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0ADA19_HUMAN*   SwissProt (?) | Description Local Annotation Link Reference
General Information
DescriptionAdam 19 precursor (ec 3.4.24.-) (a disintegrin and metalloproteinase domain 19) (meltrin beta) (metalloprotease and disintegrin dentritic antigen marker) (maddam).
SpeciesHomo sapiens (NCBI taxonomy ID: 9606)
Domain Architecture (Details)
InterPro domains unassigned to SynO:
Metalloproteases are the most diverse of the four main types of protease.ith more than 30 families identified to date . In these enzymes. divalent cation.sually zinc.ctivates the water molecule. The metal ion is held in place by amino acid ligands.sually three in number. The known metal ligands are or Lys and at least one other residue is required for catalysis.hich may play an electrophillic role. Of the known metalloproteases.round half contain an HEXXH motif.hich has been shown in crystallographic studies to form part of the metal-binding site . The HEXXH motif is relatively common.ut can be more stringently defined for metalloproteases as a is most often valine or threonine and forms part of the S1 subsite in thermolysin and neprilysin. is an uncharged residue.nd c a hydrophobic residue. Proline is never found in this site.ossibly because it would break the helical structure adopted by this motif in metalloproteases .Peptidases are grouped into clans and families. Clans are groups of families for which there is evidence of common ancestry. Families are grouped by their catalytic type.he first character representing the catalytic type: A.spartic; C.ysteine; G.lutamic acid; M.etallo; S.erine; T.hreonine; and U.nknown. A clan that contains families of more than one type is described as being of type P. The serine.hreonine and cysteine peptidases utilise the catalytic part of an amino acid as a nucleophile and form an acyl intermediate - these peptidases can also readily act as transferases. In the case of aspartic.lutamic and metallopeptidases.he nucleophile is an activated water molecule. This group of metallopeptidases belong to the MEROPS peptidase family M12.ubfamily M12B (adamalysin family.lan (MA(M)). The protein fold of the peptidase domain for members of this family resembles that of thermolysin.he 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 .nd 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. CD molecules are leucocyte antigens on cell surfaces (CD antigens nomenclature is updated at
  IPR001590:Peptidase M12B, ADAM/reprolysin
An ADAM is a transmembrane protein that contains a disintegrin and metalloprotease domain (MEROPS peptidase family M12B). All members of the ADAM family display a common domain organization - a pro-domain.he metalloprotease.isintigrin.ysteine-rich.pidermal-growth factor like.nd transmembrane domains and a C-terminal cytoplasmic tail. They possess four potential functions: proteolysis.ell adhesion.ell fusion.nd cell signaling. ADAMs are membrane-anchored proteases that proteolytically modify cell surface and extracellular matrix (ECM) in order to alter cell behaviour.They are responsible for the proteolytic cleavage of transmembrane proteins and release of their extracellular domain .The ADAM cysteine-rich domain is not found in plant.rchaeal.acterial or viral proteins. The cysteine-rich domain complements the binding capacity of the disintegrindomain.nd perhaps imparts specificity to disintegrin domain-mediated interactions. It has been shown that the cysteine-rich domain of ADAM13 regulates the proteins metalloprotease activity .
  IPR006586:ADAM, cysteine-rich
This signature covers the region of the propeptide for members of the MEROPS peptidase family M12B (clan MA(M).damalysin family). The propeptide contains a sequence motif similar to the "cysteine switch" of the matrixins.hich mediate cell-cell or cell-matrix interactions.
  IPR002870:Peptidase M12B, propeptide
The adhesion of platelets to the extracellular matrix.nd platelet-platelet essential in thrombosis and haemostasis . Platelets adhere to damaged blood vessels.elease biologically active chemicals.nd aggregate. function that is inhibited in normal blood . The binding of fibrinogen to the glycoprotein IIb/IIIa complex of activated platelets is essential to platelet aggregation and is induced by many agonists.ncluding ADP.ollagen.hrombin.pinephrine and prostaglandin endoperoxide analogue.Snake venoms affect blood coagulation and platelet function in a complex manner : some induce aggregation and release reactions.nd some inhibit them . Disintegrin. component of some snake venoms.ather than inhibiting the release reactions.perates by inhibiting platelet aggregation.locking the binding of fibrinogen to the receptor-glyco-protein complex of activated platelets . They act by binding to the integrin glycoprotein IIb-IIIa receptor on the platelet surface and inhibit aggregation induced by ADP.hrombin.latelet-activating factor and collagen. The role of disintegrin in preventing blood coagulation renders it of medical interest.articularly with regard to its use as an anti-coagulant .Disintegrins are peptides of about 70 amino acid residues that contain many cysteines all involved in disulphide bonds . Disintegrins contain an Arg-Gly-Asp (RGD) sequence. recognition site of many adhesion proteins. The RGD sequence of disintegrins is postulated to interact with the glycoprotein IIb-IIIa complex.The sequences of disintegrins from different snake species are known. These proteins are known as: albolabrin.pplagin.arbourin.atroxostatin.itistatin.chistatin.legantin.risticophin.lavoridin.alysin.istrin.ergeminin and triflavin.Some other proteins are known to contain a disintegrin domain:Some snake venom zinc metalloproteinases consist of an N-terminal catalytic domain fused to a disintegrin domain. Such is the case for trimerelysin I (HR1B).trolysin e (Ht-e) and trigramin. It has been suggested that these proteinases are able to cleave themselves from the disintegrin domains and that the latter may arise from such a post-translational processing.The beta-subunit of guinea pig sperm surface protein PH30 . PH30 is a protein involved in sperm-egg fusion. The beta subunit contains a disintegrin at the N-terminal extremity.Mammalian epididymial apical protein 1 (EAP I) . EAP I is associated with the sperm membrane and may play a role in sperm maturation. Structurally.AP I consists of an N-terminal domain.ollowed by a zinc metalloproteinase domain. disintegrin domain.nd a large C-terminal domain that contains a transmembrane region.The schematic representation of the structure of a typical disintegrin is shown below:
A sequence of about thirty to forty amino-acid residues long found in the sequence of epidermal growth factor (EGF)has been shown to be present.n a moreor less conserved form.n a large number of other.ostly animal proteins. The list of proteins currently known tocontain one or more copies of an EGF-like pattern is large and varied. The functional significance of EGF domains inwhat appear to be unrelated proteins is not yet clear. However. common feature is that these repeats are found inthe extracellular domain of membrane-bound proteins or in proteins known to be secreted (exception: prostaglandinG/H synthase). The EGF domain includes six cysteine residues which have been shown (in EGF) to be involved in disulphidebonds. The main structure is a two-stranded beta-sheet followed by a loop to a C-terminal short two-stranded sheet.Subdomains between the conserved cysteines vary in length.This entry contains EGF domains found in a variety of extracellular and membrane proteins
  IPR013111:EGF, extracellular
SequencesProtein: ADA19_HUMAN (956 aa)
mRNA: NM_023038
Local Annotation
Synapse Ontology
The formation of a synapse.
sdb:0034 synaptogenesis  (Evidence:keywords)
KO assignmentK01417
  Level 3 annotation:
  Level 2 annotation:
    Other enzymes
Loci Structure (Details)Loci index, Chromosomal location, Length, Possible relational loci clusterExon1: 171 residues, 156841019-156841529Exon2: 77 residues, 156847850-156848075Exon3: 30 residues, 156848687-156848772Exon4: 50 residues, 156849895-156850040Exon5: 38 residues, 156851200-156851309Exon6: 28 residues, 156851420-156851498Exon7: 70 residues, 156852558-156852763Exon8: 38 residues, 156854272-156854381Exon9: 67 residues, 156856479-156856675Exon10: 32 residues, 156859158-156859248Exon11: 61 residues, 156862388-156862566Exon12: 48 residues, 156865254-156865394Exon13: 30 residues, 156866641-156866726Exon14: 57 residues, 156868886-156869053Exon15: 26 residues, 156873019-156873091Exon16: 24 residues, 156878408-156878474Exon17: 66 residues, 156879424-156879617Exon18: 27 residues, 156890392-156890469Exon19: 28 residues, 156897498-156897577Exon20: 25 residues, 156923958-156924029Exon21: 30 residues, 156930480-156930565Exon22: 56 residues, 156935184-156935346Exon23: 2 residues, -Jump to ADA19_HUMAN  
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Loci Cluster (Details)Loci: 4749 157145874-157218746 ~-73K 29851(EPN4)(-)Loci: 4748 156841019-156935346 ~-94K 29845(ADAM19)(-)Link out to UCSC