SynDB Home Page
SynDB Home Page

blue bulletSynDB protein details  

Parse error: syntax error, unexpected T_VARIABLE in /home/kongl/syndb/www/sdb_nats.php on line 52
0ATS18_HUMAN*   SwissProt (?) | Description Local Annotation Link Reference
General Information
DescriptionAdamts-18 precursor (ec 3.4.24.-) (a disintegrin and metalloproteinase with thrombospondin motifs 18) (adam-ts 18) (adam-ts18).
SpeciesHomo sapiens (NCBI taxonomy ID: 9606)
Domain Architecture (Details)
InterPro domains unassigned to SynO:
This domain represents the Spacer-1 region from the ADAM-TS family of metalloproteinases .
  IPR010294:ADAM-TS Spacer 1
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
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
This repeat was first described in 1986 by Lawler and Hynes . It was found in the thrombospondin protein where it is repeated 3 times. Now a number of proteins involved in the complement pathway (properdin.6.7.8A.8B.9) as well as extracellular matrix protein like mindin.-spondin .CO-spondin and even the circumsporozoite surface protein 2 and TRAP proteins of Plasmodium .ontain one or more instance of this repeat.It has been involved in cell-cell interraction.nhibition of angiogenesis andapoptosis . The intron-exon organisation of the properdin gene confirms the hypothesis that the repeat might have evolved by a process involving exon shuffling .A study of properdin structure provides some information about the structure ofthe thrombospondin type I repeat .
  IPR000884:Thrombospondin, type I
The TSP1 (thrombospondin 1) repeat was first identified in thethrombospondin it is repeated 3 times . The domain is ~60 amino acid residues in length and is characterised by a highly conserved W-S-X-W motif and six cysteine residues. TSP1 repeats have been identified in a number of proteins including: the complement pathwayproteins properdin.6.7.8A.8B and C9; extracellular matrix proteins.ncluding mindin.DAMTS and F-spondin; Plasmodium TRAP proteins; and G protein-coupled receptors.uch as the brain-specific angiogenesis inhibitors. The domains have a number of functions.ncluding effects on cell attachment.otility.roliferation.he activities of extracellularproteases.nd inhibition of angiogenesis.ontributing to vascular homeostasis. A study of the structure of properdin indicates that the TSP1 repeat contains two amphipathic turn regions and a hydrophilic beta-strand .
  IPR008085:Thrombospondin, subtype 1
Proteolysis of the extracellular matrix plays a critical role in establishing tissue architecture during development and in tissue degradation in diseases such as cancer.rthritis.lzheimers disease and a variety of inflammatory conditions . The proteolytic enzymes responsible for this process are members of diverse protease families.ncluding the secreted zinc metalloproteases (MPs) . Recently. new MP family.DAM-TS (a disintegrin-like and metalloprotease domain with thrombospondin type I modules) has been identified. The family consists of at least 20 members that share a high degree of sequence similarity and conserved domain organisation . The defining domains of the ADAM-TS family are (from N- to C-termini) a pre-pro metalloprotease domain of the reprolysin type. snake venom disintegrin-like domain. thrombospondin type-I (TS) module. cysteine-rich region.nd a cysteine-free (spacer) domain . Domain organisation following the spacer domain C-terminus shows some variability in certain ADAM-TS members.rincipally in the number of additional TS domains. Members of the ADAM-TS family have been implicated in a range of diseases. ADAM-TS1.or example.s reported to be involved in inflammation and cancer cachexia .hilst recessively inherited ADAM-TS2 mutations cause Ehlers-Danlos syndrome type VIIC. disorder characterised clinically by severe skin fragility . ADAM-TS4 is an aggrecanase involved in arthritic destruction of cartilage .
SequencesProtein: ATS18_HUMAN (1221 aa)
mRNA: NM_199355
Local Annotation
Synapse Ontology
Calcium release from RyR (Ryanodine Receptor) in the SR (Sarcoplasmic Reticulum) is activated by the calcium induced-calcium-release
sdb:0325 RyR-CICR  (Evidence:keywords)
KO assignmentK01417
  Level 3 annotation:
  Level 2 annotation:
    Other enzymes
Loci Structure (Details)Loci index, Chromosomal location, Length, Possible relational loci clusterExon1: 514 residues, 75873928-75875469Exon2: 51 residues, 75880661-75880809Exon3: 73 residues, 75882663-75882876Exon4: 63 residues, 75884473-75884656Exon5: 70 residues, 75886320-75886525Exon6: 44 residues, 75888686-75888813Exon7: 49 residues, 75891660-75891802Exon8: 83 residues, 75911246-75911491Exon9: 43 residues, 75912476-75912600Exon10: 45 residues, 75913733-75913864Exon11: 59 residues, 75917263-75917436Exon12: 51 residues, 75927153-75927302Exon13: 34 residues, 75933101-75933197Exon14: 53 residues, 75945130-75945284Exon15: 48 residues, 75947337-75947475Exon16: 37 residues, 75950715-75950821Exon17: 55 residues, 75953502-75953662Exon18: 30 residues, 75955199-75955283Exon19: 66 residues, 75955585-75955779Exon20: 96 residues, 75958838-75959121Exon21: 107 residues, 76022692-76023009Exon22: 31 residues, 76025815-76025903Exon23: 171 residues, 76026003-76026512Exon24: 2 residues, -Jump to ATS18_HUMAN  
Tune and view alternative isoforms
Loci Cluster (Details)Loci: 4238 75873928-76026512 ~-153K 14550(ADAMTS18)(-)Loci: 2954 75782336-75791042 ~-9K 14547(+)Link out to UCSC