BFSP1_BOVIN
ID BFSP1_BOVIN Reviewed; 757 AA.
AC Q06002; F1MH65;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 11-DEC-2019, sequence version 3.
DT 03-AUG-2022, entry version 111.
DE RecName: Full=Filensin {ECO:0000303|PubMed:8491777};
DE AltName: Full=Beaded filament structural protein 1;
DE Contains:
DE RecName: Full=Filensin C-terminal fragment {ECO:0000303|PubMed:19875662};
DE Contains:
DE RecName: Full=Filensin N-terminal fragment {ECO:0000303|PubMed:19875662};
GN Name=BFSP1;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND PARTIAL PROTEIN SEQUENCE.
RC TISSUE=Lens;
RX PubMed=8491777; DOI=10.1083/jcb.121.4.847;
RA Gounari F., Merdes A., Quinlan R., Hess J.F., Fitzgerald P.G.,
RA Ouzounis C.A., Georgatos S.D.;
RT "Bovine filensin possesses primary and secondary structure similarity to
RT intermediate filament proteins.";
RL J. Cell Biol. 121:847-853(1993).
RN [2]
RP SEQUENCE REVISION.
RA Hess J.F.;
RL Submitted (DEC-1997) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000312|Proteomes:UP000009136}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Hereford {ECO:0000312|Proteomes:UP000009136};
RX PubMed=19393038; DOI=10.1186/gb-2009-10-4-r42;
RA Zimin A.V., Delcher A.L., Florea L., Kelley D.R., Schatz M.C., Puiu D.,
RA Hanrahan F., Pertea G., Van Tassell C.P., Sonstegard T.S., Marcais G.,
RA Roberts M., Subramanian P., Yorke J.A., Salzberg S.L.;
RT "A whole-genome assembly of the domestic cow, Bos taurus.";
RL Genome Biol. 10:R42.01-R42.10(2009).
RN [4]
RP SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RC TISSUE=Lens;
RX PubMed=7504675; DOI=10.1083/jcb.123.6.1507;
RA Merdes A., Gounari F., Georgatos S.D.;
RT "The 47-kD lens-specific protein phakinin is a tailless intermediate
RT filament protein and an assembly partner of filensin.";
RL J. Cell Biol. 123:1507-1516(1993).
RN [5]
RP SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND PROTEOLYTIC CLEAVAGE.
RX PubMed=7588880;
RA Sandilands A., Prescott A.R., Hutcheson A.M., Quinlan R.A., Casselman J.T.,
RA FitzGerald P.G.;
RT "Filensin is proteolytically processed during lens fiber cell
RT differentiation by multiple independent pathways.";
RL Eur. J. Cell Biol. 67:238-253(1995).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY, TISSUE SPECIFICITY, PROTEOLYTIC
RP CLEAVAGE, MYRISTOYLATION AT GLY-433, ACETYLATION AT ALA-41, AND
RP PHOSPHORYLATION AT SER-5; SER-340; SER-419; SER-512; THR-628; THR-674;
RP SER-701; SER-754 AND SER-755.
RX PubMed=19875662; DOI=10.1167/iovs.09-4565;
RA Wang Z., Obidike J.E., Schey K.L.;
RT "Posttranslational modifications of the bovine lens beaded filament
RT proteins filensin and CP49.";
RL Invest. Ophthalmol. Vis. Sci. 51:1565-1574(2010).
RN [7]
RP INTERACTION WITH MIP.
RX PubMed=28259670; DOI=10.1016/j.exer.2017.02.012;
RA Wang Z., Schey K.L.;
RT "Identification of a direct Aquaporin-0 binding site in the lens-specific
RT cytoskeletal protein filensin.";
RL Exp. Eye Res. 159:23-29(2017).
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 (PubMed:28259670).
CC {ECO:0000250|UniProtKB:A2AMT1, ECO:0000250|UniProtKB:Q12934,
CC ECO:0000269|PubMed:28259670}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:7504675,
CC ECO:0000269|PubMed:7588880}; Peripheral membrane protein
CC {ECO:0000269|PubMed:7504675}; Cytoplasmic side
CC {ECO:0000269|PubMed:7504675}. Cytoplasm {ECO:0000269|PubMed:7588880}.
CC Cytoplasm, cytoskeleton {ECO:0000269|PubMed:7504675}. Cytoplasm, cell
CC cortex {ECO:0000269|PubMed:7504675}.
CC -!- TISSUE SPECIFICITY: Abundantly expressed in both the inner and outer
CC cortex of the retina, expressed at a lower level in the nucleus of the
CC retina (at protein level) (PubMed:19875662). Detected in eye lens fiber
CC cells (at protein level) (PubMed:7504675, PubMed:7588880).
CC {ECO:0000269|PubMed:19875662, ECO:0000269|PubMed:7504675,
CC ECO:0000269|PubMed:7588880}.
CC -!- PTM: Proteolytically cleaved during lens cell fiber differentiation
CC with increased fragmentation as fiber cell age increases.
CC {ECO:0000269|PubMed:7588880}.
CC -!- PTM: [Filensin C-terminal fragment]: Myristoylated at Gly-433 following
CC proteolytic cleavage at Asp-432. {ECO:0000269|PubMed:19875662}.
CC -!- PTM: [Filensin N-terminal fragment]: Acetylated at Ala-41 following
CC proteolytic cleavage at Leu-40. {ECO:0000269|PubMed:19875662}.
CC -!- SIMILARITY: Belongs to the intermediate filament family.
CC {ECO:0000255|PROSITE-ProRule:PRU01188}.
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DR EMBL; X72388; CAA51081.1; -; mRNA.
DR PIR; S32103; S32103.
DR AlphaFoldDB; Q06002; -.
DR SMR; Q06002; -.
DR STRING; 9913.ENSBTAP00000029150; -.
DR iPTMnet; Q06002; -.
DR PaxDb; Q06002; -.
DR PRIDE; Q06002; -.
DR Ensembl; ENSBTAT00000029150; ENSBTAP00000029150; ENSBTAG00000021867.
DR VEuPathDB; HostDB:ENSBTAG00000021867; -.
DR VGNC; VGNC:26478; BFSP1.
DR eggNOG; ENOG502QRCH; Eukaryota.
DR GeneTree; ENSGT00390000016976; -.
DR HOGENOM; CLU_028949_0_0_1; -.
DR InParanoid; Q06002; -.
DR OMA; MIVETMI; -.
DR OrthoDB; 677568at2759; -.
DR TreeFam; TF331671; -.
DR Proteomes; UP000009136; Chromosome 13.
DR Bgee; ENSBTAG00000021867; Expressed in pigment epithelium of eye and 66 other tissues.
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; IBA:GO_Central.
DR GO; GO:0048469; P:cell maturation; IEA:Ensembl.
DR GO; GO:0045109; P:intermediate filament organization; ISS:UniProtKB.
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 Acetylation; Cell membrane; Coiled coil; Cytoplasm; Cytoskeleton;
KW Direct protein sequencing; Eye lens protein; Intermediate filament;
KW Lipoprotein; Membrane; Myristate; Phosphoprotein; Reference proteome;
KW Repeat.
FT CHAIN 1..757
FT /note="Filensin"
FT /id="PRO_0000063846"
FT CHAIN 41..432
FT /note="Filensin N-terminal fragment"
FT /evidence="ECO:0000305|PubMed:19875662"
FT /id="PRO_0000448668"
FT CHAIN 433..757
FT /note="Filensin C-terminal fragment"
FT /evidence="ECO:0000305|PubMed:19875662"
FT /id="PRO_0000448669"
FT DOMAIN 39..319
FT /note="IF rod"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01188"
FT REPEAT 532..545
FT /note="1"
FT REPEAT 546..552
FT /note="2; truncated"
FT REPEAT 553..566
FT /note="3"
FT REPEAT 567..580
FT /note="4"
FT REPEAT 581..594
FT /note="5"
FT REPEAT 595..608
FT /note="6"
FT REPEAT 609..622
FT /note="7"
FT REGION 1..39
FT /note="Head"
FT REGION 40..74
FT /note="Coil 1A"
FT REGION 75..83
FT /note="Linker 1"
FT REGION 84..183
FT /note="Coil 1B"
FT REGION 184..200
FT /note="Linker 12"
FT REGION 201..319
FT /note="Coil 2"
FT REGION 320..756
FT /note="Tail"
FT REGION 406..436
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 493..705
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 532..622
FT /note="7 X 14 AA tandem repeats"
FT COMPBIAS 509..523
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 524..658
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 40..41
FT /note="Cleavage"
FT /evidence="ECO:0000269|PubMed:19875662"
FT SITE 432..433
FT /note="Cleavage (by CASP2, CASP3, and CASP7)"
FT /evidence="ECO:0000269|PubMed:19875662"
FT SITE 456
FT /note="Interaction with MIP"
FT /evidence="ECO:0000269|PubMed:28259670"
FT MOD_RES 5
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:19875662"
FT MOD_RES 41
FT /note="N-acetylalanine"
FT /evidence="ECO:0000269|PubMed:19875662"
FT MOD_RES 340
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:19875662"
FT MOD_RES 419
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:19875662"
FT MOD_RES 512
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:19875662"
FT MOD_RES 628
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:19875662"
FT MOD_RES 674
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:19875662"
FT MOD_RES 701
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:19875662"
FT MOD_RES 754
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:19875662"
FT MOD_RES 755
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:19875662"
FT LIPID 433
FT /note="N-myristoyl glycine"
FT /evidence="ECO:0000269|PubMed:19875662"
FT CONFLICT 21..22
FT /note="AP -> G (in Ref. 2; CAA51081)"
FT /evidence="ECO:0000305"
FT CONFLICT 166
FT /note="D -> G (in Ref. 2; CAA51081)"
FT /evidence="ECO:0000305"
FT CONFLICT 208
FT /note="E -> R (in Ref. 2; CAA51081)"
FT /evidence="ECO:0000305"
FT CONFLICT 620..626
FT /note="KKEDGRP -> EKEDGQS (in Ref. 2; CAA51081)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 757 AA; 83181 MW; E6E5819C8AE0B97A CRC64;
MYRRSYVFQT RKEQYERAEE APRAAEPDRL AEARAAAPNL AALQGLGERV AAHVQRARAL
EQRHAVLRRQ LDAFQRLDEL AGPEDALARH VEGNRQRARD LAAERTRLER QGAEAQRALD
EFRSKYENEC ECQLLLKEML ERLNKEADEA LLRNLRLQIE AQFLQDDISA AKDRYKKNLL
EIQTYVTILQ QIIQTTPQAA AITSGMREEK LLTEREAAAL QCQLEDGREM ICLLQAQRTE
LQAQTAALEQ AIRDAHECYD DEIQLYNEQI DTLRKEIEEA ERSLERSSYD CRQLVVVQQT
LRNELDRYHR IIENEGNRLS SAFIETPITL YTASHGASLS PRHGGKDLTR AVQDITAAKP
RLKGLPKNLP RKKEMVAKDR ADEILEETLL RGPEDMKPGR VVIKEEGESK LEPGDEEASP
PTQEGAPEDV PDGGKISKAF EKLGKMIKEK VKGPKEPEPP ADLYTKGRYV MVSGDGSFVD
PGFCVFSVPA KGGVVVSKGD DSVPPDSGVE PSPQQPEPPL EEGQGPPQEK EDGLKEEGGP
PEGKGEPPEG KGDSVKEEGG PPEGKGDGVK EEGGPPEGKG DGVKEEGGPP EGKGDGVKKE
GEPPEGKGEG LKEEEGPLQK KEDGRPPTPH PADKGDEKNA KELKGLQGKQ DDQKEEGARG
PCPMVAPGPE GPSTPRSQGP QVILGGSEGH GARSGSRLAR SPPRKLAYEK VEVMESIEKF
STESIQTYEE TAVIVETMIE KTKANKKKLG EKGSSSA
