LNP1_CAEEL
ID LNP1_CAEEL Reviewed; 342 AA.
AC Q17667;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 06-JUN-2002, sequence version 2.
DT 03-AUG-2022, entry version 121.
DE RecName: Full=Endoplasmic reticulum junction formation protein lunapark-1 {ECO:0000305};
DE AltName: Full=ER junction formation factor lunapark {ECO:0000250|UniProtKB:Q9C0E8};
GN Name=lnp-1; ORFNames=C05E11.1;
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 [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, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND DISRUPTION
RP PHENOTYPE.
RX PubMed=18279315; DOI=10.1111/j.1460-9568.2008.06049.x;
RA Ghila L., Gomez M.;
RT "The evolutionarily conserved gene LNP-1 is required for synaptic vesicle
RT trafficking and synaptic transmission.";
RL Eur. J. Neurosci. 27:621-630(2008).
CC -!- FUNCTION: Plays a role in tubular endoplasmic reticulum network
CC formation and maintenance (By similarity). May be involved in central
CC nervous system development. Has a presynaptic role in
CC neurotransmission. Likely to operate in synaptogenesis by regulating
CC vesicular transport or localization. Required for correct localization
CC of rab-3 and snb-1. {ECO:0000250, ECO:0000269|PubMed:18279315}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250};
CC Multi-pass membrane protein {ECO:0000269|PubMed:18279315}.
CC Note=Localizes to three-way ER tubule junctions. {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Expressed in cell bodies along the ventral cord
CC around the pharynx and the tail both in larvae and adults. Also
CC expressed in muscles and hypodermal cells.
CC {ECO:0000269|PubMed:18279315}.
CC -!- DISRUPTION PHENOTYPE: Worms exhibit increased resistance to aldicarb
CC indicative of an affect on neurotransmission but equal sensitivity to
CC levamisole which specifically inhibits the postsynapse. Mutants also
CC show mislocalized rab-3 and snb-1 proteins.
CC {ECO:0000269|PubMed:18279315}.
CC -!- SIMILARITY: Belongs to the lunapark family. {ECO:0000305}.
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DR EMBL; FO080371; CCD63258.1; -; Genomic_DNA.
DR PIR; T15418; T15418.
DR RefSeq; NP_508788.1; NM_076387.4.
DR AlphaFoldDB; Q17667; -.
DR SMR; Q17667; -.
DR STRING; 6239.C05E11.1; -.
DR EPD; Q17667; -.
DR PaxDb; Q17667; -.
DR PeptideAtlas; Q17667; -.
DR PRIDE; Q17667; -.
DR EnsemblMetazoa; C05E11.1a.1; C05E11.1a.1; WBGene00015492.
DR GeneID; 180731; -.
DR CTD; 180731; -.
DR WormBase; C05E11.1a; CE29561; WBGene00015492; lnp-1.
DR eggNOG; KOG2846; Eukaryota.
DR GeneTree; ENSGT00390000001859; -.
DR HOGENOM; CLU_797505_0_0_1; -.
DR InParanoid; Q17667; -.
DR OMA; SICHTHN; -.
DR PhylomeDB; Q17667; -.
DR PRO; PR:Q17667; -.
DR Proteomes; UP000001940; Chromosome X.
DR Bgee; WBGene00015492; Expressed in embryo and 4 other tissues.
DR ExpressionAtlas; Q17667; baseline and differential.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0071782; C:endoplasmic reticulum tubular network; IBA:GO_Central.
DR GO; GO:0016021; C:integral component of membrane; IDA:UniProtKB.
DR GO; GO:0016020; C:membrane; IDA:WormBase.
DR GO; GO:0043005; C:neuron projection; IDA:WormBase.
DR GO; GO:0043025; C:neuronal cell body; IDA:WormBase.
DR GO; GO:0008021; C:synaptic vesicle; IDA:WormBase.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0007268; P:chemical synaptic transmission; IMP:UniProtKB.
DR GO; GO:0071786; P:endoplasmic reticulum tubular network organization; IBA:GO_Central.
DR GO; GO:0007626; P:locomotory behavior; IMP:WormBase.
DR GO; GO:0046662; P:regulation of oviposition; IMP:WormBase.
DR GO; GO:0032880; P:regulation of protein localization; IDA:UniProtKB.
DR GO; GO:0050803; P:regulation of synapse structure or activity; IMP:WormBase.
DR GO; GO:0007416; P:synapse assembly; IMP:UniProtKB.
DR GO; GO:0048489; P:synaptic vesicle transport; IMP:WormBase.
DR InterPro; IPR040115; Lnp.
DR InterPro; IPR019273; Lunapark_dom.
DR PANTHER; PTHR22166; PTHR22166; 1.
DR Pfam; PF10058; zinc_ribbon_10; 1.
PE 2: Evidence at transcript level;
KW Coiled coil; Developmental protein; Endoplasmic reticulum; Membrane;
KW Metal-binding; Reference proteome; Transmembrane; Transmembrane helix;
KW Zinc; Zinc-finger.
FT CHAIN 1..342
FT /note="Endoplasmic reticulum junction formation protein
FT lunapark-1"
FT /id="PRO_0000065153"
FT TOPO_DOM 1..39
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 40..60
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 61..68
FT /note="Lumenal"
FT /evidence="ECO:0000250"
FT TRANSMEM 69..89
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 90..342
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT ZN_FING 236..261
FT /note="C4-type; plays a role in ER morphology"
FT /evidence="ECO:0000250"
FT REGION 161..191
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 278..342
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 13..34
FT /evidence="ECO:0000255"
FT COILED 102..136
FT /evidence="ECO:0000255"
FT COMPBIAS 291..322
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 323..342
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 342 AA; 38558 MW; BF3AF0DF4ED01877 CRC64;
MGNLFSRNKS PATELERVAL SIDDLKKRLQ TISSSNTNTL YYYYMSIVVI LSIAMAHTWL
RFEDPQKTYV ACALMLGAIG IVLAGRYVIN GFFSWRTNRT TQKLENAISQ KTTLLDLVKE
TLKFKEAKEI LDRYEKIEQN TTIDKNDSTL KSPSPIKKLT ADSSMFATPK QEQKRVETPT
AQGPNSAMNS MNMTPYHQRN RNAVPIRPFL RQTTAFDRVL DYFMSDGPNC RNALICSICH
THNGMSTPAE YPYISFRCFE CGHLNPAKKM GPQIPLTRPP MGPKGIQHNG RVGPSENTHN
MMENQKPSTD LTPSASQNGS EKGSDSENEK VPESKTMETE FH
