LNPA_DANRE
ID LNPA_DANRE Reviewed; 393 AA.
AC Q7ZU80; Q6TEM1;
DT 05-SEP-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 87.
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=lnp, lnpa; ORFNames=zgc:56261;
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 TISSUE=Kidney marrow;
RX PubMed=15520368; DOI=10.1073/pnas.0407241101;
RA Song H.-D., Sun X.-J., Deng M., Zhang G.-W., Zhou Y., Wu X.-Y., Sheng Y.,
RA Chen Y., Ruan Z., Jiang C.-L., Fan H.-Y., Zon L.I., Kanki J.P., Liu T.X.,
RA Look A.T., Chen Z.;
RT "Hematopoietic gene expression profile in zebrafish kidney marrow.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:16240-16245(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=SJD;
RG NIH - Zebrafish Gene Collection (ZGC) project;
RL Submitted (APR-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}.
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DR EMBL; AY423028; AAQ98004.1; -; mRNA.
DR EMBL; BC050510; AAH50510.1; -; mRNA.
DR RefSeq; NP_955774.1; NM_199480.1.
DR AlphaFoldDB; Q7ZU80; -.
DR GeneID; 326761; -.
DR KEGG; dre:326761; -.
DR CTD; 326761; -.
DR ZFIN; ZDB-GENE-030131-4960; lnpa.
DR eggNOG; KOG2846; Eukaryota.
DR InParanoid; Q7ZU80; -.
DR OrthoDB; 1595535at2759; -.
DR PhylomeDB; Q7ZU80; -.
DR PRO; PR:Q7ZU80; -.
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..393
FT /note="Endoplasmic reticulum junction formation protein
FT lunapark-A"
FT /id="PRO_0000248313"
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..69
FT /note="Lumenal"
FT /evidence="ECO:0000250|UniProtKB:Q9C0E8"
FT TRANSMEM 70..90
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 91..393
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:Q9C0E8"
FT ZN_FING 269..294
FT /note="C4-type; plays a role in ER morphology"
FT /evidence="ECO:0000250|UniProtKB:Q9C0E8"
FT REGION 146..209
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 314..393
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 95..130
FT /evidence="ECO:0000255"
FT COMPBIAS 174..197
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 360..387
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 96
FT /note="I -> V (in Ref. 1; AAQ98004)"
FT /evidence="ECO:0000305"
FT CONFLICT 158
FT /note="V -> A (in Ref. 1; AAQ98004)"
FT /evidence="ECO:0000305"
FT CONFLICT 352
FT /note="G -> E (in Ref. 1; AAQ98004)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 393 AA; 43841 MW; 88308C21187E2D3D CRC64;
MGAVVSRWRA KPSTVEVLEG LDKDIQVLEE YREKNHKQLK LWVYRLLLYS ALLYLMACAV
VYAWYIPERM IGKLIVASPF LLFPLLIWLL RKLLIILYNK RTERNNEKLE ELKAEKKKIL
EQVMETETYK NAKLILERFD PDSKKKLELE TQPIGPTVTP RQGQELRHRL VSPRPTGRPP
PVPVPGPSVP GTPLSAPGGP PEKGLSASTP QALIRRPGTP VGTPIPVMGM HPPGPPLARP
VLPRERGAVD RVIEYLVGDG PQNRYALICQ QCLSHNGMAL KEEFEYIAFR CAYCYFLNPA
RKTRPQAPRL PEFAAEAKTS QDPPAVAMET DLPVSPPAPE SKEAGPEPVK AGDGDPQTDE
IPTEEMKPGD PEPHTDIPDK SDGEQDVSAM EVE
