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      <location issue="15" pages="3589-97" volume="30"/>
      <year>1991</year>
    </publication>
    <publication id="PUB00003499">
      <author_list>Pallas DC, Weller W, Jaspers S, Miller TB, Lane WS, Roberts TM.</author_list>
      <title>The third subunit of protein phosphatase 2A (PP2A), a 55-kilodalton protein which is apparently substituted for by T antigens in complexes with the 36- and 63-kilodalton PP2A subunits, bears little resemblance to T antigens.</title>
      <db_xref db="PUBMED" dbkey="1370560"/>
      <journal>J. Virol.</journal>
      <location issue="2" pages="886-93" volume="66"/>
      <year>1992</year>
    </publication>
  </pub_list>
  <contains>
    <rel_ref ipr_ref="IPR001680"/>
    <rel_ref ipr_ref="IPR011046"/>
    <rel_ref ipr_ref="IPR018067"/>
    <rel_ref ipr_ref="IPR019775"/>
    <rel_ref ipr_ref="IPR019781"/>
  </contains>
  <member_list>
    <db_xref protein_count="326" db="PANTHER" dbkey="PTHR11871" name="Pp2A_PR55"/>
    <db_xref protein_count="224" db="PIRSF" dbkey="PIRSF037309" name="PP2A_PR55"/>
    <db_xref protein_count="332" db="PRINTS" dbkey="PR00600" name="PP2APR55"/>
  </member_list>
  <external_doc_list>
    <db_xref db="MSDsite" dbkey="PS01024"/>
    <db_xref db="MSDsite" dbkey="PS01025"/>
    <db_xref db="BLOCKS" dbkey="IPB000009"/>
    <db_xref db="PROSITEDOC" dbkey="PDOC00785"/>
  </external_doc_list>
  <taxonomy_distribution>
    <taxon_data name="Bacteria" proteins_count="2"/>
    <taxon_data name="Cyanobacteria" proteins_count="1"/>
    <taxon_data name="Eukaryota" proteins_count="337"/>
    <taxon_data name="Arabidopsis thaliana" proteins_count="5"/>
    <taxon_data name="Rice spp." proteins_count="15"/>
    <taxon_data name="Fungi" proteins_count="73"/>
    <taxon_data name="Saccharomyces cerevisiae" proteins_count="6"/>
    <taxon_data name="Other Eukaryotes" proteins_count="3"/>
    <taxon_data name="Other Eukaryotes" proteins_count="1"/>
    <taxon_data name="Nematoda" proteins_count="1"/>
    <taxon_data name="Caenorhabditis elegans" proteins_count="1"/>
    <taxon_data name="Arthropoda" proteins_count="77"/>
    <taxon_data name="Fruit Fly" proteins_count="2"/>
    <taxon_data name="Chordata" proteins_count="76"/>
    <taxon_data name="Human" proteins_count="18"/>
    <taxon_data name="Mouse" proteins_count="10"/>
    <taxon_data name="Other Eukaryotes" proteins_count="2"/>
    <taxon_data name="Plastid Group" proteins_count="59"/>
    <taxon_data name="Green Plants" proteins_count="59"/>
    <taxon_data name="Metazoa" proteins_count="243"/>
    <taxon_data name="Plastid Group" proteins_count="4"/>
    <taxon_data name="Plastid Group" proteins_count="14"/>
    <taxon_data name="Other Eukaryotes" proteins_count="6"/>
    <taxon_data name="Other Eukaryotes" proteins_count="4"/>
  </taxonomy_distribution>
</interpro>
<interpro id="IPR000010" protein_count="956" short_name="Prot_inh_cystat" type="Domain">
  <name>Proteinase inhibitor I25, cystatin</name>
  <abstract>
<p>Peptide proteinase inhibitors can be found as single domain proteins or as single or multiple domains within proteins; these are referred to as either simple or compound inhibitors, respectively. In many cases they are synthesised as part of a lar...
<p>The cystatins are cysteine proteinase inhibitors belonging to MEROPS inhibitor family I25, clan IH [<cite idref="PUB00003412"/>, <cite idref="PUB00014312"/>, <cite idref="PUB00001614"/>]. They mainly inhibit peptidases belonging to peptidase famil...
<ul>
<li>
The Type 1 cystatins, which are intracellular cystatins that are present in the cytosol of many cell types, but can also appear in body fluids at significant concentrations. They are single-chain polypeptides of about 100 residues, which have neither...
<li>The Type 2 cystatins, which are mainly extracellular secreted polypeptides synthesised with a 19-28 residue signal peptide. They are broadly distributed  and found in most body fluids. </li>
<li>The Type 3 cystatins, which are multidomain proteins. The mammalian representatives of this group are the kininogens. There are three different kininogens in mammals: H- (high molecular mass, <db_xref db="INTERPRO" dbkey="IPR002395"/>) and L- (lo...
<li>Unclassified cystatins. These are cystatin-like proteins found in a range of organisms: plant phytocystatins, fetuin in mammals, insect cystatins and a puff adder venom cystatin which inhibits metalloproteases  of the MEROPS peptidase family M12 ...
    </ul>
<p>All true cystatins inhibit cysteine peptidases of the papain family (MEROPS peptidase family C1), and some also inhibit legumain family enzymes (MEROPS peptidase family C13). These peptidases play key roles in physiological processes, such as intr...
</abstract>
  <class_list>
    <classification id="GO:0004869" class_type="GO">
      <category>Molecular Function</category>
      <description>cysteine-type endopeptidase inhibitor activity</description>
    </classification>
  </class_list>
  <example_list>
    <example>
      <db_xref db="SWISSPROT" dbkey="O08677"/>
    </example>
    <example>
      <db_xref db="SWISSPROT" dbkey="O76096"/>
    </example>
    <example>
      <db_xref db="SWISSPROT" dbkey="P09229"/>
    </example>
    <example>
      <db_xref db="SWISSPROT" dbkey="P23779"/>
    </example>
    <example>
      <db_xref db="SWISSPROT" dbkey="Q41906"/>
    </example>
  </example_list>
  <pub_list>
    <publication id="PUB00001614">
      <author_list>Turk V, Bode W.</author_list>
      <title>The cystatins: protein inhibitors of cysteine proteinases.</title>
      <db_xref db="PUBMED" dbkey="1855589"/>
      <journal>FEBS Lett.</journal>
      <location issue="2" pages="213-9" volume="285"/>
      <year>1991</year>
    </publication>
    <publication id="PUB00003412">
      <author_list>Rawlings ND, Barrett AJ.</author_list>
      <title>Evolution of proteins of the cystatin superfamily.</title>
      <db_xref db="PUBMED" dbkey="2107324"/>
      <journal>J. Mol. Evol.</journal>
      <location issue="1" pages="60-71" volume="30"/>
      <year>1990</year>
    </publication>
    <publication id="PUB00014312">
      <author_list>Abrahamson M, Alvarez-Fernandez M, Nathanson CM.</author_list>
      <title>Cystatins.</title>
      <db_xref db="PUBMED" dbkey="14587292"/>
      <journal>Biochem. Soc. Symp.</journal>
      <location issue="70" pages="179-99"/>
      <year>2003</year>
    </publication>
  </pub_list>
  <child_list>