ID   IFB1_CAEEL              Reviewed;         589 AA.
AC   Q19289; Q19290; Q21063;
DT   26-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   27-MAR-2024, entry version 171.
DE   RecName: Full=Intermediate filament protein ifb-1;
DE   AltName: Full=Cel IF B1;
DE   AltName: Full=Intermediate filament protein B1;
DE            Short=IF-B1;
GN   Name=ifb-1; ORFNames=F10C1.2;
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] (ISOFORM B).
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, AND TISSUE SPECIFICITY.
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, AND INTERACTION WITH IFA-1; IFA-2; IFA-3 AND IFA-4.
RX   PubMed=14529618; DOI=10.1016/j.jmb.2003.08.041;
RA   Karabinos A., Schulze E., Schuenemann J., Parry D.A.D., Weber K.;
RT   "In vivo and in vitro evidence that the four essential intermediate
RT   filament (IF) proteins A1, A2, A3 and B1 of the nematode Caenorhabditis
RT   elegans form an obligate heteropolymeric IF system.";
RL   J. Mol. Biol. 333:307-319(2003).
RN   [5]
RP   FUNCTION, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX   PubMed=14975728; DOI=10.1016/j.ydbio.2003.11.007;
RA   Woo W.-M., Goncharov A., Jin Y., Chisholm A.D.;
RT   "Intermediate filaments are required for C. elegans epidermal elongation.";
RL   Dev. Biol. 267:216-229(2004).
RN   [6]
RP   DISRUPTION PHENOTYPE.
RX   PubMed=21130760; DOI=10.1016/j.ydbio.2010.11.025;
RA   Hetherington S., Gally C., Fritz J.A., Polanowska J., Reboul J., Schwab Y.,
RA   Zahreddine H., Behm C., Labouesse M.;
RT   "PAT-12, a potential anti-nematode target, is a new spectraplakin partner
RT   essential for Caenorhabditis elegans hemidesmosome integrity and embryonic
RT   morphogenesis.";
RL   Dev. Biol. 350:267-278(2011).
CC   -!- FUNCTION: Cytoplasmic intermediate filaments provide mechanical
CC       strength to cells. Essential protein, involved in attachment structures
CC       in epidermal cells that connect muscles to the external cuticle.
CC       Required in morphogenesis and epidermal integrity. Probable component
CC       of embryonic epidermal attachment structures. Functions in larval
CC       muscle attachment independently of ifa-2. {ECO:0000269|PubMed:11427699,
CC       ECO:0000269|PubMed:14529618, ECO:0000269|PubMed:14975728}.
CC   -!- SUBUNIT: Forms some heteromeric filaments with ifa-1, ifa-2, ifa-3 and
CC       probably ifa-4.
CC   -!- INTERACTION:
CC       Q19289; A7DTF5: CELE_Y56A3A.7; NbExp=4; IntAct=EBI-316236, EBI-2413939;
CC       Q19289; Q8MPT2: T04C9.1; NbExp=5; IntAct=EBI-316236, EBI-2315635;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=a; Synonyms=B1b, IFB-1B;
CC         IsoId=Q19289-1; Sequence=Displayed;
CC       Name=b; Synonyms=B1a IFB-1A;
CC         IsoId=Q19289-2; Sequence=VSP_010147;
CC   -!- TISSUE SPECIFICITY: Expressed in epidermal cells. Expressed in amphid
CC       sensory neurons, the excretory cells, the vulva, the uterus, the rectum
CC       and some neurons of the tail. Isoform a and isoform b display a similar
CC       pattern of expression. Isoform a is predominant in pharyngeal
CC       tonofilaments. {ECO:0000269|PubMed:11427699,
CC       ECO:0000269|PubMed:14975728}.
CC   -!- DISRUPTION PHENOTYPE: RNAi-mediated knockdown results in 79% embryonic
CC       lethality and 19% larval lethality. Abnormal localization of epidermal
CC       structural protein pat-12 during embryogenesis.
CC       {ECO:0000269|PubMed:21130760}.
CC   -!- SIMILARITY: Belongs to the intermediate filament family.
CC       {ECO:0000255|PROSITE-ProRule:PRU01188}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=CAA50178.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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; X70830; CAA50178.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; FO080600; CCD65029.1; -; Genomic_DNA.
DR   EMBL; FO080600; CCD65030.1; -; Genomic_DNA.
DR   PIR; D88163; D88163.
DR   PIR; T16018; S46326.
DR   RefSeq; NP_495136.1; NM_062735.4.
DR   RefSeq; NP_495137.1; NM_062736.3. [Q19289-2]
DR   AlphaFoldDB; Q19289; -.
DR   SMR; Q19289; -.
DR   BioGRID; 39317; 22.
DR   DIP; DIP-26309N; -.
DR   IntAct; Q19289; 9.
DR   STRING; 6239.F10C1.2b.1; -.
DR   EPD; Q19289; -.
DR   PaxDb; 6239-F10C1-2b; -.
DR   PeptideAtlas; Q19289; -.
DR   EnsemblMetazoa; F10C1.2a.1; F10C1.2a.1; WBGene00002053. [Q19289-2]
DR   EnsemblMetazoa; F10C1.2b.1; F10C1.2b.1; WBGene00002053. [Q19289-1]
DR   GeneID; 173976; -.
DR   UCSC; F10C1.2b; c. elegans. [Q19289-1]
DR   AGR; WB:WBGene00002053; -.
DR   WormBase; F10C1.2a; CE02618; WBGene00002053; ifb-1. [Q19289-2]
DR   WormBase; F10C1.2b; CE02619; WBGene00002053; ifb-1. [Q19289-1]
DR   eggNOG; KOG0977; Eukaryota.
DR   InParanoid; Q19289; -.
DR   OMA; VYSWEST; -.
DR   OrthoDB; 72418at2759; -.
DR   PhylomeDB; Q19289; -.
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; Q19289; -.
DR   PRO; PR:Q19289; -.
DR   Proteomes; UP000001940; Chromosome II.
DR   Bgee; WBGene00002053; Expressed in larva and 4 other cell types or tissues.
DR   GO; GO:0016324; C:apical plasma membrane; IDA:WormBase.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
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: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; IPR018039; IF_conserved.
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:SF6; INTERMEDIATE FILAMENT PROTEIN IFB-1; 1.
DR   PANTHER; PTHR45721; LAMIN DM0-RELATED; 1.
DR   Pfam; PF00038; Filament; 1.
DR   Pfam; PF00932; LTD; 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; PS00226; IF_ROD_1; 1.
DR   PROSITE; PS51842; IF_ROD_2; 1.
DR   PROSITE; PS51841; LTD; 1.
DR   World-2DPAGE; 0020:Q19289; -.
PE   1: Evidence at protein level;
KW   Alternative splicing; Coiled coil; Cytoplasm; Intermediate filament;
KW   Reference proteome.
FT   CHAIN           1..589
FT                   /note="Intermediate filament protein ifb-1"
FT                   /id="PRO_0000063838"
FT   DOMAIN          81..433
FT                   /note="IF rod"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01188"
FT   DOMAIN          466..584
FT                   /note="LTD"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01187"
FT   REGION          1..42
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          8..84
FT                   /note="Head"
FT   REGION          85..116
FT                   /note="Coil 1A"
FT   REGION          117..130
FT                   /note="Linker 1"
FT   REGION          131..268
FT                   /note="Coil 1B"
FT   REGION          269..285
FT                   /note="Linker 12"
FT   REGION          286..433
FT                   /note="Coil 2"
FT   REGION          434..588
FT                   /note="Tail"
FT   REGION          444..470
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        12..38
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   VAR_SEQ         1..42
FT                   /note="MSSHKESSEYEMQYRSTIQPRTAVRSQSRQSGNYVSGGNGAG -> MEAESA
FT                   PQAPM (in isoform b)"
FT                   /evidence="ECO:0000305"
FT                   /id="VSP_010147"
SQ   SEQUENCE   589 AA;  67149 MW;  C4B6231224ED9AB0 CRC64;
     MSSHKESSEY EMQYRSTIQP RTAVRSQSRQ SGNYVSGGNG AGSGGRVLKM VTEMGSATVG
     GISPALSANA AKSFLEATDK EKKTLQGLND RLGNYIDRVK KLEEQNRKLV ADLDELRGKW
     GKDTSEIKIK YSESLSTARK DIDDAARRKA EVDVKVARHR DDLAEYRSRY EDIQQRRESD
     REKISQWTNA IADAQSEVEM LRARFKQLTD EEKRVTADNS RIWEELQKAR SDLDDETIGR
     IDFQNQVQTL MEELEFLRRV HEQEVKELQA LLAQAPADTR EFFKNELALA IRDIKDEYDI
     IAKQGKQDME SWYKLKVSEV QGSANRANME STYQRDEVKR MRDNIGDLRG KLGDLENKNS
     LLEKEVQNLN YQLTDDQRQY EAALNDRDAT LRRMREECQT LVAELQALLD TKQMLDAEIA
     IYRKMLEGEE TRVGLTQMVE QAVKTHSLQQ QENTDSTRSV RGEVSTKTTF QRSAKGNVTI
     SECDPNGKFI KLENSHRNKD ENVGEHKIRR KLDGRREIVY SIPANVVIKP GKNLTIYARD
     QGGINNPPES LVFDGENTWG IGANVVTSLV NKDGEERATH TQKTIQSGQ
//