ID   LNP1_CAEBR              Reviewed;         344 AA.
AC   A8XK26;
DT   04-NOV-2008, integrated into UniProtKB/Swiss-Prot.
DT   15-JAN-2008, sequence version 1.
DT   03-AUG-2022, entry version 64.
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 {ECO:0000312|EMBL:CAP33002.1}; ORFNames=CBG14500;
OS   Caenorhabditis briggsae.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC   Caenorhabditis.
OX   NCBI_TaxID=6238;
RN   [1] {ECO:0000312|EMBL:CAP33002.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AF16 {ECO:0000312|EMBL:CAP33002.1};
RX   PubMed=14624247; DOI=10.1371/journal.pbio.0000045;
RA   Stein L.D., Bao Z., Blasiar D., Blumenthal T., Brent M.R., Chen N.,
RA   Chinwalla A., Clarke L., Clee C., Coghlan A., Coulson A., D'Eustachio P.,
RA   Fitch D.H.A., Fulton L.A., Fulton R.E., Griffiths-Jones S., Harris T.W.,
RA   Hillier L.W., Kamath R., Kuwabara P.E., Mardis E.R., Marra M.A.,
RA   Miner T.L., Minx P., Mullikin J.C., Plumb R.W., Rogers J., Schein J.E.,
RA   Sohrmann M., Spieth J., Stajich J.E., Wei C., Willey D., Wilson R.K.,
RA   Durbin R.M., Waterston R.H.;
RT   "The genome sequence of Caenorhabditis briggsae: a platform for comparative
RT   genomics.";
RL   PLoS Biol. 1:166-192(2003).
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 (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250};
CC       Multi-pass membrane protein {ECO:0000250|UniProtKB:Q17667}.
CC       Note=Localizes to three-way ER tubule junctions. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the lunapark family. {ECO:0000255}.
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DR   EMBL; HE600983; CAP33002.1; -; Genomic_DNA.
DR   RefSeq; XP_002644563.1; XM_002644517.1.
DR   AlphaFoldDB; A8XK26; -.
DR   SMR; A8XK26; -.
DR   STRING; 6238.CBG14500; -.
DR   EnsemblMetazoa; CBG14500.1; CBG14500.1; WBGene00034972.
DR   GeneID; 8586559; -.
DR   KEGG; cbr:CBG_14500; -.
DR   CTD; 8586559; -.
DR   WormBase; CBG14500; CBP18052; WBGene00034972; Cbr-lnp-1.
DR   eggNOG; KOG2846; Eukaryota.
DR   HOGENOM; CLU_797505_0_0_1; -.
DR   InParanoid; A8XK26; -.
DR   OMA; SICHTHN; -.
DR   OrthoDB; 1595535at2759; -.
DR   Proteomes; UP000008549; Chromosome X.
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; ISS:UniProtKB.
DR   GO; GO:0045202; C:synapse; IEA:GOC.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0007268; P:chemical synaptic transmission; ISS:UniProtKB.
DR   GO; GO:0071786; P:endoplasmic reticulum tubular network organization; IBA:GO_Central.
DR   GO; GO:0032880; P:regulation of protein localization; ISS:UniProtKB.
DR   GO; GO:0007416; P:synapse assembly; ISS:UniProtKB.
DR   InterPro; IPR040115; Lnp.
DR   InterPro; IPR019273; Lunapark_dom.
DR   PANTHER; PTHR22166; PTHR22166; 1.
DR   Pfam; PF10058; zinc_ribbon_10; 1.
PE   3: Inferred from homology;
KW   Coiled coil; Endoplasmic reticulum; Membrane; Metal-binding;
KW   Reference proteome; Transmembrane; Transmembrane helix; Zinc; Zinc-finger.
FT   CHAIN           1..344
FT                   /note="Endoplasmic reticulum junction formation protein
FT                   lunapark-1"
FT                   /id="PRO_0000353201"
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..344
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250"
FT   ZN_FING         239..264
FT                   /note="C4-type; plays a role in ER morphology"
FT                   /evidence="ECO:0000250"
FT   REGION          136..155
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          171..192
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          275..344
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          116..140
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        308..328
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        329..344
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   344 AA;  38549 MW;  511A218F2566F14E CRC64;
     MGNLFSRTKS PATELERVVL SIEDFKKRLQ TISASNSSTL YYYYMGVIII LSIAMAHTWL
     RFDDPTKTYV ACALVFGATV IVLTGRYIIN CFFAWRTNRT TQKLENAITQ KTVLLDLVKE
     TLKFKEAKEI LDRYEEKTEA GNTPTENSKL IHQQKQQNET LVSKTIMKPD QKRVETPVSQ
     KPVPSKPGIA FDSMNMTPYQ QRNSNATPVR PFLRQSTALD RILDYFMSDG PNCRNALICS
     ICHTHNGMSV PAEYPFISFR CFECGHLNAA KKMGPHLPIT RPPMGPKGIQ HNGRAGPVPP
     KNQQPVVPME NPNPSTDLTP SASQHGSDSE PEKNADETAV VEKS