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IFB2_CAEEL
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   03-AUG-2022, entry version 159.
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; 16.
DR   DIP; DIP-26763N; -.
DR   IntAct; Q19286; 12.
DR   MINT; Q19286; -.
DR   STRING; 6239.F10C1.7e; -.
DR   iPTMnet; Q19286; -.
DR   World-2DPAGE; 0011:Q19286; -.
DR   World-2DPAGE; 0020:Q19286; -.
DR   EPD; Q19286; -.
DR   PaxDb; Q19286; -.
DR   PeptideAtlas; Q19286; -.
DR   PRIDE; 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   CTD; 173973; -.
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   SignaLink; Q19286; -.
DR   PRO; PR:Q19286; -.
DR   Proteomes; UP000001940; Chromosome II.
DR   Bgee; WBGene00002054; Expressed in larva and 3 other 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 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; 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   PIRSF; PIRSF005546; Intermed_filamnt_Ifb-2; 1.
DR   SMART; SM01391; Filament; 1.
DR   SUPFAM; SSF74853; SSF74853; 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
 
 
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