ID IFB2_CAEEL Reviewed; 543 AA.
AC Q19286; Q21064; Q95QM2;
DT 26-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 24-JAN-2024, entry version 165.
DE RecName: Full=Intermediate filament protein ifb-2;
DE AltName: Full=Cel IF B2;
DE AltName: Full=Intermediate filament protein B2;
DE Short=IF-B2;
GN Name=ifb-2; ORFNames=F10C1.7;
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORMS A AND C), AND ALTERNATIVE
RP SPLICING.
RC STRAIN=Bristol N2;
RX PubMed=8013462; DOI=10.1002/j.1460-2075.1994.tb06553.x;
RA Dodemont H., Riemer D., Ledger T.N., Weber K.;
RT "Eight genes and alternative RNA processing pathways generate an
RT unexpectedly large diversity of cytoplasmic intermediate filament proteins
RT in the nematode Caenorhabditis elegans.";
RL EMBO J. 13:2625-2638(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND ALTERNATIVE SPLICING.
RC STRAIN=Bristol N2;
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RT "Genome sequence of the nematode C. elegans: a platform for investigating
RT biology.";
RL Science 282:2012-2018(1998).
RN [3]
RP FUNCTION.
RX PubMed=11427699; DOI=10.1073/pnas.121169998;
RA Karabinos A., Schmidt H., Harborth J., Schnabel R., Weber K.;
RT "Essential roles for four cytoplasmic intermediate filament proteins in
RT Caenorhabditis elegans development.";
RL Proc. Natl. Acad. Sci. U.S.A. 98:7863-7868(2001).
RN [4]
RP FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND DEVELOPMENTAL
RP STAGE.
RX PubMed=15063180; DOI=10.1016/j.ydbio.2004.01.003;
RA Bossinger O., Fukushige T., Claeys M., Borgonie G., McGhee J.D.;
RT "The apical disposition of the Caenorhabditis elegans intestinal terminal
RT web is maintained by LET-413.";
RL Dev. Biol. 268:448-456(2004).
CC -!- FUNCTION: Cytoplasmic intermediate filaments provide mechanical
CC strength to cells. Not essential protein. Component of the terminal web
CC (organelle-depleted, intermediate filament-rich layer of cytoplasm that
CC underlies the apical microvilli of polarized epithelial cells) in
CC embryonic through to adult gut cells. Correct localization of filaments
CC requires let-413. {ECO:0000269|PubMed:11427699,
CC ECO:0000269|PubMed:15063180}.
CC -!- INTERACTION:
CC Q19286; A7DTF5: CELE_Y56A3A.7; NbExp=4; IntAct=EBI-320062, EBI-2413939;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:15063180}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=a; Synonyms=b2-H;
CC IsoId=Q19286-1; Sequence=Displayed;
CC Name=c; Synonyms=b2-L;
CC IsoId=Q19286-2; Sequence=VSP_010148;
CC -!- TISSUE SPECIFICITY: Expression is restricted to a discrete
CC circumferential subapical layer within the intestinal terminal web
CC (known as the 'endotube'); this layer joins directly to the apical
CC junction complexes that connect adjacent gut cells.
CC {ECO:0000269|PubMed:15063180}.
CC -!- DEVELOPMENTAL STAGE: Lima bean stage of embryogenesis into adulthood.
CC {ECO:0000269|PubMed:15063180}.
CC -!- SIMILARITY: Belongs to the intermediate filament family.
CC {ECO:0000255|PROSITE-ProRule:PRU01188}.
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DR EMBL; X78553; CAA55296.1; -; Genomic_DNA.
DR EMBL; X78554; CAA55296.1; JOINED; Genomic_DNA.
DR EMBL; FO080600; CCD65033.1; -; Genomic_DNA.
DR EMBL; FO080600; CCD65034.1; -; Genomic_DNA.
DR PIR; T16015; T16015.
DR RefSeq; NP_495133.1; NM_062732.5. [Q19286-1]
DR RefSeq; NP_495134.1; NM_062733.4. [Q19286-2]
DR AlphaFoldDB; Q19286; -.
DR SMR; Q19286; -.
DR BioGRID; 39315; 18.
DR DIP; DIP-26763N; -.
DR IntAct; Q19286; 12.
DR MINT; Q19286; -.
DR STRING; 6239.F10C1.7e.1; -.
DR iPTMnet; Q19286; -.
DR World-2DPAGE; 0011:Q19286; -.
DR World-2DPAGE; 0020:Q19286; -.
DR EPD; Q19286; -.
DR PaxDb; 6239-F10C1-7e; -.
DR PeptideAtlas; Q19286; -.
DR EnsemblMetazoa; F10C1.7a.1; F10C1.7a.1; WBGene00002054. [Q19286-1]
DR EnsemblMetazoa; F10C1.7c.1; F10C1.7c.1; WBGene00002054. [Q19286-2]
DR GeneID; 173973; -.
DR UCSC; F10C1.7c.1; c. elegans. [Q19286-1]
DR AGR; WB:WBGene00002054; -.
DR WormBase; F10C1.7a; CE02622; WBGene00002054; ifb-2. [Q19286-1]
DR WormBase; F10C1.7c; CE27941; WBGene00002054; ifb-2. [Q19286-2]
DR eggNOG; KOG0977; Eukaryota.
DR GeneTree; ENSGT00970000196708; -.
DR InParanoid; Q19286; -.
DR PhylomeDB; Q19286; -.
DR Reactome; R-CEL-2559584; Formation of Senescence-Associated Heterochromatin Foci (SAHF).
DR Reactome; R-CEL-4419969; Depolymerization of the Nuclear Lamina.
DR Reactome; R-CEL-9013405; RHOD GTPase cycle.
DR Reactome; R-CEL-9035034; RHOF GTPase cycle.
DR SignaLink; Q19286; -.
DR PRO; PR:Q19286; -.
DR Proteomes; UP000001940; Chromosome II.
DR Bgee; WBGene00002054; Expressed in larva and 3 other cell types or tissues.
DR ExpressionAtlas; Q19286; baseline and differential.
DR GO; GO:0045179; C:apical cortex; IDA:WormBase.
DR GO; GO:0030054; C:cell junction; IDA:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005882; C:intermediate filament; IEA:UniProtKB-KW.
DR GO; GO:0005635; C:nuclear envelope; IBA:GO_Central.
DR GO; GO:0005652; C:nuclear lamina; IBA:GO_Central.
DR GO; GO:1990357; C:terminal web; IDA:WormBase.
DR GO; GO:0005200; F:structural constituent of cytoskeleton; IBA:GO_Central.
DR GO; GO:0031507; P:heterochromatin formation; IBA:GO_Central.
DR GO; GO:0006998; P:nuclear envelope organization; IBA:GO_Central.
DR GO; GO:0007097; P:nuclear migration; IBA:GO_Central.
DR GO; GO:0051664; P:nuclear pore localization; IBA:GO_Central.
DR GO; GO:0090435; P:protein localization to nuclear envelope; IBA:GO_Central.
DR Gene3D; 1.20.5.170; -; 1.
DR Gene3D; 2.60.40.1260; Lamin Tail domain; 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; IPR016451; Intermed_filament_ifa/ifb.
DR InterPro; IPR001322; Lamin_tail_dom.
DR InterPro; IPR036415; Lamin_tail_dom_sf.
DR PANTHER; PTHR45721:SF7; INTERMEDIATE FILAMENT PROTEIN IFB-2; 1.
DR PANTHER; PTHR45721; LAMIN DM0-RELATED; 1.
DR Pfam; PF00038; Filament; 1.
DR PIRSF; PIRSF005546; Intermed_filamnt_Ifb-2; 1.
DR SMART; SM01391; Filament; 1.
DR SUPFAM; SSF64593; Intermediate filament protein, coiled coil region; 2.
DR SUPFAM; SSF74853; Lamin A/C globular tail domain; 1.
DR PROSITE; PS51842; IF_ROD_2; 1.
DR PROSITE; PS51841; LTD; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Coiled coil; Cytoplasm; Intermediate filament;
KW Reference proteome.
FT CHAIN 1..543
FT /note="Intermediate filament protein ifb-2"
FT /id="PRO_0000063839"
FT DOMAIN 39..388
FT /note="IF rod"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01188"
FT DOMAIN 420..538
FT /note="LTD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01187"
FT REGION 1..42
FT /note="Head"
FT REGION 1..27
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 43..74
FT /note="Coil 1A"
FT REGION 75..88
FT /note="Linker 1"
FT REGION 89..223
FT /note="Coil 1B"
FT REGION 224..240
FT /note="Linker 12"
FT REGION 241..387
FT /note="Coil 2"
FT REGION 388..542
FT /note="Tail"
FT COMPBIAS 1..23
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 388..404
FT /note="Missing (in isoform c)"
FT /evidence="ECO:0000305"
FT /id="VSP_010148"
FT CONFLICT 532
FT /note="A -> R (in Ref. 1; CAA55296)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 543 AA; 61611 MW; 1DA20856DB1312D9 CRC64;
MSAVSYSMHR TTTTTSSSSH GGVSAGHAAE EFVASAEREK QEMQQLNSRL EVYISRVRQL
EDRNKELVIE LDTLRGSLGN DIGQIKFKFN DSLVKVRREI SEAHSGTIGV EVKVDRLRDD
LNDYRHRYEE ARREVEREKT TWGGAISQAQ AELDTNKSRY AAILDEEKRL YAEQDQLYLQ
LAAAKDELDA AIVDRRRLQA EEDDLKIELE FLGRIHSQEI TELRTLLAQA PADTREFFKN
ELALAIREIK AEYDKIIQTT RVDLETIFQS KISAVESSIV SKNEAAVFRQ EEIRKMNESI
TTLRAKLSEL EARNSALERE ANTLQIQLGE DQRAYESELH KRDNALRFMR EDCQTLIAEL
QALLNTKQTL DTEIAIYRKL VESEEGRFTH VGQGVVVAQQ ETTRLVPVEQ DHWDSGEVQT
RSSFKRHAKG NVSIVECDPQ GKYIILENTS GSVAEDVSNF EIRRVIDGVQ AFVFRLPSHL
VIQQHGHLKI YGRNSGGINS PPDSIVMESH PSWGQGGQVE TFLYNSHGIE KASHIQTTVA
SSR
//
