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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_RAT               Reviewed;         827 AA.
Q9Z1K9;
20-JUN-2001, integrated into UniProtKB/Swiss-Prot.
01-MAY-1999, sequence version 1.
23-MAY-2018, entry version 138.
RecName: Full=Disintegrin and metalloproteinase domain-containing protein 17;
Short=ADAM 17;
EC=3.4.24.86;
AltName: Full=TNF-alpha convertase;
AltName: Full=TNF-alpha-converting enzyme;
AltName: CD_antigen=CD156b;
Flags: Precursor;
Name=Adam17; Synonyms=Tace;
Rattus norvegicus (Rat).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Rattus.
NCBI_TaxID=10116;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Testis;
Hall L., Beaumont A.J., Jury J.A., Frayne J.;
"Sequence analysis of rat TNF-alpha converting enzyme (TACE) cDNA.";
Submitted (NOV-1998) to the EMBL/GenBank/DDBJ databases.
[2]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-770 AND SER-794, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22673903; DOI=10.1038/ncomms1871;
Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A.,
Lundby C., Olsen J.V.;
"Quantitative maps of protein phosphorylation sites across 14
different rat organs and tissues.";
Nat. Commun. 3:876-876(2012).
[3]
CLEAVAGE OF SIGNAL PEPTIDE AFTER ALA-17, AND IDENTIFICATION BY MASS
SPECTROMETRY.
PubMed=26479776; DOI=10.1021/acs.jproteome.5b00820;
Tsuchiya T., Osaki T., Minamino N., Sasaki K.;
"Peptidomics for studying limited proteolysis.";
J. Proteome Res. 14:4921-4931(2015).
-!- 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). Plays a role in the proteolytic processing of ACE2 (By
similarity). {ECO:0000250}.
-!- 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:
Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
Evidence={ECO:0000250|UniProtKB:P78536};
Note=Binds 1 zinc ion per subunit. {ECO:0000250|UniProtKB:P78536};
-!- SUBUNIT: Interacts with MAD2L1, MAPK14 and MUC1. {ECO:0000250}.
-!- SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane
protein.
-!- 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-822 but
decreases phosphorylation of Ser-794. Phosphorylation at THR-735
by MAPK14 is required for ADAM17-mediated ectodomain shedding (By
similarity). {ECO:0000250}.
-----------------------------------------------------------------------
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EMBL; AJ012603; CAA10072.1; -; mRNA.
RefSeq; NP_064702.1; NM_020306.2.
UniGene; Rn.144585; -.
ProteinModelPortal; Q9Z1K9; -.
SMR; Q9Z1K9; -.
IntAct; Q9Z1K9; 1.
STRING; 10116.ENSRNOP00000010648; -.
BindingDB; Q9Z1K9; -.
ChEMBL; CHEMBL2523; -.
MEROPS; M12.217; -.
iPTMnet; Q9Z1K9; -.
PhosphoSitePlus; Q9Z1K9; -.
PaxDb; Q9Z1K9; -.
PRIDE; Q9Z1K9; -.
GeneID; 57027; -.
KEGG; rno:57027; -.
CTD; 6868; -.
RGD; 620404; Adam17.
eggNOG; KOG3658; Eukaryota.
eggNOG; ENOG410XQWB; LUCA.
HOGENOM; HOG000033797; -.
HOVERGEN; HBG050457; -.
InParanoid; Q9Z1K9; -.
KO; K06059; -.
PhylomeDB; Q9Z1K9; -.
BRENDA; 3.4.24.86; 5301.
PRO; PR:Q9Z1K9; -.
Proteomes; UP000002494; Unplaced.
GO; GO:0009986; C:cell surface; IDA:RGD.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0005886; C:plasma membrane; IDA:RGD.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0004222; F:metalloendopeptidase activity; IMP:RGD.
GO; GO:0008237; F:metallopeptidase activity; IMP:RGD.
GO; GO:0005112; F:Notch binding; ISS:UniProtKB.
GO; GO:0017124; F:SH3 domain binding; IEA:UniProtKB-KW.
GO; GO:0006509; P:membrane protein ectodomain proteolysis; IMP:RGD.
GO; GO:0043066; P:negative regulation of apoptotic process; IDA:RGD.
GO; GO:0007220; P:Notch receptor processing; ISS:UniProtKB.
GO; GO:0007219; P:Notch signaling pathway; IEA:UniProtKB-KW.
GO; GO:0006508; P:proteolysis; ISS:UniProtKB.
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;
Cleavage on pair of basic residues; Complete proteome; Disulfide bond;
Glycoprotein; Hydrolase; Membrane; Metal-binding; Metalloprotease;
Notch signaling pathway; Phosphoprotein; Protease; Reference proteome;
SH3-binding; Signal; Transmembrane; Transmembrane helix; Zinc;
Zymogen.
SIGNAL 1 17 {ECO:0000269|PubMed:26479776}.
PROPEP 18 214 {ECO:0000250|UniProtKB:P78536}.
/FTId=PRO_0000029092.
CHAIN 215 827 Disintegrin and metalloproteinase domain-
containing protein 17.
/FTId=PRO_0000029093.
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; by MAPK14.
{ECO:0000250|UniProtKB:P78536}.
MOD_RES 764 764 Phosphothreonine.
{ECO:0000250|UniProtKB:P78536}.
MOD_RES 770 770 Phosphoserine.
{ECO:0000244|PubMed:22673903}.
MOD_RES 794 794 Phosphoserine.
{ECO:0000244|PubMed:22673903}.
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}.
SEQUENCE 827 AA; 93017 MW; EF82239C067F2AFF CRC64;
MRQRLLFLTT LVPFVLAPRP PEEPGSGSHL RLEKLDSLLS DYDILSLSNI QQHSIRKRDL
QSATHLETLL TFSALKRHFK LYLTSSTERF SQNLRVVVVD GKEESEYSVK WQDFFSGHVV
GEPDSRVLAH IGDDDVTVRI NTDGAEYNIE PLWRFVNDTK DKRMLVYKSE DIKDFSRLQS
PKVCGYLNAD SEELLPKGLI DREPSEEFVR RVKRRAEPNP LKNTCKLLVV ADHRFYKYMG
RGEESTTTNY LIELIDRVDD IYRNTSWDNA GFKGYGVQIE QIRILKSPQE VKPGERHFNM
AKSFPNEEKD AWDVKMLLEQ FSLDIAEEAS KVCLAHLFTY QDFDMGTLGL AYVGSPRANS
HGGVCPKAYY NPGVKKNIYL NSGLTSTKNY GKTILTKEAD LVTTHELGHN FGAEHDPDGL
AECAPNEDQG GKYVMYPIAV SGDHENNKMF SNCSKQSIYK TIESKAQECF QERSNKVCGN
SRVDEGEECD PGIMYLNNDT CCNSDCTLKP GVQCSDRNSP CCKNCQFETA QKKCQEAINA
TCKGVSYCTG NSSECPPPGD AEDDTVCLDL GKCKAGKCIP FCKREQELES CACADTDNSC
KVCCRNLSGP CVPYVDAEQK NLFLRKGKPC TVGFCDMNGK CEKRVQDVIE RFWDFIDQLS
INTFGKFLAD NIVGSVLVFS LIFWIPFSIL VHCVDKKLDK QYESLSLFHH SNIEMLSSMD
SASVRIIKPF PAPQTPGRLQ ALQPAAMMPP VSAAPKLDHQ RMDTIQEDPS TDSHVDDDGF
EKDPFPNSSA AAKSFEDLTD HPVTRSEKAA SFKLQRQSRV DSKETEC


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