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Phakinin (49 kDa cytoskeletal protein) (Beaded filament structural protein 2) (Lens fiber cell beaded filament protein CP 49) (CP49)

 BFSP2_MOUSE             Reviewed;         416 AA.
Q6NVD9; Q63832; Q6P5N4; Q8VDD6;
19-JUL-2004, integrated into UniProtKB/Swiss-Prot.
05-JUL-2004, sequence version 1.
23-MAY-2018, entry version 105.
RecName: Full=Phakinin {ECO:0000303|PubMed:21745462};
AltName: Full=49 kDa cytoskeletal protein;
AltName: Full=Beaded filament structural protein 2;
AltName: Full=Lens fiber cell beaded filament protein CP 49;
Short=CP49 {ECO:0000303|PubMed:12573667};
Name=Bfsp2;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1] {ECO:0000312|EMBL:AAH68172.1}
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
STRAIN=C57BL/6J {ECO:0000312|EMBL:AAH62815.1,
ECO:0000312|EMBL:AAH68172.1};
TISSUE=Eye {ECO:0000312|EMBL:AAH68172.1}, and
Thymus {ECO:0000312|EMBL:AAH62815.1};
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[2] {ECO:0000305, ECO:0000312|EMBL:CAC83162.1}
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-164 (ISOFORM 1), AND FUNCTION.
STRAIN=129/SvJ {ECO:0000269|PubMed:12573667};
PubMed=12573667; DOI=10.1016/S0014-4835(02)00330-5;
Sandilands A., Prescott A.R., Wegener A., Zoltoski R.K.,
Hutcheson A.M., Masaki S., Kuszak J.R., Quinlan R.A.;
"Knockout of the intermediate filament protein CP49 destabilises the
lens fibre cell cytoskeleton and decreases lens optical quality, but
does not induce cataract.";
Exp. Eye Res. 76:385-391(2003).
[3]
PROTEIN SEQUENCE OF 6-22; 30-44; 54-73; 78-104; 123-138; 147-247;
252-340; 371-389 AND 402-416.
STRAIN=C57BL/6J; TISSUE=Lens;
PubMed=15744838; DOI=10.1002/pmic.200300878;
Hoehenwarter W., Kumar N.M., Wacker M., Zimny-Arndt U., Klose J.,
Jungblut P.R.;
"Eye lens proteomics: from global approach to detailed information
about phakinin and gamma E and F crystallin genes.";
Proteomics 5:245-257(2005).
[4] {ECO:0000305, ECO:0000312|EMBL:AAB25419.1}
NUCLEOTIDE SEQUENCE [MRNA] OF 198-416 (ISOFORM 1), AND TISSUE
SPECIFICITY.
TISSUE=Lens {ECO:0000269|PubMed:7679620};
PubMed=7679620; DOI=10.3109/02713689308999499;
Hess J.F., Casselman J.T., FitzGerald P.G.;
"cDNA analysis of the 49 kDa lens fiber cell cytoskeletal protein: a
new, lens-specific member of the intermediate filament family?";
Curr. Eye Res. 12:77-88(1993).
[5] {ECO:0000305, ECO:0000312|EMBL:CAC83162.1}
POLYMORPHISM.
STRAIN=129/SvJ {ECO:0000269|PubMed:15037121};
PubMed=15037121; DOI=10.1016/j.exer.2003.09.028;
Sandilands A., Wang X., Hutcheson A.M., James J., Prescott A.R.,
Wegener A., Pekny M., Gong X., Quinlan R.A.;
"Bfsp2 mutation found in mouse 129 strains causes the loss of CP49'
and induces vimentin-dependent changes in the lens fibre cell
cytoskeleton.";
Exp. Eye Res. 78:875-889(2004).
[6]
INTERACTION WITH LGSN.
PubMed=18178558; DOI=10.1074/jbc.M709144200;
Wyatt K., Gao C., Tsai J.-Y., Fariss R.N., Ray S., Wistow G.;
"A role for lengsin, a recruited enzyme, in terminal differentiation
in the vertebrate lens.";
J. Biol. Chem. 283:6607-6615(2008).
[7]
TISSUE SPECIFICITY, AND IDENTIFICATION IN A COMPLEX WITH EZR; AHNAK;
BFSP1; PRX; ANK2; PLEC; VIM AND SPECTRIN.
PubMed=21745462; DOI=10.1016/j.ydbio.2011.06.036;
Maddala R., Skiba N.P., Lalane R. III, Sherman D.L., Brophy P.J.,
Rao P.V.;
"Periaxin is required for hexagonal geometry and membrane organization
of mature lens fibers.";
Dev. Biol. 357:179-190(2011).
-!- FUNCTION: Involved in stabilization of lens fiber cell
cytoskeleton. {ECO:0000269|PubMed:12573667}.
-!- SUBUNIT: Associates with BFSP1 (By similarity). Interacts with
LGSN (PubMed:18178558). Identified in complexes that contain VIM,
EZR, AHNAK, BFSP1, BFSP2, ANK2, PLEC, PRX and spectrin
(PubMed:21745462). {ECO:0000250|UniProtKB:Q28177,
ECO:0000269|PubMed:18178558, ECO:0000269|PubMed:21745462}.
-!- SUBCELLULAR LOCATION: Cell membrane
{ECO:0000250|UniProtKB:Q28177}; Peripheral membrane protein
{ECO:0000250|UniProtKB:Q28177}; Cytoplasmic side
{ECO:0000250|UniProtKB:Q28177}. Cytoplasm, cytoskeleton
{ECO:0000250|UniProtKB:Q28177}. Cytoplasm, cell cortex
{ECO:0000250|UniProtKB:Q28177}. Note=Detected adjacent to the cell
membrane. {ECO:0000250|UniProtKB:Q28177}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=Q6NVD9-1; Sequence=Displayed;
Name=2;
IsoId=Q6NVD9-2; Sequence=VSP_011111;
Note=No experimental confirmation available.;
-!- TISSUE SPECIFICITY: Detected in eye lens fiber cells (at protein
level) (PubMed:21745462). Lens (PubMed:7679620).
{ECO:0000269|PubMed:21745462, ECO:0000269|PubMed:7679620}.
-!- POLYMORPHISM: In strains 101, 129/SvJ and CBA, a polymorphism
deletes the acceptor site of exon 2 which causes exon 1 to be
spliced to exon 3 and generates a frameshift and premature stop
codon. {ECO:0000269|PubMed:15037121}.
-!- MISCELLANEOUS: Knockout of the protein does not result in cataract
formation but causes deterioration of light scatter and lens
optical properties and changes organization of plasma membrane.
{ECO:0000269|PubMed:12573667}.
-!- SIMILARITY: Belongs to the intermediate filament family.
{ECO:0000255|PROSITE-ProRule:PRU01188}.
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EMBL; BC062815; AAH62815.1; -; mRNA.
EMBL; BC068172; AAH68172.1; -; mRNA.
EMBL; AJ304861; CAC83162.1; -; Genomic_DNA.
EMBL; S55549; AAB25419.1; -; mRNA.
CCDS; CCDS52903.1; -. [Q6NVD9-1]
PIR; I52911; I52911.
RefSeq; NP_001002896.1; NM_001002896.2. [Q6NVD9-1]
UniGene; Mm.335403; -.
ProteinModelPortal; Q6NVD9; -.
SMR; Q6NVD9; -.
BioGrid; 223747; 1.
STRING; 10090.ENSMUSP00000116249; -.
iPTMnet; Q6NVD9; -.
PhosphoSitePlus; Q6NVD9; -.
PaxDb; Q6NVD9; -.
PRIDE; Q6NVD9; -.
Ensembl; ENSMUST00000124310; ENSMUSP00000116249; ENSMUSG00000032556. [Q6NVD9-1]
GeneID; 107993; -.
KEGG; mmu:107993; -.
UCSC; uc009rgu.1; mouse. [Q6NVD9-2]
UCSC; uc009rgv.1; mouse. [Q6NVD9-1]
CTD; 8419; -.
MGI; MGI:1333828; Bfsp2.
eggNOG; ENOG410IHF9; Eukaryota.
eggNOG; ENOG410XQY0; LUCA.
GeneTree; ENSGT00910000144173; -.
HOGENOM; HOG000230975; -.
HOVERGEN; HBG013015; -.
InParanoid; Q6NVD9; -.
KO; K10379; -.
OMA; RMHLESK; -.
OrthoDB; EOG091G09SM; -.
PhylomeDB; Q6NVD9; -.
TreeFam; TF332742; -.
ChiTaRS; Bfsp2; mouse.
PRO; PR:Q6NVD9; -.
Proteomes; UP000000589; Chromosome 9.
Bgee; ENSMUSG00000032556; -.
CleanEx; MM_BFSP2; -.
Genevisible; Q6NVD9; MM.
GO; GO:0005938; C:cell cortex; IEA:UniProtKB-SubCell.
GO; GO:0005737; C:cytoplasm; IDA:MGI.
GO; GO:0005882; C:intermediate filament; IDA:MGI.
GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
GO; GO:0005212; F:structural constituent of eye lens; IDA:MGI.
GO; GO:0048469; P:cell maturation; IMP:MGI.
GO; GO:0007010; P:cytoskeleton organization; IMP:MGI.
GO; GO:0045104; P:intermediate filament cytoskeleton organization; IMP:MGI.
GO; GO:0070307; P:lens fiber cell development; IMP:MGI.
GO; GO:0050896; P:response to stimulus; IEA:UniProtKB-KW.
GO; GO:0007601; P:visual perception; IEA:UniProtKB-KW.
InterPro; IPR001664; IF.
InterPro; IPR039008; IF_rod_dom.
InterPro; IPR002957; Keratin_I.
InterPro; IPR027694; Phakinin.
PANTHER; PTHR23239; PTHR23239; 1.
PANTHER; PTHR23239:SF32; PTHR23239:SF32; 1.
Pfam; PF00038; Filament; 1.
PRINTS; PR01248; TYPE1KERATIN.
SMART; SM01391; Filament; 1.
PROSITE; PS51842; IF_ROD_2; 1.
1: Evidence at protein level;
Alternative splicing; Cell membrane; Coiled coil; Complete proteome;
Cytoplasm; Cytoskeleton; Direct protein sequencing; Eye lens protein;
Intermediate filament; Membrane; Polymorphism; Reference proteome;
Repeat; Sensory transduction; Vision.
CHAIN 1 416 Phakinin.
/FTId=PRO_0000063852.
DOMAIN 105 416 IF rod. {ECO:0000255|PROSITE-
ProRule:PRU01188}.
REGION 1 115 Head.
REGION 397 416 Tail.
COILED 116 146 {ECO:0000255}.
COILED 170 249 {ECO:0000255}.
COILED 308 402 {ECO:0000255}.
VAR_SEQ 1 264 Missing (in isoform 2).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_011111.
CONFLICT 353 353 A -> T (in Ref. 4; AAB25419).
{ECO:0000305}.
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


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