D3ZHA0 · FLNC_RAT
- ProteinFilamin-C
- GeneFlnc
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids2726 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Muscle-specific filamin, which plays a central role in sarcomere assembly and organization. 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.
GO annotations
all annotations | all molecular function | virus receptor activity | dna binding | rna binding | cytoskeletal motor activity | catalytic activity | gtpase activity | structural molecule activity | transporter activity | cytoskeletal protein binding | lipid binding | cyclase activity | antioxidant activity | oxidoreductase activity | transferase activity | hydrolase activity | lyase activity | isomerase activity | ligase activity | protein tag activity | cargo receptor activity | histone binding | protein folding chaperone | translation regulator activity | nutrient reservoir activity | receptor ligand activity | molecular transducer activity | molecular adaptor activity | toxin activity | cell adhesion mediator activity | molecular function regulator activity | virus coreceptor activity | catalytic activity, acting on a protein | catalytic activity, acting on dna | catalytic activity, acting on rna | molecular carrier activity | transcription regulator activity | general transcription initiation factor activity | molecular sensor activity | molecular sequestering activity | atp-dependent activity | other molecular function | all biological process | mitotic cell cycle | cytokinesis | cytoplasmic translation | immune system process | muscle system process | circulatory system process | renal system process | respiratory system process | carbohydrate metabolic process | generation of precursor metabolites and energy | dna replication | dna repair | dna recombination | chromatin organization | dna-templated transcription | regulation of dna-templated transcription | trna metabolic process | protein folding | protein glycosylation | amino acid metabolic process | modified amino acid metabolic process | lipid metabolic process | vitamin metabolic process | sulfur compound metabolic process | intracellular protein transport | nucleocytoplasmic transport | autophagy | inflammatory response | mitochondrion organization | cytoskeleton organization | microtubule-based movement | peroxisome organization | lysosome organization | chromosome segregation | cell adhesion | establishment or maintenance of cell polarity | programmed cell death | photosynthesis | mrna metabolic process | snrna metabolic process | vesicle-mediated transport | reproductive process | digestive system process | signaling | cell differentiation | protein catabolic process | extracellular matrix organization | regulatory ncrna-mediated gene silencing | telomere organization | cell junction organization | wound healing | ribosome biogenesis | cilium organization | anatomical structure development | cell motility | nervous system process | endocrine process | protein maturation | transmembrane transport | nucleobase-containing small molecule metabolic process | hepaticobiliary system process | membrane organization | protein-containing complex assembly | cell wall organization or biogenesis | nitrogen cycle metabolic process | protein localization to plasma membrane | defense response to other organism | detoxification | meiotic nuclear division | mitotic nuclear division | mitochondrial gene expression | carbohydrate derivative metabolic process | other biological process | all cellular component | nuclear chromosome | extracellular region | extracellular space | cell wall | nucleus | nuclear envelope | nucleoplasm | chromosome | nucleolus | mitochondrion | lysosome | endosome | vacuole | peroxisome | endoplasmic reticulum | golgi apparatus | lipid droplet | microtubule organizing center | cytosol | ribosome | cytoskeleton | plasma membrane | cilium | plastid | thylakoid | external encapsulating structure | extracellular matrix | cytoplasmic vesicle | organelle | other cellular component | |||
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Aspect | Term | |
---|---|---|
Cellular Component | costamere | |
Cellular Component | cytoplasm | |
Cellular Component | cytoskeleton | |
Cellular Component | cytosol | |
Cellular Component | intercellular bridge | |
Cellular Component | sarcolemma | |
Cellular Component | sarcoplasm | |
Cellular Component | Z disc | |
Molecular Function | actin filament binding | |
Molecular Function | ankyrin binding | |
Molecular Function | cytoskeletal protein binding | |
Biological Process | muscle cell development | |
Biological Process | sarcomere organization |
Keywords
- Molecular function
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameFilamin-C
- Short namesFLN-C
- Alternative names
Gene names
Organism names
- Organism
- Strain
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Glires > Rodentia > Myomorpha > Muroidea > Muridae > Murinae > Rattus
Accessions
- Primary accessionD3ZHA0
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Membrane ; Peripheral membrane protein
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 (By similarity).
Keywords
- Cellular component
PTM/Processing
Features
Showing features for chain, modified residue.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000429633 | 1-2726 | Filamin-C | |||
Sequence: MMNNSNYSDASGLGLLDEADEMPSTEKDLAEDAPWKKIQQNTFTRWCNEHLKCVGKRLTDLQRDLSDGLRLIALLEVLSQKRMYRKFHPRPNFRQMKLENVSVALEFLEREHIKLVSIDSKAIVDGNLKLILGLIWTLILHYSISMPMWEDEDDEDARKQTPKQRLLGWIQNKVPQLPITNFNRDWQDGKALGALVDNCAPGLCPDWEAWDPNQPVQNAREAMQQADDWLGVPQVIAPEEIVDPNVDEHSVMTYLSQFPKAKLKPGAPVRSKQLNPKKAIAYGPGIEPQGNTVLQPAHFTVQTVDAGVGEVLVYIEDPEGHTEEAKVVPNNDKDRTYAVSYVPKVAGLHKVTVLFAGQNIERSPFEVNVGMALGDANKVSARGPGLEPVGNVANKPTYFDIYTAGAGTGDVAVVIVDPQGRRDTVEVALEDKGDNTFRCTYRPVMEGPHTVHVAFAGAPITRSPFPVHVAEACNPNACRASGRGLQPKGVRVKEVADFKVFTKGAGSGELKVTVKGPKGTEEPVKVREAGDGVFECEYYPVIPGKYVVTITWGGYAIPRSPFEVQVSPEAGAQKVRAWGPGLETGQVGKSADFVVEAIGTEVGTLGFSIEGPSQAKIECDDRGDGSCDVRYWPTEPGEYAVHVICDDEDIRDSPFIAHIQPAPPDCFPDKVKAFGPGLEPTGCIVDRPAEFTIDARAAGKGDLKLYAQDADGCPIDIKVIPNGDGTFRCSYVPTKPIKHTVIISWGGVNVPKSPFRVNVGEGSHPERVKVYGPGVEKTGLKANEPTYFTVDCSEAGQGDVSIGIKCAPGVVGPAEADIDFDIIKNDNDTFTVKYTPPGAGHYTIMVLFANQEIPASPFHIKVDPSHDASKVKAEGPGLSRTGVEVGKPTHFTVLTKGAGKAKLDVHFAGAAKGEAVRDFEIIDNHDYSYTVKYTAVQQGNMAVTVTYGGDPVPKSPFVVNVAPPLDLSKVKVQGLNSKVAVGEEQAFLVNTRGAGGQGQLDVRMTSPSRRPIPCKLEPGSGAEAQAVRYMPPEEGPYKVDITYDGHPVPGSPFAVEGVLPPDPSKVCAYGPGLKGGLVGTPAPFSIDTKGAGTGGLGLTVEGPCEAKIECQDNGDGSCAVSYLPTEPGEYTINILFAEAHIPGSPFKATIQPVFDPSKVRASGPGLERGKAGEAATFTVDCSEAGEAELTIEILSDAGVKAEVLIHNNADGTYHITYSPAFPGTYTITIKYGGHPIPKFPTRVHVQPAVDTSGIKVSGPGVEPHGVLREVTTEFTVDARSLTATGGNHVTARVLNPSGAKTDTYVTDNGDGTYRVQYTAYEEGVHLVEVLYDEVAVPKSPFRVGVTEGCDPTRVRAFGPGLEGGLVNKANRFTVETRGAGTGGLGLAIEGPSEAKMSCKDNKDGSCTVEYVPFTPGDYDVNITFGGQPIPGSPFRVPVKDVVDPGKVKCSGPGLGTGVRARVPQTFTVDCSQAGRAPLQVAVLGPTGVAEPVEVRDNGDGTHTVHYTPATDGPYTVAVKYADQEVPRSPFKIKVLPAHDASKVRASGPGLNASGIPASLPVEFTIDARDAGEGLLTVQILDPEGKPKKANIRDNGDGTYTVSYLPDMSGRYTITIKYGGDEIPYSPFRIHALPTGDASKCLVTVSIGGHGLGACLGPRIQIGEETVITVDAKAAGKGKVTCTVSTPDGAELDVDVVENHDGTFDIYYTAPEPGKYVITIRFGGEHIPNSPFHVLACDPLPHVEEPAEVLQLHQPYAPLRPGTCPTHWATEEPVVPVEPLESMLRPFNLVIPFTVQKGELTGEVRMPSGKTARPNITDNKDGTITVRYAPTEKGLHQMGIKYDGNHIPGSPLQFYVDAINSGHVSAYGPGLSHGMVNKPATFTIVTKDAGEGGLSLAVEGPSKAEITCKDNKDGTCTVSYLPTAPGDYSIIVRFDDKHIPGSPFTAKITGDDSMRTSQLNVGTSTDVSLKITEGDLSQLTASIRAPSGNEEPCLLKRLPNRHIGISFTPKEVGEHVVSVRKSGKHVTNSPFKILVGPSEIGDASKVRVWGKGLSEGQTFQVAEFIVDTRNAGYGGLGLSIEGPSKVDINCEDMEDGTCKVTYCPTEPGTYIINIKFADKHVPGSPFTVKVTGEGRMKESITRRRQAPSIATIGSTCDLNLKIPGNWFQMVSAQERLTRTFTRSSHTYTRTERTEISKTRGGETKREVRVEESTQVGGDPFPAVFGDFLGRERLGSFGSITRQQEGEASSQDMTAQVTSPSGKTEAAEIVEGEDSAYSVRFVPQEMGPHTVAVKYRGQHVPGSPFQFTVGPLGEGGAHKVRAGGTGLERGVAGVPAEFSIWTREAGAGGLSIAVEGPSKAEIAFEDRKDGSCGVSYVVQEPGDYEVSIKFNDEHIPDSPFVVPVASLSDDARRLTVTSLQETGLKVNQPASFAVQLNGARGVIDARVHTPSGAVEECYVSELDSDKHTIRFIPHENGVHSIDVKFNGAHIPGSPFKIRVGEQSQAGDPGLVSAYGPGLEGGTTGVSSEFIVNTQNAGSGALSVTIDGPSKVQLDCRECPEGHVVTYTPMAPGNYLIAIKYGGPQHIVGSPFKAKVTGPRLSGGHSLHETSTVLVETVTKSSSSRGASYSSIPKFSSDASKVVTRGPGLSQAFVGQKNSFTVDCSKAGTNMMMVGVHGPKTPCEEVYVKHMGNRVYNVTYTVKEKGDYILIVKWGDESVPGSPFKVNVP | ||||||
Modified residue | 5 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 1003 | Omega-N-methylarginine | ||||
Sequence: R | ||||||
Modified residue | 1162 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 1339 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 2043 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 2234 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 2237 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 2239 | Phosphothreonine | ||||
Sequence: T | ||||||
Modified residue | 2587 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 2618 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 2621 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 2633 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 2715 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 2719 | Phosphoserine | ||||
Sequence: S |
Post-translational modification
Ubiquitinated by FBXL22, leading to proteasomal degradation.
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Gene expression databases
Interaction
Subunit
Homodimer; the filamin repeat 24 and the second hinge domain are important for dimer formation (By similarity).
Interacts with FLNB, KCND2, INPPL1, ITGB1A, MYOT, MYOZ1 and MYOZ3 (By similarity).
Interacts with sarcoglycans SGCD and SGCG (By similarity).
Interacts (via filament repeats 17-18, 20-21 and 24) with USP25 (isoform USP25m only) (By similarity).
Interacts with FBLIM1 (By similarity).
Interacts with KY (By similarity).
Interacts with IGFN1 (By similarity).
Interacts with MICALL2 (By similarity).
Interacts with XIRP1; this interaction is mediated by filamin 20 repeat (By similarity).
Interacts with ANK3. Interacts with SYNPO2 (By similarity).
Interacts with FLNB, KCND2, INPPL1, ITGB1A, MYOT, MYOZ1 and MYOZ3 (By similarity).
Interacts with sarcoglycans SGCD and SGCG (By similarity).
Interacts (via filament repeats 17-18, 20-21 and 24) with USP25 (isoform USP25m only) (By similarity).
Interacts with FBLIM1 (By similarity).
Interacts with KY (By similarity).
Interacts with IGFN1 (By similarity).
Interacts with MICALL2 (By similarity).
Interacts with XIRP1; this interaction is mediated by filamin 20 repeat (By similarity).
Interacts with ANK3. Interacts with SYNPO2 (By similarity).
Protein-protein interaction databases
Family & Domains
Features
Showing features for region, domain, repeat, compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 1-260 | Actin-binding | ||||
Sequence: MMNNSNYSDASGLGLLDEADEMPSTEKDLAEDAPWKKIQQNTFTRWCNEHLKCVGKRLTDLQRDLSDGLRLIALLEVLSQKRMYRKFHPRPNFRQMKLENVSVALEFLEREHIKLVSIDSKAIVDGNLKLILGLIWTLILHYSISMPMWEDEDDEDARKQTPKQRLLGWIQNKVPQLPITNFNRDWQDGKALGALVDNCAPGLCPDWEAWDPNQPVQNAREAMQQADDWLGVPQVIAPEEIVDPNVDEHSVMTYLSQFPK | ||||||
Domain | 37-143 | Calponin-homology (CH) 1 | ||||
Sequence: KIQQNTFTRWCNEHLKCVGKRLTDLQRDLSDGLRLIALLEVLSQKRMYRKFHPRPNFRQMKLENVSVALEFLEREHIKLVSIDSKAIVDGNLKLILGLIWTLILHYS | ||||||
Domain | 160-263 | Calponin-homology (CH) 2 | ||||
Sequence: QTPKQRLLGWIQNKVPQLPITNFNRDWQDGKALGALVDNCAPGLCPDWEAWDPNQPVQNAREAMQQADDWLGVPQVIAPEEIVDPNVDEHSVMTYLSQFPKAKL | ||||||
Repeat | 271-369 | Filamin 1 | ||||
Sequence: SKQLNPKKAIAYGPGIEPQGNTVLQPAHFTVQTVDAGVGEVLVYIEDPEGHTEEAKVVPNNDKDRTYAVSYVPKVAGLHKVTVLFAGQNIERSPFEVNV | ||||||
Repeat | 371-469 | Filamin 2 | ||||
Sequence: MALGDANKVSARGPGLEPVGNVANKPTYFDIYTAGAGTGDVAVVIVDPQGRRDTVEVALEDKGDNTFRCTYRPVMEGPHTVHVAFAGAPITRSPFPVHV | ||||||
Repeat | 470-566 | Filamin 3 | ||||
Sequence: AEACNPNACRASGRGLQPKGVRVKEVADFKVFTKGAGSGELKVTVKGPKGTEEPVKVREAGDGVFECEYYPVIPGKYVVTITWGGYAIPRSPFEVQV | ||||||
Repeat | 567-659 | Filamin 4 | ||||
Sequence: SPEAGAQKVRAWGPGLETGQVGKSADFVVEAIGTEVGTLGFSIEGPSQAKIECDDRGDGSCDVRYWPTEPGEYAVHVICDDEDIRDSPFIAHI | ||||||
Repeat | 663-759 | Filamin 5 | ||||
Sequence: PPDCFPDKVKAFGPGLEPTGCIVDRPAEFTIDARAAGKGDLKLYAQDADGCPIDIKVIPNGDGTFRCSYVPTKPIKHTVIISWGGVNVPKSPFRVNV | ||||||
Repeat | 760-862 | Filamin 6 | ||||
Sequence: GEGSHPERVKVYGPGVEKTGLKANEPTYFTVDCSEAGQGDVSIGIKCAPGVVGPAEADIDFDIIKNDNDTFTVKYTPPGAGHYTIMVLFANQEIPASPFHIKV | ||||||
Repeat | 863-961 | Filamin 7 | ||||
Sequence: DPSHDASKVKAEGPGLSRTGVEVGKPTHFTVLTKGAGKAKLDVHFAGAAKGEAVRDFEIIDNHDYSYTVKYTAVQQGNMAVTVTYGGDPVPKSPFVVNV | ||||||
Repeat | 962-1057 | Filamin 8 | ||||
Sequence: APPLDLSKVKVQGLNSKVAVGEEQAFLVNTRGAGGQGQLDVRMTSPSRRPIPCKLEPGSGAEAQAVRYMPPEEGPYKVDITYDGHPVPGSPFAVEG | ||||||
Repeat | 1058-1150 | Filamin 9 | ||||
Sequence: VLPPDPSKVCAYGPGLKGGLVGTPAPFSIDTKGAGTGGLGLTVEGPCEAKIECQDNGDGSCAVSYLPTEPGEYTINILFAEAHIPGSPFKATI | ||||||
Repeat | 1151-1245 | Filamin 10 | ||||
Sequence: QPVFDPSKVRASGPGLERGKAGEAATFTVDCSEAGEAELTIEILSDAGVKAEVLIHNNADGTYHITYSPAFPGTYTITIKYGGHPIPKFPTRVHV | ||||||
Repeat | 1246-1345 | Filamin 11 | ||||
Sequence: QPAVDTSGIKVSGPGVEPHGVLREVTTEFTVDARSLTATGGNHVTARVLNPSGAKTDTYVTDNGDGTYRVQYTAYEEGVHLVEVLYDEVAVPKSPFRVGV | ||||||
Repeat | 1346-1438 | Filamin 12 | ||||
Sequence: TEGCDPTRVRAFGPGLEGGLVNKANRFTVETRGAGTGGLGLAIEGPSEAKMSCKDNKDGSCTVEYVPFTPGDYDVNITFGGQPIPGSPFRVPV | ||||||
Repeat | 1439-1534 | Filamin 13 | ||||
Sequence: KDVVDPGKVKCSGPGLGTGVRARVPQTFTVDCSQAGRAPLQVAVLGPTGVAEPVEVRDNGDGTHTVHYTPATDGPYTVAVKYADQEVPRSPFKIKV | ||||||
Repeat | 1535-1631 | Filamin 14 | ||||
Sequence: LPAHDASKVRASGPGLNASGIPASLPVEFTIDARDAGEGLLTVQILDPEGKPKKANIRDNGDGTYTVSYLPDMSGRYTITIKYGGDEIPYSPFRIHA | ||||||
Repeat | 1636-1735 | Filamin 15 | ||||
Sequence: DASKCLVTVSIGGHGLGACLGPRIQIGEETVITVDAKAAGKGKVTCTVSTPDGAELDVDVVENHDGTFDIYYTAPEPGKYVITIRFGGEHIPNSPFHVLA | ||||||
Region | 1736-1759 | Hinge 1 | ||||
Sequence: CDPLPHVEEPAEVLQLHQPYAPLR | ||||||
Repeat | 1760-1854 | Filamin 16 | ||||
Sequence: PGTCPTHWATEEPVVPVEPLESMLRPFNLVIPFTVQKGELTGEVRMPSGKTARPNITDNKDGTITVRYAPTEKGLHQMGIKYDGNHIPGSPLQFY | ||||||
Repeat | 1855-1947 | Filamin 17 | ||||
Sequence: VDAINSGHVSAYGPGLSHGMVNKPATFTIVTKDAGEGGLSLAVEGPSKAEITCKDNKDGTCTVSYLPTAPGDYSIIVRFDDKHIPGSPFTAKI | ||||||
Repeat | 1948-2034 | Filamin 18 | ||||
Sequence: TGDDSMRTSQLNVGTSTDVSLKITEGDLSQLTASIRAPSGNEEPCLLKRLPNRHIGISFTPKEVGEHVVSVRKSGKHVTNSPFKILV | ||||||
Repeat | 2037-2129 | Filamin 19 | ||||
Sequence: SEIGDASKVRVWGKGLSEGQTFQVAEFIVDTRNAGYGGLGLSIEGPSKVDINCEDMEDGTCKVTYCPTEPGTYIINIKFADKHVPGSPFTVKV | ||||||
Region | 2163-2244 | Intradomain insert; mediate targeting to Z lines | ||||
Sequence: GNWFQMVSAQERLTRTFTRSSHTYTRTERTEISKTRGGETKREVRVEESTQVGGDPFPAVFGDFLGRERLGSFGSITRQQEG | ||||||
Compositional bias | 2194-2211 | Basic and acidic residues | ||||
Sequence: ISKTRGGETKREVRVEES | ||||||
Region | 2194-2214 | Disordered | ||||
Sequence: ISKTRGGETKREVRVEESTQV | ||||||
Region | 2241-2261 | Disordered | ||||
Sequence: QQEGEASSQDMTAQVTSPSGK | ||||||
Repeat | 2245-2307 | Filamin 20; mediates interaction with XIRP1 | ||||
Sequence: EASSQDMTAQVTSPSGKTEAAEIVEGEDSAYSVRFVPQEMGPHTVAVKYRGQHVPGSPFQFTV | ||||||
Repeat | 2310-2402 | Filamin 21 | ||||
Sequence: LGEGGAHKVRAGGTGLERGVAGVPAEFSIWTREAGAGGLSIAVEGPSKAEIAFEDRKDGSCGVSYVVQEPGDYEVSIKFNDEHIPDSPFVVPV | ||||||
Repeat | 2404-2497 | Filamin 22 | ||||
Sequence: SLSDDARRLTVTSLQETGLKVNQPASFAVQLNGARGVIDARVHTPSGAVEECYVSELDSDKHTIRFIPHENGVHSIDVKFNGAHIPGSPFKIRV | ||||||
Region | 2404-2725 | Interaction with INPPL1 | ||||
Sequence: SLSDDARRLTVTSLQETGLKVNQPASFAVQLNGARGVIDARVHTPSGAVEECYVSELDSDKHTIRFIPHENGVHSIDVKFNGAHIPGSPFKIRVGEQSQAGDPGLVSAYGPGLEGGTTGVSSEFIVNTQNAGSGALSVTIDGPSKVQLDCRECPEGHVVTYTPMAPGNYLIAIKYGGPQHIVGSPFKAKVTGPRLSGGHSLHETSTVLVETVTKSSSSRGASYSSIPKFSSDASKVVTRGPGLSQAFVGQKNSFTVDCSKAGTNMMMVGVHGPKTPCEEVYVKHMGNRVYNVTYTVKEKGDYILIVKWGDESVPGSPFKVNV | ||||||
Repeat | 2501-2593 | Filamin 23 | ||||
Sequence: SQAGDPGLVSAYGPGLEGGTTGVSSEFIVNTQNAGSGALSVTIDGPSKVQLDCRECPEGHVVTYTPMAPGNYLIAIKYGGPQHIVGSPFKAKV | ||||||
Region | 2594-2630 | Hinge 2 | ||||
Sequence: TGPRLSGGHSLHETSTVLVETVTKSSSSRGASYSSIP | ||||||
Region | 2594-2726 | Self-association site, tail | ||||
Sequence: TGPRLSGGHSLHETSTVLVETVTKSSSSRGASYSSIPKFSSDASKVVTRGPGLSQAFVGQKNSFTVDCSKAGTNMMMVGVHGPKTPCEEVYVKHMGNRVYNVTYTVKEKGDYILIVKWGDESVPGSPFKVNVP | ||||||
Repeat | 2631-2725 | Filamin 24 | ||||
Sequence: KFSSDASKVVTRGPGLSQAFVGQKNSFTVDCSKAGTNMMMVGVHGPKTPCEEVYVKHMGNRVYNVTYTVKEKGDYILIVKWGDESVPGSPFKVNV |
Sequence similarities
Belongs to the filamin family.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length2,726
- Mass (Da)290,986
- Last updated2010-04-20 v1
- ChecksumA91CE65E935EC2CD
Computationally mapped potential isoform sequences
There are 3 potential isoforms mapped to this entry
Entry | Entry name | Gene name | Length | ||
---|---|---|---|---|---|
A0A8L2R384 | A0A8L2R384_RAT | Flnc | 2717 | ||
A0A0H2UHR7 | A0A0H2UHR7_RAT | Flnc | 2693 | ||
A0A8I5ZMA0 | A0A8I5ZMA0_RAT | Flnc | 2606 |
Features
Showing features for compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 2194-2211 | Basic and acidic residues | ||||
Sequence: ISKTRGGETKREVRVEES |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AABR06030202 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. |