CHE13_CAEEL
ID CHE13_CAEEL Reviewed; 412 AA.
AC Q93833; E9P884;
DT 08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 2.
DT 03-AUG-2022, entry version 130.
DE RecName: Full=Intraflagellar transport protein che-13;
DE AltName: Full=Chemotaxis abnormal protein 13;
GN Name=che-13 {ECO:0000312|WormBase:F59C6.7a};
GN ORFNames=F59C6.7 {ECO:0000312|WormBase:F59C6.7a};
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 [MRNA] (ISOFORM A), FUNCTION, SUBCELLULAR LOCATION,
RP INDUCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=12651157; DOI=10.1016/s0014-4827(02)00089-7;
RA Haycraft C.J., Schafer J.C., Zhang Q., Taulman P.D., Yoder B.K.;
RT "Identification of CHE-13, a novel intraflagellar transport protein
RT required for cilia formation.";
RL Exp. Cell Res. 284:251-263(2003).
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 DISRUPTION PHENOTYPE.
RX PubMed=2428682; DOI=10.1016/0012-1606(86)90314-3;
RA Perkins L.A., Hedgecock E.M., Thomson J.N., Culotti J.G.;
RT "Mutant sensory cilia in the nematode Caenorhabditis elegans.";
RL Dev. Biol. 117:456-487(1986).
RN [4]
RP FUNCTION, IDENTIFICATION IN IFT COMPLEX B, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RX PubMed=28479320; DOI=10.1016/j.cub.2017.04.015;
RA Yi P., Li W.J., Dong M.Q., Ou G.;
RT "Dynein-driven retrograde intraflagellar transport is triphasic in C.
RT elegans sensory cilia.";
RL Curr. Biol. 27:1448-1461(2017).
CC -!- FUNCTION: Component of the intraflagellar transport (IFT) complex B
CC required for transport of proteins in the motile cilium
CC (PubMed:12651157, PubMed:28479320). May be required for ciliary
CC entrance and transport of specific ciliary cargo proteins such as che-3
CC which are related to motility (PubMed:28479320). Required for the
CC formation of chemosensory cilia that detect chemosensory cues
CC (PubMed:12651157). {ECO:0000269|PubMed:12651157,
CC ECO:0000269|PubMed:28479320}.
CC -!- SUBUNIT: Component of the IFT complex B composed of at least che-2,
CC che-13, dyf-1, dyf-3, dyf-6, dyf-11, dyf-13, ift-20, ift-74, ift-81,
CC ifta-2, osm-1, osm-5 and osm-6. {ECO:0000269|PubMed:28479320}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, cilium axoneme
CC {ECO:0000269|PubMed:12651157}. Note=Moves along the axoneme.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=a;
CC IsoId=Q93833-1; Sequence=Displayed;
CC Name=b;
CC IsoId=Q93833-2; Sequence=VSP_043944, VSP_043945;
CC -!- INDUCTION: Regulated by the RFX-type transcription factor daf-19.
CC {ECO:0000269|PubMed:12651157}.
CC -!- DISRUPTION PHENOTYPE: Worms display defects in ciliary structure
CC resulting in defects in ability and osmotic avoidance behavior. It also
CC affects the localization of IFT complex B proteins, osm-5 and osm-6.
CC Shortened axonemes of all classes of sensory cilia in the head.
CC Required for mating. {ECO:0000269|PubMed:12651157,
CC ECO:0000269|PubMed:2428682}.
CC -!- SIMILARITY: Belongs to the IFT57 family. {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; AF520567; AAM75345.1; -; mRNA.
DR EMBL; Z79600; CAB01878.2; -; Genomic_DNA.
DR EMBL; Z79600; CAB01880.1; -; Genomic_DNA.
DR PIR; T22992; T22992.
DR RefSeq; NP_001251397.1; NM_001264468.1. [Q93833-1]
DR RefSeq; NP_001251398.1; NM_001264469.1. [Q93833-2]
DR AlphaFoldDB; Q93833; -.
DR SMR; Q93833; -.
DR BioGRID; 51341; 2.
DR ComplexPortal; CPX-1290; Intraflagellar transport complex B.
DR STRING; 6239.F59C6.7a; -.
DR PaxDb; Q93833; -.
DR EnsemblMetazoa; F59C6.7a.1; F59C6.7a.1; WBGene00000492. [Q93833-1]
DR EnsemblMetazoa; F59C6.7b.1; F59C6.7b.1; WBGene00000492. [Q93833-2]
DR GeneID; 186607; -.
DR KEGG; cel:CELE_F59C6.7; -.
DR UCSC; F59C6.7; c. elegans. [Q93833-1]
DR CTD; 186607; -.
DR WormBase; F59C6.7a; CE31704; WBGene00000492; che-13. [Q93833-1]
DR WormBase; F59C6.7b; CE11472; WBGene00000492; che-13. [Q93833-2]
DR eggNOG; KOG0972; Eukaryota.
DR GeneTree; ENSGT00390000006307; -.
DR HOGENOM; CLU_039132_0_0_1; -.
DR InParanoid; Q93833; -.
DR OMA; VHAHDQD; -.
DR OrthoDB; 839892at2759; -.
DR PhylomeDB; Q93833; -.
DR Reactome; R-CEL-5620924; Intraflagellar transport.
DR PRO; PR:Q93833; -.
DR Proteomes; UP000001940; Chromosome I.
DR Bgee; WBGene00000492; Expressed in pharyngeal muscle cell (C elegans) and 3 other tissues.
DR GO; GO:0005930; C:axoneme; IDA:WormBase.
DR GO; GO:0005813; C:centrosome; IBA:GO_Central.
DR GO; GO:0036064; C:ciliary basal body; IDA:MGI.
DR GO; GO:0035869; C:ciliary transition zone; IDA:WormBase.
DR GO; GO:0005929; C:cilium; IBA:GO_Central.
DR GO; GO:0005794; C:Golgi apparatus; IBA:GO_Central.
DR GO; GO:0030992; C:intraciliary transport particle B; IDA:WormBase.
DR GO; GO:0007635; P:chemosensory behavior; IMP:WormBase.
DR GO; GO:0060271; P:cilium assembly; IGI:UniProtKB.
DR GO; GO:0035720; P:intraciliary anterograde transport; IEP:WormBase.
DR GO; GO:0035721; P:intraciliary retrograde transport; IEP:WormBase.
DR GO; GO:0042073; P:intraciliary transport; IBA:GO_Central.
DR GO; GO:1905515; P:non-motile cilium assembly; IMP:WormBase.
DR GO; GO:0008104; P:protein localization; IMP:WormBase.
DR InterPro; IPR019530; Intra-flagellar_transport_57.
DR PANTHER; PTHR16011; PTHR16011; 1.
DR Pfam; PF10498; IFT57; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cell projection; Cilium; Coiled coil; Cytoplasm;
KW Cytoskeleton; Reference proteome.
FT CHAIN 1..412
FT /note="Intraflagellar transport protein che-13"
FT /id="PRO_0000328889"
FT REGION 1..21
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 162..193
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 302..393
FT /evidence="ECO:0000255"
FT COMPBIAS 167..193
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 1..87
FT /note="Missing (in isoform b)"
FT /evidence="ECO:0000305"
FT /id="VSP_043944"
FT VAR_SEQ 88..119
FT /note="IKKSGDESYNMPQEFDDPNSTLANIMAAAKNK -> MLHHIKSLKSVLSRGQ
FT EGRFGEKRHSNTTFIT (in isoform b)"
FT /evidence="ECO:0000305"
FT /id="VSP_043945"
SQ SEQUENCE 412 AA; 46504 MW; 715BA9E68C14A446 CRC64;
MEEEHEEESH LSQSDTVGSA IVEDGPGKEY EIYIKNEELV DKLKLLNYED GFLKLGVVYK
PILKHYFVKS KNVGEQFFLF TSLAAWLIKK SGDESYNMPQ EFDDPNSTLA NIMAAAKNKG
IATDFTAAKL KSGAGENVIF ILNSLADASL VHVGFQWQKM IPPKEEDEDT AVDEQDEDDD
NDDIVEEPMN FLDDDDDDNV IEIDLKAQGL ATESKNPLQS VLQSNTDAIT WKQEVERVAP
QLKITLKQDA KDWRLHLEQM NSMHKNVEQK VGNVGPYLDN MSKDIAKALE RIASREKSLN
SQLASMMSKF RRATDTRAEL REKYKAASVG VSSRTETLDR ISDDIEQLKQ QIEEQGAKSS
DGAPLVKIKQ AVSKLEEELQ TMNVQIGVFE QSILNTYLRD HFNFSANLLN IM
