LNP_XENLA
ID LNP_XENLA Reviewed; 440 AA.
AC Q6DFJ8;
DT 05-SEP-2006, integrated into UniProtKB/Swiss-Prot.
DT 16-AUG-2004, sequence version 1.
DT 03-AUG-2022, entry version 63.
DE RecName: Full=Endoplasmic reticulum junction formation protein lunapark {ECO:0000305};
DE AltName: Full=ER junction formation factor lunapark {ECO:0000250|UniProtKB:Q9C0E8};
GN Name=lnpk; Synonyms=lnp;
OS Xenopus laevis (African clawed frog).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX NCBI_TaxID=8355;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Embryo;
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (JUL-2004) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP FUNCTION, SUBUNIT, PHOSPHORYLATION AT THR-159; SER-177; SER-179; SER-188;
RP SER-192; THR-198; SER-206; SER-215; THR-219; SER-222; SER-231 AND SER-325,
RP AND IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=27619977; DOI=10.7554/elife.18605;
RA Wang S., Tukachinsky H., Romano F.B., Rapoport T.A.;
RT "Cooperation of the ER-shaping proteins atlastin, lunapark, and reticulons
RT to generate a tubular membrane network.";
RL Elife 5:0-0(2016).
CC -!- FUNCTION: Endoplasmic reticulum (ER)-shaping membrane protein that
CC plays a role in determining ER morphology. Involved in the
CC stabilization of nascent three-way ER tubular junctions within the ER
CC network (PubMed:27619977). May also play a role as a curvature-
CC stabilizing protein within three-way ER tubular junction network (By
CC similarity). {ECO:0000250|UniProtKB:Q7TQ95,
CC ECO:0000250|UniProtKB:Q9C0E8, ECO:0000269|PubMed:27619977}.
CC -!- SUBUNIT: Homodimer; homodimerization requires the C4-type zinc finger
CC motif and decreases during mitosis in a phosphorylation-dependent
CC manner (PubMed:27619977). {ECO:0000269|PubMed:27619977}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000250|UniProtKB:Q9C0E8}; Multi-pass membrane protein
CC {ECO:0000250|UniProtKB:Q9C0E8}; Cytoplasmic side
CC {ECO:0000250|UniProtKB:Q9C0E8}. Note=Localizes at endoplasmic reticulum
CC (ER) three-way tubular junctions, which represent crossing-points at
CC which the tubules build a polygonal network.
CC {ECO:0000250|UniProtKB:Q9C0E8}.
CC -!- DOMAIN: The transmembrane domain 1 and 2 function as a signal-anchor
CC and stop-transfer sequence, respectively, generating a double-spanning
CC integral membrane protein with a N- and C-terminal cytoplasmic
CC orientation. Transmembrane domain 1 and 2 are probably sufficient to
CC mediate membrane translocation and topology formation in a N-
CC myristoylation-independent manner. Transmembrane domain 2 is sufficient
CC to block the protein secretion pathway. The two coiled-coil domains are
CC necessary for its endoplasmic reticulum (ER) three-way tubular junction
CC localization. The C4-type zinc finger motif is necessary both for its
CC ER three-way tubular junction localization and formation.
CC {ECO:0000250|UniProtKB:Q9C0E8}.
CC -!- PTM: Phosphorylated. Phosphorylation at Thr-159 and Ser-325 occurs
CC during interphase (PubMed:27619977). Phosphorylation at Ser-177, Ser-
CC 179, Ser-188, Ser-192, Thr-198, Ser-206, Ser-215, Thr-219, Ser-222 and
CC Ser-231 occurs during mitosis; these phosphorylations reduce both its
CC homodimerization and the ER three-way tubular junction formation
CC (PubMed:27619977). {ECO:0000269|PubMed:27619977}.
CC -!- SIMILARITY: Belongs to the lunapark 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; BC076738; AAH76738.1; -; mRNA.
DR RefSeq; NP_001086514.1; NM_001093045.1.
DR RefSeq; XP_018089910.1; XM_018234421.1.
DR RefSeq; XP_018089911.1; XM_018234422.1.
DR AlphaFoldDB; Q6DFJ8; -.
DR BioGRID; 103209; 1.
DR iPTMnet; Q6DFJ8; -.
DR MaxQB; Q6DFJ8; -.
DR PRIDE; Q6DFJ8; -.
DR DNASU; 446349; -.
DR GeneID; 446349; -.
DR KEGG; xla:446349; -.
DR CTD; 446349; -.
DR Xenbase; XB-GENE-972748; lnpk.L.
DR OMA; VSFWPWK; -.
DR OrthoDB; 1595535at2759; -.
DR Proteomes; UP000186698; Chromosome 9_10L.
DR Bgee; 446349; Expressed in egg cell and 19 other tissues.
DR GO; GO:0098826; C:endoplasmic reticulum tubular network membrane; ISS:UniProtKB.
DR GO; GO:0030176; C:integral component of endoplasmic reticulum membrane; ISS:UniProtKB.
DR GO; GO:0042802; F:identical protein binding; IDA:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0071788; P:endoplasmic reticulum tubular network maintenance; IMP:UniProtKB.
DR GO; GO:1903373; P:positive regulation of endoplasmic reticulum tubular network organization; ISS:UniProtKB.
DR InterPro; IPR040115; Lnp.
DR InterPro; IPR019273; Lunapark_dom.
DR PANTHER; PTHR22166; PTHR22166; 1.
DR Pfam; PF10058; zinc_ribbon_10; 1.
PE 1: Evidence at protein level;
KW Coiled coil; Endoplasmic reticulum; Membrane; Metal-binding;
KW Phosphoprotein; Reference proteome; Transmembrane; Transmembrane helix;
KW Zinc; Zinc-finger.
FT CHAIN 1..440
FT /note="Endoplasmic reticulum junction formation protein
FT lunapark"
FT /id="PRO_0000248317"
FT TOPO_DOM 1..45
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:Q9C0E8"
FT TRANSMEM 46..66
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 67..77
FT /note="Lumenal"
FT /evidence="ECO:0000250|UniProtKB:Q9C0E8"
FT TRANSMEM 78..98
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 99..440
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:Q9C0E8"
FT ZN_FING 280..305
FT /note="C4-type; plays a role in ER morphology"
FT /evidence="ECO:0000250|UniProtKB:Q9C0E8"
FT REGION 149..169
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 202..247
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 316..440
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 16..40
FT /evidence="ECO:0000255"
FT COILED 100..128
FT /evidence="ECO:0000255"
FT COMPBIAS 216..230
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 331..360
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 362..407
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 159
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:27619977"
FT MOD_RES 177
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:27619977"
FT MOD_RES 179
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:27619977"
FT MOD_RES 188
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:27619977"
FT MOD_RES 192
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:27619977"
FT MOD_RES 198
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:27619977"
FT MOD_RES 206
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:27619977"
FT MOD_RES 215
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:27619977"
FT MOD_RES 219
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:27619977"
FT MOD_RES 222
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:27619977"
FT MOD_RES 231
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:27619977"
FT MOD_RES 325
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:27619977"
SQ SEQUENCE 440 AA; 49768 MW; C244648E8AF7D2D3 CRC64;
MGALLAKWRA KPSTVEVLEK MEKDIQSLEE FRDKNQKLRK IWVARLFFYS TILYILTSLT
VYLWYLPGGM TARLLTTLLF LLFPVLIWFV RTLLILWFSR RTERNNDALE LLKAEKKKIL
EEVMEKETYK AAKIILERFD PDSRKIKELE LPVPGPPITP RPGQDLRQRT AAQRNISVST
PVNPGQGSPQ VSGLLAATPA LQRDTSAPGG PPERSVQPTP QSNILQRRPG SPATAVSGMA
LHPPGPPLAR PILPRERGAM DRVIEYLVGD GPQNRYALIC QQCFSHNGMA LKEEFEYVAF
RCAYCYFLNP ARKTRPQAPR LQEISFDRQR QRTDSQGSVN TLQLPAADQL ENQQSPEAME
EDSPAQAEEQ AIEEQVIEEQ VTEEQLIEDQ VIEEDSTCSE QQWEEAPDDT EKDNLPAAEV
NPSLPAPAAN ESEESFMETE
