| IED ID | IndEnz0002005935 |
| Enzyme Type ID | protease005935 |
| Protein Name |
Filamin-C FLN-C FLNc ABP-280-like protein ABP-L Actin-binding-like protein Filamin-2 Gamma-filamin |
| Gene Name | FLNC ABPL FLN2 |
| Organism | Homo sapiens (Human) |
| Taxonomic Lineage | cellular organisms Eukaryota Opisthokonta Metazoa Eumetazoa Bilateria Deuterostomia Chordata Craniata Vertebrata Gnathostomata (jawed vertebrates) Teleostomi Euteleostomi Sarcopterygii Dipnotetrapodomorpha Tetrapoda Amniota Mammalia Theria Eutheria Boreoeutheria Euarchontoglires Primates Haplorrhini Simiiformes Catarrhini Hominoidea (apes) Hominidae (great apes) Homininae Homo Homo sapiens (Human) |
| Enzyme Sequence | MMNNSGYSDAGLGLGDETDEMPSTEKDLAEDAPWKKIQQNTFTRWCNEHLKCVGKRLTDLQRDLSDGLRLIALLEVLSQKRMYRKFHPRPNFRQMKLENVSVALEFLEREHIKLVSIDSKAIVDGNLKLILGLIWTLILHYSISMPMWEDEDDEDARKQTPKQRLLGWIQNKVPQLPITNFNRDWQDGKALGALVDNCAPGLCPDWEAWDPNQPVENAREAMQQADDWLGVPQVIAPEEIVDPNVDEHSVMTYLSQFPKAKLKPGAPVRSKQLNPKKAIAYGPGIEPQGNTVLQPAHFTVQTVDAGVGEVLVYIEDPEGHTEEAKVVPNNDKDRTYAVSYVPKVAGLHKVTVLFAGQNIERSPFEVNVGMALGDANKVSARGPGLEPVGNVANKPTYFDIYTAGAGTGDVAVVIVDPQGRRDTVEVALEDKGDSTFRCTYRPAMEGPHTVHVAFAGAPITRSPFPVHVSEACNPNACRASGRGLQPKGVRVKEVADFKVFTKGAGSGELKVTVKGPKGTEEPVKVREAGDGVFECEYYPVVPGKYVVTITWGGYAIPRSPFEVQVSPEAGVQKVRAWGPGLETGQVGKSADFVVEAIGTEVGTLGFSIEGPSQAKIECDDKGDGSCDVRYWPTEPGEYAVHVICDDEDIRDSPFIAHILPAPPDCFPDKVKAFGPGLEPTGCIVDKPAEFTIDARAAGKGDLKLYAQDADGCPIDIKVIPNGDGTFRCSYVPTKPIKHTIIISWGGVNVPKSPFRVNVGEGSHPERVKVYGPGVEKTGLKANEPTYFTVDCSEAGQGDVSIGIKCAPGVVGPAEADIDFDIIKNDNDTFTVKYTPPGAGRYTIMVLFANQEIPASPFHIKVDPSHDASKVKAEGPGLNRTGVEVGKPTHFTVLTKGAGKAKLDVQFAGTAKGEVVRDFEIIDNHDYSYTVKYTAVQQGNMAVTVTYGGDPVPKSPFVVNVAPPLDLSKIKVQGLNSKVAVGQEQAFSVNTRGAGGQGQLDVRMTSPSRRPIPCKLEPGGGAEAQAVRYMPPEEGPYKVDITYDGHPVPGSPFAVEGVLPPDPSKVCAYGPGLKGGLVGTPAPFSIDTKGAGTGGLGLTVEGPCEAKIECQDNGDGSCAVSYLPTEPGEYTINILFAEAHIPGSPFKATIRPVFDPSKVRASGPGLERGKVGEAATFTVDCSEAGEAELTIEILSDAGVKAEVLIHNNADGTYHITYSPAFPGTYTITIKYGGHPVPKFPTRVHVQPAVDTSGVKVSGPGVEPHGVLREVTTEFTVDARSLTATGGNHVTARVLNPSGAKTDTYVTDNGDGTYRVQYTAYEEGVHLVEVLYDEVAVPKSPFRVGVTEGCDPTRVRAFGPGLEGGLVNKANRFTVETRGAGTGGLGLAIEGPSEAKMSCKDNKDGSCTVEYIPFTPGDYDVNITFGGRPIPGSPFRVPVKDVVDPGKVKCSGPGLGAGVRARVPQTFTVDCSQAGRAPLQVAVLGPTGVAEPVEVRDNGDGTHTVHYTPATDGPYTVAVKYADQEVPRSPFKIKVLPAHDASKVRASGPGLNASGIPASLPVEFTIDARDAGEGLLTVQILDPEGKPKKANIRDNGDGTYTVSYLPDMSGRYTITIKYGGDEIPYSPFRIHALPTGDASKCLVTVSIGGHGLGACLGPRIQIGQETVITVDAKAAGEGKVTCTVSTPDGAELDVDVVENHDGTFDIYYTAPEPGKYVITIRFGGEHIPNSPFHVLACDPLPHEEEPSEVPQLRQPYAPPRPGARPTHWATEEPVVPVEPMESMLRPFNLVIPFAVQKGELTGEVRMPSGKTARPNITDNKDGTITVRYAPTEKGLHQMGIKYDGNHIPGSPLQFYVDAINSRHVSAYGPGLSHGMVNKPATFTIVTKDAGEGGLSLAVEGPSKAEITCKDNKDGTCTVSYLPTAPGDYSIIVRFDDKHIPGSPFTAKITGDDSMRTSQLNVGTSTDVSLKITESDLSQLTASIRAPSGNEEPCLLKRLPNRHIGISFTPKEVGEHVVSVRKSGKHVTNSPFKILVGPSEIGDASKVRVWGKGLSEGHTFQVAEFIVDTRNAGYGGLGLSIEGPSKVDINCEDMEDGTCKVTYCPTEPGTYIINIKFADKHVPGSPFTVKVTGEGRMKESITRRRQAPSIATIGSTCDLNLKIPGNWFQMVSAQERLTRTFTRSSHTYTRTERTEISKTRGGETKREVRVEESTQVGGDPFPAVFGDFLGRERLGSFGSITRQQEGEASSQDMTAQVTSPSGKVEAAEIVEGEDSAYSVRFVPQEMGPHTVAVKYRGQHVPGSPFQFTVGPLGEGGAHKVRAGGTGLERGVAGVPAEFSIWTREAGAGGLSIAVEGPSKAEIAFEDRKDGSCGVSYVVQEPGDYEVSIKFNDEHIPDSPFVVPVASLSDDARRLTVTSLQETGLKVNQPASFAVQLNGARGVIDARVHTPSGAVEECYVSELDSDKHTIRFIPHENGVHSIDVKFNGAHIPGSPFKIRVGEQSQAGDPGLVSAYGPGLEGGTTGVSSEFIVNTLNAGSGALSVTIDGPSKVQLDCRECPEGHVVTYTPMAPGNYLIAIKYGGPQHIVGSPFKAKVTGPRLSGGHSLHETSTVLVETVTKSSSSRGSSYSSIPKFSSDASKVVTRGPGLSQAFVGQKNSFTVDCSKAGTNMMMVGVHGPKTPCEEVYVKHMGNRVYNVTYTVKEKGDYILIVKWGDESVPGSPFKVKVP |
| Enzyme Length | 2725 |
| Uniprot Accession Number | Q14315 |
| Absorption | |
| Active Site | |
| Activity Regulation | |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | |
| DNA Binding | |
| EC Number | |
| Enzyme Function | FUNCTION: Muscle-specific filamin, which plays a central role in sarcomere assembly and organization (PubMed:34405687). Critical for normal myogenesis, it probably functions as a large actin-cross-linking protein with structural functions at the Z lines in muscle cells. May be involved in reorganizing the actin cytoskeleton in response to signaling events (By similarity). {ECO:0000250|UniProtKB:Q8VHX6, ECO:0000269|PubMed:34405687}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Alternative sequence (1); Beta strand (73); Chain (1); Compositional bias (1); Domain (2); Erroneous initiation (2); Frameshift (2); Helix (11); Modified residue (15); Mutagenesis (2); Natural variant (18); Region (9); Repeat (24); Sequence conflict (29); Turn (4) |
| Keywords | 3D-structure;Actin-binding;Alternative splicing;Cardiomyopathy;Cytoplasm;Cytoskeleton;Direct protein sequencing;Disease variant;Membrane;Methylation;Myofibrillar myopathy;Phosphoprotein;Reference proteome;Repeat;Ubl conjugation |
| Interact With | P00519; P46108; P62993; Q9UBF9; Q702N8; O70511-7; Itself; Q9ERP3 |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:11038172, ECO:0000269|PubMed:25351925}. Membrane {ECO:0000269|PubMed:11038172}; Peripheral membrane protein {ECO:0000269|PubMed:11038172}. Cytoplasm, cytoskeleton {ECO:0000269|PubMed:11038172}. Cytoplasm, myofibril, sarcomere, Z line {ECO:0000269|PubMed:11038172}. Note=A small amount localizes at membranes. In striated muscle cells, it predominantly localizes in myofibrillar Z lines, while a minor fraction localizes with subsarcolemme. Targeting to developing and mature Z lines is mediated by the intradomain insert. |
| Modified Residue | MOD_RES 5; /note="Phosphoserine"; /evidence="ECO:0007744|PubMed:23186163"; MOD_RES 1002; /note="Omega-N-methylarginine"; /evidence="ECO:0000250|UniProtKB:Q8VHX6"; MOD_RES 1161; /note="Phosphoserine"; /evidence="ECO:0007744|PubMed:18088087"; MOD_RES 1338; /note="Phosphoserine"; /evidence="ECO:0007744|PubMed:24275569"; MOD_RES 2042; /note="Phosphoserine"; /evidence="ECO:0007744|PubMed:23186163"; MOD_RES 2233; /note="Phosphoserine"; /evidence="ECO:0000269|Ref.8, ECO:0007744|PubMed:19369195, ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569"; MOD_RES 2236; /note="Phosphoserine"; /evidence="ECO:0007744|PubMed:23186163"; MOD_RES 2238; /note="Phosphothreonine"; /evidence="ECO:0007744|PubMed:23186163"; MOD_RES 2586; /note="Phosphoserine"; /evidence="ECO:0007744|PubMed:23186163"; MOD_RES 2617; /note="Phosphoserine"; /evidence="ECO:0007744|PubMed:23186163"; MOD_RES 2620; /note="Phosphoserine"; /evidence="ECO:0007744|PubMed:23186163"; MOD_RES 2623; /note="Phosphoserine"; /evidence="ECO:0007744|PubMed:23186163"; MOD_RES 2632; /note="Phosphoserine"; /evidence="ECO:0007744|PubMed:23186163"; MOD_RES 2714; /note="Phosphoserine"; /evidence="ECO:0007744|PubMed:23186163"; MOD_RES 2718; /note="Phosphoserine"; /evidence="ECO:0007744|PubMed:23186163" |
| Post Translational Modification | PTM: Ubiquitinated by FBXL22, leading to proteasomal degradation. {ECO:0000269|PubMed:22972877}. |
| Signal Peptide | |
| Structure 3D | NMR spectroscopy (6); X-ray crystallography (4) |
| Cross Reference PDB | 1V05; 2D7M; 2D7N; 2D7O; 2D7P; 2D7Q; 2K9U; 2NQC; 3V8O; 4MGX; |
| Mapped Pubmed ID | 12480088; 12679033; 14506720; 15159586; 15461588; 15525470; 17174070; 17353931; 17412757; 17474147; 17825253; 17987659; 18157088; 18457437; 19050726; 19151983; 19367725; 19463016; 19472918; 19615732; 19913121; 20085233; 20417099; 20562859; 20628086; 20706999; 20732627; 20936779; 21182203; 21565611; 21569246; 21988832; 22131542; 22194892; 22623428; 22802962; 23238331; 23292007; 23414517; 23864608; 24349473; 24469451; 24963132; 25110951; 25447537; 25577646; 25609649; 25666618; 26956495; 26969713; 27339502; 27601210; 27626164; 27908349; 28031525; 28356264; 28436997; 28866788; 29073160; 29212899; 29551499; 29858533; 29866061; 30063986; 30118858; 30194514; 30260051; 30354339; 30411535; 30685713; 30867563; 31131323; 31627847; 31843279; 31924696; 32022900; 32112656; 32444788; 32532510; 32607581; 33455984; 33978673; 34411373; 34587765; |
| Motif | |
| Gene Encoded By | |
| Mass | 291,022 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda |