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0NALD2_HUMAN*   SwissProt (?) | Description Local Annotation Link Reference
General Information
DescriptionN-acetylated-alpha-linked acidic dipeptidase ii (ec (naaladase ii).
SpeciesHomo sapiens (NCBI taxonomy ID: 9606)
GO0016021 integral to membrane (NAS)
0004180 carboxypeptidase activity (NAS)
0016805 dipeptidase activity (NAS)
0004274 dipeptidyl-peptidase IV activity (NAS)
0006508 proteolysis and peptidolysis (NAS)

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schematic display of those terms with internal associations, click the node and browse the corresponding GO term
Domain Architecture (Details)
InterPro domains unassigned to SynO:
This entry represents the dimerisation domain found in the transferrin receptor.s well as in a number of other proteins including glutamate carboxypeptidase II and N-acetylated-alpha-linked acidic dipeptidase like protein. The transferrin receptor (TfR) assists iron uptake into vertebrate cells through a cycle of endo- and exocytosis of the iron transport protein transferrin (Tf). TfR binds iron-loaded (diferric) Tf at the cell surface and carries it to the the iron dissociates from Tf. The apo-Tf remains bound to TfR until it reaches the cell apo-Tf is replaced by diferric Tf from the serum to begin the cycle again. Human TfR is a homodimeric type II transmembrane protein. The crystal structure of a TfR monomer reveals a 3-domain structure: a protease-like domain that closely resembles carboxy- and amino-peptidases; an apical domain consisting of a beta-sandwich; and a helical dimerisation domain. The dimerisation domain consists of a 4-helical bundle that makes contact with each of the three domains in the dimer partner .
  IPR007365:Transferrin receptor-like dimerisation region
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 domain is found in metallopeptidases belonging to the MEROPS peptidase family M28 (aminopeptidase Y.lan MH) . They also contain a transferrin receptor-like dimerisation domain () and a protease-associated PA domain ().
  IPR007484:Peptidase M28
The PA (Protease associated) domain is found as an insert domain in diverse proteases.hich include the MEROPS peptidase families A22B.28.nd S8A . The PA domain is also found in a plant vacuolar sorting receptor and members of the RZF family..g. .
  IPR003137:Protease-associated PA
SequencesProtein: NALD2_HUMAN (740 aa)
mRNA: NM_005467
Local Annotation
Synapse Ontology
sdb:0328 transmitters release and endocytosis  (Evidence:keywords)
KO assignmentK01301
  Level 3 annotation:
    glutamate carboxypeptidase II
  Level 2 annotation:
    Other amino acid metabolism
Loci Structure (Details)Loci index, Chromosomal location, Length, Possible relational loci clusterExon1: 43 residues, 89507529-89507656Exon2: 39 residues, 89508374-89508486Exon3: 64 residues, 89520145-89520332Exon4: 36 residues, 89521821-89521923Exon5: 44 residues, 89523297-89523423Exon6: 64 residues, 89525113-89525300Exon7: 33 residues, 89530960-89531054Exon8: 35 residues, 89532054-89532153Exon9: 30 residues, 89535764-89535850Exon10: 42 residues, 89536125-89536245Exon11: 29 residues, 89536350-89536433Exon12: 23 residues, 89541744-89541808Exon13: 24 residues, 89542884-89542952Exon14: 32 residues, 89546639-89546731Exon15: 32 residues, 89548787-89548878Exon16: 90 residues, 89550668-89550933Exon17: 29 residues, 89554435-89554517Exon18: 33 residues, 89555731-89555824Exon19: 350 residues, 89564373-89565418Exon20: 2 residues, -Jump to NALD2_HUMAN  
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