIYL NSGLTSTKNY GKTILTKEAD LVTTHELGHN FGAEHDPDGL
AECAPNEDQG GKYVMYPIAV SGDHENNKMF SNCSKQSIYK TIESKAQECF QERSNKVCGN
SRVDEGEECD PGIMYLNNDT CCNSDCTLKE GVQCSDRNSP CCKNCQFETA QKKCQEAINA
TCKGVSYCTG NSSECPPPGN AEDDTVCLDL GKCKDGKCIP FCEREQQLES CACNETDNSC
KVCCRDLSGR CVPYVDAEQK NLFLRKGKPC TVGFCDMNGK CEKRVQDVIE RFWDFIDQLS
INTFGKFLAD NIVGSVLVFS LIFWIPFSIL VHCVDKKLDK QYESLSLFHP SNVEMLSSMD
SASVRIIKPF PAPQTPGRLQ PAPVIPSAPA APKLDHQRMD TIQEDPSTDS HMDEDGFEKD
PFPNSSTAAK SFEDLTDHPV TRSEKAASFK LQRQNRVDSK ETEC


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