ID BFSP1_CHICK Reviewed; 657 AA.
AC Q06637;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 27-MAR-2024, entry version 119.
DE RecName: Full=Filensin;
DE AltName: Full=Beaded filament structural protein 1;
DE AltName: Full=Lens fiber cell beaded-filament structural protein CP 95;
DE Short=CP95;
DE Contains:
DE RecName: Full=Filensin C-terminal fragment {ECO:0000250|UniProtKB:Q06002};
DE Contains:
DE RecName: Full=Filensin N-terminal fragment {ECO:0000250|UniProtKB:Q06002};
GN Name=BFSP1;
OS Gallus gallus (Chicken).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Phasianinae; Gallus.
OX NCBI_TaxID=9031;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RC STRAIN=White leghorn; TISSUE=Lens;
RX PubMed=7693735; DOI=10.1242/jcs.105.4.1057;
RA Remington S.G.;
RT "Chicken filensin: a lens fiber cell protein that exhibits sequence
RT similarity to intermediate filament proteins.";
RL J. Cell Sci. 105:1057-1068(1993).
CC -!- FUNCTION: Required for the correct formation of lens intermediate
CC filaments. {ECO:0000250|UniProtKB:Q12934}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q06002};
CC Peripheral membrane protein {ECO:0000250|UniProtKB:Q06002}; Cytoplasmic
CC side {ECO:0000250|UniProtKB:Q06002}. Cytoplasm
CC {ECO:0000250|UniProtKB:Q02435}. Cytoplasm, cytoskeleton
CC {ECO:0000250|UniProtKB:Q06002}. Cytoplasm, cell cortex
CC {ECO:0000250|UniProtKB:Q06002}.
CC -!- TISSUE SPECIFICITY: Detected in eye lens fiber cells (at protein
CC level). Detected in embryonic eye lens. {ECO:0000269|PubMed:7693735}.
CC -!- SIMILARITY: Belongs to the intermediate filament family.
CC {ECO:0000255|PROSITE-ProRule:PRU01188}.
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DR EMBL; X72873; CAA51387.1; -; mRNA.
DR PIR; S32739; S32739.
DR RefSeq; NP_990482.1; NM_205151.1.
DR AlphaFoldDB; Q06637; -.
DR SMR; Q06637; -.
DR STRING; 9031.ENSGALP00000038611; -.
DR PaxDb; 9031-ENSGALP00000038611; -.
DR Ensembl; ENSGALT00010043312.1; ENSGALP00010025742.1; ENSGALG00010017915.1.
DR GeneID; 396056; -.
DR KEGG; gga:396056; -.
DR CTD; 631; -.
DR VEuPathDB; HostDB:geneid_396056; -.
DR eggNOG; ENOG502QRCH; Eukaryota.
DR GeneTree; ENSGT00390000016976; -.
DR InParanoid; Q06637; -.
DR OMA; IQTTPRV; -.
DR OrthoDB; 5314345at2759; -.
DR PhylomeDB; Q06637; -.
DR PRO; PR:Q06637; -.
DR Proteomes; UP000000539; Chromosome 3.
DR GO; GO:0005938; C:cell cortex; IEA:UniProtKB-SubCell.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005882; C:intermediate filament; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005212; F:structural constituent of eye lens; IBA:GO_Central.
DR GO; GO:0070307; P:lens fiber cell development; IBA:GO_Central.
DR Gene3D; 1.20.5.170; -; 1.
DR Gene3D; 1.20.5.1160; Vasodilator-stimulated phosphoprotein; 1.
DR InterPro; IPR042358; BFSP1.
DR InterPro; IPR039008; IF_rod_dom.
DR PANTHER; PTHR14069; FILENSIN; 1.
DR PANTHER; PTHR14069:SF0; FILENSIN; 1.
DR Pfam; PF00038; Filament; 1.
DR SMART; SM01391; Filament; 1.
DR SUPFAM; SSF64593; Intermediate filament protein, coiled coil region; 2.
DR PROSITE; PS51842; IF_ROD_2; 1.
PE 1: Evidence at protein level;
KW Cell membrane; Coiled coil; Cytoplasm; Cytoskeleton; Eye lens protein;
KW Intermediate filament; Membrane; Phosphoprotein; Reference proteome;
KW Repeat.
FT CHAIN 1..657
FT /note="Filensin"
FT /id="PRO_0000063849"
FT CHAIN 1..432
FT /note="Filensin N-terminal fragment"
FT /evidence="ECO:0000250|UniProtKB:Q06002"
FT /id="PRO_0000448676"
FT CHAIN 433..657
FT /note="Filensin C-terminal fragment"
FT /evidence="ECO:0000250|UniProtKB:Q06002"
FT /id="PRO_0000448677"
FT DOMAIN 38..318
FT /note="IF rod"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01188"
FT REGION 1..38
FT /note="Head"
FT REGION 39..73
FT /note="Coil 1A"
FT REGION 74..82
FT /note="Linker 1"
FT REGION 83..182
FT /note="Coil 1B"
FT REGION 183..199
FT /note="Linker 12"
FT REGION 200..318
FT /note="Coil 2"
FT REGION 319..657
FT /note="Tail"
FT REGION 503..530
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 565..593
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 515..530
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 432..433
FT /note="Cleavage (by CASP2, CASP3, and CASP7)"
FT /evidence="ECO:0000250|UniProtKB:Q06002"
FT VARIANT 122
FT /note="H -> R"
FT VARIANT 534
FT /note="F -> I"
SQ SEQUENCE 657 AA; 76105 MW; F85117C887048FBF CRC64;
MYRSSFLREV RKEKYERSDA YDELRGSPEF DSLAQAQGLE NLQELNERFA SYINRARVLE
QRNTILRKQL ETFQRMDELV GLDEAFAGQI EFNRQRMREL ASDRAKLERE EKDAQRMLDE
YHNKYRNERE YQQKLKETLE RLNKEADEAL LCNLELQIES QFLQDDINAT KDRYKKNLME
IQTYVNILQQ IIQTTPRVSP ITTGISEEKL VAERRIPVLQ SQLEEYKSIL CQLQAQKYKL
QTETTMLEQA IKNTQESYDD EIQLYNEQIE NLRKGIEEAE RTLEKYTTDC RQLVIYQQSL
ENELERYKRI IENEDSRLNS AIAGTPVTLF TQIYRPVQPQ ASRGRDITQA MQEIASVKPR
QKALTKKLSR KKEIMSKDIT DGLSPEKLYE RTVEVFDQDQ LEFRHEGSVT CEPGQEELEL
VEKEAVPEDV PDGAQISKAF DKLCNLVKEK IRVYKRPEAK VDSHPKGRYV LVTGEEGYEE
PCFSSIPAGG GITVSTSNGK VTIGGDVEPI PELPEPSEPS EKEKRDICER RDEFETQDKL
KEEEKEDLFE WGKIRGKIEQ VTKYPDVSEP EAVPSPGLIS PAEPGVLQET DHDREDKQGL
LFREAGLPGS VSYEKVEVVE SIEKFSDDRI QTYEETAMIV ETMIEKTSKK KPGDKGS
//
