UN119_CAEEL
ID UN119_CAEEL Reviewed; 219 AA.
AC Q10658;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 131.
DE RecName: Full=Protein unc-119;
DE AltName: Full=Uncoordinated protein 119;
GN Name=unc-119; ORFNames=M142.1;
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 [GENOMIC DNA], FUNCTION, TISSUE SPECIFICITY, AND
RP DISRUPTION PHENOTYPE.
RC STRAIN=Bristol N2;
RX PubMed=8582641; DOI=10.1093/genetics/141.3.977;
RA Maduro M.F., Pilgrim D.B.;
RT "Identification and cloning of unc-119, a gene expressed in the
RT Caenorhabditis elegans nervous system.";
RL Genetics 141:977-988(1995).
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 FUNCTION.
RX PubMed=22085962; DOI=10.1101/gad.173443.111;
RA Wright K.J., Baye L.M., Olivier-Mason A., Mukhopadhyay S., Sang L.,
RA Kwong M., Wang W., Pretorius P.R., Sheffield V.C., Sengupta P.,
RA Slusarski D.C., Jackson P.K.;
RT "An ARL3-UNC119-RP2 GTPase cycle targets myristoylated NPHP3 to the primary
RT cilium.";
RL Genes Dev. 25:2347-2360(2011).
RN [4]
RP DISRUPTION PHENOTYPE.
RX PubMed=21642972; DOI=10.1038/nn.2835;
RA Zhang H., Constantine R., Vorobiev S., Chen Y., Seetharaman J., Huang Y.J.,
RA Xiao R., Montelione G.T., Gerstner C.D., Davis M.W., Inana G., Whitby F.G.,
RA Jorgensen E.M., Hill C.P., Tong L., Baehr W.;
RT "UNC119 is required for G protein trafficking in sensory neurons.";
RL Nat. Neurosci. 14:874-880(2011).
CC -!- FUNCTION: Myristoyl-binding protein that acts as a cargo adapter:
CC specifically binds the myristoyl moiety of a subset of N-terminally
CC myristoylated proteins and is required for their localization. Plays a
CC key role in ciliary membrane localization of proteins. Required for the
CC establishment or function of the nervous system.
CC {ECO:0000269|PubMed:22085962, ECO:0000269|PubMed:8582641}.
CC -!- INTERACTION:
CC Q10658; O45379: arl-3; NbExp=5; IntAct=EBI-325431, EBI-325438;
CC -!- TISSUE SPECIFICITY: Predominantly neuron-specific.
CC {ECO:0000269|PubMed:8582641}.
CC -!- DOMAIN: Adopts an immunoglobulin-like beta-sandwich fold forming a
CC hydrophobic cavity that capture N-terminally myristoylated target
CC peptides. Phe residues within the hydrophobic beta sandwich are
CC required for myristate binding (By similarity). {ECO:0000250}.
CC -!- DISRUPTION PHENOTYPE: Worms exhibit diverse nervous system defects
CC including defects in feeding behavior and chemosensation. Phenotypes
CC are due to defects in protein trafficking, such as mislocalization of
CC odr-3 and gpa-13 proteins in olfactory neurons.
CC {ECO:0000269|PubMed:21642972, ECO:0000269|PubMed:8582641}.
CC -!- SIMILARITY: Belongs to the PDE6D/unc-119 family. {ECO:0000305}.
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DR EMBL; U32854; AAC46919.1; -; Genomic_DNA.
DR EMBL; Z73428; CAA97807.1; -; Genomic_DNA.
DR PIR; T23761; T23761.
DR RefSeq; NP_001255089.1; NM_001268160.1.
DR AlphaFoldDB; Q10658; -.
DR SMR; Q10658; -.
DR BioGRID; 41706; 4.
DR DIP; DIP-26782N; -.
DR IntAct; Q10658; 2.
DR STRING; 6239.M142.1c; -.
DR PaxDb; Q10658; -.
DR EnsemblMetazoa; M142.1a.1; M142.1a.1; WBGene00006843.
DR GeneID; 176519; -.
DR UCSC; M142.1; c. elegans.
DR CTD; 31664; -.
DR WormBase; M142.1a; CE06203; WBGene00006843; unc-119.
DR eggNOG; KOG4037; Eukaryota.
DR GeneTree; ENSGT00390000014595; -.
DR HOGENOM; CLU_088825_1_1_1; -.
DR InParanoid; Q10658; -.
DR PhylomeDB; Q10658; -.
DR Reactome; R-CEL-5624138; Trafficking of myristoylated proteins to the cilium.
DR PRO; PR:Q10658; -.
DR Proteomes; UP000001940; Chromosome III.
DR Bgee; WBGene00006843; Expressed in pharyngeal muscle cell (C elegans) and 3 other tissues.
DR ExpressionAtlas; Q10658; baseline and differential.
DR GO; GO:0030424; C:axon; IDA:WormBase.
DR GO; GO:0005929; C:cilium; IBA:GO_Central.
DR GO; GO:0008289; F:lipid binding; IBA:GO_Central.
DR GO; GO:0010171; P:body morphogenesis; IMP:WormBase.
DR GO; GO:0007635; P:chemosensory behavior; IMP:WormBase.
DR GO; GO:0060271; P:cilium assembly; IMP:WormBase.
DR GO; GO:0040024; P:dauer larval development; IMP:WormBase.
DR GO; GO:0007631; P:feeding behavior; IMP:WormBase.
DR GO; GO:0042953; P:lipoprotein transport; IBA:GO_Central.
DR GO; GO:0040011; P:locomotion; IMP:WormBase.
DR GO; GO:0030517; P:negative regulation of axon extension; IMP:WormBase.
DR GO; GO:0007399; P:nervous system development; IBA:GO_Central.
DR GO; GO:0046662; P:regulation of oviposition; IMP:WormBase.
DR GO; GO:0043051; P:regulation of pharyngeal pumping; IMP:WormBase.
DR GO; GO:0000003; P:reproduction; IMP:WormBase.
DR Gene3D; 2.70.50.40; -; 1.
DR InterPro; IPR014756; Ig_E-set.
DR InterPro; IPR008015; PDED_dom.
DR InterPro; IPR037036; PDED_dom_sf.
DR Pfam; PF05351; GMP_PDE_delta; 1.
DR SUPFAM; SSF81296; SSF81296; 1.
PE 1: Evidence at protein level;
KW Cilium biogenesis/degradation; Developmental protein; Lipid-binding;
KW Protein transport; Reference proteome; Transport.
FT CHAIN 1..219
FT /note="Protein unc-119"
FT /id="PRO_0000221216"
FT REGION 1..27
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..16
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 112
FT /ligand="tetradecanoate"
FT /ligand_id="ChEBI:CHEBI:30807"
FT /evidence="ECO:0000250"
SQ SEQUENCE 219 AA; 25264 MW; 26F43457C5CDEB45 CRC64;
MKAEQQQQSI APGSATFPSQ MPRPPPVTEQ AITTEAELLA KNQITPNDVL ALPGITQGFL
CSPSANVYNI EFTKFQIRDL DTEHVLFEIA KPENETEENL QAQAESARYV RYRFAPNFLK
LKTVGATVEF KVGDVPITHF RMIERHFFKD RLLKCFDFEF GFCMPNSRNN CEHIYEFPQL
SQQLMDDMIN NPNETRSDSF YFVENKLVMH NKADYSYDA
