LNP_XENTR
ID LNP_XENTR Reviewed; 423 AA.
AC Q28HF6; Q5FW43;
DT 05-SEP-2006, integrated into UniProtKB/Swiss-Prot.
DT 04-APR-2006, sequence version 1.
DT 03-AUG-2022, entry version 76.
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; ORFNames=TEgg059h15.1;
OS Xenopus tropicalis (Western clawed frog) (Silurana tropicalis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Silurana.
OX NCBI_TaxID=8364;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Egg;
RG Sanger Xenopus tropicalis EST/cDNA project;
RL Submitted (JUN-2006) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (FEB-2005) to the EMBL/GenBank/DDBJ databases.
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. May also play a role as a curvature-stabilizing protein within
CC three-way ER tubular junction network (By similarity).
CC {ECO:0000250|UniProtKB:Q7TQ95, ECO:0000250|UniProtKB:Q9C0E8}.
CC -!- SUBUNIT: Homodimer; homodimerization requires the C4-type zinc finger
CC motif and decreases during mitosis in a phosphorylation-dependent
CC manner. {ECO:0000250|UniProtKB:Q6DFJ8}.
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 occurs during
CC interphase. Phosphorylation at Ser-177, Ser-179, Ser-188, Thr-198, Ser-
CC 206, Ser-215, Thr-219, Ser-222 and Ser-231 occurs during mitosis; these
CC phosphorylations reduce both its homodimerization and the ER three-way
CC tubular junction formation. {ECO:0000250|UniProtKB:Q6DFJ8}.
CC -!- SIMILARITY: Belongs to the lunapark family. {ECO:0000305}.
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DR EMBL; CR760905; CAJ83652.1; -; mRNA.
DR EMBL; BC089636; AAH89636.1; -; mRNA.
DR RefSeq; NP_001016474.1; NM_001016474.3.
DR RefSeq; XP_012825883.1; XM_012970429.2.
DR RefSeq; XP_012825884.1; XM_012970430.2.
DR AlphaFoldDB; Q28HF6; -.
DR STRING; 8364.ENSXETP00000016481; -.
DR PaxDb; Q28HF6; -.
DR PRIDE; Q28HF6; -.
DR GeneID; 549228; -.
DR KEGG; xtr:549228; -.
DR CTD; 80856; -.
DR Xenbase; XB-GENE-972741; lnpk.
DR eggNOG; KOG2846; Eukaryota.
DR HOGENOM; CLU_036951_0_0_1; -.
DR InParanoid; Q28HF6; -.
DR OrthoDB; 1595535at2759; -.
DR PhylomeDB; Q28HF6; -.
DR TreeFam; TF315086; -.
DR Proteomes; UP000008143; Chromosome 9.
DR Proteomes; UP000790000; Unplaced.
DR Bgee; ENSXETG00000007570; Expressed in 4-cell stage embryo and 14 other tissues.
DR GO; GO:0071782; C:endoplasmic reticulum tubular network; IBA:GO_Central.
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; ISS:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0071788; P:endoplasmic reticulum tubular network maintenance; ISS:UniProtKB.
DR GO; GO:0071786; P:endoplasmic reticulum tubular network organization; IBA:GO_Central.
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 2: Evidence at transcript level;
KW Coiled coil; Endoplasmic reticulum; Membrane; Metal-binding;
KW Phosphoprotein; Reference proteome; Transmembrane; Transmembrane helix;
KW Zinc; Zinc-finger.
FT CHAIN 1..423
FT /note="Endoplasmic reticulum junction formation protein
FT lunapark"
FT /id="PRO_0000248318"
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..423
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 147..169
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 200..247
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 318..423
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 16..40
FT /evidence="ECO:0000255"
FT COILED 101..128
FT /evidence="ECO:0000255"
FT COMPBIAS 216..233
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 331..350
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 362..387
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 399..417
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 159
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q6DFJ8"
FT MOD_RES 177
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6DFJ8"
FT MOD_RES 179
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6DFJ8"
FT MOD_RES 188
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6DFJ8"
FT MOD_RES 198
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q6DFJ8"
FT MOD_RES 206
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6DFJ8"
FT MOD_RES 215
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6DFJ8"
FT MOD_RES 219
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q6DFJ8"
FT MOD_RES 222
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6DFJ8"
FT MOD_RES 231
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6DFJ8"
FT CONFLICT 413
FT /note="N -> S (in Ref. 2; AAH89636)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 423 AA; 47873 MW; 3E93BA6F7C535896 CRC64;
MGALLAKWRA KPSTVEVLEK MEKDIQSLEE FRDKNQKLRK IWVARLFFYS TILYILTSLT
VYLWYLPDGM TARLLTMLLF LSFPVLIWFV RTLLILWFSR RTERNNDALE LLKTEKKKIL
EEVMEKETYK AAKLILERFD PDSRKIKELE LPVPGPPITP RPGQDLRQRT AAQRNISVST
PVNPGQESPQ VPGLLAATPS LQRDTSAPGG PPERSVQPTP QSNILQRRPG SPATTVSGMA
IHPPGPPLAR PILPRERGAM DRVIEYLVGD GPQNRYALIC QQCFSHNGMA LKEEFEYVAF
RCAYCYFLNP ARKTRPQAPR LQEINFDRQR QRTDSQGSVS SVQPPAAEQL ENPQSPEAME
EDSPAQAEEQ AIEEDSTCSE QQWEEAPDDS EKDPSPVAEL NPSESNPSPP AANETEESFM
ETE
