LNPB_DANRE
ID LNPB_DANRE Reviewed; 402 AA.
AC Q6PFM4;
DT 05-SEP-2006, integrated into UniProtKB/Swiss-Prot.
DT 05-SEP-2006, sequence version 2.
DT 03-AUG-2022, entry version 77.
DE RecName: Full=Endoplasmic reticulum junction formation protein lunapark-B {ECO:0000305};
DE AltName: Full=ER junction formation factor lunapark {ECO:0000250|UniProtKB:Q9C0E8};
GN Name=lnpkb; Synonyms=lnpb; ORFNames=wu:fj80c12;
OS Danio rerio (Zebrafish) (Brachydanio rerio).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Danionidae; Danioninae; Danio.
OX NCBI_TaxID=7955;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=AB;
RG NIH - Zebrafish Gene Collection (ZGC) project;
RL Submitted (SEP-2003) 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 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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH57494.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; BC057494; AAH57494.1; ALT_INIT; mRNA.
DR AlphaFoldDB; Q6PFM4; -.
DR STRING; 7955.ENSDARP00000123589; -.
DR PaxDb; Q6PFM4; -.
DR ZFIN; ZDB-GENE-030131-9455; lnpk.
DR eggNOG; KOG2846; Eukaryota.
DR InParanoid; Q6PFM4; -.
DR PhylomeDB; Q6PFM4; -.
DR PRO; PR:Q6PFM4; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; Unplaced.
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 Reference proteome; Transmembrane; Transmembrane helix; Zinc; Zinc-finger.
FT CHAIN 1..402
FT /note="Endoplasmic reticulum junction formation protein
FT lunapark-B"
FT /id="PRO_0000248314"
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..402
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 142..240
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 311..402
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 100..128
FT /evidence="ECO:0000255"
FT COMPBIAS 207..226
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 379..402
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 402 AA; 45219 MW; D788268CD4ED969E CRC64;
MGAIISRWKT KPSTVELLES LDKDIKDLEE FRAKNQRLLK LWVGRLLFYS SALYLLTCLC
VYYLYFPQQW GARLITALPL LAFPALVLLL RKMLIFLFSK RTERNNDKLE DLKTQKRKIL
EEVMETETYK NAKLILERFD PESKKKAEAE ATPVRPHMTP RPGQELRQRH IAMATPGPVL
GPMSPGTTPL RTAPGGPPEK GLAGSASTPA GASQAETPQQ MMRRSMNPYS PGPGSGMRPP
GPPLARPILP RERGAVDRVI EYLVGDGPQN RYALICQQCF SHNGMALKEE FEFVAFRCAY
CYFMNPARKT RPQAPRLPEF SFERRLRSES PETQSSAATE TPEDSDAPED DMERTTSADP
QNPAADEAPV LQESETEESQ PQDVPHAEAE ALEEQKKEDE SN
