PALM_RAT
ID PALM_RAT Reviewed; 383 AA.
AC Q920Q0;
DT 27-JUL-2011, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 112.
DE RecName: Full=Paralemmin-1;
DE AltName: Full=Paralemmin;
DE Flags: Precursor;
GN Name=Palm;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Kumanogoh H., Maekawa S.;
RT "Characterization of synaptic membrane proteins of rat brain.";
RL Submitted (MAR-2001) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Brown Norway;
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Lung;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4]
RP TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RX PubMed=16386234; DOI=10.1016/j.abb.2005.10.027;
RA Basile M., Lin R., Kabbani N., Karpa K., Kilimann M., Simpson I.,
RA Kester M.;
RT "Paralemmin interacts with D3 dopamine receptors: implications for membrane
RT localization and cAMP signaling.";
RL Arch. Biochem. Biophys. 446:60-68(2006).
RN [5]
RP SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=16847661; DOI=10.1007/s00418-006-0209-y;
RA Kutzleb C., Petrasch-Parwez E., Kilimann M.W.;
RT "Cellular and subcellular localization of paralemmin-1, a protein involved
RT in cell shape control, in the rat brain, adrenal gland and kidney.";
RL Histochem. Cell Biol. 127:13-30(2007).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-116; SER-122; THR-141;
RP THR-145; SER-157; SER-244 AND SER-345, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
CC -!- FUNCTION: Involved in plasma membrane dynamics and cell process
CC formation. Necessary for axonal and dendritic filopodia induction, for
CC dendritic spine maturation and synapse formation in a palmitoylation-
CC dependent manner (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Interacts with dopamine receptor DRD3. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:16847661};
CC Lipid-anchor {ECO:0000269|PubMed:16847661}; Cytoplasmic side
CC {ECO:0000269|PubMed:16847661}. Cell projection, filopodium membrane
CC {ECO:0000250}; Lipid-anchor {ECO:0000250}. Cell projection, axon
CC {ECO:0000269|PubMed:16847661}. Cell projection, dendrite
CC {ECO:0000269|PubMed:16847661}. Cell projection, dendritic spine
CC {ECO:0000269|PubMed:16847661}. Basolateral cell membrane
CC {ECO:0000269|PubMed:16847661}; Lipid-anchor
CC {ECO:0000269|PubMed:16847661}. Apicolateral cell membrane
CC {ECO:0000269|PubMed:16847661}; Lipid-anchor
CC {ECO:0000269|PubMed:16847661}. Note=Translocation to the plasma
CC membrane is enhanced upon stimulation of neuronal activity.
CC {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Expressed in neurons cells of neuropil-rich areas
CC of the brain, in the Purkinje cells of the cerebellum, in cells of the
CC cerebral cortex, hippocampus, brainstem nuclei and glial processes and
CC sheaths. Expressed in the medulla of the adrenal chromaffin cells and
CC renal duct cells (at protein level). {ECO:0000269|PubMed:16386234,
CC ECO:0000269|PubMed:16847661}.
CC -!- DEVELOPMENTAL STAGE: Expressed in pyramidal neurons of the hippocampus
CC at 18 dpc. {ECO:0000269|PubMed:16386234}.
CC -!- SIMILARITY: Belongs to the paralemmin family. {ECO:0000305}.
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DR EMBL; AB058889; BAB68565.1; -; mRNA.
DR EMBL; CH474029; EDL89390.1; -; Genomic_DNA.
DR EMBL; BC072525; AAH72525.1; -; mRNA.
DR RefSeq; NP_570842.1; NM_130829.1.
DR AlphaFoldDB; Q920Q0; -.
DR SMR; Q920Q0; -.
DR BioGRID; 250977; 1.
DR STRING; 10116.ENSRNOP00000013762; -.
DR iPTMnet; Q920Q0; -.
DR PhosphoSitePlus; Q920Q0; -.
DR jPOST; Q920Q0; -.
DR PaxDb; Q920Q0; -.
DR PRIDE; Q920Q0; -.
DR Ensembl; ENSRNOT00000013762; ENSRNOP00000013762; ENSRNOG00000009760.
DR GeneID; 170673; -.
DR KEGG; rno:170673; -.
DR UCSC; RGD:620341; rat.
DR CTD; 5064; -.
DR RGD; 620341; Palm.
DR eggNOG; ENOG502QQ2W; Eukaryota.
DR GeneTree; ENSGT00940000160580; -.
DR HOGENOM; CLU_038333_2_0_1; -.
DR InParanoid; Q920Q0; -.
DR OMA; VDGSTMM; -.
DR OrthoDB; 944013at2759; -.
DR PhylomeDB; Q920Q0; -.
DR TreeFam; TF105402; -.
DR PRO; PR:Q920Q0; -.
DR Proteomes; UP000002494; Chromosome 7.
DR Proteomes; UP000234681; Chromosome 7.
DR Bgee; ENSRNOG00000009760; Expressed in frontal cortex and 19 other tissues.
DR Genevisible; Q920Q0; RN.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0016327; C:apicolateral plasma membrane; IDA:UniProtKB.
DR GO; GO:0030424; C:axon; IDA:UniProtKB.
DR GO; GO:0016323; C:basolateral plasma membrane; IDA:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; ISO:RGD.
DR GO; GO:0009898; C:cytoplasmic side of plasma membrane; TAS:RGD.
DR GO; GO:0032590; C:dendrite membrane; IDA:UniProtKB.
DR GO; GO:0032591; C:dendritic spine membrane; IDA:UniProtKB.
DR GO; GO:0030175; C:filopodium; ISO:RGD.
DR GO; GO:0031527; C:filopodium membrane; ISO:RGD.
DR GO; GO:0044309; C:neuron spine; ISO:RGD.
DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR GO; GO:0014069; C:postsynaptic density; ISO:RGD.
DR GO; GO:0031750; F:D3 dopamine receptor binding; ISO:RGD.
DR GO; GO:0007193; P:adenylate cyclase-inhibiting G protein-coupled receptor signaling pathway; ISO:RGD.
DR GO; GO:0071257; P:cellular response to electrical stimulus; ISO:RGD.
DR GO; GO:0007010; P:cytoskeleton organization; ISO:RGD.
DR GO; GO:0007194; P:negative regulation of adenylate cyclase activity; ISO:RGD.
DR GO; GO:0060160; P:negative regulation of dopamine receptor signaling pathway; ISO:RGD.
DR GO; GO:0060999; P:positive regulation of dendritic spine development; ISO:RGD.
DR GO; GO:0051491; P:positive regulation of filopodium assembly; ISO:RGD.
DR GO; GO:0008104; P:protein localization; ISO:RGD.
DR GO; GO:0072659; P:protein localization to plasma membrane; ISO:RGD.
DR GO; GO:0008360; P:regulation of cell shape; ISO:RGD.
DR GO; GO:0060074; P:synapse maturation; ISO:RGD.
DR InterPro; IPR004965; Paralemmin.
DR Pfam; PF03285; Paralemmin; 1.
PE 1: Evidence at protein level;
KW Acetylation; Cell membrane; Cell projection; Cell shape; Coiled coil;
KW Lipoprotein; Membrane; Methylation; Palmitate; Phosphoprotein; Prenylation;
KW Reference proteome; Synapse.
FT CHAIN 1..380
FT /note="Paralemmin-1"
FT /id="PRO_0000411054"
FT PROPEP 381..383
FT /note="Removed in mature form"
FT /evidence="ECO:0000255"
FT /id="PRO_0000411055"
FT REGION 51..164
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 242..293
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 333..374
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 7..101
FT /evidence="ECO:0000255"
FT COMPBIAS 64..99
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 129..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:0007744|PubMed:22673903"
FT MOD_RES 122
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 124
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O75781"
FT MOD_RES 141
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 145
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 153
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9Z0P4"
FT MOD_RES 157
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 161
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O75781"
FT MOD_RES 242
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9Z0P4"
FT MOD_RES 244
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 345
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 361
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9Z0P4"
FT MOD_RES 362
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9Z0P4"
FT MOD_RES 363
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9Z0P4"
FT MOD_RES 365
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9Z0P4"
FT MOD_RES 367
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9Z0P4"
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"
SQ SEQUENCE 383 AA; 41927 MW; 8D3878AACD02F953 CRC64;
MEVLATDTVS QQERLQAIAE KRRKQAEIES KRRQLEDDRR QLQYLKSKAL RERWLLEGTP
SSASEGDEDM RKQMQEDEQK ARSLEESITR LEKEIDVLEF GESAPAAPKE NSAAPSPIRP
HSTSPAKEEQ KSETMVNAQQ TPLGTPKENR KSTPVRSPGG STMMKAAMYS VEITVEKDKV
TGETRVLSST TLLPRDPLPQ GVKVYEDETK VVHAVDGLSE NGIQPLSSSE VDELIHKADE
VTLSEAGSTT GPAEPRGLAE DVTRTTPSRR EITGVEAQPG EATSGPPGIQ PGQEPPVTMV
FMGYQNVEDE AETKKVLGLQ DTIKAELVVI EDSVTPREPA PLNGSAAELP ATKEENQTGP
TTTPSDTQDL DMKKPRCRCC SVM
