Lipid Modification Database
Tag Content
LipidDB ID
LipidDB-9606-00498
Entry Name
UniProt Accession
Theoretical PI
5.05
Molecular Weight
47739.92
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
Protein lunapark
Protein Synonyms/Alias
Gene Name
LNP
Gene Synonyms/Alias
KIAA1715;
Created Date
05-SEP-2006
 Lipid Modification Sites 
 Position   Sequence Form   Peptide   References   Modification Type 
2
Canonical
******MGGLFSRWR
[1][2]
N-Myristoylation
Organism
Homo sapiens (Human)
NCBI Taxa ID
9606
Reference
[1] Suzuki T, Moriya K, Nagatoshi K, Ota Y, Ezure T, Ando E, Tsunasawa S, UtsumiT. Strategy for comprehensive identification of human N-myristoylated proteinsusing an insect cell-free protein synthesis system. Proteomics. 2010May;10(9):1780-93. doi: 10.1002/pmic.200900783.[PMID:20213681]
[2] Moriya K, Nagatoshi K, Noriyasu Y, Okamura T, Takamitsu E, Suzuki T, Utsumi T.Protein N-myristoylation plays a critical role in the endoplasmic reticulummorphological change induced by overexpression of protein Lunapark, an integralmembrane protein of the endoplasmic reticulum. PLoS One. 2013 Nov 4;8(11):e78235.doi: 10.1371/journal.pone.0078235. eCollection 2013.[PMID:24223779]
Functional Description
Plays a role in tubular endoplasmic reticulum network formation and maintenance. May be involved in limb and central nervous system development.
Sequence Annotation
Topological domain: 2 45 Cytoplasmic.
Transmembrane: 46 66 Helical.
Topological domain: 67 77 Lumenal.
Transmembrane: 78 98 Helical.
Topological domain: 99 428 Cytoplasmic.
Modified residue: 177 177 Phosphoserine.
Modified residue: 182 182 Phosphoserine.
Modified residue: 194 194 Phosphoserine.
Modified residue: 321 321 Phosphoserine.
Modified residue: 414 414 Phosphoserine.
Protein Length
428 AA.
Protein Sequence
(Canonical)
MGGLFSRWRT KPSTVEVLES IDKEIQALEE FREKNQRLQK LWVGRLILYS SVLYLFTCLI  60
VYLWYLPDEF TARLAMTLPF FAFPLIIWSI RTVIIFFFSK RTERNNEALD DLKSQRKKIL  120
EEVMEKETYK TAKLILERFD PDSKKAKECE PPSAGAAVTA RPGQEIRQRT AAQRNLSPTP  180
ASPNQGPPPQ VPVSPGPPKD SSAPGGPPER TVTPALSSNV LPRHLGSPAT SVPGMGLHPP  240
GPPLARPILP RERGALDRIV EYLVGDGPQN RYALICQQCF SHNGMALKEE FEYIAFRCAY  300
CFFLNPARKT RPQAPRLPEF SFEKRQVVEG SSSVGPLPSG SVLSSDNQFN EESLEHDVLD  360
DNTEQTDDKI PATEQTNQVI EKASDSEEPE EKQETENEEA SVIETNSTVP GADSIPDPEL  420
SGESLTAE                                                           428
FASTA
(Canonical)
>LipidDB-9606-00498|Q9C0E8
MGGLFSRWRTKPSTVEVLESIDKEIQALEEFREKNQRLQKLWVGRLILYSSVLYLFTCLI
VYLWYLPDEFTARLAMTLPFFAFPLIIWSIRTVIIFFFSKRTERNNEALDDLKSQRKKIL
EEVMEKETYKTAKLILERFDPDSKKAKECEPPSAGAAVTARPGQEIRQRTAAQRNLSPTP
ASPNQGPPPQVPVSPGPPKDSSAPGGPPERTVTPALSSNVLPRHLGSPATSVPGMGLHPP
GPPLARPILPRERGALDRIVEYLVGDGPQNRYALICQQCFSHNGMALKEEFEYIAFRCAY
CFFLNPARKTRPQAPRLPEFSFEKRQVVEGSSSVGPLPSGSVLSSDNQFNEESLEHDVLD
DNTEQTDDKIPATEQTNQVIEKASDSEEPEEKQETENEEASVIETNSTVPGADSIPDPEL
SGESLTAE
Gene Ontology
GO:0005789; C:endoplasmic reticulum membrane; IDA:MGI
GO:0016021; C:integral component of membrane; NAS:UniProtKB
GO:0046872; F:metal ion binding; IEA:UniProtKB-KW
GO:0007596; P:blood coagulation; IEA:Ensembl
GO:0042733; P:embryonic digit morphogenesis; IEA:Ensembl
GO:0035115; P:embryonic forelimb morphogenesis; IEA:Ensembl
GO:0060173; P:limb development; NAS:UniProtKB
GO:0032330; P:regulation of chondrocyte differentiation; IEA:Ensembl
Interpro
InterPro; IPR019273; DUF2296
Pfam
Pfam; PF10058; DUF2296;
SMART
PROSITE
PRINTS