NPHP1_CAEEL
ID NPHP1_CAEEL Reviewed; 682 AA.
AC O17972; Q21570;
DT 16-NOV-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1998, sequence version 2.
DT 03-AUG-2022, entry version 122.
DE RecName: Full=Nephrocystin-1-like protein;
DE AltName: Full=Nephronophthisis homolog;
GN Name=nphp-1 {ECO:0000312|WormBase:M28.7};
GN ORFNames=M28.7 {ECO:0000312|WormBase:M28.7};
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=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 FUNCTION, TISSUE SPECIFICITY, AND DISRUPTION PHENOTYPE.
RX PubMed=15659564; DOI=10.1681/asn.2003121025;
RA Wolf M.T., Lee J., Panther F., Otto E.A., Guan K.L., Hildebrandt F.;
RT "Expression and phenotype analysis of the nephrocystin-1 and nephrocystin-4
RT homologs in Caenorhabditis elegans.";
RL J. Am. Soc. Nephrol. 16:676-687(2005).
RN [3]
RP FUNCTION.
RX PubMed=34115759; DOI=10.1371/journal.pgen.1009618;
RA Hong H., Chen H., Zhang Y., Wu Z., Zhang Y., Zhang Y., Hu Z., Zhang J.V.,
RA Ling K., Hu J., Wei Q.;
RT "DYF-4 regulates patched-related/DAF-6-mediated sensory compartment
RT formation in C. elegans.";
RL PLoS Genet. 17:e1009618-e1009618(2021).
CC -!- FUNCTION: Plays a role in the extension of dendrites from phasmid
CC ciliated sensory neurons (PubMed:34115759). May be necessary for
CC initial assembly of the cilium. {ECO:0000269|PubMed:15659564,
CC ECO:0000269|PubMed:34115759}.
CC -!- TISSUE SPECIFICITY: Expressed in ciliated sensory neurons of the head
CC (amphid neurons) and the tail in hermaphrodites (phasmid neurons) and
CC males (sensory ray neurons). {ECO:0000269|PubMed:15659564}.
CC -!- DISRUPTION PHENOTYPE: Impaired male mating behavior.
CC {ECO:0000269|PubMed:15659564}.
CC -!- SIMILARITY: Belongs to the nephrocystin-1 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; BX284602; CAA90133.1; -; Genomic_DNA.
DR PIR; T23813; T23813.
DR RefSeq; NP_496298.1; NM_063897.4.
DR AlphaFoldDB; O17972; -.
DR SMR; O17972; -.
DR BioGRID; 39957; 11.
DR IntAct; O17972; 11.
DR STRING; 6239.M28.7; -.
DR EPD; O17972; -.
DR PaxDb; O17972; -.
DR EnsemblMetazoa; M28.7.1; M28.7.1; WBGene00010898.
DR GeneID; 174643; -.
DR KEGG; cel:CELE_M28.7; -.
DR UCSC; M28.7; c. elegans.
DR CTD; 174643; -.
DR WormBase; M28.7; CE16278; WBGene00010898; nphp-1.
DR eggNOG; ENOG502QU7K; Eukaryota.
DR GeneTree; ENSGT00390000007701; -.
DR HOGENOM; CLU_403986_0_0_1; -.
DR InParanoid; O17972; -.
DR OMA; SHSHLAF; -.
DR OrthoDB; 676699at2759; -.
DR PhylomeDB; O17972; -.
DR PRO; PR:O17972; -.
DR Proteomes; UP000001940; Chromosome II.
DR Bgee; WBGene00010898; Expressed in pharyngeal muscle cell (C elegans) and 3 other tissues.
DR GO; GO:0036064; C:ciliary basal body; IDA:UniProtKB.
DR GO; GO:0097546; C:ciliary base; IDA:WormBase.
DR GO; GO:0035869; C:ciliary transition zone; IDA:WormBase.
DR GO; GO:0005929; C:cilium; IBA:GO_Central.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0097730; C:non-motile cilium; IDA:WormBase.
DR GO; GO:0008340; P:determination of adult lifespan; IMP:WormBase.
DR GO; GO:0023041; P:neuronal signal transduction; IC:WormBase.
DR GO; GO:1905515; P:non-motile cilium assembly; IMP:WormBase.
DR GO; GO:0008104; P:protein localization; IGI:WormBase.
DR GO; GO:0090251; P:protein localization involved in establishment of planar polarity; IBA:GO_Central.
DR GO; GO:0034606; P:response to hermaphrodite contact; IGI:WormBase.
DR GO; GO:0034607; P:turning behavior involved in mating; IGI:WormBase.
DR InterPro; IPR039687; NPHP1.
DR InterPro; IPR036028; SH3-like_dom_sf.
DR InterPro; IPR001452; SH3_domain.
DR PANTHER; PTHR15176:SF1; PTHR15176:SF1; 1.
DR SMART; SM00326; SH3; 1.
DR SUPFAM; SSF50044; SSF50044; 1.
DR PROSITE; PS50002; SH3; 1.
PE 2: Evidence at transcript level;
KW Behavior; Cilium biogenesis/degradation; Coiled coil; Reference proteome;
KW SH3 domain.
FT CHAIN 1..682
FT /note="Nephrocystin-1-like protein"
FT /id="PRO_0000159587"
FT DOMAIN 215..275
FT /note="SH3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
FT REGION 96..188
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 10..100
FT /evidence="ECO:0000255"
FT COMPBIAS 108..130
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 131..145
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 152..166
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 167..182
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 682 AA; 78796 MW; F30CCFF8B44B552D CRC64;
MSIFGSILSL QDAINRFPQF EYQINRLEKE QKDTEAASRA SFRKHFVRQC QELHRQLDDH
RNRIEKAKTD ETYKKENALE QLDKLKQRLT ALSPEKEQLS FSVSVDSQSE EEKPKMAAIG
RRKSTMYNDD ESEDSDNDSE IIETDVQLDD PLPSQPQPPQ QQHQQPQPKP RQPITITKPL
ESKTLNERQE LDEVISRLQN PSRGDSGEVM EPVVVRGNVF VAIDSWDAEA EGDLELIKGK
KYRITQTRSD GWWTALDEYG QRGLVPKTYL QHVKEKPKNV PSKVSSRLGV RDSVIGISTT
TDPSRREANR QASRVDDCLG KAYDNDTHLS LVCHMAPRLS TSNIGFHDLF WSHYKDQVYK
RTVHISKIIR LVRFEKMPLI EHKALVRMAL VDITNPKSTQ IVSNVHTLVP RVKSSTWYFE
KKESQTRSCI EFSDFVLRSN YRSPTVVLVV EASHLVKTQI GIEEKSLGHT YLRLIIDDKA
VPSRTNVLYL DDEVMTKMKL PEASKRRVLV QVMDVPKDKV SYVDSLPDVI VFNALYLPFF
HFYRRRAGTI LIRDNRNPLS AEFISDPLLS VFPFVCDQHD IMDIMLKIWK TKKKVLAKKN
EAEQTAEFFQ TFLHTAFFIH GIRMISYDVK DDLTLSIRQQ TMQRFVDALN KGLFKQFIAD
QQCKPINIID YSLDLLGNHS ID
