IFA2_CAEEL
ID IFA2_CAEEL Reviewed; 581 AA.
AC O02365;
DT 16-FEB-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1997, sequence version 1.
DT 03-AUG-2022, entry version 156.
DE RecName: Full=Intermediate filament protein ifa-2;
DE AltName: Full=Cel IF A2;
DE AltName: Full=Intermediate filament protein A2;
DE Short=IF-A2;
GN Name=mua-6 {ECO:0000312|WormBase:W10G6.3};
GN Synonyms=ifa-2 {ECO:0000312|WormBase:W10G6.3};
GN ORFNames=W10G6.3 {ECO:0000312|WormBase:W10G6.3};
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].
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].
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 TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RX PubMed=12204276; DOI=10.1016/s0925-4773(02)00192-2;
RA Karabinos A., Schulze E., Klisch T., Wang J., Weber K.;
RT "Expression profiles of the essential intermediate filament (IF) protein A2
RT and the IF protein C2 in the nematode Caenorhabditis elegans.";
RL Mech. Dev. 117:311-314(2002).
RN [5]
RP FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND DEVELOPMENTAL
RP STAGE.
RX PubMed=14597206; DOI=10.1016/j.ydbio.2003.08.001;
RA Hapiak V., Hresko M.C., Schriefer L.A., Saiyasisongkhram K., Bercher M.,
RA Plenefisch J.;
RT "mua-6, a gene required for tissue integrity in Caenorhabditis elegans,
RT encodes a cytoplasmic intermediate filament.";
RL Dev. Biol. 263:330-342(2003).
RN [6]
RP INTERACTION WITH IFB-1.
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).
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 Probably acts by forming hypodermal hemidesmosome complexes that help
CC mediate muscle-cuticle force transduction. Although expressed during
CC embryogenesis, it is not required for embryonic development of muscle-
CC cuticle linkages nor for the localization of other proteins to the
CC hemidesmosomes in embryos. {ECO:0000269|PubMed:11427699,
CC ECO:0000269|PubMed:14597206}.
CC -!- SUBUNIT: Forms some heteromeric filaments with ifb-1.
CC -!- SUBCELLULAR LOCATION: Cell junction, hemidesmosome
CC {ECO:0000269|PubMed:14597206}. Note=Colocalizes with myoactin.
CC -!- TISSUE SPECIFICITY: Mainly expressed in regions of the hypodermis
CC adjacent to muscle. Expressed in longitudinal stripes where the
CC mechanosensory neurons interface with the hypodermis. Also expressed to
CC the uterine seam and within the uterine-vulval cells.
CC {ECO:0000269|PubMed:12204276, ECO:0000269|PubMed:14597206}.
CC -!- DEVELOPMENTAL STAGE: First expressed in embryos that are starting to
CC elongate, before hemidesmosomes-associated filaments are recruited to
CC regions of the hypodermis adjacent to muscle. Expressed throughout
CC larval stages and in adults. {ECO:0000269|PubMed:12204276,
CC ECO:0000269|PubMed:14597206}.
CC -!- SIMILARITY: Belongs to the intermediate filament family.
CC {ECO:0000255|PROSITE-ProRule:PRU01188}.
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DR EMBL; X70835; CAA50183.1; -; Genomic_DNA.
DR EMBL; Z81140; CAB03486.1; -; Genomic_DNA.
DR PIR; T26335; T26335.
DR RefSeq; NP_510648.1; NM_078247.7.
DR AlphaFoldDB; O02365; -.
DR SMR; O02365; -.
DR BioGRID; 46584; 28.
DR DIP; DIP-26450N; -.
DR IntAct; O02365; 9.
DR MINT; O02365; -.
DR STRING; 6239.W10G6.3; -.
DR iPTMnet; O02365; -.
DR EPD; O02365; -.
DR PaxDb; O02365; -.
DR PeptideAtlas; O02365; -.
DR EnsemblMetazoa; W10G6.3.1; W10G6.3.1; WBGene00003485.
DR GeneID; 181698; -.
DR KEGG; cel:CELE_W10G6.3; -.
DR UCSC; W10G6.3.1; c. elegans.
DR CTD; 181698; -.
DR WormBase; W10G6.3; CE18354; WBGene00003485; mua-6.
DR eggNOG; KOG0977; Eukaryota.
DR GeneTree; ENSGT00970000196730; -.
DR HOGENOM; CLU_012560_7_0_1; -.
DR InParanoid; O02365; -.
DR OMA; HPFQSVK; -.
DR OrthoDB; 701388at2759; -.
DR PhylomeDB; O02365; -.
DR SignaLink; O02365; -.
DR PRO; PR:O02365; -.
DR Proteomes; UP000001940; Chromosome X.
DR Bgee; WBGene00003485; Expressed in larva and 4 other tissues.
DR GO; GO:0030056; C:hemidesmosome; IDA:WormBase.
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:0098609; P:cell-cell adhesion; IMP:WormBase.
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 Pfam; PF00932; LTD; 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 Cell junction; Coiled coil; Intermediate filament; Reference proteome.
FT CHAIN 1..581
FT /note="Intermediate filament protein ifa-2"
FT /id="PRO_0000063835"
FT DOMAIN 71..424
FT /note="IF rod"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01188"
FT DOMAIN 457..574
FT /note="LTD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01187"
FT REGION 1..74
FT /note="Head"
FT REGION 1..35
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 47..68
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 75..106
FT /note="Coil 1A"
FT REGION 107..120
FT /note="Linker 1"
FT REGION 121..258
FT /note="Coil 1B"
FT REGION 259..276
FT /note="Linker 12"
FT REGION 277..424
FT /note="Coil 2"
FT REGION 425..578
FT /note="Tail"
FT REGION 449..469
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..32
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 47..63
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 454..469
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 581 AA; 67094 MW; DA0E68EBF6FBA499 CRC64;
MTDPDSYRSS ITSRPSFNRT VTSSSQNYGA PGSGNRVLKI VTETHSSSVS SGLSPYGQNA
ASTIRDNRER EKKEIMELND RLASYIEKVR FLDAQNRKLD ADLKMLQGRF GKSTGSVKVM
YEMEITTATN VVKQTGKDHG ETEKEIRKLQ DQLDELRKKF EEAQRGRAED RLKIDDLLVT
LSNLEAEINL LKRRIALLEE EVARLKKENF RLTSELQRVR IELDQETLLR IDNQNKVKTI
LEEIDFMKRG FETELKELQA QAARDTTSEN REYFKNELAN AMRDIRAEYD QIMNGNRNDM
ESWYQLRVQE INTQSNRQNA ENNYQKEEVK RLRNQTSELR QKLSDLESRN LLLEKQIEDL
NYQLEDDQRS YEAALNDKDA QIRKLREECQ ALMVELQMLL DTKQTLDGEL KVYRQMLEGN
SEGNGLRQLV EKVVRTSAIN EEADTETMRV VKGEHSSRTS YQRSAKGNVA IKETSPEGKF
VILENTHRAK EEPLGDWKLK RKIDGKREIV FTFPSDYILH PFQSVKIFAR GQGIANPPEV
LIFEGDETFG VGANVQTILY NNKGEERATH IQRQSQQTTS S
