I5P2_CAEEL
ID I5P2_CAEEL Reviewed; 398 AA.
AC P34370;
DT 01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1994, sequence version 1.
DT 03-AUG-2022, entry version 128.
DE RecName: Full=Inositol polyphosphate 5-phosphatase;
DE EC=3.1.3.-;
DE AltName: Full=Ciliary localization protein 1;
GN Name=cil-1; ORFNames=C50C3.7;
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 [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2;
RX PubMed=7906398; DOI=10.1038/368032a0;
RA Wilson R., Ainscough R., Anderson K., Baynes C., Berks M., Bonfield J.,
RA Burton J., Connell M., Copsey T., Cooper J., Coulson A., Craxton M.,
RA Dear S., Du Z., Durbin R., Favello A., Fraser A., Fulton L., Gardner A.,
RA Green P., Hawkins T., Hillier L., Jier M., Johnston L., Jones M.,
RA Kershaw J., Kirsten J., Laisster N., Latreille P., Lightning J., Lloyd C.,
RA Mortimore B., O'Callaghan M., Parsons J., Percy C., Rifken L., Roopra A.,
RA Saunders D., Shownkeen R., Sims M., Smaldon N., Smith A., Smith M.,
RA Sonnhammer E., Staden R., Sulston J., Thierry-Mieg J., Thomas K.,
RA Vaudin M., Vaughan K., Waterston R., Watson A., Weinstock L.,
RA Wilkinson-Sproat J., Wohldman P.;
RT "2.2 Mb of contiguous nucleotide sequence from chromosome III of C.
RT elegans.";
RL Nature 368:32-38(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 DISRUPTION PHENOTYPE.
RX PubMed=18407554; DOI=10.1002/dvdy.21531;
RA Bae Y.K., Lyman-Gingerich J., Barr M.M., Knobel K.M.;
RT "Identification of genes involved in the ciliary trafficking of C. elegans
RT PKD-2.";
RL Dev. Dyn. 237:2021-2029(2008).
RN [4]
RP FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, DISRUPTION PHENOTYPE,
RP AND MUTAGENESIS OF ASN-175.
RX PubMed=19781942; DOI=10.1016/j.cub.2009.08.045;
RA Bae Y.K., Kim E., L'hernault S.W., Barr M.M.;
RT "The CIL-1 PI 5-phosphatase localizes TRP polycystins to cilia and
RT activates sperm in C. elegans.";
RL Curr. Biol. 19:1599-1607(2009).
CC -!- FUNCTION: Dephosphorylates a number of phosphatidylinositols. Controls
CC the cellular levels and subcellular distribution of
CC phosphatidylinositol 3,5-bisphosphate and phosphatidylinositol 3,4,5-
CC trisphosphate. Has a role in sperm activation and motility. Influences
CC the localization of the transient receptor potential polycystin (TRPP)
CC complex proteins lov-1 and pkd-2. {ECO:0000269|PubMed:19781942}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:19781942}.
CC Note=Observed in reticular structures.
CC -!- TISSUE SPECIFICITY: Expressed in tail, cilia, dendrites, axon and male
CC head. {ECO:0000269|PubMed:19781942}.
CC -!- DISRUPTION PHENOTYPE: Reduced mating efficiency. Defective sperm.
CC Abnormal distribution of pkd-2. {ECO:0000269|PubMed:18407554,
CC ECO:0000269|PubMed:19781942}.
CC -!- SIMILARITY: Belongs to the inositol 1,4,5-trisphosphate 5-phosphatase
CC type II family. {ECO:0000305}.
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DR EMBL; FO080718; CCD66123.1; -; Genomic_DNA.
DR PIR; S44627; S44627.
DR RefSeq; NP_498783.1; NM_066382.4.
DR AlphaFoldDB; P34370; -.
DR SMR; P34370; -.
DR STRING; 6239.C50C3.7; -.
DR EPD; P34370; -.
DR PaxDb; P34370; -.
DR PeptideAtlas; P34370; -.
DR EnsemblMetazoa; C50C3.7.1; C50C3.7.1; WBGene00086546.
DR GeneID; 183643; -.
DR KEGG; cel:CELE_C50C3.7; -.
DR UCSC; C50C3.7; c. elegans.
DR CTD; 183643; -.
DR WormBase; C50C3.7; CE00123; WBGene00086546; cil-1.
DR eggNOG; KOG0565; Eukaryota.
DR HOGENOM; CLU_730033_0_0_1; -.
DR InParanoid; P34370; -.
DR OMA; EHLPTWY; -.
DR OrthoDB; 772410at2759; -.
DR PhylomeDB; P34370; -.
DR Reactome; R-CEL-1660499; Synthesis of PIPs at the plasma membrane.
DR Reactome; R-CEL-1855183; Synthesis of IP2, IP, and Ins in the cytosol.
DR Reactome; R-CEL-1855204; Synthesis of IP3 and IP4 in the cytosol.
DR PRO; PR:P34370; -.
DR Proteomes; UP000001940; Chromosome III.
DR Bgee; WBGene00086546; Expressed in adult organism and 4 other tissues.
DR GO; GO:0030424; C:axon; IDA:WormBase.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0030425; C:dendrite; IDA:WormBase.
DR GO; GO:0043025; C:neuronal cell body; IDA:WormBase.
DR GO; GO:0097730; C:non-motile cilium; IDA:WormBase.
DR GO; GO:0005634; C:nucleus; IDA:WormBase.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0001726; C:ruffle; IBA:GO_Central.
DR GO; GO:0004439; F:phosphatidylinositol-4,5-bisphosphate 5-phosphatase activity; IBA:GO_Central.
DR GO; GO:0009566; P:fertilization; IC:UniProtKB.
DR GO; GO:0046855; P:inositol phosphate dephosphorylation; IBA:GO_Central.
DR GO; GO:0046856; P:phosphatidylinositol dephosphorylation; IBA:GO_Central.
DR GO; GO:0046488; P:phosphatidylinositol metabolic process; TAS:UniProtKB.
DR GO; GO:0090216; P:positive regulation of 1-phosphatidylinositol-4-phosphate 5-kinase activity; TAS:UniProtKB.
DR GO; GO:1902093; P:positive regulation of flagellated sperm motility; IMP:UniProtKB.
DR GO; GO:0060378; P:regulation of brood size; IDA:UniProtKB.
DR Gene3D; 3.60.10.10; -; 1.
DR InterPro; IPR036691; Endo/exonu/phosph_ase_sf.
DR InterPro; IPR005135; Endo/exonuclease/phosphatase.
DR InterPro; IPR000300; IPPc.
DR InterPro; IPR041611; SKICH.
DR Pfam; PF03372; Exo_endo_phos; 1.
DR Pfam; PF17751; SKICH; 1.
DR SMART; SM00128; IPPc; 1.
DR SUPFAM; SSF56219; SSF56219; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Hydrolase; Reference proteome.
FT CHAIN 1..398
FT /note="Inositol polyphosphate 5-phosphatase"
FT /id="PRO_0000209746"
FT MUTAGEN 175
FT /note="N->A: Loss of phosphatase activity."
FT /evidence="ECO:0000269|PubMed:19781942"
SQ SEQUENCE 398 AA; 45206 MW; BF42AF62060E7569 CRC64;
MDWKITIFTY NLAMKASDSE AVHNMLNGMI DDHTHLVAIG LQEVAHSETI GGAVLTWATT
IASWMNTNGR MVLLAKTFQA TNQVLIFGRK QLIGQIKRID YRFQRNTMGG LTGHKGSIGV
RLQLASPYSI VFVDSHFIHG PENYGKRVEQ YHTNRNCSFP EDKSVRAAFW FGDFNFRVEE
DVNTVIRKIK NGTHLELLDT REQLKRALVE RDAFIGFHEQ PVTFEPTYRV TVGTTEQDGK
RVPSWTDRIL YKGDGITGLS YTNNKKAVAS DHLPVVAMFR VTAPAAPKPQ WEVIFEHLPT
WYTSIPLVGR FQVNELYYKE NGSYRDWIGV FPSSINDCTT ATNWIYAATC FEQVIEGSKF
LACEFNNIPA GNYRLGYFSC HLHCLVGLSK VFQIVEQP
