BFSP2_RAT
ID BFSP2_RAT Reviewed; 416 AA.
AC D3ZER2;
DT 11-DEC-2019, integrated into UniProtKB/Swiss-Prot.
DT 22-JUL-2015, sequence version 2.
DT 03-AUG-2022, entry version 77.
DE RecName: Full=Phakinin {ECO:0000303|PubMed:18449355};
DE AltName: Full=49 kDa cytoskeletal protein {ECO:0000305};
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:0000250|UniProtKB:Q6NVD9};
DE Short=CP49 {ECO:0000250|UniProtKB:Q6NVD9};
DE AltName: Full=Lens intermediate filament-like light {ECO:0000250|UniProtKB:Q13515};
DE Short=LIFL-L {ECO:0000250|UniProtKB:Q13515};
GN Name=Bfsp2 {ECO:0000312|RGD:1591927};
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116 {ECO:0000312|Proteomes:UP000002494};
RN [1] {ECO:0000312|Proteomes:UP000002494}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Brown Norway {ECO:0000312|Proteomes:UP000002494};
RX PubMed=15057822; DOI=10.1038/nature02426;
RA Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J.,
RA Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G.,
RA Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G.,
RA Morgan M., Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G.,
RA Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S.,
RA Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T.,
RA Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D.,
RA Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L.,
RA Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D.,
RA Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M.,
RA Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C.,
RA Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J.,
RA Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H.,
RA Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X.,
RA Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q.,
RA Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P.,
RA Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A.,
RA Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C.,
RA Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J.,
RA Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J.,
RA Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F.,
RA Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A.,
RA Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A.,
RA Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J.,
RA Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E.,
RA Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M.,
RA Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C.,
RA Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L.,
RA Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W.,
RA Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y.,
RA Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V.,
RA Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M.,
RA Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S.,
RA Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B.,
RA Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R.,
RA Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J.,
RA Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D.,
RA Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S.,
RA Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S.,
RA Mockrin S., Collins F.S.;
RT "Genome sequence of the Brown Norway rat yields insights into mammalian
RT evolution.";
RL Nature 428:493-521(2004).
RN [2] {ECO:0000305}
RP SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=18449355;
RA Oka M., Kudo H., Sugama N., Asami Y., Takehana M.;
RT "The function of filensin and phakinin in lens transparency.";
RL Mol. Vis. 14:815-822(2008).
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:Q6NVD9}.
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 (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:Q13515, ECO:0000250|UniProtKB:Q6NVD9}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:18449355};
CC Peripheral membrane protein {ECO:0000250|UniProtKB:Q28177}; Cytoplasmic
CC side {ECO:0000250|UniProtKB:Q28177}. Cytoplasm
CC {ECO:0000269|PubMed:18449355}. 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 -!- TISSUE SPECIFICITY: Expressed in the deep and shallow cortices of the
CC retina lens (at protein level). {ECO:0000269|PubMed:18449355}.
CC -!- SIMILARITY: Belongs to the intermediate filament family.
CC {ECO:0000255|PROSITE-ProRule:PRU01188}.
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DR EMBL; AABR07071368; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; NP_001264363.1; NM_001277434.1.
DR AlphaFoldDB; D3ZER2; -.
DR SMR; D3ZER2; -.
DR STRING; 10116.ENSRNOP00000029527; -.
DR jPOST; D3ZER2; -.
DR PaxDb; D3ZER2; -.
DR Ensembl; ENSRNOT00000032376; ENSRNOP00000029527; ENSRNOG00000010899.
DR GeneID; 501046; -.
DR KEGG; rno:501046; -.
DR CTD; 8419; -.
DR RGD; 1591927; Bfsp2.
DR eggNOG; ENOG502QTD1; Eukaryota.
DR GeneTree; ENSGT00940000159820; -.
DR HOGENOM; CLU_012560_0_0_1; -.
DR InParanoid; D3ZER2; -.
DR OMA; ETIRIQW; -.
DR OrthoDB; 803338at2759; -.
DR TreeFam; TF332742; -.
DR PRO; PR:D3ZER2; -.
DR Proteomes; UP000002494; Chromosome 8.
DR Bgee; ENSRNOG00000010899; Expressed in thymus and 8 other tissues.
DR GO; GO:0005938; C:cell cortex; IEA:UniProtKB-SubCell.
DR GO; GO:0005737; C:cytoplasm; ISO:RGD.
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; ISO:RGD.
DR GO; GO:0048469; P:cell maturation; ISO:RGD.
DR GO; GO:0007010; P:cytoskeleton organization; ISO:RGD.
DR GO; GO:0045104; P:intermediate filament cytoskeleton organization; ISO:RGD.
DR GO; GO:0045109; P:intermediate filament organization; ISS:UniProtKB.
DR GO; GO:0070307; P:lens fiber cell development; ISO:RGD.
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; Cell membrane; Coiled coil; Cytoplasm; Cytoskeleton;
KW Eye lens protein; Intermediate filament; Membrane; Phosphoprotein;
KW Reference proteome; 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_0000448680"
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 /evidence="ECO:0000250|UniProtKB:Q13515"
FT REGION 397..416
FT /note="Tail"
FT /evidence="ECO:0000250|UniProtKB:Q13515"
FT COILED 199..240
FT /evidence="ECO:0000255"
FT COILED 314..391
FT /evidence="ECO:0000255"
FT COMPBIAS 14..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"
SQ SEQUENCE 416 AA; 45685 MW; 05E4A9B30788CD84 CRC64;
MSERRVAMDL PSGSNASMPL QRHRVSSLRG TRSPSSLDSP PASRTSAVGS LVRAPGVYVG
VAPSGGIGGL GARVTRRALG ISSVFLQGLR SSGLATAPAP GPERNHATAE DLGGCLVEYM
TKVHALEQVS QELETQLRAH LESKAKRSGG WDALRASWAS SYQQVGEAVL ENARLMLQME
TIQAGADDFK ERYENEQPFR KAAEEEVSSL YKVIDEANLT KTDLEHQIES LKEELGSLSR
SYEEDVKVLY KQLAGSELEQ TDVPMGTGLD DVLETIRVQW ERDVEKNRAE AGAVLQAKQQ
TEVVHVSQTQ EEKLAAALSV ELHDTSRQVQ SLQAETESLR ALKRGLENTL HDAKHWHDME
LQNLGAVVGR LEAELAEIHS ETEQQQQERA HLLACKGQLQ KDVASYHALL DREESN
