IFB1_CAEEL
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 03-AUG-2022, entry version 163.
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};
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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; 20.
DR DIP; DIP-26309N; -.
DR IntAct; Q19289; 9.
DR STRING; 6239.F10C1.2b; -.
DR World-2DPAGE; 0020:Q19289; -.
DR EPD; Q19289; -.
DR PaxDb; Q19289; -.
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 CTD; 173976; -.
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; GKQDMES; -.
DR OrthoDB; 701388at2759; -.
DR PhylomeDB; Q19289; -.
DR SignaLink; Q19289; -.
DR PRO; PR:Q19289; -.
DR Proteomes; UP000001940; Chromosome II.
DR Bgee; WBGene00002053; Expressed in larva and 4 other 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 assembly; 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; 2.60.40.1260; -; 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 Pfam; PF00038; Filament; 1.
DR Pfam; PF00932; LTD; 1.
DR PIRSF; PIRSF005546; Intermed_filamnt_Ifb-2; 1.
DR SMART; SM01391; Filament; 1.
DR SUPFAM; SSF74853; SSF74853; 1.
DR PROSITE; PS00226; IF_ROD_1; 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..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
