LNP_PONAB
ID LNP_PONAB Reviewed; 428 AA.
AC Q5R891; Q5RBZ5;
DT 05-SEP-2006, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 1.
DT 25-MAY-2022, entry version 69.
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 {ECO:0000250|UniProtKB:Q9C0E8}; Synonyms=LNP;
OS Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pongo.
OX NCBI_TaxID=9601;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Kidney;
RG The German cDNA consortium;
RL Submitted (NOV-2004) 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. May be involved in limb and
CC central nervous system development. {ECO:0000250|UniProtKB:Q7TQ95,
CC 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:Q9C0E8}.
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 -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q5R891-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q5R891-2; Sequence=VSP_020240;
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: Myristoylated; myristoylation is necessary for the endoplasmic
CC reticulum (ER) three-way ER tubular junction formation, but is not
CC required neither for membrane translocation, membrane topology
CC formation, nor for the specific localization to ER membranes.
CC {ECO:0000250|UniProtKB:Q9C0E8}.
CC -!- PTM: Phosphorylated. Phosphorylation occurs at Ser-177, Ser-182, Ser-
CC 217, Ser-227, Ser-321 and Ser-384 during interphase. Phosphorylation
CC occurs at Ser-114, Ser-153, Ser-194, Thr-211 and Ser-353 during
CC mitosis; these phosphorylations reduce both its homodimerization and
CC the ER three-way tubular junction formation.
CC {ECO:0000250|UniProtKB:Q9C0E8}.
CC -!- PTM: Subject to proteasomal degradation following phosphorylation
CC during mitosis. {ECO:0000250|UniProtKB:Q9C0E8}.
CC -!- SIMILARITY: Belongs to the lunapark family. {ECO:0000305}.
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DR EMBL; CR858487; CAH90715.1; -; mRNA.
DR EMBL; CR859863; CAH92019.1; -; mRNA.
DR RefSeq; NP_001126172.1; NM_001132700.1.
DR AlphaFoldDB; Q5R891; -.
DR STRING; 9601.ENSPPYP00000014463; -.
DR GeneID; 100173134; -.
DR KEGG; pon:100173134; -.
DR CTD; 80856; -.
DR eggNOG; KOG2846; Eukaryota.
DR InParanoid; Q5R891; -.
DR Proteomes; UP000001595; Unplaced.
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: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 Alternative splicing; Coiled coil; Developmental protein;
KW Endoplasmic reticulum; Lipoprotein; Membrane; Metal-binding; Myristate;
KW Phosphoprotein; Reference proteome; Transmembrane; Transmembrane helix;
KW Zinc; Zinc-finger.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:Q9C0E8"
FT CHAIN 2..428
FT /note="Endoplasmic reticulum junction formation protein
FT lunapark"
FT /id="PRO_0000248312"
FT TOPO_DOM 2..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..428
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:Q9C0E8"
FT ZN_FING 276..301
FT /note="C4-type; plays a role in ER morphology"
FT /evidence="ECO:0000250|UniProtKB:Q9C0E8"
FT REGION 143..248
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 361..428
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 16..43
FT /evidence="ECO:0000255"
FT COILED 102..128
FT /evidence="ECO:0000255"
FT COMPBIAS 166..180
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 181..204
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 361..380
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 114
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9C0E8"
FT MOD_RES 153
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9C0E8"
FT MOD_RES 177
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9C0E8"
FT MOD_RES 182
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9C0E8"
FT MOD_RES 194
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9C0E8"
FT MOD_RES 211
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9C0E8"
FT MOD_RES 213
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9C0E8"
FT MOD_RES 217
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9C0E8"
FT MOD_RES 227
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9C0E8"
FT MOD_RES 321
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9C0E8"
FT MOD_RES 353
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9C0E8"
FT MOD_RES 384
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9C0E8"
FT MOD_RES 414
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q7TQ95"
FT LIPID 2
FT /note="N-myristoyl glycine"
FT /evidence="ECO:0000250|UniProtKB:Q9C0E8"
FT VAR_SEQ 236..240
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|Ref.1"
FT /id="VSP_020240"
FT CONFLICT 12
FT /note="L -> P (in Ref. 1; CAH90715)"
FT /evidence="ECO:0000305"
FT CONFLICT 42
FT /note="R -> W (in Ref. 1; CAH90715)"
FT /evidence="ECO:0000305"
FT CONFLICT 427
FT /note="A -> T (in Ref. 1; CAH90715)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 428 AA; 47729 MW; 38952D156588C348 CRC64;
MGGLFSRWRT KLSTVEVLES IDKEIQALEE FREKNQRLQK LRVGRLILYS SVLYLFTCLI
VYLWYLPDEF TARLAMTLPF FAFPLIIWSI RTVIIFFFSK RTERNNEALD DLKSQRKKIL
EEVMEKETYK TAKLILERFD PDSKKAKECE PPSAGGAVTA RPGQEIRQRT AAQRNLSPTP
ASPNQGPPPQ VPVSPGPPKD SSAPGGPPER TVTPALSSNV LPRHLGSPAT SVPGMGLHPP
GPPLARPILP RERGALDRIV EYLVGDGPQN RYALICQQCF SHNGMALKEE FEYIAFRCAY
CFFLNPARKT RPQAPRLPEF SFEKRQVVEG SSSVGPLPSG SVLSSDNQFN EESLEQDVLD
NNTEQTDDKI PATEQTNQVI EKASDSEEPE EKQETENEEA SVIETNSTVP GADSIPDPEL
NGESLTAE
