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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>
t/data/interpro_relationship.xml view on Meta::CPAN
<li>The ligand-binding domain contains seven or eight 40-amino acid LDLR class A (cysteine-rich) repeats, each of which contains a coordinated calcium ion and six cysteine residues involved in disulphide bond formation [<cite idref="PUB000007...
</ul>
</p>
<p>
<ul>
<li>The second conserved region contains two EGF repeats, followed by six LDLR class B (YWTD) repeats, and another EGF repeat. The LDLR class B repeats each contain a conserved YWTD motif, and is predicted to form a beta-propeller structure [...
</ul>
</p>
<p>
<ul>
<li>The third domain is rich in serine and threonine residues and contains clustered O-linked carbohydrate chains.</li>
</ul>
</p>
<p>
<ul>
<li>The fourth domain is the hydrophobic transmembrane region.</li>
</ul>
</p>
<p>
<ul>
<li>The fifth domain is the cytoplasmic tail that directs the receptor to clathrin-coated pits.</li>
</ul>
</p>
<p>LDLR is closely related in structure to several other receptors, including LRP1, LRP1b, megalin/LRP2, VLDL receptor, lipoprotein receptor, MEGF7/LRP4, and LRP8/apolipoprotein E receptor2); these proteins participate in a wide range of physiologica...
<p>This entry represents the LDLR classB (YWTD) repeat, the structure of which has been solved [<cite idref="PUB00017010"/>]. The six YWTD repeats together fold into a six-bladed beta-propeller. Each blade of the propeller consists of four antiparall...
</abstract>
<class_list>
<classification id="GO:0016020" class_type="GO">
<category>Cellular Component</category>
<description>membrane</description>
</classification>
</class_list>
<example_list>
<example>
<db_xref db="SWISSPROT" dbkey="P01130"/>
</example>
<example>
<db_xref db="SWISSPROT" dbkey="P01132"/>
</example>
<example>
<db_xref db="SWISSPROT" dbkey="P13368"/>
</example>
<example>
<db_xref db="SWISSPROT" dbkey="P98158"/>
</example>
<example>
<db_xref db="SWISSPROT" dbkey="Q04833"/>
</example>
</example_list>
<pub_list>
<publication id="PUB00000798">
<author_list>Yamamoto T, Davis CG, Brown MS, Schneider WJ, Casey ML, Goldstein JL, Russell DW.</author_list>
<title>The human LDL receptor: a cysteine-rich protein with multiple Alu sequences in its mRNA.</title>
<db_xref db="PUBMED" dbkey="6091915"/>
<journal>Cell</journal>
<location issue="1" pages="27-38" volume="39"/>
<year>1984</year>
</publication>
<publication id="PUB00003391">
<author_list>Springer TA.</author_list>
<title>An extracellular beta-propeller module predicted in lipoprotein and scavenger receptors, tyrosine kinases, epidermal growth factor precursor, and extracellular matrix components.</title>
<db_xref db="PUBMED" dbkey="9790844"/>
<journal>J. Mol. Biol.</journal>
<location issue="4" pages="837-62" volume="283"/>
<year>1998</year>
</publication>
<publication id="PUB00004868">
<author_list>Daly NL, Scanlon MJ, Djordjevic JT, Kroon PA, Smith R.</author_list>
<title>Three-dimensional structure of a cysteine-rich repeat from the low-density lipoprotein receptor.</title>
<db_xref db="PUBMED" dbkey="7603991"/>
<journal>Proc. Natl. Acad. Sci. U.S.A.</journal>
<location issue="14" pages="6334-8" volume="92"/>
<year>1995</year>
</publication>
<publication id="PUB00042617">
<author_list>May P, Woldt E, Matz RL, Boucher P.</author_list>
<title>The LDL receptor-related protein (LRP) family: an old family of proteins with new physiological functions.</title>
<db_xref db="PUBMED" dbkey="17457719"/>
<journal>Ann. Med.</journal>
<location issue="3" pages="219-28" volume="39"/>
<year>2007</year>
</publication>
<publication id="PUB00017008">
<author_list>Brown MS, Goldstein JL.</author_list>
<title>A receptor-mediated pathway for cholesterol homeostasis.</title>
<db_xref db="PUBMED" dbkey="3513311"/>
<journal>Science</journal>
<location issue="4746" pages="34-47" volume="232"/>
<year>1986</year>
</publication>
<publication id="PUB00017009">
<author_list>Davis CG, Goldstein JL, Sudhof TC, Anderson RG, Russell DW, Brown MS.</author_list>
<title>Acid-dependent ligand dissociation and recycling of LDL receptor mediated by growth factor homology region.</title>
<db_xref db="PUBMED" dbkey="3494949"/>
<journal>Nature</journal>
<location issue="6115" pages="760-5" volume="326"/>
<year>1987</year>
</publication>
<publication id="PUB00017010">
<author_list>Jeon H, Meng W, Takagi J, Eck MJ, Springer TA, Blacklow SC.</author_list>
<title>Implications for familial hypercholesterolemia from the structure of the LDL receptor YWTD-EGF domain pair.</title>
<db_xref db="PUBMED" dbkey="11373616"/>
<journal>Nat. Struct. Biol.</journal>
<location issue="6" pages="499-504" volume="8"/>
<year>2001</year>
</publication>
</pub_list>
<found_in>
<rel_ref ipr_ref="IPR011042"/>
<rel_ref ipr_ref="IPR016317"/>
<rel_ref ipr_ref="IPR017049"/>
</found_in>
<member_list>
<db_xref protein_count="546" db="PFAM" dbkey="PF00058" name="Ldl_recept_b"/>
<db_xref protein_count="561" db="PROFILE" dbkey="PS51120" name="LDLRB"/>
<db_xref protein_count="709" db="SMART" dbkey="SM00135" name="LY"/>
</member_list>
<external_doc_list>
<db_xref db="PANDIT" dbkey="PF00058"/>
<db_xref db="BLOCKS" dbkey="IPB000033"/>
<db_xref db="PROSITEDOC" dbkey="PDOC51120"/>
t/data/interpro_relationship.xml view on Meta::CPAN
<taxon_data name="Other Eukaryotes" proteins_count="2"/>
</taxonomy_distribution>
</interpro>
<interpro id="IPR000044" protein_count="25" short_name="Uncharacterised_lipoprot_MG045" type="Family">
<name>Uncharacterised lipoprotein MG045</name>
<abstract>
<p> Mycoplasma genitalium has the smallest known genome of any free-living organism. Its complete genome sequence has been determined by whole-genome random sequencing and assembly [<cite idref="PUB00005212"/>]. Only 470 putative coding regions were...
</abstract>
<class_list>
<classification id="GO:0016020" class_type="GO">
<category>Cellular Component</category>
<description>membrane</description>
</classification>
</class_list>
<example_list>
<example>
<db_xref db="SWISSPROT" dbkey="P47291"/>
</example>
</example_list>
<pub_list>
<publication id="PUB00002233">
<author_list>Peterson SN, Hu PC, Bott KF, Hutchison CA 3rd.</author_list>
<title>A survey of the Mycoplasma genitalium genome by using random sequencing.</title>
<db_xref db="PUBMED" dbkey="8253680"/>
<journal>J. Bacteriol.</journal>
<location issue="24" pages="7918-30" volume="175"/>
<year>1993</year>
</publication>
<publication id="PUB00005212">
<author_list>Fraser CM, Gocayne JD, White O, Adams MD, Clayton RA, Fleischmann RD, Bult CJ, Kerlavage AR, Sutton G, Kelley JM, Fritchman RD, Weidman JF, Small KV, Sandusky M, Fuhrmann J, Nguyen D, Utterback TR, Saudek DM, Phillips CA, Merrick J...
<title>The minimal gene complement of Mycoplasma genitalium.</title>
<db_xref db="PUBMED" dbkey="7569993"/>
<journal>Science</journal>
<location issue="5235" pages="397-403" volume="270"/>
<year>1995</year>
</publication>
</pub_list>
<member_list>
<db_xref protein_count="25" db="PRINTS" dbkey="PR00905" name="MG045FAMILY"/>
</member_list>
<external_doc_list>
<db_xref db="PANDIT" dbkey="PF02030"/>
</external_doc_list>
<taxonomy_distribution>
<taxon_data name="Bacteria" proteins_count="25"/>
</taxonomy_distribution>
</interpro>
<interpro id="IPR000045" protein_count="2278" short_name="Peptidase_A24A_prepilin_IV" type="Domain">
<name>Peptidase A24A, prepilin type IV</name>
<abstract>
<p>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:</p>
<ul>
<li>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...
<li>Peptidase families are grouped by their catalytic type, the first character representing the catalytic type: A, aspartic; C, cysteine; G, glutamic acid; M, metallo; S, serine; T, threonine; and U, unknown. The serine, threonine and cysteine pepti...
</ul>
<p>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. </p>
<p>Aspartic endopeptidases <db_xref db="EC" dbkey="3.4.23."/> of vertebrate, fungal and retroviral origin have been characterised [<cite idref="PUB00006548"/>]. More recently, aspartic endopeptidases associated with the processing of bacterial type ...
<p>Structurally, aspartic endopeptidases are bilobal enzymes, each lobe contributing a catalytic Asp residue, with an extended active site cleft localised between the two lobes of the molecule. One lobe has probably evolved from the other through a g...
All or most aspartate peptidases are endopeptidases. These enzymes have been assigned into clans (proteins which are evolutionary related), and further sub-divided into families, largely on the basis of their tertiary structure.</p>
<p>This group of aspartic endopeptidases belong to MEROPS peptidase family A24 (type IV prepilin peptidase family, clan AD), subfamily A24A.</p>
<p>Bacteria produce a number of protein precursors that undergo post-translational methylation and proteolysis prior to secretion as active
proteins. Type IV prepilin leader peptidases are enzymes that mediate this type of post-translational modification. Type IV pilin is a protein found on the surface of <taxon tax_id="287">Pseudomonas aeruginosa</taxon>, <taxon tax_id="485">Neisseria g...
pathogens. Pilin subunits attach the infecting organism to the surface of
host epithelial cells. They are synthesised as prepilin subunits, which
differ from mature pilin by virtue of containing a 6-8 residue leader
peptide consisting of charged amino acids. Mature type IV pilins also
contain a methylated N-terminal phenylalanine residue.</p>
<p> The bifunctional enzyme prepilin peptidase (PilD) from <taxon tax_id="287">Pseudomonas aeruginosa</taxon> is a key determinant in both type-IV pilus biogenesis and extracellular protein secretion, in its roles as a leader peptidase and methyl tra...
</abstract>
<class_list>
<classification id="GO:0004190" class_type="GO">
<category>Molecular Function</category>
<description>aspartic-type endopeptidase activity</description>
</classification>
<classification id="GO:0016020" class_type="GO">
<category>Cellular Component</category>
<description>membrane</description>
</classification>
</class_list>
<example_list>
<example>
<db_xref db="SWISSPROT" dbkey="A2T195"/>
</example>
<example>
<db_xref db="SWISSPROT" dbkey="O26521"/>
</example>
<example>
<db_xref db="SWISSPROT" dbkey="P72640"/>
</example>
</example_list>
<pub_list>
<publication id="PUB00006548">
<author_list>Szecsi PB.</author_list>
<title>The aspartic proteases.</title>
<db_xref db="PUBMED" dbkey="1455179"/>
<journal>Scand. J. Clin. Lab. Invest. Suppl.</journal>
<location pages="5-22" volume="210"/>
<year>1992</year>
</publication>
<publication id="PUB00014343">
<author_list>Bardy SL, Jarrell KF.</author_list>
<title>Cleavage of preflagellins by an aspartic acid signal peptidase is essential for flagellation in the archaeon Methanococcus voltae.</title>
<db_xref db="PUBMED" dbkey="14622420"/>
<journal>Mol. Microbiol.</journal>
<location issue="4" pages="1339-47" volume="50"/>
<year>2003</year>
</publication>
<publication id="PUB00014532">
<author_list>Lory S, Strom MS.</author_list>
<title>Structure-function relationship of type-IV prepilin peptidase of Pseudomonas aeruginosa--a review.</title>
<db_xref db="PUBMED" dbkey="9224881"/>
<journal>Gene</journal>
<location issue="1" pages="117-21" volume="192"/>
<year>1997</year>
</publication>
<publication id="PUB00020023">
<author_list>LaPointe CF, Taylor RK.</author_list>
<title>The type 4 prepilin peptidases comprise a novel family of aspartic acid proteases.</title>
<db_xref db="PUBMED" dbkey="10625704"/>
<journal>J. Biol. Chem.</journal>
<location issue="2" pages="1502-10" volume="275"/>
<year>2000</year>
</publication>
<publication id="PUB00035904">
<author_list>Ng SY, Chaban B, Jarrell KF.</author_list>
<title>Archaeal flagella, bacterial flagella and type IV pili: a comparison of genes and posttranslational modifications.</title>
<db_xref db="PUBMED" dbkey="16983194"/>
<journal>J. Mol. Microbiol. Biotechnol.</journal>
t/data/interpro_relationship.xml view on Meta::CPAN
<db_xref db="PDB" dbkey="1n5k"/>
<db_xref db="PDB" dbkey="1n5l"/>
<db_xref db="PDB" dbkey="1nmx"/>
<db_xref db="PDB" dbkey="1nmy"/>
<db_xref db="PDB" dbkey="1nmz"/>
<db_xref db="PDB" dbkey="1nn0"/>
<db_xref db="PDB" dbkey="1nn1"/>
<db_xref db="PDB" dbkey="1nn3"/>
<db_xref db="PDB" dbkey="1nn5"/>
<db_xref db="PDB" dbkey="1tmk"/>
<db_xref db="PDB" dbkey="1w2g"/>
<db_xref db="PDB" dbkey="1w2h"/>
<db_xref db="PDB" dbkey="2axp"/>
<db_xref db="PDB" dbkey="2tmk"/>
<db_xref db="PDB" dbkey="2v54"/>
<db_xref db="PDB" dbkey="2w0s"/>
<db_xref db="PDB" dbkey="3tmk"/>
<db_xref db="PDB" dbkey="4tmk"/>
<db_xref db="PDB" dbkey="5tmp"/>
<db_xref db="CATH" dbkey="3.40.50.300"/>
<db_xref db="SCOP" dbkey="c.37.1.1"/>
</structure_db_links>
<taxonomy_distribution>
<taxon_data name="Bacteria" proteins_count="1953"/>
<taxon_data name="Cyanobacteria" proteins_count="55"/>
<taxon_data name="Synechocystis PCC 6803" proteins_count="1"/>
<taxon_data name="Archaea" proteins_count="127"/>
<taxon_data name="Eukaryota" proteins_count="215"/>
<taxon_data name="Arabidopsis thaliana" proteins_count="5"/>
<taxon_data name="Rice spp." proteins_count="4"/>
<taxon_data name="Fungi" proteins_count="68"/>
<taxon_data name="Saccharomyces cerevisiae" proteins_count="6"/>
<taxon_data name="Other Eukaryotes" proteins_count="2"/>
<taxon_data name="Nematoda" proteins_count="1"/>
<taxon_data name="Caenorhabditis elegans" proteins_count="1"/>
<taxon_data name="Arthropoda" proteins_count="28"/>
<taxon_data name="Fruit Fly" proteins_count="7"/>
<taxon_data name="Chordata" proteins_count="30"/>
<taxon_data name="Human" proteins_count="5"/>
<taxon_data name="Mouse" proteins_count="5"/>
<taxon_data name="Virus" proteins_count="54"/>
<taxon_data name="Unclassified" proteins_count="1"/>
<taxon_data name="Other Eukaryotes" proteins_count="2"/>
<taxon_data name="Plastid Group" proteins_count="29"/>
<taxon_data name="Green Plants" proteins_count="29"/>
<taxon_data name="Metazoa" proteins_count="139"/>
<taxon_data name="Plastid Group" proteins_count="21"/>
<taxon_data name="Plastid Group" proteins_count="13"/>
<taxon_data name="Other Eukaryotes" proteins_count="2"/>
<taxon_data name="Other Eukaryotes" proteins_count="4"/>
</taxonomy_distribution>
<sec_list>
<sec_ac acc="IPR014505"/>
<sec_ac acc="IPR018094"/>
</sec_list>
</interpro>
<interpro id="IPR000064" protein_count="4879" short_name="NLP_P60" type="Domain">
<name>NLP/P60</name>
<abstract>
<p>The <taxon tax_id="562">Escherichia coli</taxon> NLPC/Listeria P60 domain occurs at the C terminus of a number of different bacterial and viral proteins. The viral proteins are either described as tail assembly proteins or Gp19. In bacteria, the ...
<p>The E. coli NLPC/Listeria P60 domain is contained within the boundaries of the cysteine peptidase domain that defines the MEROPS peptidase family C40 (clan C-). A type example being dipeptidyl-peptidase VI from <taxon tax_id="1421">Bacillus sphaer...
</p>
</abstract>
<example_list>
<example>
<db_xref db="SWISSPROT" dbkey="P03729"/>
</example>
<example>
<db_xref db="SWISSPROT" dbkey="P0AFV4"/>
</example>
</example_list>
<pub_list/>
<found_in>
<rel_ref ipr_ref="IPR011929"/>
</found_in>
<member_list>
<db_xref protein_count="4879" db="PFAM" dbkey="PF00877" name="NLPC_P60"/>
</member_list>
<external_doc_list>
<db_xref db="PANDIT" dbkey="PF00877"/>
<db_xref db="BLOCKS" dbkey="IPB000064"/>
<db_xref db="MEROPS" dbkey="C40"/>
</external_doc_list>
<structure_db_links>
<db_xref db="PDB" dbkey="2hbw"/>
<db_xref db="CATH" dbkey="3.90.1720.10"/>
</structure_db_links>
<taxonomy_distribution>
<taxon_data name="Bacteria" proteins_count="4787"/>
<taxon_data name="Cyanobacteria" proteins_count="52"/>
<taxon_data name="Synechocystis PCC 6803" proteins_count="1"/>
<taxon_data name="Archaea" proteins_count="3"/>
<taxon_data name="Eukaryota" proteins_count="37"/>
<taxon_data name="Rice spp." proteins_count="1"/>
<taxon_data name="Fungi" proteins_count="16"/>
<taxon_data name="Other Eukaryotes" proteins_count="9"/>
<taxon_data name="Other Eukaryotes" proteins_count="3"/>
<taxon_data name="Arthropoda" proteins_count="1"/>
<taxon_data name="Chordata" proteins_count="1"/>
<taxon_data name="Mouse" proteins_count="1"/>
<taxon_data name="Virus" proteins_count="52"/>
<taxon_data name="Plastid Group" proteins_count="4"/>
<taxon_data name="Green Plants" proteins_count="4"/>
<taxon_data name="Metazoa" proteins_count="18"/>
<taxon_data name="Plastid Group" proteins_count="1"/>
<taxon_data name="Other Eukaryotes" proteins_count="2"/>
</taxonomy_distribution>
</interpro>
<interpro id="IPR000065" protein_count="150" short_name="Leptin" type="Family">
<name>Obesity factor</name>
<abstract>
Leptin, a metabolic monitor of food intake and energy need, is expressed
by the ob obesity gene. The protein may function as part of a signalling
pathway from adipose tissue that acts to regulate the size of the body
fat depot [<cite idref="PUB00004193"/>], the hormone effectively turning the brain's appetite
message off when it senses that the body is satiated. Obese humans have
high levels of the protein, suggesting a similarity to type II (adult
onset) diabetes, in which sufferers over-produce insulin, but can't respond
to it metabolically - they have become insulin resistant. Similarly, it is
thought that obese individuals may be leptin resistant.
</abstract>
t/data/interpro_relationship.xml view on Meta::CPAN
<book_title>ISBN:0127384405</book_title>
<location pages="130-41"/>
<year>1994</year>
</publication>
<publication id="PUB00005138">
<author_list>Houamed KM, Kuijper JL, Gilbert TL, Haldeman BA, O'Hara PJ, Mulvihill ER, Almers W, Hagen FS.</author_list>
<title>Cloning, expression, and gene structure of a G protein-coupled glutamate receptor from rat brain.</title>
<db_xref db="PUBMED" dbkey="1656524"/>
<journal>Science</journal>
<location issue="5010" pages="1318-21" volume="252"/>
<year>1991</year>
</publication>
<publication id="PUB00004090">
<author_list>Masu M, Tanabe Y, Tsuchida K, Shigemoto R, Nakanishi S.</author_list>
<title>Sequence and expression of a metabotropic glutamate receptor.</title>
<db_xref db="PUBMED" dbkey="1847995"/>
<journal>Nature</journal>
<location issue="6312" pages="760-5" volume="349"/>
<year>1991</year>
</publication>
<publication id="PUB00004309">
<author_list>Tanabe Y, Masu M, Ishii T, Shigemoto R, Nakanishi S.</author_list>
<title>A family of metabotropic glutamate receptors.</title>
<db_xref db="PUBMED" dbkey="1309649"/>
<journal>Neuron</journal>
<location issue="1" pages="169-79" volume="8"/>
<year>1992</year>
</publication>
</pub_list>
<parent_list>
<rel_ref ipr_ref="IPR000337"/>
</parent_list>
<child_list>
<rel_ref ipr_ref="IPR015531"/>
</child_list>
<contains>
<rel_ref ipr_ref="IPR001828"/>
</contains>
<member_list>
<db_xref protein_count="101" db="PRINTS" dbkey="PR00592" name="CASENSINGR"/>
</member_list>
<external_doc_list>
<db_xref db="BLOCKS" dbkey="IPB000068"/>
<db_xref db="IUPHAR" dbkey="2926"/>
</external_doc_list>
<taxonomy_distribution>
<taxon_data name="Eukaryota" proteins_count="101"/>
<taxon_data name="Chordata" proteins_count="93"/>
<taxon_data name="Human" proteins_count="13"/>
<taxon_data name="Mouse" proteins_count="10"/>
<taxon_data name="Metazoa" proteins_count="101"/>
</taxonomy_distribution>
<sec_list>
<sec_ac acc="IPR015531"/>
</sec_list>
</interpro>
<interpro id="IPR000069" protein_count="3797" short_name="Env_glycoprot_M_flavivir" type="Domain">
<name>Envelope glycoprotein M, flavivirus</name>
<abstract>
<p>Flaviviruses are small enveloped viruses with virions comprised of
three proteins called C, M and E [<cite idref="PUB00003522"/>, <cite idref="PUB00000171"/>, <cite idref="PUB00003500"/>]. The envelope glycoprotein M is made as a precursor, called prM. The precursor portion of the protein is the signal peptide for t...
</abstract>
<class_list>
<classification id="GO:0019028" class_type="GO">
<category>Cellular Component</category>
<description>viral capsid</description>
</classification>
<classification id="GO:0019058" class_type="GO">
<category>Biological Process</category>
<description>viral infectious cycle</description>
</classification>
</class_list>
<example_list>
<example>
<db_xref db="SWISSPROT" dbkey="P03314"/>
</example>
</example_list>
<pub_list>
<publication id="PUB00000171">
<author_list>Heinz FX, Auer G, Stiasny K, Holzmann H, Mandl C, Guirakhoo F, Kunz C.</author_list>
<title>The interactions of the flavivirus envelope proteins: implications for virus entry and release.</title>
<db_xref db="PUBMED" dbkey="7913359"/>
<journal>Arch. Virol. Suppl.</journal>
<location pages="339-48" volume="9"/>
<year>1994</year>
</publication>
<publication id="PUB00003500">
<author_list>Konishi E, Mason PW.</author_list>
<title>Proper maturation of the Japanese encephalitis virus envelope glycoprotein requires cosynthesis with the premembrane protein.</title>
<db_xref db="PUBMED" dbkey="8437237"/>
<journal>J. Virol.</journal>
<location issue="3" pages="1672-5" volume="67"/>
<year>1993</year>
</publication>
<publication id="PUB00003522">
<author_list>Schalich J, Allison SL, Stiasny K, Mandl CW, Kunz C, Heinz FX.</author_list>
<title>Recombinant subviral particles from tick-borne encephalitis virus are fusogenic and provide a model system for studying flavivirus envelope glycoprotein functions.</title>
<db_xref db="PUBMED" dbkey="8676481"/>
<journal>J. Virol.</journal>
<location issue="7" pages="4549-57" volume="70"/>
<year>1996</year>
</publication>
</pub_list>
<found_in>
<rel_ref ipr_ref="IPR014412"/>
</found_in>
<member_list>
<db_xref protein_count="3797" db="PFAM" dbkey="PF01004" name="Flavi_M"/>
</member_list>
<external_doc_list>
<db_xref db="PANDIT" dbkey="PF01004"/>
<db_xref db="EC" dbkey="2.1.1.56"/>
<db_xref db="EC" dbkey="2.1.1.57"/>
<db_xref db="EC" dbkey="2.7.7.48"/>
<db_xref db="EC" dbkey="3.4.21.91"/>
<db_xref db="EC" dbkey="3.6.1.15"/>
</external_doc_list>
<taxonomy_distribution>
<taxon_data name="Virus" proteins_count="3797"/>
</taxonomy_distribution>
</interpro>
t/data/interpro_relationship.xml view on Meta::CPAN
<location issue="3" pages="849-58" volume="17"/>
<year>2005</year>
</publication>
<publication id="PUB00016280">
<author_list>Jenkins J, Mayans O, Smith D, Worboys K, Pickersgill RW.</author_list>
<title>Three-dimensional structure of Erwinia chrysanthemi pectin methylesterase reveals a novel esterase active site.</title>
<db_xref db="PUBMED" dbkey="11162105"/>
<journal>J. Mol. Biol.</journal>
<location issue="4" pages="951-60" volume="305"/>
<year>2001</year>
</publication>
</pub_list>
<parent_list>
<rel_ref ipr_ref="IPR012334"/>
</parent_list>
<contains>
<rel_ref ipr_ref="IPR018040"/>
</contains>
<member_list>
<db_xref protein_count="1141" db="PFAM" dbkey="PF01095" name="Pectinesterase"/>
</member_list>
<external_doc_list>
<db_xref db="PANDIT" dbkey="PF01095"/>
<db_xref db="MSDsite" dbkey="PS00503"/>
<db_xref db="MSDsite" dbkey="PS00800"/>
<db_xref db="BLOCKS" dbkey="IPB000070"/>
<db_xref db="EC" dbkey="3.1.1.11"/>
<db_xref db="PROSITEDOC" dbkey="PDOC00413"/>
</external_doc_list>
<structure_db_links>
<db_xref db="PDB" dbkey="1gq8"/>
<db_xref db="PDB" dbkey="1qjv"/>
<db_xref db="PDB" dbkey="1xg2"/>
<db_xref db="PDB" dbkey="2nsp"/>
<db_xref db="PDB" dbkey="2nst"/>
<db_xref db="PDB" dbkey="2nt6"/>
<db_xref db="PDB" dbkey="2nt9"/>
<db_xref db="PDB" dbkey="2ntb"/>
<db_xref db="PDB" dbkey="2ntp"/>
<db_xref db="PDB" dbkey="2ntq"/>
<db_xref db="CATH" dbkey="2.160.20.10"/>
<db_xref db="SCOP" dbkey="b.80.1.5"/>
</structure_db_links>
<taxonomy_distribution>
<taxon_data name="Bacteria" proteins_count="353"/>
<taxon_data name="Cyanobacteria" proteins_count="3"/>
<taxon_data name="Archaea" proteins_count="2"/>
<taxon_data name="Eukaryota" proteins_count="786"/>
<taxon_data name="Arabidopsis thaliana" proteins_count="79"/>
<taxon_data name="Rice spp." proteins_count="142"/>
<taxon_data name="Fungi" proteins_count="84"/>
<taxon_data name="Arthropoda" proteins_count="1"/>
<taxon_data name="Plastid Group" proteins_count="690"/>
<taxon_data name="Green Plants" proteins_count="690"/>
<taxon_data name="Metazoa" proteins_count="85"/>
</taxonomy_distribution>
</interpro>
<interpro id="IPR000071" protein_count="24951" short_name="Lentvrl_matrix_N" type="Domain">
<name>Immunodeficiency lentiviral matrix, N-terminal</name>
<abstract>
<p>Retroviral matrix proteins (or major core proteins) are components of envelope-associated capsids, which line the inner surface of virus envelopes and are associated with viral membranes [<cite idref="PUB00014063"/>]. Matrix proteins are produced ...
<p>This entry represents matrix proteins from immunodeficiency lentiviruses, such as <taxon tax_id="12721">Human immunodeficiency virus</taxon> (HIV) and <taxon tax_id="11723">Simian immunodeficiency virus</taxon> (SIV-cpz) [<cite idref="PUB00016321"...
</abstract>
<class_list>
<classification id="GO:0005198" class_type="GO">
<category>Molecular Function</category>
<description>structural molecule activity</description>
</classification>
</class_list>
<example_list>
<example>
<db_xref db="SWISSPROT" dbkey="O12158"/>
</example>
</example_list>
<pub_list>
<publication id="PUB00003338">
<author_list>Massiah MA, Starich MR, Paschall C, Summers MF, Christensen AM, Sundquist WI.</author_list>
<title>Three-dimensional structure of the human immunodeficiency virus type 1 matrix protein.</title>
<db_xref db="PUBMED" dbkey="7966331"/>
<journal>J. Mol. Biol.</journal>
<location issue="2" pages="198-223" volume="244"/>
<year>1994</year>
</publication>
<publication id="PUB00014063">
<author_list>Conte MR, Matthews S.</author_list>
<title>Retroviral matrix proteins: a structural perspective.</title>
<db_xref db="PUBMED" dbkey="9657938"/>
<journal>Virology</journal>
<location issue="2" pages="191-8" volume="246"/>
<year>1998</year>
</publication>
<publication id="PUB00016321">
<author_list>Freed EO.</author_list>
<title>HIV-1 replication.</title>
<db_xref db="PUBMED" dbkey="12465460"/>
<journal>Somat. Cell Mol. Genet.</journal>
<location issue="1-6" pages="13-33" volume="26"/>
<year>2001</year>
</publication>
</pub_list>
<parent_list>
<rel_ref ipr_ref="IPR012344"/>
</parent_list>
<member_list>
<db_xref protein_count="24951" db="PFAM" dbkey="PF00540" name="Gag_p17"/>
<db_xref protein_count="24741" db="PRINTS" dbkey="PR00234" name="HIV1MATRIX"/>
</member_list>
<external_doc_list>
<db_xref db="PANDIT" dbkey="PF00540"/>
<db_xref db="BLOCKS" dbkey="IPB000071"/>
</external_doc_list>
<structure_db_links>
<db_xref db="PDB" dbkey="1ecw"/>
<db_xref db="PDB" dbkey="1ed1"/>
<db_xref db="PDB" dbkey="1hiw"/>
<db_xref db="PDB" dbkey="1l6n"/>
<db_xref db="PDB" dbkey="1m9c"/>
<db_xref db="PDB" dbkey="1m9d"/>
<db_xref db="PDB" dbkey="1m9e"/>
<db_xref db="PDB" dbkey="1m9f"/>
<db_xref db="PDB" dbkey="1m9x"/>
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