ID   ADA17_PIG               Reviewed;         112 AA.
AC   O77636;
DT   20-JUN-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1998, sequence version 1.
DT   16-JUN-2009, entry version 65.
DE   RecName: Full=Disintegrin and metalloproteinase domain-containing protein 17;
DE            Short=ADAM 17;
DE            EC=3.4.24.86;
DE   AltName: Full=TNF-alpha-converting enzyme;
DE   AltName: Full=TNF-alpha convertase;
DE   AltName: CD_antigen=CD156b;
DE   Flags: Fragment;
GN   Name=ADAM17; Synonyms=TACE;
OS   Sus scrofa (Pig).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Suina; Suidae;
OC   Sus.
OX   NCBI_TaxID=9823;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   MEDLINE=99357011; PubMed=10429942; DOI=10.1016/S0945-053X(99)00024-4;
RA   Flannery C.R., Little C.B., Caterson B., Hughes C.E.;
RT   "Effects of culture conditions and exposure to catabolic stimulators
RT   (IL-1 and retinoic acid) on the expression of matrix
RT   metalloproteinases (MMPs) and disintegrin metalloproteinases (ADAMs)
RT   by articular cartilage chondrocytes.";
RL   Matrix Biol. 18:225-237(1999).
CC   -!- FUNCTION: Cleaves the membrane-bound precursor of TNF-alpha to its
CC       mature soluble form. Responsible for the proteolytic release of
CC       several other cell-surface proteins, including p75 TNF-receptor,
CC       interleukin 1 receptor type II, p55 TNF-receptor, transforming
CC       growth factor-alpha, L-selectin, growth hormone receptor, MUC1 and
CC       the amyloid precursor protein. Also involved in the activation of
CC       Notch pathway (By similarity).
CC   -!- CATALYTIC ACTIVITY: Narrow endopeptidase specificity. Cleaves Pro-
CC       Leu-Ala-Gln-Ala-|-Val-Arg-Ser-Ser-Ser in the membrane-bound, 26-
CC       kDa form of tumor necrosis factor alpha (TNF-alpha). Similarly
CC       cleaves other membrane-anchored, cell-surface proteins to 'shed'
CC       the extracellular domains.
CC   -!- COFACTOR: Binds 1 zinc ion per subunit (By similarity).
CC   -!- SUBUNIT: Interacts with MAD2L1 and MUC1 (By similarity).
CC   -!- SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane
CC       protein (By similarity).
CC   -!- DOMAIN: Must be membrane anchored to cleave the different
CC       substrates. The cytoplasmic domain is not required for the this
CC       activity. Only the catalytic domain is essential to shed TNF and
CC       p75 TNFR (By similarity).
CC   -!- PTM: The precursor is cleaved by a furin endopeptidase (By
CC       similarity).
CC   -!- PTM: Phosphorylated (By similarity).
CC   -!- SIMILARITY: Contains 1 peptidase M12B domain.
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DR   EMBL; AF069648; AAC23532.1; -; mRNA.
DR   UniGene; Ssc.57075; -.
DR   HSSP; P78536; 1BKC.
DR   SMR; O77636; 1-112.
DR   MEROPS; M12.217; -.
DR   HOVERGEN; O77636; -.
DR   BRENDA; 3.4.24.86; 249.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0004222; F:metalloendopeptidase activity; IMP:UniProtKB.
DR   GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0006509; P:membrane protein ectodomain proteolysis; IMP:UniProtKB.
DR   GO; GO:0007219; P:Notch signaling pathway; IEA:UniProtKB-KW.
DR   InterPro; IPR006025; Pept_M_Zn_BS.
DR   InterPro; IPR001590; Peptidase_M12B.
DR   PROSITE; PS50215; ADAM_MEPRO; 1.
DR   PROSITE; PS00142; ZINC_PROTEASE; 1.
PE   3: Inferred from homology;
KW   Hydrolase; Membrane; Metal-binding; Metalloprotease;
KW   Notch signaling pathway; Phosphoprotein; Protease; Zinc.
FT   CHAIN        <1   >112       Disintegrin and metalloproteinase domain-
FT                                containing protein 17.
FT                                /FTId=PRO_0000078207.
FT   DOMAIN       <1   >112       Peptidase M12B.
FT   ACT_SITE     91     91       By similarity.
FT   METAL        90     90       Zinc; catalytic (By similarity).
FT   METAL        94     94       Zinc; catalytic (By similarity).
FT   METAL       100    100       Zinc; catalytic (By similarity).
FT   MOD_RES      64     64       Phosphotyrosine (By similarity).
FT   MOD_RES      67     67       Phosphoserine (By similarity).
FT   NON_TER       1      1
FT   NON_TER     112    112
SQ   SEQUENCE   112 AA;  12201 MW;  B840FBE7C2EE69FC CRC64;
     MLREQFSFDI AEEASKVCLA HLFTYQDFDM GTLGLAYVGS PRANSHGGVC PKAYYSPIGK
     KNIYLNSGLT STKNYGKTIL TKEADLVTTH ELGHNFGAEH DPDGLAECAP NE
//