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Protein Domain : IPR001590

Name  Peptidase M12B, ADAM/reprolysin Short Name  Peptidase_M12B
Type  Domain Description  In the MEROPS database peptidases and peptidase homologues are grouped into clans and families. Clans are groups of families for which there is evidence of common ancestry based on a common structural fold:Each clan is identified with two letters, the first representing the catalytic type of the families included in the clan (with the letter 'P' being used for a clan containing families of more than one of the catalytic types serine, threonine and cysteine). Some families cannot yet be assigned to clans, and when a formal assignment is required, such a family is described as belonging to clan A-, C-, M-, N-, S-, T- or U-, according to the catalytic type. Some clans are divided into subclans because there is evidence of a very ancient divergence within the clan, for example MA(E), the gluzincins, and MA(M), the metzincins.Peptidase families are grouped by their catalytic type, the first character representing the catalytic type: A, aspartic; C, cysteine; G, glutamic acid; M, metallo; N, asparagine; S, serine; T, threonine; and U, unknown. The serine, threonine and cysteine peptidases utilise the amino acid as a nucleophile and form an acyl intermediate - these peptidases can also readily act as transferases. In the case of aspartic, glutamic and metallopeptidases, the nucleophile is an activated water molecule. In the case of the asparagine endopeptidases, the nucleophile is asparagine and all are self-processing endopeptidases. In many instances the structural protein fold that characterises the clan or family may have lost its catalytic activity, yet retain its function in protein recognition and binding. Metalloproteases are the most diverse of the four main types of protease, with more than 50 families identified to date. In these enzymes, a divalent cation, usually zinc, activates the water molecule. The metal ion is held in place by amino acid ligands, usually three in number. The known metal ligands are His, Glu, Asp or Lys and at least one other residue is required for catalysis, which may play an electrophillic role. Of the known metalloproteases, around half contain an HEXXH motif, which has been shown in crystallographic studies to form part of the metal-binding site []. The HEXXH motif is relatively common, but can be more stringently defined for metalloproteases as 'abXHEbbHbc', where 'a' is most often valine or threonine and forms part of the S1' subsite in thermolysin and neprilysin, 'b' is an uncharged residue, and 'c' a hydrophobic residue. Proline is never found in this site, possibly because it would break the helical structure adopted by this motif in metalloproteases [].This group of metallopeptidases belong to the MEROPS peptidase family M12, subfamily M12B (adamalysin family, clan (MA(M)). The protein fold of the peptidase domain for members of this family resembles that of thermolysin, the type example for clan MA and the predicted active site residues for members of this family and thermolysin occur in the motif HEXXH [].The adamalysins are zinc dependent endopeptidases found in snake venom. There are some mammalian proteins such as ,and fertilin . Fertilin and closely relatedproteins appear to not have some active site residues andmay not be active enzymes.CD156 (also called ADAM8 () or MS2 human) has been implicated in extravasation of leukocytes.

Publication Counts Displayer

0 Child Features

0 Contains

2 Cross References

Identifier
Source . Name

Subject . Primary Identifier
PF01421 PFAM IPR001590
PS50215 PROFILE IPR001590

3 Data Sets

Name URL
TrEMBL data set http://www.ebi.ac.uk/trembl/
InterPro data set  
InterPro GO Annotation data set  

5 Found In

DB identifier Name Short Name Type
IPR013273 Peptidase M12B, ADAM-TS Peptidase_M12B_ADAM-TS Family
IPR013277 Peptidase M12B, ADAM-TS8 Pept_M12B_ADAM-TS8 Family
IPR013276 Peptidase M12B, ADAM-TS5 Pept_M12B_ADAM-TS5 Family
IPR013275 Peptidase M12B, ADAM-TS2 Pept_M12B_ADAM-TS2 Family
IPR013274 Peptidase M12B, ADAM-TS1 Pept_M12B_ADAM-TS1 Family

2 GO Annotation


Subject . Secondary Identifier

Subject . Name

Subject . Symbol

Ontology Term . Identifier

Ontology Term . Name
Peptidase M12B, ADAM/reprolysin   GO:0004222 metalloendopeptidase activity
Peptidase M12B, ADAM/reprolysin   GO:0006508 proteolysis

2 Ontology Annotations


Subject . Secondary Identifier

Subject . Name

Subject . Symbol

Ontology Term . Identifier

Ontology Term . Name
Peptidase M12B, ADAM/reprolysin   GO:0004222 metalloendopeptidase activity
Peptidase M12B, ADAM/reprolysin   GO:0006508 proteolysis

0 Parent Features

127 Proteins

DB identifier Primary Accession
Organism . Name
FBpp0084826 Q9VAI2 Drosophila melanogaster
FBpp0084917 Q9VAC5 Drosophila melanogaster
FBpp0100122 Q59DZ3 Drosophila melanogaster
FBpp0290306 Q8MRL5 Drosophila melanogaster
FBpp0290305 Q9W493 Drosophila melanogaster
FBpp0072001 Q9W1J9 Drosophila melanogaster
FBpp0080087 Q9VJW9 Drosophila melanogaster
FBpp0300197 M9NDY9 Drosophila melanogaster
FBpp0288809 Q7KUY7 Drosophila melanogaster
FBpp0288810 B7Z0Y2 Drosophila melanogaster
FBpp0082614 Q8SXB0 Drosophila melanogaster
FBpp0308490 Q7KSH7 Drosophila melanogaster
FBpp0301591 Q9W1Z6 Drosophila melanogaster
FBpp0309702 A8DZ03 Drosophila melanogaster
FBpp0290713 Q6QU65 Drosophila melanogaster
FBpp0290714 Q400M8 Drosophila melanogaster
FBpp0290626 A8DZ02 Drosophila melanogaster
FBpp0288559 B7YZP6 Drosophila melanogaster
FBpp0301989 M9PER2 Drosophila melanogaster
FBpp0301990 M9PH86 Drosophila melanogaster
FBpp0300195 M9NH46 Drosophila melanogaster
FBpp0300196 Q9VXL1 Drosophila melanogaster
FBpp0308908 B5DZ02 Drosophila pseudoobscura
FBpp0272126 Q29FR8 Drosophila pseudoobscura
FBpp0277571 Q291N2 Drosophila pseudoobscura
FBpp0279058 Q29PB0 Drosophila pseudoobscura
FBpp0293329 Q29BU0 Drosophila pseudoobscura
FBpp0283482 Q29AS9 Drosophila pseudoobscura
FBpp0293326 I5AN91 Drosophila pseudoobscura
FBpp0283737 B5DVG7 Drosophila pseudoobscura