Q12934 · BFSP1_HUMAN
- ProteinFilensin
- GeneBFSP1
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids665 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Required for the correct formation of lens intermediate filaments as part of a complex composed of BFSP1, BFSP2 and CRYAA (PubMed:28935373).
Involved in altering the calcium regulation of MIP water permeability (PubMed:30790544).
Involved in altering the calcium regulation of MIP water permeability (PubMed:30790544).
Features
Showing features for site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Site | 41-42 | Cleavage | ||||
Sequence: LA | ||||||
Site | 433-434 | Cleavage (by CASP2, CASP3, and CASP7) | ||||
Sequence: DG | ||||||
Site | 457 | Interaction with MIP | ||||
Sequence: E |
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 | cell cortex | |
Cellular Component | cytoplasm | |
Cellular Component | intermediate filament | |
Cellular Component | plasma membrane | |
Molecular Function | structural constituent of cytoskeleton | |
Molecular Function | structural constituent of eye lens | |
Biological Process | cell maturation | |
Biological Process | intermediate filament organization | |
Biological Process | lens fiber cell development |
Keywords
- Molecular function
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameFilensin
- Alternative names
- Cleaved into 2 chains
Gene names
Organism names
- Organism
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Hominidae > Homo
Accessions
- Primary accessionQ12934
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Cell membrane ; Peripheral membrane protein
Keywords
- Cellular component
Disease & Variants
Involvement in disease
Cataract 33, multiple types (CTRCT33)
- Note
- DescriptionAn opacification of the crystalline lens of the eye that frequently results in visual impairment or blindness. Opacities vary in morphology, are often confined to a portion of the lens, and may be static or progressive. In general, the more posteriorly located and dense an opacity, the greater the impact on visual function. CTRCT33 has juvenile-onset and the opacities are restricted to the cortex of the lens, not involving the nucleus.
- See alsoMIM:611391
Natural variants in CTRCT33
Variant ID | Position(s) | Change | Description | |
---|---|---|---|---|
VAR_078861 | 348 | D>N | in CTRCT33; dbSNP:rs1085307126 |
Features
Showing features for natural variant, mutagenesis.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Natural variant | VAR_024492 | 345 | in dbSNP:rs6080719 | |||
Sequence: G → S | ||||||
Natural variant | VAR_078861 | 348 | in CTRCT33; dbSNP:rs1085307126 | |||
Sequence: D → N | ||||||
Mutagenesis | 433 | Abolishes cleavage by CASP2. | ||||
Sequence: D → A | ||||||
Mutagenesis | 434 | No effect on cleavage. | ||||
Sequence: G → A | ||||||
Natural variant | VAR_036683 | 656 | in dbSNP:rs16999317 | |||
Sequence: D → E |
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 797 variants from UniProt as well as other sources including ClinVar and dbSNP.
Keywords
- Disease
Organism-specific databases
Miscellaneous
Genetic variation databases
PTM/Processing
Features
Showing features for chain, modified residue, lipidation.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000063847 | 1-665 | Filensin | |||
Sequence: MYRRSYVFQTRKEQYEHADEASRAAEPERPADEGWAGATSLAALQGLGERVAAHVQRARALEQRHAGLRRQLDAFQRLGELAGPEDALARQVESNRQRVRDLEAERARLERQGTEAQRALDEFRSKYENECECQLLLKEMLERLNKEADEALLHNLRLQLEAQFLQDDISAAKDRHKKNLLEVQTYISILQQIIHTTPPASIVTSGMREEKLLTEREVAALRSQLEEGREVLSHLQAQRVELQAQTTTLEQAIKSAHECYDDEIQLYNEQIETLRKEIEETERVLEKSSYDCRQLAVAQQTLKNELDRYHRIIEIEGNRLTSAFIETPIPLFTQSHGVSLSTGSGGKDLTRALQDITAAKPRQKALPKNVPRRKEIITKDKTNGALEDAPLKGLEDTKLVQVVLKEESESKFESESKEVSPLTQEGAPEDVPDGGQISKGFGKLYRKVKEKVRSPKEPETPTELYTKERHVLVTGDANYVDPRFYVSSITAKGGVAVSVAEDSVLYDGQVEPSPESPKPPLENGQVGLQEKEDGQPIDQQPIDKEIEPDGAELEGPEEKREGEERDEESRRPCAMVTPGAEEPSIPEPPKPAADQDGAEVLGTRSRSLPEKGPPKALAYKTVEVVESIEKISTESIQTYEETAVIVETMIGKTKSDKKKSGEKSS | ||||||
Modified residue | 5 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 42 | N-acetylalanine | ||||
Sequence: A | ||||||
Chain | PRO_0000448670 | 42-433 | Filensin N-terminal fragment | |||
Sequence: AALQGLGERVAAHVQRARALEQRHAGLRRQLDAFQRLGELAGPEDALARQVESNRQRVRDLEAERARLERQGTEAQRALDEFRSKYENECECQLLLKEMLERLNKEADEALLHNLRLQLEAQFLQDDISAAKDRHKKNLLEVQTYISILQQIIHTTPPASIVTSGMREEKLLTEREVAALRSQLEEGREVLSHLQAQRVELQAQTTTLEQAIKSAHECYDDEIQLYNEQIETLRKEIEETERVLEKSSYDCRQLAVAQQTLKNELDRYHRIIEIEGNRLTSAFIETPIPLFTQSHGVSLSTGSGGKDLTRALQDITAAKPRQKALPKNVPRRKEIITKDKTNGALEDAPLKGLEDTKLVQVVLKEESESKFESESKEVSPLTQEGAPEDVPD | ||||||
Modified residue | 341 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 420 | Phosphoserine | ||||
Sequence: S | ||||||
Lipidation | 434 | N-myristoyl glycine | ||||
Sequence: G | ||||||
Chain | PRO_0000448671 | 434-665 | Filensin C-terminal fragment | |||
Sequence: GGQISKGFGKLYRKVKEKVRSPKEPETPTELYTKERHVLVTGDANYVDPRFYVSSITAKGGVAVSVAEDSVLYDGQVEPSPESPKPPLENGQVGLQEKEDGQPIDQQPIDKEIEPDGAELEGPEEKREGEERDEESRRPCAMVTPGAEEPSIPEPPKPAADQDGAEVLGTRSRSLPEKGPPKALAYKTVEVVESIEKISTESIQTYEETAVIVETMIGKTKSDKKKSGEKSS | ||||||
Modified residue | 513 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 665 | Phosphoserine | ||||
Sequence: S |
Post-translational modification
Proteolytically cleaved during lens cell fiber differentiation with increased fragmentation as fiber cell age increases.
Filensin C-terminal fragment
Myristoylated at Gly-434 following proteolytic cleavage at Asp-433.
Filensin N-terminal fragment
Acetylated at Ala-42 following proteolytic cleavage at Leu-41.
Keywords
- PTM
Proteomic databases
PTM databases
Interaction
Subunit
Part of a complex required for lens intermediate filament formation composed of BFSP1, BFSP2 and CRYAA (PubMed:28935373).
Identified in a complex that contains VIM, EZR, AHNAK, BFSP1, BFSP2, ANK2, PLEC, PRX and spectrin (By similarity).
Found in a complex composed of PPL (via C-terminal linker domain), BFSP1 and BFSP2 in the retinal lens (By similarity).
Within the complex interacts with BFSP2 (By similarity).
Interacts (via C-terminus) with MIP (via C-terminus) in aged lens fiber cells (By similarity).
Identified in a complex that contains VIM, EZR, AHNAK, BFSP1, BFSP2, ANK2, PLEC, PRX and spectrin (By similarity).
Found in a complex composed of PPL (via C-terminal linker domain), BFSP1 and BFSP2 in the retinal lens (By similarity).
Within the complex interacts with BFSP2 (By similarity).
Interacts (via C-terminus) with MIP (via C-terminus) in aged lens fiber cells (By similarity).
Binary interactions
Type | Entry 1 | Entry 2 | Number of experiments | Intact | |
---|---|---|---|---|---|
BINARY | Q12934 | NUP62 P37198 | 3 | EBI-10227494, EBI-347978 | |
BINARY | Q12934-2 | BFSP2 Q13515 | 5 | EBI-12123320, EBI-10229433 | |
BINARY | Q12934-2 | BYSL Q13895 | 3 | EBI-12123320, EBI-358049 | |
BINARY | Q12934-2 | CCHCR1 Q8TD31-3 | 3 | EBI-12123320, EBI-10175300 | |
BINARY | Q12934-2 | EMILIN1 Q9Y6C2-2 | 3 | EBI-12123320, EBI-11748557 | |
BINARY | Q12934-2 | KIFC3 Q9BVG8-5 | 3 | EBI-12123320, EBI-14069005 | |
BINARY | Q12934-2 | KRT27 Q7Z3Y8 | 3 | EBI-12123320, EBI-3044087 | |
BINARY | Q12934-2 | NUP62 P37198 | 3 | EBI-12123320, EBI-347978 | |
BINARY | Q12934-2 | SNAPIN O95295 | 3 | EBI-12123320, EBI-296723 | |
BINARY | Q12934-2 | USHBP1 Q8N6Y0 | 3 | EBI-12123320, EBI-739895 | |
BINARY | Q12934-2 | ZWINT O95229 | 3 | EBI-12123320, EBI-1001132 |
Protein-protein interaction databases
Miscellaneous
Structure
Family & Domains
Features
Showing features for region, domain, compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 1-40 | Head | ||||
Sequence: MYRRSYVFQTRKEQYEHADEASRAAEPERPADEGWAGATS | ||||||
Domain | 40-320 | IF rod | ||||
Sequence: SLAALQGLGERVAAHVQRARALEQRHAGLRRQLDAFQRLGELAGPEDALARQVESNRQRVRDLEAERARLERQGTEAQRALDEFRSKYENECECQLLLKEMLERLNKEADEALLHNLRLQLEAQFLQDDISAAKDRHKKNLLEVQTYISILQQIIHTTPPASIVTSGMREEKLLTEREVAALRSQLEEGREVLSHLQAQRVELQAQTTTLEQAIKSAHECYDDEIQLYNEQIETLRKEIEETERVLEKSSYDCRQLAVAQQTLKNELDRYHRIIEIEGNRL | ||||||
Region | 41-75 | Coil 1A | ||||
Sequence: LAALQGLGERVAAHVQRARALEQRHAGLRRQLDAF | ||||||
Region | 76-84 | Linker 1 | ||||
Sequence: QRLGELAGP | ||||||
Region | 85-184 | Coil 1B | ||||
Sequence: EDALARQVESNRQRVRDLEAERARLERQGTEAQRALDEFRSKYENECECQLLLKEMLERLNKEADEALLHNLRLQLEAQFLQDDISAAKDRHKKNLLEVQ | ||||||
Region | 185-201 | Linker 12 | ||||
Sequence: TYISILQQIIHTTPPAS | ||||||
Region | 202-320 | Coil 2 | ||||
Sequence: IVTSGMREEKLLTEREVAALRSQLEEGREVLSHLQAQRVELQAQTTTLEQAIKSAHECYDDEIQLYNEQIETLRKEIEETERVLEKSSYDCRQLAVAQQTLKNELDRYHRIIEIEGNRL | ||||||
Region | 321-665 | Tail | ||||
Sequence: TSAFIETPIPLFTQSHGVSLSTGSGGKDLTRALQDITAAKPRQKALPKNVPRRKEIITKDKTNGALEDAPLKGLEDTKLVQVVLKEESESKFESESKEVSPLTQEGAPEDVPDGGQISKGFGKLYRKVKEKVRSPKEPETPTELYTKERHVLVTGDANYVDPRFYVSSITAKGGVAVSVAEDSVLYDGQVEPSPESPKPPLENGQVGLQEKEDGQPIDQQPIDKEIEPDGAELEGPEEKREGEERDEESRRPCAMVTPGAEEPSIPEPPKPAADQDGAEVLGTRSRSLPEKGPPKALAYKTVEVVESIEKISTESIQTYEETAVIVETMIGKTKSDKKKSGEKSS | ||||||
Region | 410-439 | Disordered | ||||
Sequence: SKFESESKEVSPLTQEGAPEDVPDGGQISK | ||||||
Region | 506-614 | Disordered | ||||
Sequence: YDGQVEPSPESPKPPLENGQVGLQEKEDGQPIDQQPIDKEIEPDGAELEGPEEKREGEERDEESRRPCAMVTPGAEEPSIPEPPKPAADQDGAEVLGTRSRSLPEKGPP | ||||||
Compositional bias | 536-572 | Basic and acidic residues | ||||
Sequence: PIDQQPIDKEIEPDGAELEGPEEKREGEERDEESRRP |
Sequence similarities
Belongs to the intermediate filament family.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence & Isoforms
- Sequence statusComplete
This entry describes 3 isoforms produced by Alternative splicing.
Q12934-1
This isoform has been chosen as the canonical sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
- Name1
- Length665
- Mass (Da)74,544
- Last updated2001-09-26 v3
- ChecksumA99FE174A8B63E9C
Q12934-2
- Name2
Q12934-3
- Name3
- Differences from canonical
- 1-139: Missing
Sequence caution
Features
Showing features for alternative sequence, sequence conflict, compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Alternative sequence | VSP_024921 | 1-125 | in isoform 2 | |||
Sequence: Missing | ||||||
Alternative sequence | VSP_055064 | 1-139 | in isoform 3 | |||
Sequence: Missing | ||||||
Sequence conflict | 96 | in Ref. 6; AAG17186 | ||||
Sequence: R → P | ||||||
Alternative sequence | VSP_024922 | 126 | in isoform 2 | |||
Sequence: K → M | ||||||
Sequence conflict | 176-177 | in Ref. 5; AAA74423 | ||||
Sequence: HK → TR | ||||||
Sequence conflict | 248 | in Ref. 5; AAA74423 | ||||
Sequence: T → A | ||||||
Sequence conflict | 398 | in Ref. 1; AAB94939 | ||||
Sequence: K → R | ||||||
Compositional bias | 536-572 | Basic and acidic residues | ||||
Sequence: PIDQQPIDKEIEPDGAELEGPEEKREGEERDEESRRP | ||||||
Sequence conflict | 568 | in Ref. 1; AAB94939 | ||||
Sequence: E → G |
Keywords
- Coding sequence diversity
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AF039655 EMBL· GenBank· DDBJ | AAB94939.1 EMBL· GenBank· DDBJ | mRNA | ||
Y16717 EMBL· GenBank· DDBJ | CAA76348.1 EMBL· GenBank· DDBJ | mRNA | ||
Y16718 EMBL· GenBank· DDBJ | CAA76349.1 EMBL· GenBank· DDBJ | Genomic DNA | Sequence problems. | |
Y16719 EMBL· GenBank· DDBJ | CAA76349.1 EMBL· GenBank· DDBJ | Genomic DNA | Sequence problems. | |
Y16720 EMBL· GenBank· DDBJ | CAA76349.1 EMBL· GenBank· DDBJ | Genomic DNA | Sequence problems. | |
Y16722 EMBL· GenBank· DDBJ | CAA76349.1 EMBL· GenBank· DDBJ | Genomic DNA | Sequence problems. | |
Y16723 EMBL· GenBank· DDBJ | CAA76349.1 EMBL· GenBank· DDBJ | Genomic DNA | Sequence problems. | |
Y16721 EMBL· GenBank· DDBJ | CAA76349.1 EMBL· GenBank· DDBJ | Genomic DNA | Sequence problems. | |
AL031664 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
AL132765 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
BC041483 EMBL· GenBank· DDBJ | AAH41483.1 EMBL· GenBank· DDBJ | mRNA | ||
U12622 EMBL· GenBank· DDBJ | AAA74423.1 EMBL· GenBank· DDBJ | mRNA | ||
AH009849 EMBL· GenBank· DDBJ | AAG17186.1 EMBL· GenBank· DDBJ | Genomic DNA |