ID BFSP2_HUMAN Reviewed; 415 AA. AC Q13515; Q14D32; Q9HBW5; DT 16-NOV-2001, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 24-JAN-2024, entry version 181. DE RecName: Full=Phakinin {ECO:0000303|PubMed:28935373}; DE AltName: Full=49 kDa cytoskeletal protein; DE AltName: Full=Beaded filament structural protein 2 {ECO:0000303|PubMed:10729115}; DE AltName: Full=Lens fiber cell beaded filament protein CP 47 {ECO:0000303|PubMed:28935373}; DE Short=CP47 {ECO:0000303|PubMed:28935373}; DE AltName: Full=Lens fiber cell beaded filament protein CP 49 {ECO:0000303|PubMed:8636093}; DE Short=CP49 {ECO:0000303|PubMed:8636093}; DE AltName: Full=Lens intermediate filament-like light {ECO:0000303|PubMed:10729115}; DE Short=LIFL-L {ECO:0000303|PubMed:10729115}; GN Name=BFSP2; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; OC Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RC TISSUE=Lens; RX PubMed=8636093; DOI=10.1074/jbc.271.12.6729; RA Hess J.F., Casselman J.T., FitzGerald P.G.; RT "Gene structure and cDNA sequence identify the beaded filament protein CP49 RT as a highly divergent type I intermediate filament protein."; RL J. Biol. Chem. 271:6729-6735(1996). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC 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 [3] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 164-415, AND VARIANT CTRCT12 GLU-233 RP DEL. RX PubMed=10739768; DOI=10.1086/302872; RA Jakobs P.M., Hess J.F., FitzGerald P.G., Kramer P., Weleber R.G., Litt M.; RT "Autosomal-dominant congenital cataract associated with a deletion mutation RT in the human beaded filament protein gene BFSP2."; RL Am. J. Hum. Genet. 66:1432-1436(2000). RN [4] RP FUNCTION, AND IDENTIFICATION IN A COMPLEX WITH BFSP1 AND CRYAA. RX PubMed=28935373; DOI=10.1016/j.bbrc.2017.09.088; RA Chaves J.M., Gupta R., Srivastava K., Srivastava O.; RT "Human alpha A-crystallin missing N-terminal domain poorly complexes with RT filensin and phakinin."; RL Biochem. Biophys. Res. Commun. 494:402-408(2017). RN [5] RP VARIANT CTRCT12 TRP-287. RX PubMed=10729115; DOI=10.1086/302871; RA Conley Y.P., Erturk D., Keverline A., Mah T.S., Keravala A., Barnes L.R., RA Bruchis A., Hess J.F., FitzGerald P.G., Weeks D.E., Ferrell R.E., RA Gorin M.B.; RT "A juvenile-onset, progressive cataract locus on chromosome 3q21-q22 is RT associated with a missense mutation in the beaded filament structural RT protein-2."; RL Am. J. Hum. Genet. 66:1426-1431(2000). RN [6] RP VARIANT CTRCT12 GLU-233 DEL. RX PubMed=15570218; RA Zhang Q., Guo X., Xiao X., Yi J., Jia X., Hejtmancik J.F.; RT "Clinical description and genome wide linkage study of Y-sutural cataract RT and myopia in a Chinese family."; RL Mol. Vis. 10:890-900(2004). RN [7] RP VARIANT CTRCT12 GLU-233 DEL. RX PubMed=17200662; RA Zhang L., Gao L., Li Z., Qin W., Gao W., Cui X., Feng G., Fu S., He L., RA Liu P.; RT "Progressive sutural cataract associated with a BFSP2 mutation in a Chinese RT family."; RL Mol. Vis. 12:1626-1631(2006). RN [8] RP VARIANT CTRCT12 GLU-233 DEL. RX PubMed=17982427; RA Cui X., Gao L., Jin Y., Zhang Y., Bai J., Feng G., Gao W., Liu P., He L., RA Fu S.; RT "The E233del mutation in BFSP2 causes a progressive autosomal dominant RT congenital cataract in a Chinese family."; RL Mol. Vis. 13:2023-2029(2007). RN [9] RP VARIANT CTRCT12 GLU-379. RX PubMed=28839118; DOI=10.1534/g3.117.300109; RA Javadiyan S., Craig J.E., Souzeau E., Sharma S., Lower K.M., Mackey D.A., RA Staffieri S.E., Elder J.E., Taranath D., Straga T., Black J., Pater J., RA Casey T., Hewitt A.W., Burdon K.P.; RT "High-Throughput Genetic Screening of 51 Pediatric Cataract Genes RT Identifies Causative Mutations in Inherited Pediatric Cataract in South RT Eastern Australia."; RL G3 (Bethesda) 7:3257-3268(2017). RN [10] RP VARIANT CTRCT12 GLU-233 DEL. RX PubMed=29914532; DOI=10.1186/s13023-018-0828-0; RA Li J., Leng Y., Han S., Yan L., Lu C., Luo Y., Zhang X., Cao L.; RT "Clinical and genetic characteristics of Chinese patients with familial or RT sporadic pediatric cataract."; RL Orphanet J. Rare Dis. 13:94-94(2018). 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:28935373). Plays a role in maintenance of retinal lens optical CC clarity (By similarity). {ECO:0000250|UniProtKB:Q6NVD9, CC ECO:0000269|PubMed:28935373}. CC -!- SUBUNIT: Part of a complex required for lens intermediate filament CC formation composed of BFSP1, BFSP2 and CRYAA (PubMed:28935373). Found CC in 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:28935373}. CC -!- INTERACTION: CC Q13515; Q9P2A4: ABI3; NbExp=5; IntAct=EBI-10229433, EBI-742038; CC Q13515; Q9Y2J4: AMOTL2; NbExp=3; IntAct=EBI-10229433, EBI-746752; CC Q13515; Q7Z3H0-1: ANKRD33; NbExp=3; IntAct=EBI-10229433, EBI-16746154; CC Q13515; P18848: ATF4; NbExp=11; IntAct=EBI-10229433, EBI-492498; CC Q13515; Q00994: BEX3; NbExp=3; IntAct=EBI-10229433, EBI-741753; CC Q13515; Q5H9J7: BEX5; NbExp=3; IntAct=EBI-10229433, EBI-10243741; CC Q13515; Q12934-2: BFSP1; NbExp=5; IntAct=EBI-10229433, EBI-12123320; CC Q13515; Q6AI39: BICRAL; NbExp=3; IntAct=EBI-10229433, EBI-1012434; CC Q13515; Q6QNY1: BLOC1S2; NbExp=3; IntAct=EBI-10229433, EBI-465872; CC Q13515; Q6ZUJ4: C3orf62; NbExp=3; IntAct=EBI-10229433, EBI-2837036; CC Q13515; Q8TC20-4: CAGE1; NbExp=3; IntAct=EBI-10229433, EBI-11522698; CC Q13515; Q9P1Z2: CALCOCO1; NbExp=3; IntAct=EBI-10229433, EBI-749920; CC Q13515; Q494R4-2: CCDC153; NbExp=3; IntAct=EBI-10229433, EBI-11974185; CC Q13515; G5E9W6: CCDC183; NbExp=3; IntAct=EBI-10229433, EBI-17212717; CC Q13515; Q9BXL8: CDCA4; NbExp=3; IntAct=EBI-10229433, EBI-1773949; CC Q13515; Q86X02: CDR2L; NbExp=4; IntAct=EBI-10229433, EBI-11063830; CC Q13515; Q9C0F1: CEP44; NbExp=3; IntAct=EBI-10229433, EBI-744115; CC Q13515; Q96MT8-3: CEP63; NbExp=3; IntAct=EBI-10229433, EBI-11522539; CC Q13515; Q7L5N1: COPS6; NbExp=3; IntAct=EBI-10229433, EBI-486838; CC Q13515; Q8WUE5: CT55; NbExp=3; IntAct=EBI-10229433, EBI-6873363; CC Q13515; Q9NRI5-2: DISC1; NbExp=3; IntAct=EBI-10229433, EBI-11988027; CC Q13515; Q9NPF5: DMAP1; NbExp=5; IntAct=EBI-10229433, EBI-399105; CC Q13515; Q9BQ95: ECSIT; NbExp=3; IntAct=EBI-10229433, EBI-712452; CC Q13515; Q96CS2: HAUS1; NbExp=5; IntAct=EBI-10229433, EBI-2514791; CC Q13515; O14964: HGS; NbExp=3; IntAct=EBI-10229433, EBI-740220; CC Q13515; P02533: KRT14; NbExp=3; IntAct=EBI-10229433, EBI-702178; CC Q13515; Q2M2I5: KRT24; NbExp=3; IntAct=EBI-10229433, EBI-2952736; CC Q13515; Q7Z3Y8: KRT27; NbExp=3; IntAct=EBI-10229433, EBI-3044087; CC Q13515; Q15323: KRT31; NbExp=3; IntAct=EBI-10229433, EBI-948001; CC Q13515; O76014: KRT37; NbExp=3; IntAct=EBI-10229433, EBI-1045716; CC Q13515; P43360: MAGEA6; NbExp=3; IntAct=EBI-10229433, EBI-1045155; CC Q13515; Q9NS73-5: MBIP; NbExp=6; IntAct=EBI-10229433, EBI-10182361; CC Q13515; P59942: MCCD1; NbExp=3; IntAct=EBI-10229433, EBI-11987923; CC Q13515; P15173: MYOG; NbExp=3; IntAct=EBI-10229433, EBI-3906629; CC Q13515; O43482: OIP5; NbExp=3; IntAct=EBI-10229433, EBI-536879; CC Q13515; P40425: PBX2; NbExp=3; IntAct=EBI-10229433, EBI-348489; CC Q13515; Q9BYU1: PBX4; NbExp=3; IntAct=EBI-10229433, EBI-10302990; CC Q13515; P78424: POU6F2; NbExp=3; IntAct=EBI-10229433, EBI-12029004; CC Q13515; Q96KQ4: PPP1R13B; NbExp=3; IntAct=EBI-10229433, EBI-1105153; CC Q13515; P62195: PSMC5; NbExp=3; IntAct=EBI-10229433, EBI-357745; CC Q13515; Q6NUQ1: RINT1; NbExp=3; IntAct=EBI-10229433, EBI-726876; CC Q13515; Q5GAN6: RNASE10; NbExp=3; IntAct=EBI-10229433, EBI-12423312; CC Q13515; Q86UD0: SAPCD2; NbExp=3; IntAct=EBI-10229433, EBI-2561646; CC Q13515; Q9UIL1-3: SCOC; NbExp=3; IntAct=EBI-10229433, EBI-10692913; CC Q13515; Q9UJW9: SERTAD3; NbExp=3; IntAct=EBI-10229433, EBI-748621; CC Q13515; O75971-2: SNAPC5; NbExp=3; IntAct=EBI-10229433, EBI-12004298; CC Q13515; O95295: SNAPIN; NbExp=3; IntAct=EBI-10229433, EBI-296723; CC Q13515; Q9UMX1: SUFU; NbExp=4; IntAct=EBI-10229433, EBI-740595; CC Q13515; Q8N0S2: SYCE1; NbExp=11; IntAct=EBI-10229433, EBI-6872807; CC Q13515; Q96RU7: TRIB3; NbExp=3; IntAct=EBI-10229433, EBI-492476; CC Q13515; Q8N6Y0: USHBP1; NbExp=6; IntAct=EBI-10229433, EBI-739895; CC Q13515; Q70EL1-9: USP54; NbExp=3; IntAct=EBI-10229433, EBI-11975223; CC Q13515; Q9Y3C0: WASHC3; NbExp=3; IntAct=EBI-10229433, EBI-712969; CC Q13515; Q6P1L6: ZNF343; NbExp=3; IntAct=EBI-10229433, EBI-10252492; CC Q13515; Q6ZNG0: ZNF620; NbExp=3; IntAct=EBI-10229433, EBI-4395669; 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:0000250|UniProtKB:D3ZER2}. 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: Lens. CC -!- DISEASE: Cataract 12, multiple types (CTRCT12) [MIM:611597]: An CC opacification of the crystalline lens of the eye that frequently CC results in visual impairment or blindness. Opacities vary in CC morphology, are often confined to a portion of the lens, and may be CC static or progressive. In general, the more posteriorly located and CC dense an opacity, the greater the impact on visual function. The CC opacities can be nuclear, sutural, stellate cortical, lamellar, CC cortical, nuclear embryonic, Y-sutural, punctate cortical, congenital CC or with juvenile- and adult-onset. {ECO:0000269|PubMed:10729115, CC ECO:0000269|PubMed:10739768, ECO:0000269|PubMed:15570218, CC ECO:0000269|PubMed:17200662, ECO:0000269|PubMed:17982427, CC ECO:0000269|PubMed:28839118, ECO:0000269|PubMed:29914532}. Note=The CC disease is caused by variants affecting the gene represented in this CC entry. CC -!- SIMILARITY: Belongs to the intermediate filament family. CC {ECO:0000255|PROSITE-ProRule:PRU01188}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; U48224; AAC50414.1; -; mRNA. DR EMBL; BC113518; AAI13519.1; -; mRNA. DR EMBL; BC113520; AAI13521.1; -; mRNA. DR EMBL; AF195044; AAG30728.1; -; Genomic_DNA. DR CCDS; CCDS33859.1; -. DR RefSeq; NP_003562.1; NM_003571.3. DR RefSeq; XP_016862804.1; XM_017007315.1. DR AlphaFoldDB; Q13515; -. DR SMR; Q13515; -. DR BioGRID; 114005; 67. DR IntAct; Q13515; 63. DR STRING; 9606.ENSP00000304987; -. DR GlyGen; Q13515; 1 site, 1 O-linked glycan (1 site). DR iPTMnet; Q13515; -. DR PhosphoSitePlus; Q13515; -. DR BioMuta; BFSP2; -. DR DMDM; 17366451; -. DR EPD; Q13515; -. DR MassIVE; Q13515; -. DR MaxQB; Q13515; -. DR PaxDb; 9606-ENSP00000304987; -. DR PeptideAtlas; Q13515; -. DR ProteomicsDB; 59513; -. DR Antibodypedia; 33369; 221 antibodies from 19 providers. DR DNASU; 8419; -. DR Ensembl; ENST00000302334.3; ENSP00000304987.2; ENSG00000170819.5. DR GeneID; 8419; -. DR KEGG; hsa:8419; -. DR MANE-Select; ENST00000302334.3; ENSP00000304987.2; NM_003571.4; NP_003562.1. DR UCSC; uc003epn.3; human. DR AGR; HGNC:1041; -. DR CTD; 8419; -. DR DisGeNET; 8419; -. DR GeneCards; BFSP2; -. DR HGNC; HGNC:1041; BFSP2. DR HPA; ENSG00000170819; Not detected. DR MalaCards; BFSP2; -. DR MIM; 603212; gene. DR MIM; 611597; phenotype. DR neXtProt; NX_Q13515; -. DR OpenTargets; ENSG00000170819; -. DR Orphanet; 441452; Early-onset lamellar cataract. DR Orphanet; 98985; Early-onset sutural cataract. DR Orphanet; 98984; Pulverulent cataract. DR PharmGKB; PA25344; -. DR VEuPathDB; HostDB:ENSG00000170819; -. DR eggNOG; ENOG502QTD1; Eukaryota. DR GeneTree; ENSGT00940000159820; -. DR HOGENOM; CLU_012560_0_0_1; -. DR InParanoid; Q13515; -. DR OMA; ETIRIQW; -. DR OrthoDB; 4223979at2759; -. DR PhylomeDB; Q13515; -. DR TreeFam; TF332742; -. DR PathwayCommons; Q13515; -. DR SignaLink; Q13515; -. DR BioGRID-ORCS; 8419; 10 hits in 1148 CRISPR screens. DR GeneWiki; BFSP2; -. DR GenomeRNAi; 8419; -. DR Pharos; Q13515; Tbio. DR PRO; PR:Q13515; -. DR Proteomes; UP000005640; Chromosome 3. DR RNAct; Q13515; Protein. DR Bgee; ENSG00000170819; Expressed in lens of camera-type eye and 91 other cell types or 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:0005200; F:structural constituent of cytoskeleton; TAS:ProtInc. 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 GO; GO:0050896; P:response to stimulus; IEA:UniProtKB-KW. DR GO; GO:0007601; P:visual perception; IEA:UniProtKB-KW. DR Gene3D; 1.20.5.170; -; 1. DR Gene3D; 1.20.5.500; Single helix bin; 1. DR Gene3D; 1.20.5.1160; Vasodilator-stimulated phosphoprotein; 1. DR InterPro; IPR039008; IF_rod_dom. DR InterPro; IPR002957; Keratin_I. DR PANTHER; PTHR23239; INTERMEDIATE FILAMENT; 1. DR PANTHER; PTHR23239:SF32; PHAKININ; 1. DR Pfam; PF00038; Filament; 1. DR PRINTS; PR01248; TYPE1KERATIN. DR SMART; SM01391; Filament; 1. DR SUPFAM; SSF64593; Intermediate filament protein, coiled coil region; 1. DR PROSITE; PS51842; IF_ROD_2; 1. DR Genevisible; Q13515; HS. PE 1: Evidence at protein level; KW Acetylation; Cataract; Cell membrane; Coiled coil; Cytoplasm; Cytoskeleton; KW Disease variant; Eye lens protein; Intermediate filament; Membrane; KW Phosphoprotein; Reference proteome; Repeat; Sensory transduction; Vision. FT INIT_MET 1 FT /note="Removed" FT /evidence="ECO:0000250|UniProtKB:Q28177" FT CHAIN 2..415 FT /note="Phakinin" FT /evidence="ECO:0000305" FT /id="PRO_0000063851" FT DOMAIN 104..415 FT /note="IF rod" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01188" FT REGION 1..46 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..253 FT /evidence="ECO:0000255" FT COILED 309..400 FT /evidence="ECO:0000255" FT COMPBIAS 9..45 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 26 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q28177" FT MOD_RES 32 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q28177" FT MOD_RES 35 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q28177" FT MOD_RES 90 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q28177" FT VARIANT 233 FT /note="Missing (in CTRCT12; dbSNP:rs121908938)" FT /evidence="ECO:0000269|PubMed:10739768, FT ECO:0000269|PubMed:15570218, ECO:0000269|PubMed:17200662, FT ECO:0000269|PubMed:17982427, ECO:0000269|PubMed:29914532" FT /id="VAR_012163" FT VARIANT 287 FT /note="R -> W (in CTRCT12; dbSNP:rs104893685)" FT /evidence="ECO:0000269|PubMed:10729115" FT /id="VAR_012164" FT VARIANT 379 FT /note="A -> E (in CTRCT12; uncertain significance; FT dbSNP:rs774824478)" FT /evidence="ECO:0000269|PubMed:28839118" FT /id="VAR_084817" SQ SEQUENCE 415 AA; 45880 MW; 4CB899386D443FEA CRC64; MSERRVVVDL PTSASSSMPL QRRRASFRGP RSSSSLESPP ASRTNAMSGL VRAPGVYVGT APSGCIGGLG ARVTRRALGI SSVFLQGLRS SGLATVPAPG LERDHGAVED LGGCLVEYMA KVHALEQVSQ ELETQLRMHL ESKATRSGNW GALRASWASS CQQVGEAVLE NARLMLQTET IQAGADDFKE RYENEQPFRK AAEEEINSLY KVIDEANLTK MDLESQIESL KEELGSLSRN YEEDVKLLHK QLAGCELEQM DAPIGTGLDD ILETIRIQWE RDVEKNRVEA GALLQAKQQA EVAHMSQTQE EKLAAALRVE LHNTSCQVQS LQAETESLRA LKRGLENTLH DAKHWHDMEL QNLGAVVGRL EAELREIRAE AEQQQQERAH LLARKCQLQK DVASYHALLD REESG //