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BFSP1_CHICK
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   03-AUG-2022, entry version 114.
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; Q06637; -.
DR   GeneID; 396056; -.
DR   KEGG; gga:396056; -.
DR   CTD; 631; -.
DR   VEuPathDB; HostDB:geneid_396056; -.
DR   eggNOG; ENOG502QRCH; Eukaryota.
DR   InParanoid; Q06637; -.
DR   OrthoDB; 677568at2759; -.
DR   PhylomeDB; Q06637; -.
DR   PRO; PR:Q06637; -.
DR   Proteomes; UP000000539; Unplaced.
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   InterPro; IPR042358; BFSP1.
DR   InterPro; IPR039008; IF_rod_dom.
DR   PANTHER; PTHR14069; PTHR14069; 1.
DR   Pfam; PF00038; Filament; 1.
DR   SMART; SM01391; Filament; 1.
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
 
 
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