DAF25_CAEEL
ID DAF25_CAEEL Reviewed; 388 AA.
AC Q9N3Q8;
DT 05-APR-2011, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2001, sequence version 2.
DT 03-AUG-2022, entry version 139.
DE RecName: Full=Dauer abnormal formation protein 25;
DE Short=daf-25;
DE AltName: Full=suppressor of che-2 small body size 3;
DE Short=Chb-3;
GN Name=daf-25; ORFNames=Y48G1A.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 [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 [2]
RP DISRUPTION PHENOTYPE, AND FUNCTION.
RX PubMed=21124861; DOI=10.1371/journal.pgen.1001211;
RA Fujiwara M., Teramoto T., Ishihara T., Ohshima Y., McIntire S.L.;
RT "A novel zf-MYND protein, CHB-3, mediates guanylyl cyclase localization to
RT sensory cilia and controls body size of Caenorhabditis elegans.";
RL PLoS Genet. 6:E1001211-E1001211(2010).
RN [3]
RP SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND FUNCTION.
RX PubMed=21124868; DOI=10.1371/journal.pgen.1001199;
RA Jensen V.L., Bialas N.J., Bishop-Hurley S.L., Molday L.L., Kida K.,
RA Nguyen P.A., Blacque O.E., Molday R.S., Leroux M.R., Riddle D.L.;
RT "Localization of a guanylyl cyclase to chemosensory cilia requires the
RT novel ciliary MYND domain protein DAF-25.";
RL PLoS Genet. 6:E1001199-E1001199(2010).
RN [4]
RP FUNCTION.
RX PubMed=30014846; DOI=10.7554/elife.36833;
RA Hao Y., Yang W., Ren J., Hall Q., Zhang Y., Kaplan J.M.;
RT "Thioredoxin shapes the C. elegans sensory response to Pseudomonas produced
RT nitric oxide.";
RL Elife 7:0-0(2018).
CC -!- FUNCTION: May be involved in the trafficking and dendritic transport of
CC signaling proteins, such as the receptor-type guanylate cyclases gcy-12
CC and daf-11, to the cilia. In ciliated sensory neurons, required for the
CC calcium flux to the cytoplasm in response to onset and removal of a
CC nitric oxide (NO) stimulus and is thereby required for the behavioral
CC avoidance response to NO-producing organisms like P.aeruginosa
CC (PubMed:30014846). {ECO:0000269|PubMed:21124861,
CC ECO:0000269|PubMed:21124868, ECO:0000269|PubMed:30014846}.
CC -!- SUBCELLULAR LOCATION: Cell projection, cilium
CC {ECO:0000269|PubMed:21124868}.
CC -!- TISSUE SPECIFICITY: Expressed in many ciliated sensory neurons.
CC {ECO:0000269|PubMed:21124868}.
CC -!- DISRUPTION PHENOTYPE: Fails to localize guanylate cyclase gcy-12 to
CC sensory cilia. {ECO:0000269|PubMed:21124861}.
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DR EMBL; FO080938; CCD67941.1; -; Genomic_DNA.
DR RefSeq; NP_490719.1; NM_058318.3.
DR AlphaFoldDB; Q9N3Q8; -.
DR SMR; Q9N3Q8; -.
DR BioGRID; 37125; 4.
DR STRING; 6239.Y48G1A.3; -.
DR EPD; Q9N3Q8; -.
DR PaxDb; Q9N3Q8; -.
DR PeptideAtlas; Q9N3Q8; -.
DR EnsemblMetazoa; Y48G1A.3.1; Y48G1A.3.1; WBGene00000917.
DR GeneID; 171623; -.
DR KEGG; cel:CELE_Y48G1A.3; -.
DR UCSC; Y48G1A.3; c. elegans.
DR CTD; 171623; -.
DR WormBase; Y48G1A.3; CE26999; WBGene00000917; daf-25.
DR eggNOG; KOG1710; Eukaryota.
DR HOGENOM; CLU_048951_0_0_1; -.
DR InParanoid; Q9N3Q8; -.
DR OMA; AFKYHYL; -.
DR OrthoDB; 1413951at2759; -.
DR PhylomeDB; Q9N3Q8; -.
DR PRO; PR:Q9N3Q8; -.
DR Proteomes; UP000001940; Chromosome I.
DR Bgee; WBGene00000917; Expressed in germ line (C elegans) and 4 other tissues.
DR GO; GO:0097730; C:non-motile cilium; IDA:WormBase.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0007635; P:chemosensory behavior; IMP:UniProtKB.
DR GO; GO:0043054; P:dauer exit; IMP:WormBase.
DR GO; GO:0030033; P:microvillus assembly; IMP:WormBase.
DR GO; GO:0061067; P:negative regulation of dauer larval development; IMP:WormBase.
DR GO; GO:0010753; P:positive regulation of cGMP-mediated signaling; IMP:WormBase.
DR GO; GO:1904107; P:protein localization to microvillus membrane; IMP:WormBase.
DR GO; GO:0097499; P:protein localization to non-motile cilium; IMP:WormBase.
DR GO; GO:0097500; P:receptor localization to non-motile cilium; IMP:WormBase.
DR GO; GO:0050920; P:regulation of chemotaxis; IMP:WormBase.
DR GO; GO:0061065; P:regulation of dauer larval development; IGI:UniProtKB.
DR GO; GO:0046662; P:regulation of oviposition; IMP:WormBase.
DR GO; GO:0006970; P:response to osmotic stress; IMP:WormBase.
DR GO; GO:0009266; P:response to temperature stimulus; IMP:UniProtKB.
DR Gene3D; 1.25.40.20; -; 1.
DR InterPro; IPR002110; Ankyrin_rpt.
DR InterPro; IPR036770; Ankyrin_rpt-contain_sf.
DR InterPro; IPR002893; Znf_MYND.
DR Pfam; PF12796; Ank_2; 1.
DR Pfam; PF01753; zf-MYND; 1.
DR SMART; SM00248; ANK; 3.
DR SUPFAM; SSF48403; SSF48403; 1.
DR PROSITE; PS50297; ANK_REP_REGION; 1.
DR PROSITE; PS50088; ANK_REPEAT; 1.
DR PROSITE; PS50865; ZF_MYND_2; 1.
PE 2: Evidence at transcript level;
KW ANK repeat; Cell projection; Cilium; Metal-binding; Reference proteome;
KW Repeat; Zinc; Zinc-finger.
FT CHAIN 1..388
FT /note="Dauer abnormal formation protein 25"
FT /id="PRO_0000406204"
FT REPEAT 40..69
FT /note="ANK 1"
FT REPEAT 74..103
FT /note="ANK 2"
FT REPEAT 107..137
FT /note="ANK 3"
FT ZN_FING 321..357
FT /note="MYND-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00134"
FT BINDING 321
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00134"
FT BINDING 324
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00134"
FT BINDING 333
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00134"
FT BINDING 336
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00134"
FT BINDING 341
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00134"
FT BINDING 345
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00134"
FT BINDING 353
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00134"
FT BINDING 357
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00134"
SQ SEQUENCE 388 AA; 43674 MW; 673A121138ACBA9D CRC64;
MTTTEEAPKS PLFEAIDKND TEAALALLKT KEQAAQRDPS GMSVLAAAAY RGNLTLVEKA
IELKCDVNDK TDGTLYTPLM FAALSGKQDV CRLLMDSGAR MYLVNGIGKT ASELAAFVGH
HECVAIINNH ITIDVIEDLL RPKVNGKYEG AEEYPDELAV FIHSLCGSHE IHPVKIIFRF
SKYPDSLKYK KKILYVIDRV FEKQLRCKES NEIMSLKLWL ILFSMRETSK FVESNKEKSP
EEASLQYAKL ISTWQEGDET RRALDVMLRN AVASFPYKHS LLHDTLQKAL QKSQIGERPS
AYEYIVQALF GQRIAAVCQF CSVCGHPGAK KRCTQCKLAY CSQECQKFDW PIHKKVCSFL
KTRQEVSPTD ETAMSLDDIQ AQIAKIDV
