##gff-version 3 Q9WVJ9 UniProtKB Signal peptide 1 27 . . . Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17324935;Dbxref=PMID:17324935 Q9WVJ9 UniProtKB Chain 28 443 . . . ID=PRO_0000007576;Note=EGF-containing fibulin-like extracellular matrix protein 2 Q9WVJ9 UniProtKB Domain 36 81 . . . Note=EGF-like 1%3B atypical;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00076 Q9WVJ9 UniProtKB Domain 123 163 . . . Note=EGF-like 2%3B calcium-binding;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00076 Q9WVJ9 UniProtKB Domain 164 202 . . . Note=EGF-like 3%3B calcium-binding;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00076 Q9WVJ9 UniProtKB Domain 203 242 . . . Note=EGF-like 4%3B calcium-binding;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00076 Q9WVJ9 UniProtKB Domain 243 282 . . . Note=EGF-like 5%3B calcium-binding;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00076 Q9WVJ9 UniProtKB Domain 283 328 . . . Note=EGF-like 6%3B calcium-binding;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00076 Q9WVJ9 UniProtKB Region 91 117 . . . Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite Q9WVJ9 UniProtKB Site 87 88 . . . Note=Cleavage%3B by ELANE;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:O95967 Q9WVJ9 UniProtKB Site 90 91 . . . Note=Cleavage%3B by MMP2%2C MMP3%2C MMP7%2C MMP9%2C MMP12;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:O95967 Q9WVJ9 UniProtKB Site 92 93 . . . Note=Cleavage;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:O95967 Q9WVJ9 UniProtKB Modified residue 28 28 . . . Note=Pyrrolidone carboxylic acid;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17324935;Dbxref=PMID:17324935 Q9WVJ9 UniProtKB Glycosylation 198 198 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 Q9WVJ9 UniProtKB Glycosylation 394 394 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 Q9WVJ9 UniProtKB Disulfide bond 58 121 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00076 Q9WVJ9 UniProtKB Disulfide bond 65 80 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00076 Q9WVJ9 UniProtKB Disulfide bond 71 109 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00076 Q9WVJ9 UniProtKB Disulfide bond 127 140 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00076 Q9WVJ9 UniProtKB Disulfide bond 134 149 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00076 Q9WVJ9 UniProtKB Disulfide bond 151 162 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00076 Q9WVJ9 UniProtKB Disulfide bond 168 177 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00076 Q9WVJ9 UniProtKB Disulfide bond 173 186 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00076 Q9WVJ9 UniProtKB Disulfide bond 188 201 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00076 Q9WVJ9 UniProtKB Disulfide bond 207 217 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00076 Q9WVJ9 UniProtKB Disulfide bond 213 226 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00076 Q9WVJ9 UniProtKB Disulfide bond 228 241 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00076 Q9WVJ9 UniProtKB Disulfide bond 247 258 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00076 Q9WVJ9 UniProtKB Disulfide bond 254 267 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00076 Q9WVJ9 UniProtKB Disulfide bond 269 281 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00076 Q9WVJ9 UniProtKB Disulfide bond 287 300 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00076 Q9WVJ9 UniProtKB Disulfide bond 294 309 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00076 Q9WVJ9 UniProtKB Disulfide bond 315 327 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00076 Q9WVJ9 UniProtKB Mutagenesis 57 57 . . . Note=Knockin mutant mice are viable and survive into adulthood. Mice display abnormalities in multiple organ systems%2C including loose skin%2C bent forelimb%2C aortic aneurysm%2C tortuous artery%2C and pulmonary emphysema. In addition to elastic fiber abnormalities in the skin and large arteries%2C collagen fibrils are irregularly shaped%2C with many large fibrils in the dermis. Mice have large artery stiffness and systolic hypertension. Reduces protein secretion. E->K;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:26178373,ECO:0000269|PubMed:28508064;Dbxref=PMID:26178373,PMID:28508064 Q9WVJ9 UniProtKB Sequence conflict 30 30 . . . Note=P->T;Ontology_term=ECO:0000305;evidence=ECO:0000305