BFSP1_RAT
ID BFSP1_RAT Reviewed; 617 AA.
AC Q02435;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1997, sequence version 2.
DT 25-MAY-2022, 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 94;
DE Short=CP94;
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};
DE Flags: Fragment;
GN Name=Bfsp1;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RC STRAIN=Sprague-Dawley; TISSUE=Lens;
RX PubMed=1378722; DOI=10.1016/s0006-291x(05)80792-2;
RA Masaki S., Watanabe T.;
RT "cDNA sequence analysis of CP94: rat lens fiber cell beaded-filament
RT structural protein shows homology to cytokeratins.";
RL Biochem. Biophys. Res. Commun. 186:190-198(1992).
RN [2]
RP SEQUENCE REVISION.
RA Masaki S.;
RL Submitted (APR-1997) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=18449355;
RA Oka M., Kudo H., Sugama N., Asami Y., Takehana M.;
RT "The function of filensin and phakinin in lens transparency.";
RL Mol. Vis. 14:815-822(2008).
CC -!- FUNCTION: Required for the correct formation of lens intermediate
CC filaments as part of a complex composed of BFSP1, BFSP2 and CRYAA (By
CC similarity). Involved in altering the calcium regulation of MIP water
CC permeability (By similarity). {ECO:0000250|UniProtKB:A2AMT1,
CC ECO:0000250|UniProtKB:Q12934}.
CC -!- SUBUNIT: Part of a complex required for lens intermediate filament
CC formation composed of BFSP1, BFSP2 and CRYAA (By similarity).
CC Identified in a complex that contains VIM, EZR, AHNAK, BFSP1, BFSP2,
CC ANK2, PLEC, PRX and spectrin (By similarity). Found in a complex
CC composed of PPL (via C-terminal linker domain), BFSP1 and BFSP2 in the
CC retinal lens (By similarity). Within the complex interacts with BFSP2
CC (By similarity). Interacts (via C-terminus) with MIP (via C-terminus)
CC in aged lens fiber cells (By similarity).
CC {ECO:0000250|UniProtKB:A2AMT1, ECO:0000250|UniProtKB:Q06002,
CC ECO:0000250|UniProtKB:Q12934}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:18449355};
CC Peripheral membrane protein {ECO:0000250|UniProtKB:Q06002}; Cytoplasmic
CC side {ECO:0000250|UniProtKB:Q06002}. Cytoplasm
CC {ECO:0000269|PubMed:18449355}. Cytoplasm, cytoskeleton
CC {ECO:0000250|UniProtKB:Q06002}. Cytoplasm, cell cortex
CC {ECO:0000250|UniProtKB:Q06002}.
CC -!- TISSUE SPECIFICITY: Expressed in the deep and shallow cortices of the
CC retina lens (at protein level). {ECO:0000269|PubMed:1378722,
CC ECO:0000269|PubMed:18449355}.
CC -!- PTM: Proteolytically cleaved during lens cell fiber differentiation
CC with increased fragmentation as fiber cell age increases.
CC {ECO:0000250|UniProtKB:Q06002}.
CC -!- PTM: [Filensin C-terminal fragment]: Myristoylated at Gly-427 following
CC proteolytic cleavage at Asp-426. {ECO:0000250|UniProtKB:Q06002}.
CC -!- PTM: [Filensin N-terminal fragment]: Acetylated at Ala-35 following
CC proteolytic cleavage at Leu-34. {ECO:0000250|UniProtKB:Q06002}.
CC -!- SIMILARITY: Belongs to the intermediate filament family.
CC {ECO:0000255|PROSITE-ProRule:PRU01188}.
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DR EMBL; AB003104; BAA19737.1; -; mRNA.
DR RefSeq; NP_113743.1; NM_031555.1.
DR AlphaFoldDB; Q02435; -.
DR SMR; Q02435; -.
DR STRING; 10116.ENSRNOP00000007727; -.
DR iPTMnet; Q02435; -.
DR PhosphoSitePlus; Q02435; -.
DR PaxDb; Q02435; -.
DR PRIDE; Q02435; -.
DR GeneID; 25394; -.
DR KEGG; rno:25394; -.
DR UCSC; RGD:2205; rat.
DR CTD; 631; -.
DR RGD; 2205; Bfsp1.
DR eggNOG; ENOG502QRCH; Eukaryota.
DR InParanoid; Q02435; -.
DR OrthoDB; 677568at2759; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0005938; C:cell cortex; IEA:UniProtKB-SubCell.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005882; C:intermediate filament; ISS:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR GO; GO:0005212; F:structural constituent of eye lens; ISO:RGD.
DR GO; GO:0048469; P:cell maturation; ISO:RGD.
DR GO; GO:0045109; P:intermediate filament organization; ISS:UniProtKB.
DR GO; GO:0070307; P:lens fiber cell development; ISO:RGD.
DR InterPro; IPR042358; BFSP1.
DR InterPro; IPR039008; IF_rod_dom.
DR PANTHER; PTHR14069; PTHR14069; 1.
DR SMART; SM01391; Filament; 1.
DR PROSITE; PS51842; IF_ROD_2; 1.
PE 1: Evidence at protein level;
KW Acetylation; Cell membrane; Coiled coil; Cytoplasm; Cytoskeleton;
KW Eye lens protein; Intermediate filament; Lipoprotein; Membrane; Myristate;
KW Phosphoprotein; Reference proteome; Repeat.
FT CHAIN 1..>617
FT /note="Filensin"
FT /id="PRO_0000063848"
FT CHAIN 35..426
FT /note="Filensin N-terminal fragment"
FT /evidence="ECO:0000250|UniProtKB:Q06002"
FT /id="PRO_0000448674"
FT CHAIN 427..>617
FT /note="Filensin C-terminal fragment"
FT /evidence="ECO:0000250|UniProtKB:Q06002"
FT /id="PRO_0000448675"
FT DOMAIN 33..313
FT /note="IF rod"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01188"
FT REGION 1..33
FT /note="Head"
FT REGION 34..68
FT /note="Coil 1A"
FT REGION 69..77
FT /note="Linker 1"
FT REGION 78..177
FT /note="Coil 1B"
FT REGION 178..194
FT /note="Linker 12"
FT REGION 195..313
FT /note="Coil 2"
FT REGION 314..>617
FT /note="Tail"
FT REGION 381..429
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 499..617
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 539..566
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 577..608
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 34..35
FT /note="Cleavage"
FT /evidence="ECO:0000250|UniProtKB:Q06002"
FT SITE 426..427
FT /note="Cleavage (by CASP2, CASP3, and CASP7)"
FT /evidence="ECO:0000250|UniProtKB:Q12934"
FT SITE 450
FT /note="Interaction with MIP"
FT /evidence="ECO:0000250|UniProtKB:Q06002"
FT MOD_RES 5
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q06002"
FT MOD_RES 35
FT /note="N-acetylalanine"
FT /evidence="ECO:0000250|UniProtKB:Q06002"
FT MOD_RES 334
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q06002"
FT MOD_RES 508
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q06002"
FT MOD_RES 580
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q06002"
FT MOD_RES 607
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q06002"
FT LIPID 427
FT /note="N-myristoyl glycine"
FT /evidence="ECO:0000250|UniProtKB:Q06002"
FT NON_TER 617
SQ SEQUENCE 617 AA; 68038 MW; EA9303D1B0911CFF CRC64;
MYRRSYVFQA RQERYERAQP AGPTAQPGGT APGLAALQAL GERVAAQVQR ARALQQRHAG
LRRQLYAFQR LGEQPGPEEA LARHVEANLQ RARDLAAEHA RLERQEAEAQ RALDEFRSKY
ENECECQLVL KEMLERLNKE ADEALLRNLH LQLEAQFLQA DISVAKDRYK KNLLEIQTYI
TILQQIIQTA PQVSLVTGGM REEKLLTERE VAALRNQLDE GREAVTHLQA QKAELQAQTT
ALEQAIKHAH ECYDDEIQLY NGQIENLRKE IEEAERSLER SSYDCRQLAV AQQTLRNELD
RYHRIIEIEG NRLSSVFIET PISLITPSHG ASLSLGSNVK DLTRAVQDIT AAKPRQKALP
KSLPKRKEII AQDKVDETLE DAPLKTLQEP KAVQGELTGD GDSQLGAGGG HEVSPTQEGG
PEDVPDGSQI SKAFGKLCKV VKERVSGHKE PVPEPPADLF TKGRHILVTG ESSFVDPEFY
SSSIPARGGV VVSIEEDSMH HDGHVEPSPG QPMPPVENGQ GVPQGREGAH SNHQQVTDKN
GIRAKEPKDL EEKDDDSRKD DEAGRRPCPV IIPGPDGPST THSQTSGSNQ GGPEGPGSKS
SSLLAKSPSK ALSFKKV
