DYF2_CAEEL
ID DYF2_CAEEL Reviewed; 1383 AA.
AC G5ECZ4; G5EDS4;
DT 07-SEP-2016, integrated into UniProtKB/Swiss-Prot.
DT 14-DEC-2011, sequence version 1.
DT 03-AUG-2022, entry version 76.
DE RecName: Full=WD repeat-containing protein dyf-2 {ECO:0000250|UniProtKB:Q8NEZ3};
DE AltName: Full=Abnormal dye filling protein 2 {ECO:0000312|WormBase:ZK520.3a};
GN Name=dyf-2 {ECO:0000312|WormBase:ZK520.3a};
GN ORFNames=ZK520.3 {ECO:0000312|WormBase:ZK520.3a};
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239 {ECO:0000312|EMBL:ABC42046.1};
RN [1] {ECO:0000312|EMBL:ABC42046.1}
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM A), FUNCTION, SUBCELLULAR LOCATION,
RP TISSUE SPECIFICITY, AND DISRUPTION PHENOTYPE.
RX PubMed=16957054; DOI=10.1091/mbc.e06-04-0260;
RA Efimenko E., Blacque O.E., Ou G., Haycraft C.J., Yoder B.K., Scholey J.M.,
RA Leroux M.R., Swoboda P.;
RT "Caenorhabditis elegans DYF-2, an orthologue of human WDR19, is a component
RT of the intraflagellar transport machinery in sensory cilia.";
RL Mol. Biol. Cell 17:4801-4811(2006).
RN [2] {ECO:0000312|Proteomes:UP000001940}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2 {ECO:0000312|Proteomes:UP000001940};
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] {ECO:0000305}
RP FUNCTION, SUBCELLULAR LOCATION, AND MUTAGENESIS OF GLY-361.
RX PubMed=22922713; DOI=10.1038/ncb2560;
RA Wei Q., Zhang Y., Li Y., Zhang Q., Ling K., Hu J.;
RT "The BBSome controls IFT assembly and turnaround in cilia.";
RL Nat. Cell Biol. 14:950-957(2012).
RN [4]
RP FUNCTION, IDENTIFICATION IN IFT COMPLEX A, 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 IFT complex A (IFT-A), a complex required
CC for retrograde ciliary transport (PubMed:28479320). Moves along the
CC ciliary axoneme and is involved in the assembly, localization and the
CC movement of other intraflagellar transport (IFT) proteins along the
CC cilia axoneme (PubMed:16957054, PubMed:22922713). May also associate
CC with the BBSome complex in order to mediate ciliary transport
CC (PubMed:22922713). Regulates cilia biogenesis, morphology and
CC sensitivity to environmental cues (PubMed:16957054, PubMed:22922713).
CC {ECO:0000269|PubMed:16957054, ECO:0000269|PubMed:22922713,
CC ECO:0000269|PubMed:28479320}.
CC -!- SUBUNIT: Component of the IFT complex A (IFT-A) composed of at least
CC che-11, daf-10, dyf-2, ift-139, ift-43 and ifta-1.
CC {ECO:0000269|PubMed:28479320}.
CC -!- SUBCELLULAR LOCATION: Cell projection, cilium
CC {ECO:0000269|PubMed:16957054, ECO:0000269|PubMed:22922713}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=a {ECO:0000312|WormBase:ZK520.3a};
CC IsoId=G5ECZ4-1; Sequence=Displayed;
CC Name=b {ECO:0000312|WormBase:ZK520.3b};
CC IsoId=G5ECZ4-2; Sequence=VSP_058484;
CC -!- TISSUE SPECIFICITY: Expressed in ciliated sensory neurons.
CC {ECO:0000269|PubMed:16957054}.
CC -!- DISRUPTION PHENOTYPE: Defects in cilium morphology and mislocalization
CC of intraflagellar transport proteins. Specifically, phasmid cilia are
CC shorter compared to wild-type, ciliary IFT A complex proteins such as
CC che-11, osm-5 are mislocalized, and the transport and accumulation of
CC the ciliary IFT B complex protein che-13 is impaired. Mutants also
CC display a strong osmosensory (osm) phenotype with an aversion to high
CC osmolarity, and they exhibit impaired chemotaxis in response to
CC volatile odorants such as pyrazine and iso-amyl alcohol.
CC {ECO:0000269|PubMed:16957054}.
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DR EMBL; DQ314286; ABC42046.1; -; mRNA.
DR EMBL; BX284603; CAL49447.1; -; Genomic_DNA.
DR EMBL; BX284603; CAL49448.1; -; Genomic_DNA.
DR RefSeq; NP_001076655.1; NM_001083186.1. [G5ECZ4-1]
DR RefSeq; NP_001076656.1; NM_001083187.2. [G5ECZ4-2]
DR AlphaFoldDB; G5ECZ4; -.
DR ComplexPortal; CPX-1289; Intraflagellar transport complex A.
DR DIP; DIP-61858N; -.
DR IntAct; G5ECZ4; 4.
DR STRING; 6239.ZK520.3a; -.
DR PaxDb; G5ECZ4; -.
DR PRIDE; G5ECZ4; -.
DR EnsemblMetazoa; ZK520.3a.1; ZK520.3a.1; WBGene00001118. [G5ECZ4-1]
DR EnsemblMetazoa; ZK520.3b.1; ZK520.3b.1; WBGene00001118. [G5ECZ4-2]
DR GeneID; 191342; -.
DR KEGG; cel:CELE_ZK520.3; -.
DR CTD; 191342; -.
DR WormBase; ZK520.3a; CE40489; WBGene00001118; dyf-2. [G5ECZ4-1]
DR WormBase; ZK520.3b; CE40490; WBGene00001118; dyf-2. [G5ECZ4-2]
DR eggNOG; KOG2247; Eukaryota.
DR GeneTree; ENSGT00590000083165; -.
DR HOGENOM; CLU_003002_2_0_1; -.
DR InParanoid; G5ECZ4; -.
DR OMA; KNTIPFC; -.
DR OrthoDB; 215211at2759; -.
DR PhylomeDB; G5ECZ4; -.
DR Reactome; R-CEL-5610787; Hedgehog 'off' state.
DR Reactome; R-CEL-5620924; Intraflagellar transport.
DR PRO; PR:G5ECZ4; -.
DR Proteomes; UP000001940; Chromosome III.
DR Bgee; WBGene00001118; Expressed in pharyngeal muscle cell (C elegans) and 3 other tissues.
DR GO; GO:0005929; C:cilium; IBA:GO_Central.
DR GO; GO:0030991; C:intraciliary transport particle A; IBA:GO_Central.
DR GO; GO:0030992; C:intraciliary transport particle B; IDA:WormBase.
DR GO; GO:0097730; C:non-motile cilium; IDA:WormBase.
DR GO; GO:0007635; P:chemosensory behavior; IMP:WormBase.
DR GO; GO:0006935; P:chemotaxis; IMP:WormBase.
DR GO; GO:0060271; P:cilium assembly; IMP:MGI.
DR GO; GO:0035721; P:intraciliary retrograde transport; IMP:MGI.
DR GO; GO:0042073; P:intraciliary transport; IDA:WormBase.
DR GO; GO:1905515; P:non-motile cilium assembly; IMP:WormBase.
DR GO; GO:0042048; P:olfactory behavior; IMP:WormBase.
DR GO; GO:0008104; P:protein localization; IMP:WormBase.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR Gene3D; 2.130.10.10; -; 2.
DR InterPro; IPR011990; TPR-like_helical_dom_sf.
DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR InterPro; IPR001680; WD40_repeat.
DR InterPro; IPR036322; WD40_repeat_dom_sf.
DR InterPro; IPR040379; WDR19/dyf-2.
DR InterPro; IPR039468; WDR19_WD40_rpt.
DR PANTHER; PTHR14920; PTHR14920; 1.
DR Pfam; PF15911; WD40_3; 1.
DR SMART; SM00320; WD40; 7.
DR SUPFAM; SSF48452; SSF48452; 1.
DR SUPFAM; SSF50978; SSF50978; 2.
DR PROSITE; PS50294; WD_REPEATS_REGION; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cell projection; Cilium;
KW Cilium biogenesis/degradation; Protein transport; Reference proteome;
KW Repeat; TPR repeat; Transport; WD repeat.
FT CHAIN 1..1383
FT /note="WD repeat-containing protein dyf-2"
FT /evidence="ECO:0000305"
FT /id="PRO_0000437075"
FT REPEAT 32..71
FT /note="WD 1"
FT /evidence="ECO:0000255"
FT REPEAT 72..112
FT /note="WD 2"
FT /evidence="ECO:0000255"
FT REPEAT 118..157
FT /note="WD 3"
FT /evidence="ECO:0000255"
FT REPEAT 160..198
FT /note="WD 4"
FT /evidence="ECO:0000255"
FT REPEAT 337..376
FT /note="WD 5"
FT /evidence="ECO:0000255"
FT REPEAT 756..789
FT /note="TPR 1"
FT /evidence="ECO:0000255"
FT REPEAT 810..847
FT /note="TPR 2"
FT /evidence="ECO:0000255"
FT REPEAT 885..918
FT /note="TPR 3"
FT /evidence="ECO:0000255"
FT REPEAT 940..973
FT /note="TPR 4"
FT /evidence="ECO:0000255"
FT REPEAT 996..1029
FT /note="TPR 5"
FT /evidence="ECO:0000255"
FT REPEAT 1031..1053
FT /note="TPR 6"
FT /evidence="ECO:0000255"
FT REPEAT 1064..1097
FT /note="TPR 7"
FT /evidence="ECO:0000255"
FT VAR_SEQ 1..807
FT /note="Missing (in isoform b)"
FT /evidence="ECO:0000305"
FT /id="VSP_058484"
FT MUTAGEN 361
FT /note="G->R: In jhu616; the mutated protein displays
FT abnormal accumulation within the cilia. There is also
FT impaired retrograde transport of IFT complex B proteins
FT such as osm-6 along the ciliary axoneme."
FT /evidence="ECO:0000269|PubMed:22922713"
SQ SEQUENCE 1383 AA; 155025 MW; 46B0CBD50F278CCE CRC64;
MSLKVIPCTL TKNQEVFKCV SAQLQYRRGE EEHGSGPIIH RWRPNGHTVA VACANNTVIY
YDKKGNVIDA LNPTGKLIDI AWDKEGDVLA IAVANTGTIY LWDVNSRNTD TVESGATSSK
ELPTCLAWSP STPTLVIGNN AGNIVVYNHR TSRRIAVMGK HQRSVTQITV TPEDYVISCS
DDNTLSVTTL EGTTVSTTTT NGEPTNMDYG SVNGKGGSGV TMVSVVIGKK ILMLAHYNAL
DEPVNLQFQE KYGNIHSYRW FNDGYILIGF DRGYIISISA HNNEIGSELV SFLEYRGYLA
SIAVSTSFNK LLTIGDNMVK VRDLDELTTV TMLTEIETEK NLSEIEVTED GQLVAVSSQS
GVLSIFVTKM PTLAASYNNS ICYLTNLTQV TVVAEVEKKG SSTLELNIEP TVMGLGPLNL
AVANNNTVFF YDYHTPAQMQ AAQQLQSTQS AAEKPTIVAA EPINRVEYLS TVTNIQLNYM
YAAVNFGSRL RLHRIRNSED NVSIEFPEAN RNATLYSYAL TENFLIFTTS NNYIVYFSLS
EWAIVSEYRH VVPVRSIFPH PTNVVCCCFD DRLEAMIYSA VDDEVFRLPS VGSSAHYKGA
IWETFTIDKN TFAVFDSQNI YVFLLSKQHI QGESVIYVSA TRLPHAYVPL SLNKGIVTCL
MSNGKLSSVL LDSHKTESVI SDKSETVIDD ILTRSLLMHR WSTAWKICIH SNDGSHWNQF
AMAALLDSDV GMAIKIFREI GDAAMVTALE LIETIEEKNL LHAQIYTILS RYDDAEQLYL
ESSRPMEALN MRRDLLEWPK ALVLAETMNP KEIPYLSKEY AQELELTGDH ANSLANYEKG
VMENPQNLPE LQEHNEICQS GIARMAIKTG DLRRGVQLAK QLEGRVVKRD CAIILEQMKQ
YTEAAQLYEV GLFYDRAAAV CLKANAWAKV GELLDHVKSP KIHIQYGKIM EKEKKYKVAV
KCYETGRDYD NQVRLLLDPL NDPDEAVRVV RESRSIEGAK LVAKFFVKLG DYNSAIQFLV
MSQCVQEAFE LAEKNNAVRE YAKAIEQHGN ISQALELAEY YNRVNDMFMA AKFYTQAGQY
NNAINLLFKN GDDENCVALA VDCGIKSKDK TLNNKLVKFL LGEDGNVKDP AQLFRLYVGL
GRTKDAAQTA VVVAQIHQAK GNYRIARDLL FQMHQQLREK MMRIPLDMNK SLMAIHSYII
VKALINRKET LLAARLLIRT CGEIQRFPTH VVPILTSSVV ICTQANLKKS AHKFAAQLMT
PEYRPKIHEK YKKKIEDIVR KGGNQKDLVE ENTPCPICDD LMPAYAMSCD NCKSLVPYCI
LTGRHIVASD FSRCPHCEMP GFYSEFRKLS ILNENCYMCG GDLKGAIPED AKAYLEKMEQ
DYK
