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Protein

Endoplasmic reticulum junction formation protein lunapark

Gene

LNPK

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Endoplasmic reticulum (ER)-shaping membrane protein that plays a role in determining ER morphology. Involved in the stabilization of nascent three-way ER tubular junctions within the ER network (PubMed:24223779, PubMed:25404289, PubMed:25548161, PubMed:27619977). May also play a role as a curvature-stabilizing protein within the three-way ER tubular junction network (PubMed:25404289). May be involved in limb and central nervous system development (By similarity).By similarity4 Publications

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Zinc fingeri276 – 301C4-type; plays a role in ER morphology2 PublicationsAdd BLAST26

GO - Molecular functioni

  • identical protein binding Source: UniProtKB
  • metal ion binding Source: UniProtKB-KW

GO - Biological processi

  • blood coagulation Source: Ensembl
  • embryonic digit morphogenesis Source: Ensembl
  • embryonic forelimb morphogenesis Source: Ensembl
  • endoplasmic reticulum tubular network maintenance Source: UniProtKB
  • limb development Source: UniProtKB
  • positive regulation of endoplasmic reticulum tubular network organization Source: UniProtKB
  • regulation of chondrocyte differentiation Source: Ensembl

Keywordsi

Molecular functionDevelopmental protein
LigandMetal-binding, Zinc

Names & Taxonomyi

Protein namesi
Recommended name:
Endoplasmic reticulum junction formation protein lunaparkCurated
Alternative name(s):
ER junction formation factor lunaparkImported
Gene namesi
Name:LNPKImported
Synonyms:KIAA1715Imported, LNP
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 2

Organism-specific databases

EuPathDBiHostDB:ENSG00000144320.13.
HGNCiHGNC:21610. LNPK.

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Topological domaini2 – 45Cytoplasmic1 PublicationAdd BLAST44
Transmembranei46 – 66HelicalSequence analysisAdd BLAST21
Topological domaini67 – 77Lumenal1 PublicationAdd BLAST11
Transmembranei78 – 98HelicalSequence analysisAdd BLAST21
Topological domaini99 – 428Cytoplasmic2 PublicationsAdd BLAST330

Keywords - Cellular componenti

Endoplasmic reticulum, Membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi2G → A: Abolishes myristoylation. Inhibits three-way ER tubular junction formation. Does not inhibit transmembrane domain 1-induced membrane translocation. 2 Publications1
Mutagenesisi177S → A: Inhibits phosphorylation and degradation in mitosis and prevents homodimerization and three-way ER tubular junction formations; when associated with A-179; A-182; A-194; A-202; A-211; A-213; A-218; A-227 and A-231. 1 Publication1
Mutagenesisi177S → D: Inhibits phosphorylation and degradation in mitosis but does not prevent homodimerization and three-way ER tubular junction formations; when associated with A-179; A-182; A-194; A-202; A-211; A-213; A-218; A-227 and A-231. 1 Publication1
Mutagenesisi179T → A: Inhibits phosphorylation and degradation in mitosis and prevents homodimerization and three-way ER tubular junction formations; when associated with A-177; A-182; A-194; A-202; A-211; A-213; A-218; A-227 and A-231. 1 Publication1
Mutagenesisi179T → D: Inhibits phosphorylation and degradation in mitosis but does not prevent homodimerization and three-way ER tubular junction formations; when associated with A-177; A-182; A-194; A-202; A-211; A-213; A-218; A-227 and A-231. 1 Publication1
Mutagenesisi182S → A: Inhibits phosphorylation and degradation in mitosis and prevents homodimerization and three-way ER tubular junction formations; when associated with A-177; A-179; A-194; A-202; A-211; A-213; A-218; A-227 and A-231. 1 Publication1
Mutagenesisi182S → D: Inhibits phosphorylation and degradation in mitosis but does not prevent homodimerization and three-way ER tubular junction formations; when associated with A-177; A-179; A-194; A-202; A-211; A-213; A-218; A-227 and A-231. 1 Publication1
Mutagenesisi194S → A: Inhibits phosphorylation and degradation in mitosis and prevents homodimerization and three-way ER tubular junction formations; when associated with A-177; A-179; A-182; A-202; A-211; A-213; A-218; A-227 and A-231. 1 Publication1
Mutagenesisi194S → D: Inhibits phosphorylation and degradation in mitosis but does not prevent homodimerization and three-way ER tubular junction formations; when associated with A-177; A-179; A-182; A-202; A-211; A-213; A-218; A-227 and A-231. 1 Publication1
Mutagenesisi202S → A: Inhibits phosphorylation and degradation in mitosis and prevents homodimerization and three-way ER tubular junction formations; when associated with A-177; A-179; A-182; A-194; A-211; A-213; A-218; A-227 and A-231. 1 Publication1
Mutagenesisi202S → D: Inhibits phosphorylation and degradation in mitosis but does not prevent homodimerization and three-way ER tubular junction formations; when associated with A-177; A-179; A-182; A-194; A-211; A-213; A-218; A-227 and A-231. 1 Publication1
Mutagenesisi211T → A: Inhibits phosphorylation and degradation in mitosis and prevents homodimerization and three-way ER tubular junction formations; when associated with A-177; A-179; A-182; A-194; A-202; A-213; A-218; A-227 and A-231. 1 Publication1
Mutagenesisi211T → D: Inhibits phosphorylation and degradation in mitosis but does not prevent homodimerization and three-way ER tubular junction formations; when associated with A-177; A-179; A-182; A-194; A-202; A-213; A-218; A-227 and A-231. 1 Publication1
Mutagenesisi213T → A: Inhibits phosphorylation and degradation in mitosis and prevents homodimerization and three-way ER tubular junction formations; when associated with A-177; A-179; A-182; A-194; A-202; A-211; A-218; A-227 and A-231. 1 Publication1
Mutagenesisi213T → D: Inhibits phosphorylation and degradation in mitosis but does not prevent homodimerization and three-way ER tubular junction formations; when associated with A-177; A-179; A-182; A-194; A-202; A-211; A-218; A-227 and A-231. 1 Publication1
Mutagenesisi218S → A: Inhibits phosphorylation and degradation in mitosis and prevents homodimerization and three-way ER tubular junction formations; when associated with A-177; A-179; A-182; A-194; A-202; A-211; A-213; A-227 and A-231. 1 Publication1
Mutagenesisi218S → D: Inhibits phosphorylation and degradation in mitosis but does not prevent homodimerization and three-way ER tubular junction formations; when associated with A-177; A-179; A-182; A-194; A-202; A-211; A-213; A-227 and A-231. 1 Publication1
Mutagenesisi227S → A: Inhibits phosphorylation and degradation in mitosis and prevents homodimerization and three-way ER tubular junction formations; when associated with A-177; A-179; A-182; A-194; A-202; A-211; A-213; A-218 and A-231. 1 Publication1
Mutagenesisi227S → D: Inhibits phosphorylation and degradation in mitosis but does not prevent homodimerization and three-way ER tubular junction formations; when associated with A-177; A-179; A-182; A-194; A-202; A-211; A-213; A-218 and A-231. 1 Publication1
Mutagenesisi231S → A: Inhibits phosphorylation and degradation in mitosis and prevents homodimerization and three-way ER tubular junction formations; when associated with A-177; A-179; A-182; A-194; A-202; A-211; A-213; A-218 and A-227. 1 Publication1
Mutagenesisi231S → D: Inhibits phosphorylation and degradation in mitosis but does not prevent homodimerization and three-way ER tubular junction formations; when associated with A-177; A-179; A-182; A-194; A-202; A-211; A-213; A-218 and A-227. 1 Publication1
Mutagenesisi276 – 301CQQCF…RCAYC → AQQAFSHNGMALKEEFEYIA FRAAYA: No change in N-myristoylation. Inhibits three-way ER tubular junction formation. 1 PublicationAdd BLAST26

Organism-specific databases

DisGeNETi80856.
OpenTargetsiENSG00000144320.
PharmGKBiPA134938939.

Polymorphism and mutation databases

BioMutaiLNP.
DMDMi114149979.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemoved2 Publications
ChainiPRO_00002483102 – 428Endoplasmic reticulum junction formation protein lunaparkAdd BLAST427

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Lipidationi2N-myristoyl glycine2 Publications1
Modified residuei114Phosphoserine1 Publication1
Modified residuei153Phosphoserine1 Publication1
Modified residuei177PhosphoserineCombined sources1 Publication1
Modified residuei182PhosphoserineCombined sources1 Publication1
Modified residuei194PhosphoserineCombined sources1 Publication1
Modified residuei211Phosphothreonine1 Publication1
Modified residuei213PhosphothreonineCombined sources1
Modified residuei217PhosphoserineCombined sources1 Publication1
Modified residuei227Phosphoserine1 Publication1
Modified residuei321PhosphoserineCombined sources1 Publication1
Modified residuei353Phosphoserine1 Publication1
Modified residuei384PhosphoserineCombined sources1 Publication1

Post-translational modificationi

Myristoylated; myristoylation is necessary for the endoplasmic reticulum (ER) three-way ER tubular junction formation, but is not required neither for membrane translocation, membrane topology formation, nor for the specific localization to ER membranes (PubMed:24223779).1 Publication
Phosphorylated. Phosphorylation occurs at Ser-177, Ser-182, Ser-217, Ser-227, Ser-321 and Ser-384 during interphase (PubMed:27619977). Phosphorylation occurs at Ser-114, Ser-153, Ser-194, Thr-211 and Ser-353 during mitosis; these phosphorylations reduce both its homodimerization and the ER three-way tubular junction formation (PubMed:27619977).1 Publication
Subject to proteasomal degradation following phosphorylation during mitosis (PubMed:27619977).1 Publication

Keywords - PTMi

Lipoprotein, Myristate, Phosphoprotein

Proteomic databases

EPDiQ9C0E8.
MaxQBiQ9C0E8.
PaxDbiQ9C0E8.
PeptideAtlasiQ9C0E8.
PRIDEiQ9C0E8.

PTM databases

iPTMnetiQ9C0E8.
PhosphoSitePlusiQ9C0E8.

Miscellaneous databases

PMAP-CutDBiQ9C0E8.

Expressioni

Gene expression databases

BgeeiENSG00000144320.
CleanExiHS_KIAA1715.
ExpressionAtlasiQ9C0E8. baseline and differential.
GenevisibleiQ9C0E8. HS.

Organism-specific databases

HPAiHPA014205.

Interactioni

Subunit structurei

Homodimer; homodimerization requires the C4-type zinc finger motif and decreases during mitosis in a phosphorylation-dependent manner (PubMed:27619977).1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
KLHL12Q53G594EBI-11024283,EBI-740929

GO - Molecular functioni

  • identical protein binding Source: UniProtKB

Protein-protein interaction databases

BioGridi123333. 39 interactors.
ELMiQ9C0E8.
IntActiQ9C0E8. 19 interactors.
STRINGi9606.ENSP00000272748.

Structurei

3D structure databases

ProteinModelPortaliQ9C0E8.
SMRiQ9C0E8.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Coiled coil

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Coiled coili16 – 41Sequence analysisAdd BLAST26
Coiled coili102 – 128Sequence analysisAdd BLAST27

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi178 – 250Pro-richAdd BLAST73

Domaini

The transmembrane domain 1 and 2 function as a signal-anchor and stop-transfer sequence, respectively, generating a double-spanning integral membrane protein with a N- and C-terminal cytoplasmic orientation (PubMed:24223779). Transmembrane domain 1 and 2 are probably sufficient to mediate membrane translocation and topology formation in a N-myristoylation-independent manner (PubMed:24223779). Transmembrane domain 2 is sufficient to block the protein secretion pathway (PubMed:24223779). The two coiled-coil domains are necessary for its endoplasmic reticulum (ER) three-way tubular junction localization (PubMed:27619977). The C4-type zinc finger motif is necessary both for its ER three-way tubular junction localization and formation (PubMed:24223779, PubMed:27619977).2 Publications

Sequence similaritiesi

Belongs to the lunapark family.Curated

Zinc finger

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Zinc fingeri276 – 301C4-type; plays a role in ER morphology2 PublicationsAdd BLAST26

Keywords - Domaini

Coiled coil, Transmembrane, Transmembrane helix, Zinc-finger

Phylogenomic databases

eggNOGiKOG2846. Eukaryota.
ENOG4111I2R. LUCA.
GeneTreeiENSGT00390000001859.
HOGENOMiHOG000231891.
HOVERGENiHBG079498.
InParanoidiQ9C0E8.
OMAiKECEPPS.
OrthoDBiEOG091G0IRW.
PhylomeDBiQ9C0E8.
TreeFamiTF315086.

Family and domain databases

InterProiView protein in InterPro
IPR019273. Lunapark_dom.
PfamiView protein in Pfam
PF10058. zinc_ribbon_10. 1 hit.

Sequences (4)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 4 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q9C0E8-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MGGLFSRWRT KPSTVEVLES IDKEIQALEE FREKNQRLQK LWVGRLILYS
60 70 80 90 100
SVLYLFTCLI VYLWYLPDEF TARLAMTLPF FAFPLIIWSI RTVIIFFFSK
110 120 130 140 150
RTERNNEALD DLKSQRKKIL EEVMEKETYK TAKLILERFD PDSKKAKECE
160 170 180 190 200
PPSAGAAVTA RPGQEIRQRT AAQRNLSPTP ASPNQGPPPQ VPVSPGPPKD
210 220 230 240 250
SSAPGGPPER TVTPALSSNV LPRHLGSPAT SVPGMGLHPP GPPLARPILP
260 270 280 290 300
RERGALDRIV EYLVGDGPQN RYALICQQCF SHNGMALKEE FEYIAFRCAY
310 320 330 340 350
CFFLNPARKT RPQAPRLPEF SFEKRQVVEG SSSVGPLPSG SVLSSDNQFN
360 370 380 390 400
EESLEHDVLD DNTEQTDDKI PATEQTNQVI EKASDSEEPE EKQETENEEA
410 420
SVIETNSTVP GADSIPDPEL SGESLTAE
Length:428
Mass (Da):47,740
Last modified:September 5, 2006 - v2
Checksum:iF5BBA4186C2691BF
GO
Isoform 2 (identifier: Q9C0E8-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-9: MGGLFSRWR → MEGK

Note: No experimental confirmation available.
Show »
Length:423
Mass (Da):47,094
Checksum:iCAF46E3EB956B8BC
GO
Isoform 3 (identifier: Q9C0E8-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-123: Missing.

Note: No experimental confirmation available.
Show »
Length:305
Mass (Da):33,001
Checksum:i2FDFED2CFE7C83EC
GO
Isoform 4 (identifier: Q9C0E8-4) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     235-235: M → MEMGLPHIAQAGLEHLSSSDLSTSTSQSAGIT

Note: No experimental confirmation available.
Show »
Length:459
Mass (Da):50,848
Checksum:i367198608E69DDF1
GO

Sequence cautioni

The sequence BAB21806 differs from that shown. Reason: Erroneous initiation.Curated

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti262Y → H in BAB71207 (PubMed:14702039).Curated1
Sequence conflicti374E → G in AAH31530 (PubMed:15489334).Curated1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_0202381 – 123Missing in isoform 3. 1 PublicationAdd BLAST123
Alternative sequenceiVSP_0202391 – 9MGGLFSRWR → MEGK in isoform 2. 1 Publication9
Alternative sequenceiVSP_054427235M → MEMGLPHIAQAGLEHLSSSD LSTSTSQSAGIT in isoform 4. 1 Publication1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB051502 mRNA. Translation: BAB21806.1. Different initiation.
AK056532 mRNA. Translation: BAB71207.1.
AC016751 Genomic DNA. No translation available.
AC016915 Genomic DNA. No translation available.
BC031530 mRNA. Translation: AAH31530.1.
BC105132 mRNA. Translation: AAI05133.1.
BC105134 mRNA. Translation: AAI05135.1.
BC110329 mRNA. Translation: AAI10330.1.
BC143681 mRNA. Translation: AAI43682.1.
AL832947 mRNA. Translation: CAH56306.1.
CCDSiCCDS33332.1. [Q9C0E8-1]
CCDS77488.1. [Q9C0E8-3]
CCDS77489.1. [Q9C0E8-4]
RefSeqiNP_001291937.1. NM_001305008.1.
NP_001291938.1. NM_001305009.1. [Q9C0E8-4]
NP_001291940.1. NM_001305011.1. [Q9C0E8-3]
NP_085153.1. NM_030650.2. [Q9C0E8-1]
XP_006712846.1. XM_006712783.2. [Q9C0E8-1]
XP_016860544.1. XM_017005055.1. [Q9C0E8-3]
UniGeneiHs.209561.

Genome annotation databases

EnsembliENST00000272748; ENSP00000272748; ENSG00000144320. [Q9C0E8-1]
ENST00000409660; ENSP00000386237; ENSG00000144320. [Q9C0E8-3]
ENST00000544803; ENSP00000440905; ENSG00000144320. [Q9C0E8-4]
GeneIDi80856.
KEGGihsa:80856.
UCSCiuc002ukc.2. human. [Q9C0E8-1]

Keywords - Coding sequence diversityi

Alternative splicing

Similar proteinsi

Entry informationi

Entry nameiLNP_HUMAN
AccessioniPrimary (citable) accession number: Q9C0E8
Secondary accession number(s): B7ZLA8
, Q2M2V8, Q2YD99, Q658W8, Q8N5V9, Q96MS5
Entry historyiIntegrated into UniProtKB/Swiss-Prot: September 5, 2006
Last sequence update: September 5, 2006
Last modified: November 22, 2017
This is version 118 of the entry and version 2 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Human chromosome 2
    Human chromosome 2: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. SIMILARITY comments
    Index of protein domains and families