Reviewed, UniProtKB/Swiss-Prot O77636 (ADA17_PIG)

Names and origin

Protein names

Recommended name:
    ADAM 17
    EC=3.4.24.86
Alternative name(s):
    A disintegrin and metalloproteinase domain 17
    TNF-alpha-converting enzyme
    TNF-alpha convertase
    CD_antigen=CD156b

Gene names

Name:	ADAM17
Synonyms:	TACE

Organism

Sus scrofa (Pig)

Taxonomic identifier

9823 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Laurasiatheria › Cetartiodactyla › Suina › Suidae › Sus

Protein attributes

Sequence length	112 AA.
Sequence status	Fragment.
Sequence processing	The displayed sequence is not processed.
Protein existence	Inferred from homology.

General annotation (Comments)

Function	Cleaves the membrane-bound precursor of TNF-alpha to its mature soluble form. 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. Also involved in the activation of Notch pathway By similarity.
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.
Subunit structure	Interacts with MAD2L1 and MUC1 By similarity.
Subcellular location	Membrane; Single-pass type I membrane proteinBy similarity.
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.
Post-translational modification	The precursor is cleaved by a furin endopeptidase By similarity. Phosphorylated By similarity.
Sequence similarities	Contains 1 peptidase M12B domain.

Ontologies

Keywords
Biological process	Notch signaling pathway
Cellular component	Membrane
Ligand	Metal-binding Zinc
Molecular function	Hydrolase Metalloprotease Protease
PTM	Phosphoprotein
Gene Ontology (GO)
Biological process	Notch signaling pathway Inferred from electronic annotation. Source: UniProtKB-KW proteolysis Inferred from electronic annotation. Source: InterPro
Cellular component	membrane Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	metalloendopeptidase activity Inferred from electronic annotation. Source: InterPro zinc ion binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	‹1 – ›112	›112	ADAM 17		PRO_0000078207
Regions
	Domain	‹1 – ›112	›112	Peptidase M12B
Sites
	Active site	91	1	By similarity
	Metal binding	90	1	Zinc; catalytic By similarity
	Metal binding	94	1	Zinc; catalytic By similarity
	Metal binding	100	1	Zinc; catalytic By similarity
Amino acid modifications
	Modified residue	64	1	Phosphotyrosine By similarity
	Modified residue	67	1	Phosphoserine By similarity
Experimental info
	Non-terminal residue	1	1
	Non-terminal residue	112	1

Sequences

	Sequence		Length	Mass (Da)
	O77636-1 [UniParc]. Last modified November 1, 1998. Version 1. Checksum: B840FBE7C2EE69FC	FASTA	112	12,201
	10 20 30 40 50 60 MLREQFSFDI AEEASKVCLA HLFTYQDFDM GTLGLAYVGS PRANSHGGVC PKAYYSPIGK 70 80 90 100 110 KNIYLNSGLT STKNYGKTIL TKEADLVTTH ELGHNFGAEH DPDGLAECAP NE

References

[1]

"Effects of culture conditions and exposure to catabolic stimulators (IL-1 and retinoic acid) on the expression of matrix metalloproteinases (MMPs) and disintegrin metalloproteinases (ADAMs) by articular cartilage chondrocytes." Flannery C.R., Little C.B., Caterson B., Hughes C.E. Matrix Biol. 18:225-237(1999) [PubMed: 10429942] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].

Cross-references

Sequence databases
EMBLGenBankDDBJ	AF069648 mRNA. Translation: AAC23532.1.
UniGene	Ssc.57075
3D structure databases
HSSP	HSSP built from PDB template 1BKC based on UniProtKB P78536.
SMR	O77636. Positions 1-112.
ModBase	Search...
Protein family/group databases
MEROPS	M12.217.
Phylogenomic databases
HOVERGEN	O77636.
Family and domain databases
InterPro	IPR006025. Pept_M_Zn_BS. IPR001590. Peptidase_M12B. [Graphical view]
PROSITE	PS50215. ADAM_MEPRO. 1 hit. PS00142. ZINC_PROTEASE. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

ADA17_PIG

Accession

Primary (citable) accession number: O77636

Entry history

Integrated into UniProtKB/Swiss-Prot:	June 20, 2001
Last sequence update:	November 1, 1998
Last modified:	November 25, 2008
This is version 60 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)