LNPA_TAKRU
ID LNPA_TAKRU Reviewed; 348 AA.
AC Q1KKT4;
DT 05-SEP-2006, integrated into UniProtKB/Swiss-Prot.
DT 30-MAY-2006, sequence version 1.
DT 25-MAY-2022, entry version 46.
DE RecName: Full=Endoplasmic reticulum junction formation protein lunapark-A {ECO:0000305};
DE AltName: Full=ER junction formation factor lunapark {ECO:0000250|UniProtKB:Q9C0E8};
GN Name=lnpka; Synonyms=lnpa;
OS Takifugu rubripes (Japanese pufferfish) (Fugu rubripes).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Eupercaria; Tetraodontiformes; Tetradontoidea; Tetraodontidae; Takifugu.
OX NCBI_TaxID=31033;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=16636282; DOI=10.1073/pnas.0601492103;
RA Lee A.P., Koh E.G.L., Tay A., Brenner S., Venkatesh B.;
RT "Highly conserved syntenic blocks at the vertebrate Hox loci and conserved
RT regulatory elements within and outside Hox gene clusters.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:6994-6999(2006).
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 occurs during interphase.
CC Phosphorylation occurs also during mitosis; these phosphorylations
CC reduce both its homodimerization and the ER three-way tubular junction
CC formation. {ECO:0000250|UniProtKB:Q6DFJ8}.
CC -!- SIMILARITY: Belongs to the lunapark family. {ECO:0000305}.
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DR EMBL; DQ481668; ABF22460.1; -; Genomic_DNA.
DR AlphaFoldDB; Q1KKT4; -.
DR STRING; 31033.ENSTRUP00000044963; -.
DR eggNOG; KOG2846; Eukaryota.
DR InParanoid; Q1KKT4; -.
DR Proteomes; UP000005226; 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 3: Inferred from homology;
KW Coiled coil; Endoplasmic reticulum; Membrane; Metal-binding;
KW Reference proteome; Transmembrane; Transmembrane helix; Zinc; Zinc-finger.
FT CHAIN 1..348
FT /note="Endoplasmic reticulum junction formation protein
FT lunapark-A"
FT /id="PRO_0000248315"
FT TOPO_DOM 1..43
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:Q9C0E8"
FT TRANSMEM 44..64
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 65..67
FT /note="Lumenal"
FT /evidence="ECO:0000250|UniProtKB:Q9C0E8"
FT TRANSMEM 68..88
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 89..348
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:Q9C0E8"
FT ZN_FING 277..302
FT /note="C4-type; plays a role in ER morphology"
FT /evidence="ECO:0000250|UniProtKB:Q9C0E8"
FT REGION 142..211
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 313..348
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 105..126
FT /evidence="ECO:0000255"
SQ SEQUENCE 348 AA; 38721 MW; A0CAAA9323941E5C CRC64;
MSVFCLQAKP TTVEILEGID KDIQILEDYS VKYQRQMKAV VGRLLLYSIL LYLMAGVVVY
SWYLPEQLMG RLVLGLPFLL FPLLVWILRK VLILFFARRT EKNNFKLEDL KAQKRKILED
VMETETYKNA KLILERFDPE SKKKTDFDST PVGPQMTPKP GQELRHRNVV PQTPPASVNS
ASGAAARPPL ASGPAYPGRS SHSAPGGPPE RNLLAIAAQQ SLMRKFVTPG TPIPGVGLHP
PGPPLARPVL PRERGVLDRL IEYLVGDGPQ NRLALVCQQC LSHNGMALKE EFEYVAFRCA
YCYFLNPARK TRPQAPRLPE TAGEPKLPCD LNSSSCAAEE DKQSDSGD
