BFSP2_MOUSE
ID BFSP2_MOUSE Reviewed; 416 AA.
AC Q6NVD9; Q63832; Q6P5N4; Q8VDD6;
DT 19-JUL-2004, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 127.
DE RecName: Full=Phakinin {ECO:0000303|PubMed:21745462};
DE AltName: Full=49 kDa cytoskeletal protein;
DE AltName: Full=Beaded filament structural protein 2 {ECO:0000303|PubMed:15037121};
DE AltName: Full=Lens fiber cell beaded filament protein CP 47 {ECO:0000250|UniProtKB:Q13515};
DE Short=CP47 {ECO:0000250|UniProtKB:Q13515};
DE AltName: Full=Lens fiber cell beaded filament protein CP 49 {ECO:0000303|PubMed:12573667};
DE Short=CP49 {ECO:0000303|PubMed:12573667};
DE AltName: Full=Lens intermediate filament-like light {ECO:0000250|UniProtKB:Q13515};
DE Short=LIFL-L {ECO:0000250|UniProtKB:Q13515};
GN Name=Bfsp2;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1] {ECO:0000312|EMBL:AAH68172.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC STRAIN=C57BL/6J {ECO:0000312|EMBL:AAH62815.1, ECO:0000312|EMBL:AAH68172.1};
RC TISSUE=Eye {ECO:0000312|EMBL:AAH68172.1}, and
RC Thymus {ECO:0000312|EMBL:AAH62815.1};
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [2] {ECO:0000305, ECO:0000312|EMBL:CAC83162.1}
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-164 (ISOFORM 1), AND POLYMORPHISM.
RC STRAIN=129/SvJ {ECO:0000269|PubMed:12573667};
RX PubMed=12573667; DOI=10.1016/s0014-4835(02)00330-5;
RA Sandilands A., Prescott A.R., Wegener A., Zoltoski R.K., Hutcheson A.M.,
RA Masaki S., Kuszak J.R., Quinlan R.A.;
RT "Knockout of the intermediate filament protein CP49 destabilises the lens
RT fibre cell cytoskeleton and decreases lens optical quality, but does not
RT induce cataract.";
RL Exp. Eye Res. 76:385-391(2003).
RN [3]
RP PROTEIN SEQUENCE OF 6-22; 30-44; 54-73; 78-104; 123-138; 147-247; 252-340;
RP 371-389 AND 402-416.
RC STRAIN=C57BL/6J; TISSUE=Lens;
RX PubMed=15744838; DOI=10.1002/pmic.200300878;
RA Hoehenwarter W., Kumar N.M., Wacker M., Zimny-Arndt U., Klose J.,
RA Jungblut P.R.;
RT "Eye lens proteomics: from global approach to detailed information about
RT phakinin and gamma E and F crystallin genes.";
RL Proteomics 5:245-257(2005).
RN [4] {ECO:0000305, ECO:0000312|EMBL:AAB25419.1}
RP NUCLEOTIDE SEQUENCE [MRNA] OF 198-416 (ISOFORM 1), AND TISSUE SPECIFICITY.
RC TISSUE=Lens {ECO:0000269|PubMed:7679620};
RX PubMed=7679620; DOI=10.3109/02713689308999499;
RA Hess J.F., Casselman J.T., FitzGerald P.G.;
RT "cDNA analysis of the 49 kDa lens fiber cell cytoskeletal protein: a new,
RT lens-specific member of the intermediate filament family?";
RL Curr. Eye Res. 12:77-88(1993).
RN [5]
RP FUNCTION, TISSUE SPECIFICITY, AND DISRUPTION PHENOTYPE.
RX PubMed=12454043;
RA Alizadeh A., Clark J.I., Seeberger T., Hess J., Blankenship T., Spicer A.,
RA FitzGerald P.G.;
RT "Targeted genomic deletion of the lens-specific intermediate filament
RT protein CP49.";
RL Invest. Ophthalmol. Vis. Sci. 43:3722-3727(2002).
RN [6] {ECO:0000305, ECO:0000312|EMBL:CAC83162.1}
RP FUNCTION, TISSUE SPECIFICITY, POLYMORPHISM, AND DISRUPTION PHENOTYPE.
RC STRAIN=129/SvJ {ECO:0000269|PubMed:15037121};
RX PubMed=15037121; DOI=10.1016/j.exer.2003.09.028;
RA Sandilands A., Wang X., Hutcheson A.M., James J., Prescott A.R.,
RA Wegener A., Pekny M., Gong X., Quinlan R.A.;
RT "Bfsp2 mutation found in mouse 129 strains causes the loss of CP49' and
RT induces vimentin-dependent changes in the lens fibre cell cytoskeleton.";
RL Exp. Eye Res. 78:875-889(2004).
RN [7]
RP TISSUE SPECIFICITY, AND POLYMORPHISM.
RC STRAIN=129/SvJ, and C57BL/6J {ECO:0000269|PubMed:14985306};
RX PubMed=14985306; DOI=10.1167/iovs.03-0677;
RA Alizadeh A., Clark J., Seeberger T., Hess J., Blankenship T.,
RA FitzGerald P.G.;
RT "Characterization of a mutation in the lens-specific CP49 in the 129 strain
RT of mouse.";
RL Invest. Ophthalmol. Vis. Sci. 45:884-891(2004).
RN [8]
RP INTERACTION WITH LGSN.
RX PubMed=18178558; DOI=10.1074/jbc.m709144200;
RA Wyatt K., Gao C., Tsai J.-Y., Fariss R.N., Ray S., Wistow G.;
RT "A role for lengsin, a recruited enzyme, in terminal differentiation in the
RT vertebrate lens.";
RL J. Biol. Chem. 283:6607-6615(2008).
RN [9]
RP IDENTIFICATION IN A COMPLEX WITH PPL AND BFSP1, INTERACTION WITH PPL; BFSP1
RP AND VIM, AND TISSUE SPECIFICITY.
RX PubMed=19029034; DOI=10.1167/iovs.08-2894;
RA Yoon K.H., FitzGerald P.G.;
RT "Periplakin interactions with lens intermediate and beaded filaments.";
RL Invest. Ophthalmol. Vis. Sci. 50:1283-1289(2009).
RN [10]
RP TISSUE SPECIFICITY, AND IDENTIFICATION IN A COMPLEX WITH EZR; AHNAK; BFSP1;
RP PRX; ANK2; PLEC; VIM AND SPECTRIN.
RX PubMed=21745462; DOI=10.1016/j.ydbio.2011.06.036;
RA Maddala R., Skiba N.P., Lalane R. III, Sherman D.L., Brophy P.J., Rao P.V.;
RT "Periaxin is required for hexagonal geometry and membrane organization of
RT mature lens fibers.";
RL Dev. Biol. 357:179-190(2011).
RN [11]
RP FUNCTION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, AND DISRUPTION
RP PHENOTYPE.
RX PubMed=27559293;
RA FitzGerald P., Sun N., Shibata B., Hess J.F.;
RT "Expression of the type VI intermediate filament proteins CP49 and filensin
RT in the mouse lens epithelium.";
RL Mol. Vis. 22:970-989(2016).
CC -!- FUNCTION: Required for the correct formation of lens intermediate
CC filaments as part of a complex composed of BFSP1, BFSP2 and CRYAA
CC (PubMed:15037121, PubMed:27559293). Plays a role in maintenance of
CC retinal lens optical clarity (PubMed:12454043).
CC {ECO:0000269|PubMed:12454043, ECO:0000269|PubMed:15037121,
CC ECO:0000269|PubMed:27559293}.
CC -!- SUBUNIT: Part of a complex required for lens intermediate filament
CC formation composed of BFSP1, BFSP2 and CRYAA (By similarity). Found in
CC a complex composed of PPL (via C-terminal linker domain), BFSP1 and
CC BFSP2 in the retinal lens (PubMed:19029034). Within the complex
CC interacts with PPL (via C-terminal linker domain) and with BFSP1
CC (PubMed:19029034). Identified in a complex that contains VIM, EZR,
CC AHNAK, BFSP1, BFSP2, ANK2, PLEC, PRX and spectrin (PubMed:21745462).
CC Interacts with LGSN (PubMed:18178558). Interacts with VIM
CC (PubMed:19029034). {ECO:0000250|UniProtKB:Q13515,
CC ECO:0000269|PubMed:18178558, ECO:0000269|PubMed:19029034,
CC ECO:0000269|PubMed:21745462}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q28177};
CC Peripheral membrane protein {ECO:0000250|UniProtKB:Q28177}; Cytoplasmic
CC side {ECO:0000250|UniProtKB:Q28177}. Cytoplasm
CC {ECO:0000269|PubMed:27559293}. Cytoplasm, cytoskeleton
CC {ECO:0000250|UniProtKB:Q28177}. Cytoplasm, cell cortex
CC {ECO:0000250|UniProtKB:Q28177}. Note=Expressed primarily at the plasma
CC membrane in peripheral lens fiber cells, however also localizes to the
CC cytoplasm in mature lens fiber cells. {ECO:0000250|UniProtKB:Q28177}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q6NVD9-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q6NVD9-2; Sequence=VSP_011111;
CC -!- TISSUE SPECIFICITY: Detected in retina lens fiber cells (at protein
CC level) (PubMed:7679620, PubMed:12454043, PubMed:15037121,
CC PubMed:14985306, PubMed:19029034, PubMed:21745462, PubMed:27559293).
CC Also expressed in the lens epithelium, abundantly expressed in the
CC anterior and anterolateral epithelium, less frequently expressed nearer
CC the lens coronal equator (at protein level) (PubMed:27559293).
CC {ECO:0000269|PubMed:12454043, ECO:0000269|PubMed:14985306,
CC ECO:0000269|PubMed:15037121, ECO:0000269|PubMed:19029034,
CC ECO:0000269|PubMed:21745462, ECO:0000269|PubMed:27559293,
CC ECO:0000269|PubMed:7679620}.
CC -!- DEVELOPMENTAL STAGE: Expressed in the retinal lens fiber cells from
CC postnatal day 28 (P28) to P45 (PubMed:27559293). Expressed in retinal
CC lens beaded filament structures from P37 onwards (PubMed:27559293).
CC {ECO:0000269|PubMed:27559293}.
CC -!- POLYMORPHISM: In strains 101, 129/SvJ and CBA, a polymorphism deletes
CC the acceptor site of exon 2 which causes exon 1 to be spliced to exon 3
CC and generates a frameshift and premature stop codon (PubMed:12573667,
CC PubMed:15037121). The polymorphism leads to retinal lens fiber cell
CC nuclear opacity beginning at 1 month of age, opacity becomes more
CC pronounced with age (PubMed:14985306). Reduced intermediate filaments
CC and loss of the association of the lens fiber cell cytoskeleton with
CC the plasma membrane (PubMed:15037121, PubMed:14985306).
CC {ECO:0000269|PubMed:12573667, ECO:0000269|PubMed:14985306,
CC ECO:0000269|PubMed:15037121}.
CC -!- DISRUPTION PHENOTYPE: No overall change in lens fiber cell
CC organization, regularity of hexagonal profiles, or positioning of cell
CC nuclei (PubMed:12454043). Opacification of the retinal lens is evident
CC at 1 month of age, with progressive loss of clarity to 10 months of age
CC (PubMed:12454043). Reduced abundance and loss of distinction of
CC intermediate filaments in retinal lens fiber cells (PubMed:15037121).
CC Decreased protein abundance of BFSP1 in the retinal lens
CC (PubMed:12454043). Complete loss of beaded filament structures in lens
CC epithelial cells (PubMed:27559293). BFSP2 and VIM double knockout mice
CC show a complete loss of the cytoplasmic cytoskeleton in retinal lens
CC fiber cells (PubMed:15037121). {ECO:0000269|PubMed:12454043,
CC ECO:0000269|PubMed:15037121, ECO:0000269|PubMed:27559293}.
CC -!- SIMILARITY: Belongs to the intermediate filament family.
CC {ECO:0000255|PROSITE-ProRule:PRU01188}.
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DR EMBL; BC062815; AAH62815.1; -; mRNA.
DR EMBL; BC068172; AAH68172.1; -; mRNA.
DR EMBL; AJ304861; CAC83162.1; -; Genomic_DNA.
DR EMBL; S55549; AAB25419.1; -; mRNA.
DR CCDS; CCDS52903.1; -. [Q6NVD9-1]
DR PIR; I52911; I52911.
DR RefSeq; NP_001002896.1; NM_001002896.2. [Q6NVD9-1]
DR AlphaFoldDB; Q6NVD9; -.
DR SMR; Q6NVD9; -.
DR BioGRID; 223747; 1.
DR CORUM; Q6NVD9; -.
DR STRING; 10090.ENSMUSP00000116249; -.
DR iPTMnet; Q6NVD9; -.
DR PhosphoSitePlus; Q6NVD9; -.
DR MaxQB; Q6NVD9; -.
DR PaxDb; Q6NVD9; -.
DR PRIDE; Q6NVD9; -.
DR ProteomicsDB; 273678; -. [Q6NVD9-1]
DR ProteomicsDB; 273679; -. [Q6NVD9-2]
DR Antibodypedia; 33369; 172 antibodies from 19 providers.
DR DNASU; 107993; -.
DR Ensembl; ENSMUST00000124310; ENSMUSP00000116249; ENSMUSG00000032556. [Q6NVD9-1]
DR GeneID; 107993; -.
DR KEGG; mmu:107993; -.
DR UCSC; uc009rgu.1; mouse. [Q6NVD9-2]
DR UCSC; uc009rgv.1; mouse. [Q6NVD9-1]
DR CTD; 8419; -.
DR MGI; MGI:1333828; Bfsp2.
DR VEuPathDB; HostDB:ENSMUSG00000032556; -.
DR eggNOG; ENOG502QTD1; Eukaryota.
DR GeneTree; ENSGT00940000159820; -.
DR HOGENOM; CLU_012560_0_0_1; -.
DR InParanoid; Q6NVD9; -.
DR OMA; ETIRIQW; -.
DR OrthoDB; 803338at2759; -.
DR PhylomeDB; Q6NVD9; -.
DR TreeFam; TF332742; -.
DR BioGRID-ORCS; 107993; 4 hits in 72 CRISPR screens.
DR PRO; PR:Q6NVD9; -.
DR Proteomes; UP000000589; Chromosome 9.
DR RNAct; Q6NVD9; protein.
DR Bgee; ENSMUSG00000032556; Expressed in lens of camera-type eye and 73 other tissues.
DR Genevisible; Q6NVD9; MM.
DR GO; GO:0005938; C:cell cortex; IEA:UniProtKB-SubCell.
DR GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR GO; GO:0005856; C:cytoskeleton; IBA:GO_Central.
DR GO; GO:0005882; C:intermediate filament; IDA:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005212; F:structural constituent of eye lens; IDA:MGI.
DR GO; GO:0048469; P:cell maturation; IMP:MGI.
DR GO; GO:0007010; P:cytoskeleton organization; IMP:MGI.
DR GO; GO:0045104; P:intermediate filament cytoskeleton organization; IMP:MGI.
DR GO; GO:0045109; P:intermediate filament organization; IMP:UniProtKB.
DR GO; GO:0070307; P:lens fiber cell development; IMP:MGI.
DR GO; GO:0050896; P:response to stimulus; IEA:UniProtKB-KW.
DR GO; GO:0007601; P:visual perception; IEA:UniProtKB-KW.
DR InterPro; IPR039008; IF_rod_dom.
DR InterPro; IPR002957; Keratin_I.
DR InterPro; IPR027694; Phakinin.
DR PANTHER; PTHR23239; PTHR23239; 1.
DR PANTHER; PTHR23239:SF32; PTHR23239:SF32; 1.
DR Pfam; PF00038; Filament; 1.
DR PRINTS; PR01248; TYPE1KERATIN.
DR SMART; SM01391; Filament; 1.
DR PROSITE; PS51842; IF_ROD_2; 1.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; Cell membrane; Coiled coil; Cytoplasm;
KW Cytoskeleton; Direct protein sequencing; Eye lens protein;
KW Intermediate filament; Membrane; Phosphoprotein; Reference proteome;
KW Repeat; Sensory transduction; Vision.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:Q28177"
FT CHAIN 2..416
FT /note="Phakinin"
FT /evidence="ECO:0000305"
FT /id="PRO_0000063852"
FT DOMAIN 105..416
FT /note="IF rod"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01188"
FT REGION 1..48
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2..115
FT /note="Head"
FT REGION 397..416
FT /note="Tail"
FT COILED 116..146
FT /evidence="ECO:0000255"
FT COILED 170..249
FT /evidence="ECO:0000255"
FT COILED 308..402
FT /evidence="ECO:0000255"
FT COMPBIAS 9..46
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0000250|UniProtKB:Q28177"
FT MOD_RES 27
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q28177"
FT MOD_RES 33
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q28177"
FT MOD_RES 36
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q28177"
FT MOD_RES 91
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q28177"
FT VAR_SEQ 1..264
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_011111"
FT CONFLICT 353
FT /note="A -> T (in Ref. 4; AAB25419)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 416 AA; 45740 MW; 3D86718F47F8C47E CRC64;
MSKRRVAADL PSGTNSSMPV QRHRVSSLRG THSPSSLDSP PASRTSAVGS LVRAPGVYVG
VAPSGGIGGL GARVTRRALG ISSVFLQGLR SSGLANVPAP GPERDHTTVE DLGGCLVEYM
TKVHALEQVS QELETQLRAH LESKAKSSGG WDALRASWAS SYQQVGEAVL ENARLLLQME
TIQAGADDFK ERYENEQPFR KAAEEEVSSL YKVIDEANLT KTDLEHQIES LKEELGFLSR
SYEEDVKVLY KQLAGSELEQ ADVPMGTGLD DVLETIRVQW ERDVEKNRAE AGALLQAKQQ
TEVVHVSQTQ EEKLAAALSV ELHDTSRQVQ SLQAETESLR ALKRGLENSL HDAQHWHDME
LQNLGAVVGR LEAELAEIRS ETEQQQQERA HLLACKSQLQ KDVASYHALL DREENN
