BFSP2_BOVIN
ID BFSP2_BOVIN Reviewed; 415 AA.
AC Q28177; Q05B61;
DT 16-NOV-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 108.
DE RecName: Full=Phakinin {ECO:0000303|PubMed:7504675};
DE AltName: Full=49 kDa cytoskeletal protein;
DE AltName: Full=Beaded filament structural protein 2 {ECO:0000250|UniProtKB:Q13515};
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:19875662};
DE Short=CP49 {ECO:0000303|PubMed:19875662};
DE AltName: Full=Lens intermediate filament-like light {ECO:0000250|UniProtKB:Q13515};
DE Short=LIFL-L {ECO:0000250|UniProtKB:Q13515};
DE Contains:
DE RecName: Full=Phakinin N-terminal fragment {ECO:0000303|PubMed:19875662};
DE Contains:
DE RecName: Full=Phakinin C-terminal fragment {ECO:0000303|PubMed:19875662};
GN Name=BFSP2;
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], INTERACTION WITH BFSP1, SUBCELLULAR LOCATION,
RP 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 [2]
RP SEQUENCE REVISION.
RA Merdes A.;
RL Submitted (AUG-1994) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Hypothalamus;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP PROTEIN SEQUENCE OF 222-232 AND 248-277.
RC TISSUE=Lens;
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 SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
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, ACETYLATION AT SER-2, AND PHOSPHORYLATION AT SER-26; SER-32;
RP SER-35; THR-53; SER-90 AND SER-100.
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).
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). Plays a role in maintenance of retinal lens optical
CC clarity (By similarity). {ECO:0000250|UniProtKB:Q13515,
CC ECO:0000250|UniProtKB:Q6NVD9}.
CC -!- SUBUNIT: Part of a complex required for lens intermediate filament
CC formation composed of BFSP1, BFSP2 and CRYAA (PubMed:7504675). Found in
CC a complex composed of PPL (via C-terminal linker domain), BFSP1 and
CC BFSP2 in the retinal lens (By similarity). Within the complex interacts
CC with PPL (via C-terminal linker domain) and with BFSP1 (By similarity).
CC Identified in a complex that contains VIM, EZR, AHNAK, BFSP1, BFSP2,
CC ANK2, PLEC, PRX and spectrin (By similarity). Interacts with LGSN (By
CC similarity). Interacts with VIM (By similarity).
CC {ECO:0000250|UniProtKB:Q6NVD9, ECO:0000269|PubMed:7504675}.
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}. Note=Expressed primarily at the
CC plasma membrane in peripheral lens fiber cells, however also localizes
CC to the cytoplasm in mature lens fiber cells.
CC {ECO:0000269|PubMed:7588880}.
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 -!- SIMILARITY: Belongs to the intermediate filament family.
CC {ECO:0000255|PROSITE-ProRule:PRU01188}.
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DR EMBL; X75160; CAA53003.1; -; mRNA.
DR EMBL; BC122762; AAI22763.1; -; mRNA.
DR RefSeq; NP_776673.1; NM_174248.3.
DR AlphaFoldDB; Q28177; -.
DR SMR; Q28177; -.
DR STRING; 9913.ENSBTAP00000024638; -.
DR iPTMnet; Q28177; -.
DR PRIDE; Q28177; -.
DR Ensembl; ENSBTAT00000024638; ENSBTAP00000024638; ENSBTAG00000017659.
DR GeneID; 281645; -.
DR KEGG; bta:281645; -.
DR CTD; 8419; -.
DR VEuPathDB; HostDB:ENSBTAG00000017659; -.
DR VGNC; VGNC:26479; BFSP2.
DR eggNOG; ENOG502QTD1; Eukaryota.
DR GeneTree; ENSGT00940000159820; -.
DR InParanoid; Q28177; -.
DR OMA; ETIRIQW; -.
DR OrthoDB; 803338at2759; -.
DR Proteomes; UP000009136; Chromosome 1.
DR Bgee; ENSBTAG00000017659; Expressed in temporal cortex and 76 other tissues.
DR GO; GO:0005938; C:cell cortex; IEA:UniProtKB-SubCell.
DR GO; GO:0005856; C:cytoskeleton; IBA:GO_Central.
DR GO; GO:0005882; C:intermediate filament; ISS:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005212; F:structural constituent of eye lens; IEA:UniProtKB-KW.
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; IEA:Ensembl.
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; Cell membrane; Coiled coil; Cytoplasm; Cytoskeleton;
KW Direct protein sequencing; Eye lens protein; Intermediate filament;
KW Membrane; Phosphoprotein; Reference proteome; Repeat.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:19875662"
FT CHAIN 2..415
FT /note="Phakinin"
FT /evidence="ECO:0000269|PubMed:19875662"
FT /id="PRO_0000063850"
FT CHAIN 2..37
FT /note="Phakinin N-terminal fragment"
FT /evidence="ECO:0000305|PubMed:19875662"
FT /id="PRO_0000448678"
FT CHAIN 38..415
FT /note="Phakinin C-terminal fragment"
FT /evidence="ECO:0000305|PubMed:19875662"
FT /id="PRO_0000448679"
FT DOMAIN 104..415
FT /note="IF rod"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01188"
FT REGION 1..26
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2..114
FT /note="Head"
FT REGION 396..415
FT /note="Tail"
FT COILED 115..144
FT /evidence="ECO:0000255"
FT COILED 199..248
FT /evidence="ECO:0000255"
FT COILED 295..395
FT /evidence="ECO:0000255"
FT SITE 37..38
FT /note="Cleavage"
FT /evidence="ECO:0000269|PubMed:19875662"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0000269|PubMed:19875662"
FT MOD_RES 26
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:19875662"
FT MOD_RES 32
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:19875662"
FT MOD_RES 35
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:19875662"
FT MOD_RES 53
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:19875662"
FT MOD_RES 90
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:19875662"
FT MOD_RES 100
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:19875662"
SQ SEQUENCE 415 AA; 45950 MW; F3996852E69661B6 CRC64;
MSTRRVVVDA PAGASSSMPL QRHKASFRAA QSPSSLDGLP ASRTVAVSGL VRTPRVYVGM
APSGPTGGLG ARVTRRALGI SSVFLQGLRS SGLATAPAPS LERDLGAVED LGGCLVEYMA
KVHALEKVSQ ELEAQLRMHL ESKATRSENW GALRASWASS CQQVGEAVLE NARLMLQTEN
IQAGADDFKE RYENEQPFRK AAEEEINSLY KVIDEANSSK MDLESQIESL KEELGFLSRS
YEEDVKMLYK QLAGSELEQL NVPIGTGLDD ILETIRIHWE RDVEKNRLQA GALLQAKQQA
ELARRAQTQE EKLAAALRVE LHNTSCQIQS LQAETESLRA LKRGLENTLH DAKHWHDIEL
QNLGAVVSRL EAELREMRAE AEQQLQAREH LLSHKCQLQR DVASYHALLD REESS
