<?xml version="1.0" ?>
<disprot version="5.2"><protein id="DP00489">
<general><name>Decorin</name><synonyms><synonym>PGS2_BOVIN</synonym><synonym>Bone proteoglycan II</synonym><synonym>PG-S2</synonym></synonyms><uniprot>P21793</uniprot><unigene>Bt.23178</unigene><swissprot>PGS2_BOVIN</swissprot><trembl></trembl><ncbi>68845449</ncbi><source_organism>Bos taurus (Bovine)</source_organism><native_sequence>MKATIIFLLVAQVSWAGPFQQKGLFDFMLEDEASGIGPEEHFPEVPEIEPMGPVCPFRCQCHLRVVQCSDLGLEKVPKDLPPDTALLDLQNNKITEIKDGDFKNLKNLHTLILINNKISKISPGAFAPLVKLERLYLSKNQLKELPEKMPKTLQELRVHENEITKVRKSVFNGLNQMIVVELGTNPLKSSGIENGAFQGMKKLSYIRIADTNITTIPQGLPPSLTELHLDGNKITKVDAASLKGLNNLAKLGLSFNSISAVDNGSLANTPHLRELHLNNNKLVKVPGGLADHKYIQVVYLHNNNISAIGSNDFCPPGYNTKKASYSGVSLFSNPVQYWEIQPSTFRCVYVRAAVQLGNYK</native_sequence><functional_narrative>May affect the rate of fibrils formation.</functional_narrative></general><regions><region id="1"><type>Disordered</type><name></name><start>31</start><end>51</end><sequence>DEASGIGPEEHFPEVPEIEPM</sequence><modification_types><modification_type>Native</modification_type></modification_types><pdbs></pdbs><structural_functional_types><structural_functional_type id="U">Relationship to function unknown</structural_functional_type></structural_functional_types><functional_classes><functional_class id="0">Unknown</functional_class></functional_classes><functional_subclasses><functional_subclass id="mG">Glycosylation</functional_subclass></functional_subclasses><detection_methods><detection><method id="X-ray">X-ray crystallography</method><temperature unit="K">293</temperature><ph></ph><additives><additive><name>polyethylene glycol 400</name><type>25% vol/vol</type><concentration></concentration></additive><additive><name>Tris</name><type>pH 7.75</type><concentration unit="M">0.06</concentration></additive><additive><name>beta-octyl-D-glucoside</name><type>0.01%</type><concentration></concentration></additive><additive><name>sodium azide</name><type>0.02%</type><concentration></concentration></additive></additives></detection></detection_methods><input_type>Paper</input_type><references><reference type="Journal article"><pmid>15501918</pmid><author>Scott PG, McEwan PA, Dodd CM, Bergmann EM, Bishop PN, Bella J</author><title>Crystal structure of the dimeric protein core of decorin, the archetypal small leucine-rich repeat proteoglycan</title><year>2004</year><publication>Proc Natl Acad Sci U S A</publication><volume>101</volume><number>44</number><pages>15633-8</pages></reference></references><comments><comment>This region corresponds to residues 1-21 of the mature protein.</comment></comments></region></regions><comments><comment>The decorin precursor has 360 amino acid residues which contains a 30-amino-acid residue propetide (residues 1-30).  The mature protein is 330 amino acid residues long (residues 31-360).</comment><comment>The protein sequence in the paper matches 99% with the sequence in Swiss-Prot.  In the paper, residues 283 and 289 are alanine and valine, instead of, valine and leucine.</comment></comments></protein>
</disprot>
