PALM_MOUSE
ID PALM_MOUSE Reviewed; 383 AA.
AC Q9Z0P4; Q9Z0P3;
DT 30-AUG-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 03-AUG-2022, entry version 142.
DE RecName: Full=Paralemmin-1;
DE AltName: Full=Paralemmin;
DE Flags: Precursor;
GN Name=Palm;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), SUBCELLULAR LOCATION, TISSUE
RP SPECIFICITY, DEVELOPMENTAL STAGE, AND PHOSPHORYLATION.
RC TISSUE=Brain;
RX PubMed=9813098; DOI=10.1083/jcb.143.3.795;
RA Kutzleb C., Sanders G., Yamamoto R., Wang X., Lichte B.,
RA Petrasch-Parwez E., Kilimann M.W.;
RT "Paralemmin, a prenyl-palmitoyl-anchored phosphoprotein abundant in neurons
RT and implicated in plasma membrane dynamics and cell process formation.";
RL J. Cell Biol. 143:795-813(1998).
RN [2]
RP PROTEIN SEQUENCE OF 94-109 AND 325-337, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RC STRAIN=OF1; TISSUE=Hippocampus;
RA Lubec G., Sunyer B., Chen W.-Q.;
RL Submitted (JAN-2009) to UniProtKB.
RN [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-141; THR-145 AND SER-345, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic brain;
RX PubMed=15345747; DOI=10.1074/mcp.m400085-mcp200;
RA Ballif B.A., Villen J., Beausoleil S.A., Schwartz D., Gygi S.P.;
RT "Phosphoproteomic analysis of the developing mouse brain.";
RL Mol. Cell. Proteomics 3:1093-1101(2004).
RN [4]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain cortex;
RX PubMed=17114649; DOI=10.1074/mcp.m600046-mcp200;
RA Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F.,
RA Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D., Gerrits B.,
RA Panse C., Schlapbach R., Mansuy I.M.;
RT "Qualitative and quantitative analyses of protein phosphorylation in naive
RT and stimulated mouse synaptosomal preparations.";
RL Mol. Cell. Proteomics 6:283-293(2007).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-141 AND THR-145, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT "Large-scale phosphorylation analysis of mouse liver.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN [6]
RP FUNCTION, MUTAGENESIS OF 377-CYS--CYS-380, MUTAGENESIS (ISOFORM 2), AND
RP SUBCELLULAR LOCATION.
RX PubMed=18287537; DOI=10.1091/mbc.e07-08-0802;
RA Arstikaitis P., Gauthier-Campbell C., Carolina Gutierrez Herrera R.,
RA Huang K., Levinson J.N., Murphy T.H., Kilimann M.W., Sala C., Colicos M.A.,
RA El-Husseini A.;
RT "Paralemmin-1, a modulator of filopodia induction is required for spine
RT maturation.";
RL Mol. Biol. Cell 19:2026-2038(2008).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-124; THR-141; THR-145;
RP THR-153; SER-157; SER-161; THR-242; SER-345; THR-361; THR-362; THR-363;
RP SER-365 AND THR-367, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Lung, Spleen, and
RC Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: Involved in plasma membrane dynamics and cell process
CC formation. Isoform 1 and isoform 2 are necessary for axonal and
CC dendritic filopodia induction, for dendritic spine maturation and
CC synapse formation in a palmitoylation-dependent manner.
CC {ECO:0000269|PubMed:18287537}.
CC -!- SUBUNIT: Interacts with dopamine receptor DRD3. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cell membrane; Lipid-anchor; Cytoplasmic side.
CC Cell projection, filopodium membrane; Lipid-anchor. Cell projection,
CC axon {ECO:0000250}. Cell projection, dendrite {ECO:0000250}. Cell
CC projection, dendritic spine. Basolateral cell membrane {ECO:0000250};
CC Lipid-anchor {ECO:0000250}. Apicolateral cell membrane {ECO:0000250};
CC Lipid-anchor {ECO:0000250}. Note=Translocation to the plasma membrane
CC is enhanced upon stimulation of neuronal activity. {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1; Synonyms=Paralemmin-L;
CC IsoId=Q9Z0P4-1; Sequence=Displayed;
CC Name=2; Synonyms=Paralemmin-S;
CC IsoId=Q9Z0P4-2; Sequence=VSP_003919;
CC -!- TISSUE SPECIFICITY: Expression is highest in brain, intermediate in
CC adrenal gland and kidney, and much lower or undetectable in other
CC tissues. Isoform 1 is the predominant isoform in most tissues except
CC brain and kidney where isoform 2 predominates.
CC {ECO:0000269|PubMed:9813098}.
CC -!- DEVELOPMENTAL STAGE: In brain, expression is highest in neonates and
CC declines to approximately 50% in adults. Isoform 2 is the predominant
CC isoform in neonates with isoform 1 being barely detectable at this
CC stage. Levels of isoform 1 increase with age, with the most pronounced
CC increase between postnatal days 10 and 20.
CC {ECO:0000269|PubMed:9813098}.
CC -!- MISCELLANEOUS: [Isoform 2]: Mutagenesis of Cys-333, Cys-335 and Cys-336
CC to Ser inhibit filopodia and spines induction and synapse maturation.
CC {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the paralemmin family. {ECO:0000305}.
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DR EMBL; Y14771; CAB37403.1; -; mRNA.
DR EMBL; Y14771; CAB37404.1; -; mRNA.
DR CCDS; CCDS23991.1; -. [Q9Z0P4-1]
DR CCDS; CCDS48621.1; -. [Q9Z0P4-2]
DR RefSeq; NP_001155219.1; NM_001161747.1. [Q9Z0P4-2]
DR RefSeq; NP_075617.3; NM_023128.4. [Q9Z0P4-1]
DR AlphaFoldDB; Q9Z0P4; -.
DR SMR; Q9Z0P4; -.
DR BioGRID; 202022; 10.
DR STRING; 10090.ENSMUSP00000040596; -.
DR iPTMnet; Q9Z0P4; -.
DR PhosphoSitePlus; Q9Z0P4; -.
DR SwissPalm; Q9Z0P4; -.
DR EPD; Q9Z0P4; -.
DR jPOST; Q9Z0P4; -.
DR MaxQB; Q9Z0P4; -.
DR PaxDb; Q9Z0P4; -.
DR PeptideAtlas; Q9Z0P4; -.
DR PRIDE; Q9Z0P4; -.
DR ProteomicsDB; 294324; -. [Q9Z0P4-1]
DR ProteomicsDB; 294325; -. [Q9Z0P4-2]
DR Antibodypedia; 22365; 97 antibodies from 20 providers.
DR Ensembl; ENSMUST00000046945; ENSMUSP00000040596; ENSMUSG00000035863. [Q9Z0P4-1]
DR Ensembl; ENSMUST00000105379; ENSMUSP00000101018; ENSMUSG00000035863. [Q9Z0P4-2]
DR GeneID; 18483; -.
DR KEGG; mmu:18483; -.
DR UCSC; uc007fzw.2; mouse. [Q9Z0P4-1]
DR CTD; 5064; -.
DR MGI; MGI:1261814; Palm.
DR VEuPathDB; HostDB:ENSMUSG00000035863; -.
DR eggNOG; ENOG502QQ2W; Eukaryota.
DR GeneTree; ENSGT00940000160580; -.
DR HOGENOM; CLU_038333_2_0_1; -.
DR InParanoid; Q9Z0P4; -.
DR OMA; VDGSTMM; -.
DR PhylomeDB; Q9Z0P4; -.
DR TreeFam; TF105402; -.
DR BioGRID-ORCS; 18483; 3 hits in 72 CRISPR screens.
DR ChiTaRS; Palm; mouse.
DR PRO; PR:Q9Z0P4; -.
DR Proteomes; UP000000589; Chromosome 10.
DR RNAct; Q9Z0P4; protein.
DR Bgee; ENSMUSG00000035863; Expressed in embryonic brain and 230 other tissues.
DR ExpressionAtlas; Q9Z0P4; baseline and differential.
DR Genevisible; Q9Z0P4; MM.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0016327; C:apicolateral plasma membrane; ISO:MGI.
DR GO; GO:0030424; C:axon; ISO:MGI.
DR GO; GO:0016323; C:basolateral plasma membrane; ISO:MGI.
DR GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR GO; GO:0032590; C:dendrite membrane; ISO:MGI.
DR GO; GO:0032591; C:dendritic spine membrane; ISO:MGI.
DR GO; GO:0030175; C:filopodium; IDA:UniProtKB.
DR GO; GO:0031527; C:filopodium membrane; ISO:MGI.
DR GO; GO:0044309; C:neuron spine; IDA:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR GO; GO:0014069; C:postsynaptic density; IDA:MGI.
DR GO; GO:0031750; F:D3 dopamine receptor binding; IPI:MGI.
DR GO; GO:0007193; P:adenylate cyclase-inhibiting G protein-coupled receptor signaling pathway; IDA:MGI.
DR GO; GO:0071257; P:cellular response to electrical stimulus; IDA:UniProtKB.
DR GO; GO:0007010; P:cytoskeleton organization; IDA:MGI.
DR GO; GO:0007194; P:negative regulation of adenylate cyclase activity; IDA:MGI.
DR GO; GO:0060160; P:negative regulation of dopamine receptor signaling pathway; ISO:MGI.
DR GO; GO:0060999; P:positive regulation of dendritic spine development; IDA:UniProtKB.
DR GO; GO:0051491; P:positive regulation of filopodium assembly; IDA:UniProtKB.
DR GO; GO:0008104; P:protein localization; IDA:MGI.
DR GO; GO:0072659; P:protein localization to plasma membrane; IDA:UniProtKB.
DR GO; GO:0008360; P:regulation of cell shape; IDA:MGI.
DR GO; GO:0060074; P:synapse maturation; IDA:UniProtKB.
DR InterPro; IPR004965; Paralemmin.
DR Pfam; PF03285; Paralemmin; 1.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; Cell membrane; Cell projection;
KW Cell shape; Coiled coil; Direct protein sequencing; Lipoprotein; Membrane;
KW Methylation; Palmitate; Phosphoprotein; Prenylation; Reference proteome;
KW Synapse.
FT CHAIN 1..380
FT /note="Paralemmin-1"
FT /id="PRO_0000058219"
FT PROPEP 381..383
FT /note="Removed in mature form"
FT /evidence="ECO:0000255"
FT /id="PRO_0000396690"
FT REGION 51..163
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 242..295
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 334..375
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 5..102
FT /evidence="ECO:0000255"
FT COMPBIAS 64..99
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 114..159
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 350..368
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000250|UniProtKB:O75781"
FT MOD_RES 116
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O75781"
FT MOD_RES 122
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q920Q0"
FT MOD_RES 124
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 141
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:15345747,
FT ECO:0007744|PubMed:17242355, ECO:0007744|PubMed:21183079"
FT MOD_RES 145
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:15345747,
FT ECO:0007744|PubMed:17242355, ECO:0007744|PubMed:21183079"
FT MOD_RES 153
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 157
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 161
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 242
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 244
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q920Q0"
FT MOD_RES 345
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:15345747,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 361
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 362
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 363
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 365
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 367
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 380
FT /note="Cysteine methyl ester"
FT /evidence="ECO:0000255"
FT LIPID 377
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000255"
FT LIPID 379
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000255"
FT LIPID 380
FT /note="S-farnesyl cysteine"
FT /evidence="ECO:0000255"
FT VAR_SEQ 167..210
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:9813098"
FT /id="VSP_003919"
FT MUTAGEN 377..380
FT /note="CRCC->SRSS: Inhibits axonal and dendritic filopodia
FT formation and reduces axonal and dendritic branching."
FT /evidence="ECO:0000269|PubMed:18287537"
SQ SEQUENCE 383 AA; 41614 MW; D63CAF5CFB1A70AB CRC64;
MEVLATDTAS QQERLQAIAE KRRKQAEIES KRRQLEDDRR QLQYLKSKAL RERWLLEGTP
SSASEGDEDM RKQMQEDEQK ARGLEESITR LEKEIDVLEF GESAPAASKE NSAAPSPGRP
QSASPAKEEQ KSETLVNAQQ TPLGTPKENR TSTPVRSPGG STMMKAAMYS VEITVEKDKV
TGETRVLSST TVLPRDPLPQ GVKVYEDETK VVHAVDGIAE NGIQPLSSSE VDELIHKADE
VTLSEAGSTA GPAEPRGLAE DVTRTTPSRR EITGVEAQPG EATSGPPGIQ PGQEPPVTMV
FMGYQNVEDE AETKKVLGLQ DTIKAELVVI EDAATPREPA PLNGSAAELP ATKEENQTGP
TTTPSDTQDL DMKKPRCRCC SVM
