Lipid Modification Database
Tag Content
LipidDB ID
LipidDB-10090-00008
Entry Name
UniProt Accession
Theoretical PI
4.79
Molecular Weight
41614.33
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
Paralemmin-1
Protein Synonyms/Alias
Paralemmin;
Gene Name
Palm
Gene Synonyms/Alias
Created Date
30-AUG-2002
 Lipid Modification Sites 
 Position   Sequence Form   Peptide   References   Modification Type 
379
Canonical
MKKPRCRCCSVM***
[1]
S-Palmitoylation
380
Canonical
KKPRCRCCSVM****
[1]
S-Palmitoylation
Organism
Mus musculus (Mouse)
NCBI Taxa ID
10090
Reference
[1] Predicted from GPS-Lipid
Functional Description
Involved in plasma membrane dynamics and cell process formation. Isoform 1 and isoform 2 are necessary for axonal and dendritic filopodia induction, for dendritic spine maturation and synapse formation in a palmitoylation-dependent manner.
Sequence Annotation
Modified residue: 1 1 N-acetylmethionine.
Modified residue: 116 116 Phosphoserine.
Modified residue: 124 124 Phosphoserine.
Modified residue: 141 141 Phosphothreonine.
Modified residue: 145 145 Phosphothreonine.
Modified residue: 161 161 Phosphoserine.
Modified residue: 345 345 Phosphoserine.
Modified residue: 380 380 Cysteine methyl ester.
Protein Length
383 AA.
Protein Sequence
(Canonical)
MEVLATDTAS QQERLQAIAE KRRKQAEIES KRRQLEDDRR QLQYLKSKAL RERWLLEGTP  60
SSASEGDEDM RKQMQEDEQK ARGLEESITR LEKEIDVLEF GESAPAASKE NSAAPSPGRP  120
QSASPAKEEQ KSETLVNAQQ TPLGTPKENR TSTPVRSPGG STMMKAAMYS VEITVEKDKV  180
TGETRVLSST TVLPRDPLPQ GVKVYEDETK VVHAVDGIAE NGIQPLSSSE VDELIHKADE  240
VTLSEAGSTA GPAEPRGLAE DVTRTTPSRR EITGVEAQPG EATSGPPGIQ PGQEPPVTMV  300
FMGYQNVEDE AETKKVLGLQ DTIKAELVVI EDAATPREPA PLNGSAAELP ATKEENQTGP  360
TTTPSDTQDL DMKKPRCRCC SVM                                          383
FASTA
(Canonical)
>LipidDB-10090-00008|Q9Z0P4
MEVLATDTASQQERLQAIAEKRRKQAEIESKRRQLEDDRRQLQYLKSKALRERWLLEGTP
SSASEGDEDMRKQMQEDEQKARGLEESITRLEKEIDVLEFGESAPAASKENSAAPSPGRP
QSASPAKEEQKSETLVNAQQTPLGTPKENRTSTPVRSPGGSTMMKAAMYSVEITVEKDKV
TGETRVLSSTTVLPRDPLPQGVKVYEDETKVVHAVDGIAENGIQPLSSSEVDELIHKADE
VTLSEAGSTAGPAEPRGLAEDVTRTTPSRREITGVEAQPGEATSGPPGIQPGQEPPVTMV
FMGYQNVEDEAETKKVLGLQDTIKAELVVIEDAATPREPAPLNGSAAELPATKEENQTGP
TTTPSDTQDLDMKKPRCRCCSVM
Gene Ontology
GO:0016327; C:apicolateral plasma membrane; IEA:Ensembl
GO:0030424; C:axon; IEA:Ensembl
GO:0016323; C:basolateral plasma membrane; IEA:Ensembl
GO:0005737; C:cytoplasm; IDA:MGI
GO:0032590; C:dendrite membrane; IEA:Ensembl
GO:0032591; C:dendritic spine membrane; IEA:Ensembl
GO:0030175; C:filopodium; IDA:UniProtKB
GO:0031527; C:filopodium membrane; IEA:Ensembl
GO:0044309; C:neuron spine; IDA:UniProtKB
GO:0005634; C:nucleus; IEA:Ensembl
GO:0005886; C:plasma membrane; IDA:UniProtKB
GO:0031750; F:D3 dopamine receptor binding; IPI:MGI
GO:0071257; P:cellular response to electrical stimulus; IDA:UniProtKB
GO:0007010; P:cytoskeleton organization; IDA:MGI
GO:0007194; P:negative regulation of adenylate cyclase activity; IDA:MGI
GO:0030818; P:negative regulation of cAMP biosynthetic process; IDA:MGI
GO:0060160; P:negative regulation of dopamine receptor signaling pathway; IEA:Ensembl
GO:0060999; P:positive regulation of dendritic spine development; IDA:UniProtKB
GO:0051491; P:positive regulation of filopodium assembly; IDA:UniProtKB
GO:0008104; P:protein localization; IDA:MGI
GO:0072661; P:protein targeting to plasma membrane; IDA:UniProtKB
GO:0008360; P:regulation of cell shape; IDA:MGI
GO:0060074; P:synapse maturation; IDA:UniProtKB
Interpro
InterPro; IPR004965; Paralemmin
Pfam
Pfam; PF03285; Paralemmin;
SMART
PROSITE
PRINTS