BFSP1_MOUSE
ID BFSP1_MOUSE Reviewed; 669 AA.
AC A2AMT1; O54770; Q3UPV0; Q6PFF8; Q8BKB1; Q9QWM4;
DT 01-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 20-FEB-2007, sequence version 1.
DT 03-AUG-2022, entry version 103.
DE RecName: Full=Filensin {ECO:0000303|PubMed:21745462, ECO:0000303|PubMed:9409766};
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 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]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC STRAIN=129/SvJ; TISSUE=Lens;
RX PubMed=9409766; DOI=10.1016/s0378-1119(97)00419-8;
RA Masaki S., Quinlan R.A.;
RT "Gene structure and sequence comparisons of the eye lens specific protein,
RT filensin, from rat and mouse: implications for protein classification and
RT assembly.";
RL Gene 201:11-20(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC STRAIN=C57BL/6J; TISSUE=Eye;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC STRAIN=C57BL/6J; TISSUE=Brain;
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 [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-21.
RC STRAIN=129/SvJ;
RX PubMed=9651486; DOI=10.1016/s0378-1119(98)00230-3;
RA Masaki S., Kamachi Y., Quinlan R.A., Yonezawa S., Kondoh H.;
RT "Identification and functional analysis of the mouse lens filensin gene
RT promoter.";
RL Gene 214:77-86(1998).
RN [6]
RP TISSUE SPECIFICITY.
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 [7]
RP IDENTIFICATION IN A COMPLEX WITH PPL AND BFSP2, INTERACTION WITH BFSP2,
RP SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
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 [8]
RP TISSUE SPECIFICITY, AND IDENTIFICATION IN A COMPLEX WITH EZR; AHNAK; PRX;
RP BFSP2; 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 [9]
RP FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, 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:27559293). Involved in altering the calcium regulation of MIP
CC water permeability (By similarity). {ECO:0000250|UniProtKB:Q12934,
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).
CC Identified in a complex that contains VIM, EZR, AHNAK, BFSP1, BFSP2,
CC ANK2, PLEC, PRX and spectrin (PubMed:21745462). Found in a complex
CC composed of PPL (via C-terminal linker domain), BFSP1 and BFSP2 in the
CC retinal lens (PubMed:19029034). Within the complex interacts with BFSP2
CC (PubMed:19029034). Interacts (via C-terminus) with MIP (via C-terminus)
CC in aged lens fiber cells (By similarity).
CC {ECO:0000250|UniProtKB:Q06002, ECO:0000250|UniProtKB:Q12934,
CC ECO:0000269|PubMed:19029034, ECO:0000269|PubMed:21745462}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:19029034};
CC Peripheral membrane protein {ECO:0000250|UniProtKB:Q06002}; Cytoplasmic
CC side {ECO:0000250|UniProtKB:Q06002}. Cytoplasm
CC {ECO:0000269|PubMed:19029034, ECO:0000269|PubMed:27559293}. Cytoplasm,
CC cytoskeleton {ECO:0000250|UniProtKB:Q06002}. Cytoplasm, cell cortex
CC {ECO:0000250|UniProtKB:Q06002}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=A2AMT1-1; Sequence=Displayed;
CC Name=2;
CC IsoId=A2AMT1-2; Sequence=VSP_024920;
CC -!- TISSUE SPECIFICITY: Detected in eye lens fiber cells (at protein level)
CC (PubMed:14985306, PubMed:19029034, PubMed:21745462). Expressed in
CC retinal lens epithelial cells (at protein level) (PubMed:27559293).
CC {ECO:0000269|PubMed:14985306, ECO:0000269|PubMed:19029034,
CC ECO:0000269|PubMed:21745462, ECO:0000269|PubMed:27559293}.
CC -!- DEVELOPMENTAL STAGE: First expressed in retinal lens fiber cells during
CC elongation and differentiation, becoming localized to the cytoplasm as
CC fiber cells mature and the beaded filament network forms at 3 weeks of
CC age. {ECO:0000269|PubMed:19029034}.
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-432 following
CC proteolytic cleavage at Asp-431. {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 -!- DISRUPTION PHENOTYPE: Complete loss of beaded filament structures in
CC lens epithelial cells. {ECO:0000269|PubMed:27559293}.
CC -!- SIMILARITY: Belongs to the intermediate filament family.
CC {ECO:0000255|PROSITE-ProRule:PRU01188}.
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DR EMBL; AB003147; BAA24139.1; -; mRNA.
DR EMBL; AK143180; BAE25294.1; -; mRNA.
DR EMBL; AK053766; BAC35514.1; -; mRNA.
DR EMBL; AL807801; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC057580; AAH57580.1; -; mRNA.
DR EMBL; AB010375; BAA28377.1; -; Genomic_DNA.
DR CCDS; CCDS16811.1; -. [A2AMT1-2]
DR CCDS; CCDS71154.1; -. [A2AMT1-1]
DR RefSeq; NP_001277990.1; NM_001291061.1. [A2AMT1-1]
DR RefSeq; NP_033881.2; NM_009751.2. [A2AMT1-2]
DR AlphaFoldDB; A2AMT1; -.
DR SMR; A2AMT1; -.
DR BioGRID; 198340; 1.
DR CORUM; A2AMT1; -.
DR STRING; 10090.ENSMUSP00000096899; -.
DR iPTMnet; A2AMT1; -.
DR PhosphoSitePlus; A2AMT1; -.
DR MaxQB; A2AMT1; -.
DR PaxDb; A2AMT1; -.
DR PRIDE; A2AMT1; -.
DR ProteomicsDB; 265209; -. [A2AMT1-1]
DR ProteomicsDB; 265210; -. [A2AMT1-2]
DR Antibodypedia; 9222; 287 antibodies from 29 providers.
DR DNASU; 12075; -.
DR Ensembl; ENSMUST00000028907; ENSMUSP00000028907; ENSMUSG00000027420. [A2AMT1-2]
DR Ensembl; ENSMUST00000099296; ENSMUSP00000096899; ENSMUSG00000027420. [A2AMT1-1]
DR GeneID; 12075; -.
DR KEGG; mmu:12075; -.
DR UCSC; uc008mqh.1; mouse. [A2AMT1-2]
DR UCSC; uc012cfe.1; mouse. [A2AMT1-1]
DR CTD; 631; -.
DR MGI; MGI:101770; Bfsp1.
DR VEuPathDB; HostDB:ENSMUSG00000027420; -.
DR eggNOG; ENOG502QRCH; Eukaryota.
DR GeneTree; ENSGT00390000016976; -.
DR HOGENOM; CLU_028949_0_0_1; -.
DR InParanoid; A2AMT1; -.
DR OMA; MIVETMI; -.
DR OrthoDB; 677568at2759; -.
DR PhylomeDB; A2AMT1; -.
DR TreeFam; TF331671; -.
DR BioGRID-ORCS; 12075; 0 hits in 73 CRISPR screens.
DR PRO; PR:A2AMT1; -.
DR Proteomes; UP000000589; Chromosome 2.
DR RNAct; A2AMT1; protein.
DR Bgee; ENSMUSG00000027420; Expressed in lens of camera-type eye and 57 other tissues.
DR Genevisible; A2AMT1; MM.
DR GO; GO:0005938; C:cell cortex; IEA:UniProtKB-SubCell.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005882; C:intermediate filament; IDA:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR GO; GO:0005212; F:structural constituent of eye lens; IDA:MGI.
DR GO; GO:0048469; P:cell maturation; IMP:MGI.
DR GO; GO:0045109; P:intermediate filament organization; IMP:UniProtKB.
DR GO; GO:0070307; P:lens fiber cell development; IDA:MGI.
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; Alternative splicing; Cell membrane; Coiled coil; Cytoplasm;
KW Cytoskeleton; Eye lens protein; Intermediate filament; Lipoprotein;
KW Membrane; Myristate; Phosphoprotein; Reference proteome; Repeat.
FT CHAIN 1..669
FT /note="Filensin"
FT /id="PRO_0000285854"
FT CHAIN 35..431
FT /note="Filensin N-terminal fragment"
FT /evidence="ECO:0000250|UniProtKB:Q06002"
FT /id="PRO_0000448672"
FT CHAIN 432..669
FT /note="Filensin C-terminal fragment"
FT /evidence="ECO:0000250|UniProtKB:Q06002"
FT /id="PRO_0000448673"
FT DOMAIN 33..318
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..318
FT /note="Coil 2"
FT REGION 319..669
FT /note="Tail"
FT REGION 380..435
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 449..468
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 505..618
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 449..464
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 536..570
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 582..612
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 431..432
FT /note="Cleavage (by CASP2, CASP3, and CASP7)"
FT /evidence="ECO:0000250|UniProtKB:Q12934"
FT SITE 457
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 339
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q06002"
FT MOD_RES 513
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q06002"
FT MOD_RES 585
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q06002"
FT LIPID 432
FT /note="N-myristoyl glycine"
FT /evidence="ECO:0000250|UniProtKB:Q06002"
FT VAR_SEQ 202..207
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:16141072"
FT /id="VSP_024920"
FT CONFLICT 185
FT /note="Q -> H (in Ref. 1; BAA24139)"
FT /evidence="ECO:0000305"
FT CONFLICT 291
FT /note="R -> S (in Ref. 1; BAA24139)"
FT /evidence="ECO:0000305"
FT CONFLICT 337
FT /note="P -> S (in Ref. 1; BAA24139)"
FT /evidence="ECO:0000305"
FT CONFLICT 394..395
FT /note="EP -> TR (in Ref. 1; BAA24139)"
FT /evidence="ECO:0000305"
FT CONFLICT 440
FT /note="G -> R (in Ref. 2; BAE25294)"
FT /evidence="ECO:0000305"
FT CONFLICT 463
FT /note="D -> N (in Ref. 1; BAA24139)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 669 AA; 73669 MW; 32DFEEC7F1098996 CRC64;
MYRRSYVFQA RQERYERAQP AGPAAQPGGT APGLAALQAL GERVAVQVQR ARALQQRHAG
LRRQLDAFQR LGEQPGPEDA LARHVEANLQ RARDLTAEHA RLERQEAEAQ RALDEFRSKY
ENECECQLVL KEMLERLNKE ADEALLRNLH LQLEAQFLQA DISVAKDRYK KNLLEIQTYI
TVLQQIVQTA PQVSLVTGMR ESGLLMQEKL FTEREVAALQ NQLEEGREAV THLQAQKAEL
QAQTTALEQA IKHAHECYDE ELQLYNEQIE NLRKEIEEAE RSLERSSYDC RQLAVAQQTL
RNELDRYHRI IEIEGSRLSS VFIETPISLI TPSHGAPLSL GSSVKDLARA VQDITAAKPR
QKALPKSLPK RKEIIAQDKV EETLEDAPLK PPQEPKALQV ERKAEGGSQP GAGGGHGVSP
TQEGGPEDVP DGGQISKAFG KLCKVVKERV SGHKEPEPEP PTDLFTKGRH VLVTGESSFV
DPEFYSSSIP ARGGVVISIE EDSMHHDGHV EPSPGQPMPP VENGQGVPQG REGDHSNHQQ
GTDKNGLRAK EPKDLEEKDD DGKKEAEGSR RPCPVIIPGP DEPSTSHSQT SGSNQGGPVG
PASKSSSLLA KGPSKALSIK KVEVVESIEK ISTESIQTYE ETSVIVETLI GKSKGNKKLG
EKSLPDTRA
