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

 ADA17_MOUSE             Reviewed;         827 AA.
Q9Z0F8; O88726; Q505A7; Q9R1U4; Q9Z0K3;
20-JUN-2001, integrated into UniProtKB/Swiss-Prot.
27-JUL-2011, sequence version 3.
08-MAY-2019, entry version 189.
RecName: Full=Disintegrin and metalloproteinase domain-containing protein 17;
Short=ADAM 17;
EC=3.4.24.86 {ECO:0000250|UniProtKB:P78536};
AltName: Full=TNF-alpha convertase;
AltName: Full=TNF-alpha-converting enzyme;
AltName: CD_antigen=CD156b;
Flags: Precursor;
Name=Adam17; Synonyms=Tace;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORMS LONG AND SHORT).
PubMed=10433800; DOI=10.1006/cyto.1998.0466;
Cerretti D.P., Poindexter K., Castner B.J., Means G., Copeland N.G.,
Gilbert D.J., Jenkins N.A., Black R.A., Nelson N.;
"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.";
Cytokine 11:541-551(1999).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM LONG), AND ACTIVITY REGULATION.
PubMed=9755855; DOI=10.1016/S0014-5793(98)01031-X;
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.;
"TNF-alpha converting enzyme (TACE) is inhibited by TIMP-3.";
FEBS Lett. 435:39-44(1998).
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM LONG).
PubMed=10375622; DOI=10.1016/S0378-1119(99)00155-9;
Mizui Y., Yamazaki K., Sagane K., Tanaka I.;
"cDNA cloning of mouse tumor necrosis factor-alpha converting enzyme
(TACE) and partial analysis of its promoter.";
Gene 233:67-74(1999).
[4]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM SHORT).
Cerretti D.P.;
"Isolation of murine TNF-alpha converting enzyme.";
Submitted (SEP-1996) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM LONG).
STRAIN=C57BL/6J; TISSUE=Brain cortex;
PubMed=16141072; DOI=10.1126/science.1112014;
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.;
"The transcriptional landscape of the mammalian genome.";
Science 309:1559-1563(2005).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM LONG).
STRAIN=C57BL/6J; TISSUE=Brain;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[7]
FUNCTION IN PROCESSING OF GROWTH HORMONE RECEPTOR.
PubMed=11108241; DOI=10.1210/endo.141.12.7858;
Zhang Y., Jiang J., Black R.A., Baumann G., Frank S.J.;
"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.";
Endocrinology 141:4342-4348(2000).
[8]
FUNCTION.
PubMed=10799547; DOI=10.1074/jbc.275.19.14608;
Reddy P., Slack J.L., Davis R., Cerretti D.P., Kozlosky C.J.,
Blanton R.A., Shows D., Peschon J.J., Black R.A.;
"Functional analysis of the domain structure of tumor necrosis factor-
alpha converting enzyme.";
J. Biol. Chem. 275:14608-14614(2000).
[9]
FUNCTION.
PubMed=10882063; DOI=10.1016/S1097-2765(00)80417-7;
Brou C., Logeat F., Gupta N., Bessia C., LeBail O., Doedens J.R.,
Cumano A., Roux P., Black R.A., Israel A.;
"A novel proteolytic cleavage involved in Notch signaling: the role of
the disintegrin-metalloprotease TACE.";
Mol. Cell 5:207-216(2000).
[10]
FUNCTION.
PubMed=12907434; DOI=10.1182/blood-2003-04-1305;
Bergmeier W., Burger P.C., Piffath C.L., Hoffmeister K.M.,
Hartwig J.H., Nieswandt B., Wagner D.D.;
"Metalloproteinase inhibitors improve the recovery and hemostatic
function of in vitro-aged or -injured mouse platelets.";
Blood 102:4229-4235(2003).
[11]
FUNCTION, AND CATALYTIC ACTIVITY.
PubMed=17245433; DOI=10.1038/sj.emboj.7601520;
Li N., Wang Y., Forbes K., Vignali K.M., Heale B.S., Saftig P.,
Hartmann D., Black R.A., Rossi J.J., Blobel C.P., Dempsey P.J.,
Workman C.J., Vignali D.A.;
"Metalloproteases regulate T-cell proliferation and effector function
via LAG-3.";
EMBO J. 26:494-504(2007).
[12]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-794, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
Thibault P.;
"The phagosomal proteome in interferon-gamma-activated macrophages.";
Immunity 30:143-154(2009).
[13]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-735, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Brown adipose tissue, Kidney, Lung, Spleen, and Testis;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and
expression.";
Cell 143:1174-1189(2010).
-!- 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. 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
(PubMed:10799547, PubMed:11108241). Acts as an activator of Notch
pathway by mediating cleavage of Notch, generating the membrane-
associated intermediate fragment called notch extracellular
truncation (NEXT) (PubMed:10882063). Plays a role in hemostasis
through shedding of GP1BA, the platelet glycoprotein Ib alpha
chain (PubMed:12907434). Mediates the proteolytic cleavage of
LAG3, leading to release the secreted form of LAG3
(PubMed:17245433). {ECO:0000250, ECO:0000269|PubMed:10799547,
ECO:0000269|PubMed:10882063, ECO:0000269|PubMed:11108241,
ECO:0000269|PubMed:12907434, ECO:0000269|PubMed:17245433}.
-!- CATALYTIC ACTIVITY:
Reaction=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.; EC=3.4.24.86;
Evidence={ECO:0000250|UniProtKB:P78536};
-!- COFACTOR:
Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
Evidence={ECO:0000250|UniProtKB:P78536};
Note=Binds 1 zinc ion per subunit. {ECO:0000250|UniProtKB:P78536};
-!- ACTIVITY REGULATION: Inhibited by metalloproteinase inhibitor 3
(TIMP-3), but not by TIMP-1, TIMP-2 and TIMP-4.
{ECO:0000269|PubMed:9755855}.
-!- SUBUNIT: Interacts with MAD2L1, MAPK14 and MUC1. Interacts with
iRhom1/RHBDF1 and iRhom2/RHBDF2. Interacts with FRMD8 via its
interaction with iRhom1/RHBDF1 and iRhom2/RHBDF2.
{ECO:0000250|UniProtKB:P78536}.
-!- INTERACTION:
Q80WQ6:Rhbdf2; NbExp=6; IntAct=EBI-7848498, EBI-647271;
-!- SUBCELLULAR LOCATION: Isoform Long: Cell membrane; Single-pass
type I membrane protein.
-!- SUBCELLULAR LOCATION: Isoform Short: Secreted.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=Long;
IsoId=Q9Z0F8-1; Sequence=Displayed;
Name=Short;
IsoId=Q9Z0F8-2; Sequence=VSP_005479, VSP_005480;
-!- 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.
-!- 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-822 but
decreases phosphorylation of Ser-794. Phosphorylation at THR-735
by MAPK14 is required for ADAM17-mediated ectodomain shedding (By
similarity). {ECO:0000250|UniProtKB:P78536}.
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EMBL; AF056359; AAC62934.1; -; Genomic_DNA.
EMBL; AF056345; AAC62934.1; JOINED; Genomic_DNA.
EMBL; AF056346; AAC62934.1; JOINED; Genomic_DNA.
EMBL; AF056347; AAC62934.1; JOINED; Genomic_DNA.
EMBL; AF056348; AAC62934.1; JOINED; Genomic_DNA.
EMBL; AF056349; AAC62934.1; JOINED; Genomic_DNA.
EMBL; AF056350; AAC62934.1; JOINED; Genomic_DNA.
EMBL; AF056351; AAC62934.1; JOINED; Genomic_DNA.
EMBL; AF056352; AAC62934.1; JOINED; Genomic_DNA.
EMBL; AF056353; AAC62934.1; JOINED; Genomic_DNA.
EMBL; AF056354; AAC62934.1; JOINED; Genomic_DNA.
EMBL; AF056355; AAC62934.1; JOINED; Genomic_DNA.
EMBL; AF056356; AAC62934.1; JOINED; Genomic_DNA.
EMBL; AF056357; AAC62934.1; JOINED; Genomic_DNA.
EMBL; AF056358; AAC62934.1; JOINED; Genomic_DNA.
EMBL; AJ007365; CAA07480.1; -; mRNA.
EMBL; AB021709; BAA78578.1; -; mRNA.
EMBL; U69613; AAD09627.1; -; mRNA.
EMBL; U69614; AAD09628.1; -; mRNA.
EMBL; AK139471; BAE24023.1; -; mRNA.
EMBL; BC094655; AAH94655.1; -; mRNA.
CCDS; CCDS25836.1; -. [Q9Z0F8-1]
RefSeq; NP_001264195.1; NM_001277266.1.
RefSeq; NP_001278800.1; NM_001291871.1.
RefSeq; NP_033745.4; NM_009615.6. [Q9Z0F8-1]
SMR; Q9Z0F8; -.
BioGrid; 197964; 1.
DIP; DIP-41747N; -.
IntAct; Q9Z0F8; 3.
MINT; Q9Z0F8; -.
STRING; 10090.ENSMUSP00000067953; -.
ChEMBL; CHEMBL4379; -.
MEROPS; M12.217; -.
iPTMnet; Q9Z0F8; -.
PhosphoSitePlus; Q9Z0F8; -.
SwissPalm; Q9Z0F8; -.
EPD; Q9Z0F8; -.
jPOST; Q9Z0F8; -.
PaxDb; Q9Z0F8; -.
PeptideAtlas; Q9Z0F8; -.
PRIDE; Q9Z0F8; -.
Ensembl; ENSMUST00000064536; ENSMUSP00000067953; ENSMUSG00000052593. [Q9Z0F8-1]
Ensembl; ENSMUST00000145118; ENSMUSP00000136407; ENSMUSG00000052593. [Q9Z0F8-2]
GeneID; 11491; -.
KEGG; mmu:11491; -.
UCSC; uc007ndu.2; mouse. [Q9Z0F8-1]
CTD; 6868; -.
MGI; MGI:1096335; Adam17.
eggNOG; KOG3658; Eukaryota.
eggNOG; ENOG410XQWB; LUCA.
GeneTree; ENSGT00940000155443; -.
HOGENOM; HOG000033797; -.
InParanoid; Q9Z0F8; -.
KO; K06059; -.
OMA; VCSDKNS; -.
OrthoDB; 162519at2759; -.
TreeFam; TF314733; -.
Reactome; R-MMU-193692; Regulated proteolysis of p75NTR.
Reactome; R-MMU-75893; TNF signaling.
PRO; PR:Q9Z0F8; -.
Proteomes; UP000000589; Chromosome 12.
Bgee; ENSMUSG00000052593; Expressed in 248 organ(s), highest expression level in saccule of membranous labyrinth.
ExpressionAtlas; Q9Z0F8; baseline and differential.
Genevisible; Q9Z0F8; MM.
GO; GO:0015629; C:actin cytoskeleton; ISO:MGI.
GO; GO:0045177; C:apical part of cell; ISO:MGI.
GO; GO:0016324; C:apical plasma membrane; ISO:MGI.
GO; GO:0009986; C:cell surface; ISO:MGI.
GO; GO:0005737; C:cytoplasm; IDA:MGI.
GO; GO:0031410; C:cytoplasmic vesicle; ISO:MGI.
GO; GO:0005829; C:cytosol; ISO:MGI.
GO; GO:0005576; C:extracellular region; TAS:Reactome.
GO; GO:0005615; C:extracellular space; HDA:BHF-UCL.
GO; GO:0005887; C:integral component of plasma membrane; ISO:MGI.
GO; GO:0016020; C:membrane; IDA:MGI.
GO; GO:0045121; C:membrane raft; ISO:MGI.
GO; GO:0005886; C:plasma membrane; ISO:MGI.
GO; GO:0004175; F:endopeptidase activity; ISO:MGI.
GO; GO:0005178; F:integrin binding; ISO:MGI.
GO; GO:0005138; F:interleukin-6 receptor binding; ISO:MGI.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0004222; F:metalloendopeptidase activity; ISO:MGI.
GO; GO:0008237; F:metallopeptidase activity; IDA:BHF-UCL.
GO; GO:0005112; F:Notch binding; ISS:UniProtKB.
GO; GO:0030165; F:PDZ domain binding; ISO:MGI.
GO; GO:0004252; F:serine-type endopeptidase activity; TAS:Reactome.
GO; GO:0017124; F:SH3 domain binding; IEA:UniProtKB-KW.
GO; GO:0030183; P:B cell differentiation; IMP:BHF-UCL.
GO; GO:0007155; P:cell adhesion; ISO:MGI.
GO; GO:0033627; P:cell adhesion mediated by integrin; ISO:MGI.
GO; GO:0048870; P:cell motility; IMP:BHF-UCL.
GO; GO:0071403; P:cellular response to high density lipoprotein particle stimulus; ISO:MGI.
GO; GO:0050830; P:defense response to Gram-positive bacterium; ISO:MGI.
GO; GO:0007173; P:epidermal growth factor receptor signaling pathway; ISO:MGI.
GO; GO:0002467; P:germinal center formation; IMP:BHF-UCL.
GO; GO:0006509; P:membrane protein ectodomain proteolysis; IDA:MGI.
GO; GO:0043066; P:negative regulation of apoptotic process; ISO:MGI.
GO; GO:0120163; P:negative regulation of cold-induced thermogenesis; IMP:YuBioLab.
GO; GO:0010977; P:negative regulation of neuron projection development; IGI:MGI.
GO; GO:0030512; P:negative regulation of transforming growth factor beta receptor signaling pathway; ISO:MGI.
GO; GO:0007220; P:Notch receptor processing; ISS: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:0043065; P:positive regulation of apoptotic process; ISO:MGI.
GO; GO:0043536; P:positive regulation of blood vessel endothelial cell migration; ISO:MGI.
GO; GO:0030307; P:positive regulation of cell growth; ISO:MGI.
GO; GO:0030335; P:positive regulation of cell migration; ISO:MGI.
GO; GO:0008284; P:positive regulation of cell population proliferation; ISO:MGI.
GO; GO:0051272; P:positive regulation of cellular component movement; IMP:BHF-UCL.
GO; GO:0032722; P:positive regulation of chemokine production; ISO:MGI.
GO; GO:0045737; P:positive regulation of cyclin-dependent protein serine/threonine kinase activity; ISO:MGI.
GO; GO:0045741; P:positive regulation of epidermal growth factor-activated receptor activity; ISO:MGI.
GO; GO:0070374; P:positive regulation of ERK1 and ERK2 cascade; ISO:MGI.
GO; GO:1900087; P:positive regulation of G1/S transition of mitotic cell cycle; ISO:MGI.
GO; GO:0010976; P:positive regulation of neuron projection development; ISO:MGI.
GO; GO:0001934; P:positive regulation of protein phosphorylation; ISO:MGI.
GO; GO:0010820; P:positive regulation of T cell chemotaxis; ISO:MGI.
GO; GO:0030511; P:positive regulation of transforming growth factor beta receptor signaling pathway; IMP:BHF-UCL.
GO; GO:1903265; P:positive regulation of tumor necrosis factor-mediated signaling pathway; ISO:MGI.
GO; GO:1905564; P:positive regulation of vascular endothelial cell proliferation; ISO:MGI.
GO; GO:0002532; P:production of molecular mediator involved in inflammatory response; IDA:CACAO.
GO; GO:0006508; P:proteolysis; ISS:UniProtKB.
GO; GO:0035624; P:receptor transactivation; ISO:MGI.
GO; GO:0048679; P:regulation of axon regeneration; IGI:MGI.
GO; GO:0033025; P:regulation of mast cell apoptotic process; IMP:BHF-UCL.
GO; GO:2001222; P:regulation of neuron migration; IGI:MGI.
GO; GO:0042493; P:response to drug; IMP:BHF-UCL.
GO; GO:0001666; P:response to hypoxia; ISO:MGI.
GO; GO:0032496; P:response to lipopolysaccharide; ISO:MGI.
GO; GO:0048536; P:spleen development; IMP:BHF-UCL.
GO; GO:0033077; P:T cell differentiation in thymus; IMP: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;
Alternative splicing; Cell membrane;
Cleavage on pair of basic residues; Complete proteome; Disulfide bond;
Glycoprotein; Hydrolase; Membrane; Metal-binding; Metalloprotease;
Notch signaling pathway; Phosphoprotein; Protease; Reference proteome;
Secreted; SH3-binding; Signal; Transmembrane; Transmembrane helix;
Zinc; Zymogen.
SIGNAL 1 17 {ECO:0000250|UniProtKB:Q9Z1K9}.
PROPEP 18 214 {ECO:0000250|UniProtKB:P78536}.
/FTId=PRO_0000029090.
CHAIN 215 827 Disintegrin and metalloproteinase domain-
containing protein 17.
/FTId=PRO_0000029091.
TOPO_DOM 215 671 Extracellular. {ECO:0000255}.
TRANSMEM 672 692 Helical. {ECO:0000255}.
TOPO_DOM 693 827 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}.
COMPBIAS 96 99 Poly-Val.
COMPBIAS 564 602 Cys-rich.
ACT_SITE 406 406 {ECO:0000255|PROSITE-ProRule:PRU00276,
ECO:0000255|PROSITE-ProRule:PRU10095}.
METAL 184 184 Zinc; in inhibited form. {ECO:0000250}.
METAL 405 405 Zinc; catalytic.
{ECO:0000250|UniProtKB:P78536}.
METAL 409 409 Zinc; catalytic.
{ECO:0000250|UniProtKB:P78536}.
METAL 415 415 Zinc; catalytic.
{ECO:0000250|UniProtKB:P78536}.
MOD_RES 735 735 Phosphothreonine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 764 764 Phosphothreonine.
{ECO:0000250|UniProtKB:P78536}.
MOD_RES 770 770 Phosphoserine.
{ECO:0000250|UniProtKB:Q9Z1K9}.
MOD_RES 794 794 Phosphoserine.
{ECO:0000244|PubMed:19144319}.
MOD_RES 822 822 Phosphoserine.
{ECO:0000250|UniProtKB:P78536}.
CARBOHYD 157 157 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 606 606 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 225 333 {ECO:0000250|UniProtKB:P78536}.
DISULFID 365 469 {ECO:0000250|UniProtKB:P78536}.
DISULFID 423 453 {ECO:0000250|UniProtKB:P78536}.
DISULFID 534 555 {ECO:0000250}.
DISULFID 573 582 {ECO:0000250}.
DISULFID 578 591 {ECO:0000250}.
DISULFID 593 600 {ECO:0000250}.
VAR_SEQ 639 655 GKCEKRVQDVIERFWDF -> CDFFSPYRANVRNEYRT
(in isoform Short). {ECO:0000303|Ref.4}.
/FTId=VSP_005479.
VAR_SEQ 656 827 Missing (in isoform Short).
{ECO:0000303|Ref.4}.
/FTId=VSP_005480.
CONFLICT 3 4 RR -> QS (in Ref. 2; CAA07480).
{ECO:0000305}.
CONFLICT 7 7 I -> F (in Ref. 2; CAA07480).
{ECO:0000305}.
CONFLICT 28 28 S -> A (in Ref. 2; CAA07480 and 3;
BAA78578). {ECO:0000305}.
CONFLICT 113 113 N -> D (in Ref. 1; AAC62934, 2; CAA07480,
3; BAA78578 and 4; AAD09627/AAD09628).
{ECO:0000305}.
CONFLICT 149 149 V -> I (in Ref. 2; CAA07480 and 3;
BAA78578). {ECO:0000305}.
CONFLICT 594 594 V -> I (in Ref. 1; AAC62934 and 4;
AAD09627/AAD09628). {ECO:0000305}.
CONFLICT 752 752 P -> S (in Ref. 2; CAA07480 and 3;
BAA78578). {ECO:0000305}.
CONFLICT 775 775 A -> V (in Ref. 2; CAA07480 and 3;
BAA78578). {ECO:0000305}.
SEQUENCE 827 AA; 93056 MW; 6B434F80878197F5 CRC64;
MRRRLLILTT LVPFVLAPRP PEEAGSGSHP RLEKLDSLLS DYDILSLANI QQHSIRKRDL
QSATHLETLL TFSALKRHFK LYLTSSTERF SQNLRVVVVD GKEESEYSVK WQNFFSGHVV
GEPDSRVLAH IGDDDVTVRI NTDGAEYNVE PLWRFVNDTK DKRMLVYKSE DIKDFSRLQS
PKVCGYLNAD SEELLPKGLI DREPSEEFVR RVKRRAEPNP LKNTCKLLVV ADHRFYKYMG
RGEESTTTNY LIELIDRVDD IYRNTSWDNA GFKGYGVQIE QIRILKSPQE VKPGERHFNM
AKSFPNEEKD AWDVKMLLEQ FSFDIAEEAS KVCLAHLFTY QDFDMGTLGL AYVGSPRANS
HGGVCPKAYY NPTVKKNIYL NSGLTSTKNY GKTILTKEAD LVTTHELGHN FGAEHDPDGL
AECAPNEDQG GKYVMYPIAV SGDHENNKMF SNCSKQSIYK TIESKAQECF QERSNKVCGN
SRVDEGEECD PGIMYLNNDT CCNSDCTLKP GVQCSDRNSP CCKNCQFETA QKKCQEAINA
TCKGVSYCTG NSSECPPPGD AEDDTVCLDL GKCKAGKCIP FCKREQELES CACVDTDNSC
KVCCRNLSGP CVPYVDAEQK NLFLRKGKPC TVGFCDMNGK CEKRVQDVIE RFWDFIDQLS
INTFGKFLAD NIVGSVLVFS LIFWIPFSIL VHCVDKKLDK QYESLSLFHH SNIEMLSSMD
SASVRIIKPF PAPQTPGRLQ ALQPAAMMPP VPAAPKLDHQ RMDTIQEDPS TDSHADDDGF
EKDPFPNSST AAKSFEDLTD HPVTRSEKAA SFKLQRQSRV DSKETEC


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Pathways :
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Related Genes :
[ADAM17 CSVP TACE] 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)
[Adam17 Tace] Disintegrin and metalloproteinase domain-containing protein 17 (ADAM 17) (EC 3.4.24.86) (TNF-alpha convertase) (TNF-alpha-converting enzyme) (CD antigen CD156b)
[Adam17 Tace] Disintegrin and metalloproteinase domain-containing protein 17 (ADAM 17) (EC 3.4.24.86) (TNF-alpha convertase) (TNF-alpha-converting enzyme) (CD antigen CD156b)
[ADAM10 KUZ MADM] Disintegrin and metalloproteinase domain-containing protein 10 (ADAM 10) (EC 3.4.24.81) (CDw156) (Kuzbanian protein homolog) (Mammalian disintegrin-metalloprotease) (CD antigen CD156c)
[Adam9 Kiaa0021 Mdc9 Mltng] Disintegrin and metalloproteinase domain-containing protein 9 (ADAM 9) (EC 3.4.24.-) (Meltrin-gamma) (Metalloprotease/disintegrin/cysteine-rich protein 9) (Myeloma cell metalloproteinase)
[ADAM12 MLTN UNQ346/PRO545] Disintegrin and metalloproteinase domain-containing protein 12 (ADAM 12) (EC 3.4.24.-) (Meltrin-alpha)
[sup-17 DY3.7] Disintegrin and metalloproteinase domain-containing protein 10 homolog (ADAM 10 homolog) (EC 3.4.24.81)
[Adam15 Mdc15] Disintegrin and metalloproteinase domain-containing protein 15 (ADAM 15) (EC 3.4.24.-) (AD56) (Metalloprotease RGD disintegrin protein) (Metalloproteinase-like, disintegrin-like, and cysteine-rich protein 15) (MDC-15) (Metargidin)
[ADAM19 MLTNB FKSG34] Disintegrin and metalloproteinase domain-containing protein 19 (ADAM 19) (EC 3.4.24.-) (Meltrin-beta) (Metalloprotease and disintegrin dendritic antigen marker) (MADDAM)
[ADAM28 ADAM23 MDCL] Disintegrin and metalloproteinase domain-containing protein 28 (ADAM 28) (EC 3.4.24.-) (Epididymal metalloproteinase-like, disintegrin-like, and cysteine-rich protein II) (eMDC II) (Metalloproteinase-like, disintegrin-like, and cysteine-rich protein L) (MDC-L)
[ADAM15 MDC15] Disintegrin and metalloproteinase domain-containing protein 15 (ADAM 15) (EC 3.4.24.-) (Metalloprotease RGD disintegrin protein) (Metalloproteinase-like, disintegrin-like, and cysteine-rich protein 15) (MDC-15) (Metargidin)
[TNF TNFA TNFSF2] Tumor necrosis factor (Cachectin) (TNF-alpha) (Tumor necrosis factor ligand superfamily member 2) (TNF-a) [Cleaved into: Tumor necrosis factor, membrane form (N-terminal fragment) (NTF); Intracellular domain 1 (ICD1); Intracellular domain 2 (ICD2); C-domain 1; C-domain 2; Tumor necrosis factor, soluble form]
[Adam15 Mdc15] Disintegrin and metalloproteinase domain-containing protein 15 (ADAM 15) (EC 3.4.24.-) (CRII-7) (Metalloprotease RGD disintegrin protein) (Metalloproteinase-like, disintegrin-like, and cysteine-rich protein 15) (MDC-15) (Metargidin)
[Adam24] Disintegrin and metalloproteinase domain-containing protein 24 (ADAM 24) (EC 3.4.24.-) (Testase-1)
[ADAMTS5 ADAMTS11 ADMP2] A disintegrin and metalloproteinase with thrombospondin motifs 5 (ADAM-TS 5) (ADAM-TS5) (ADAMTS-5) (EC 3.4.24.-) (A disintegrin and metalloproteinase with thrombospondin motifs 11) (ADAM-TS 11) (ADAMTS-11) (ADMP-2) (Aggrecanase-2)
[ADAMTS4 KIAA0688 UNQ769/PRO1563] A disintegrin and metalloproteinase with thrombospondin motifs 4 (ADAM-TS 4) (ADAM-TS4) (ADAMTS-4) (EC 3.4.24.82) (ADMP-1) (Aggrecanase-1)
[ADAM20] Disintegrin and metalloproteinase domain-containing protein 20 (ADAM 20) (EC 3.4.24.-)
[Adam28] Disintegrin and metalloproteinase domain-containing protein 28 (ADAM 28) (EC 3.4.24.-) (Thymic epithelial cell-ADAM) (TECADAM)
[Adam19 Mltnb] Disintegrin and metalloproteinase domain-containing protein 19 (ADAM 19) (EC 3.4.24.-) (Meltrin-beta)
[ADAMTS2 NPI] A disintegrin and metalloproteinase with thrombospondin motifs 2 (ADAM-TS 2) (ADAM-TS2) (ADAMTS-2) (EC 3.4.24.14) (Procollagen I N-proteinase) (PC I-NP) (Procollagen I/II amino propeptide-processing enzyme) (Procollagen N-endopeptidase) (pNPI)
[ADAMTS17] A disintegrin and metalloproteinase with thrombospondin motifs 17 (ADAM-TS 17) (ADAM-TS17) (ADAMTS-17) (EC 3.4.24.-)
[ADAM21] Disintegrin and metalloproteinase domain-containing protein 21 (ADAM 21) (EC 3.4.24.-)
[Adam21 Adam31] Disintegrin and metalloproteinase domain-containing protein 21 (ADAM 21) (EC 3.4.24.-) (Disintegrin and metalloproteinase domain-containing protein 31) (ADAM 31)
[Adamts2] A disintegrin and metalloproteinase with thrombospondin motifs 2 (ADAM-TS 2) (ADAM-TS2) (ADAMTS-2) (EC 3.4.24.14) (Procollagen I N-proteinase) (PC I-NP) (Procollagen I/II amino propeptide-processing enzyme) (Procollagen N-endopeptidase) (pNPI)
[ADAMTS2 PCINP PCPNI] A disintegrin and metalloproteinase with thrombospondin motifs 2 (ADAM-TS 2) (ADAM-TS2) (ADAMTS-2) (EC 3.4.24.14) (Procollagen I N-proteinase) (PC I-NP) (Procollagen I/II amino propeptide-processing enzyme) (Procollagen N-endopeptidase) (pNPI)
[TNFAIP3 OTUD7C] Tumor necrosis factor alpha-induced protein 3 (TNF alpha-induced protein 3) (EC 2.3.2.-) (EC 3.4.19.12) (OTU domain-containing protein 7C) (Putative DNA-binding protein A20) (Zinc finger protein A20) [Cleaved into: A20p50; A20p37]
[ADAMTS3 KIAA0366] A disintegrin and metalloproteinase with thrombospondin motifs 3 (ADAM-TS 3) (ADAM-TS3) (ADAMTS-3) (EC 3.4.24.-) (Procollagen II N-proteinase) (PC II-NP) (Procollagen II amino propeptide-processing enzyme)
[ADAMTS12 UNQ1918/PRO4389] A disintegrin and metalloproteinase with thrombospondin motifs 12 (ADAM-TS 12) (ADAM-TS12) (ADAMTS-12) (EC 3.4.24.-)
[MMP17 MT4MMP] Matrix metalloproteinase-17 (MMP-17) (EC 3.4.24.-) (Membrane-type matrix metalloproteinase 4) (MT-MMP 4) (MTMMP4) (Membrane-type-4 matrix metalloproteinase) (MT4-MMP) (MT4MMP)
[ADAMTS13 C9orf8 UNQ6102/PRO20085] A disintegrin and metalloproteinase with thrombospondin motifs 13 (ADAM-TS 13) (ADAM-TS13) (ADAMTS-13) (EC 3.4.24.87) (von Willebrand factor-cleaving protease) (vWF-CP) (vWF-cleaving protease)

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