PALM_PIG
ID PALM_PIG Reviewed; 387 AA.
AC Q2MJV8;
DT 28-NOV-2006, integrated into UniProtKB/Swiss-Prot.
DT 07-FEB-2006, sequence version 1.
DT 03-AUG-2022, entry version 64.
DE RecName: Full=Paralemmin-1;
DE AltName: Full=Paralemmin;
DE Flags: Precursor;
GN Name=PALM;
OS Sus scrofa (Pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX NCBI_TaxID=9823;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Brain;
RA Neumann N.G., Kilimann M.W.;
RL Submitted (DEC-2005) to the EMBL/GenBank/DDBJ databases.
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; Lipid-anchor; Cytoplasmic side.
CC Cell projection, filopodium membrane; Lipid-anchor. Cell projection,
CC axon {ECO:0000250}. Cell projection, dendrite. Cell projection,
CC dendritic spine. Basolateral cell membrane {ECO:0000250}; Lipid-anchor
CC {ECO:0000250}. Apicolateral cell membrane {ECO:0000250}; Lipid-anchor
CC {ECO:0000250}. Note=Translocation to the plasma membrane is enhanced
CC upon stimulation of neuronal activity. {ECO:0000250}.
CC -!- PTM: Phosphorylated. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the paralemmin family. {ECO:0000305}.
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DR EMBL; DQ322459; ABC50000.1; -; mRNA.
DR RefSeq; NP_001033725.1; NM_001038636.1.
DR AlphaFoldDB; Q2MJV8; -.
DR SMR; Q2MJV8; -.
DR STRING; 9823.ENSSSCP00000014273; -.
DR PaxDb; Q2MJV8; -.
DR PeptideAtlas; Q2MJV8; -.
DR GeneID; 654410; -.
DR KEGG; ssc:654410; -.
DR CTD; 5064; -.
DR eggNOG; ENOG502QQ2W; Eukaryota.
DR InParanoid; Q2MJV8; -.
DR OrthoDB; 944013at2759; -.
DR Proteomes; UP000008227; Unplaced.
DR Proteomes; UP000314985; Unplaced.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0016327; C:apicolateral plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0030424; C:axon; IEA:UniProtKB-SubCell.
DR GO; GO:0016323; C:basolateral plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0043197; C:dendritic spine; IEA:UniProtKB-SubCell.
DR GO; GO:0031527; C:filopodium membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0008360; P:regulation of cell shape; IEA:UniProtKB-KW.
DR InterPro; IPR004965; Paralemmin.
DR Pfam; PF03285; Paralemmin; 1.
PE 2: Evidence at transcript 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..384
FT /note="Paralemmin-1"
FT /id="PRO_0000262526"
FT PROPEP 385..387
FT /note="Removed in mature form"
FT /evidence="ECO:0000255"
FT /id="PRO_0000396691"
FT REGION 22..78
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 98..133
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 246..297
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 334..378
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 7..104
FT /evidence="ECO:0000255"
FT COMPBIAS 22..53
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 64..78
FT /note="Basic and acidic 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 142
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:O75781"
FT MOD_RES 146
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:O75781"
FT MOD_RES 163
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O75781"
FT MOD_RES 244
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9Z0P4"
FT MOD_RES 246
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q920Q0"
FT MOD_RES 346
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9Z0P4"
FT MOD_RES 369
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9Z0P4"
FT MOD_RES 384
FT /note="Cysteine methyl ester"
FT /evidence="ECO:0000255"
FT LIPID 381
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000255"
FT LIPID 383
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000255"
FT LIPID 384
FT /note="S-farnesyl cysteine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 387 AA; 42380 MW; 35169D1173980A67 CRC64;
MEVLAAETIS QQERLQAIAE KRRRQAEVEN RRRQLEDDRR QLQHLKSKAL RERWLLEGTP
SSASEGDEDM RKQMQEDEQK ARLLEESIAR LEKEIEELEN ADTLPAPVKE TQVAPSPGPV
VPAPCPAQED RKAEVDLNAQ QTPVGTPKEK RISNTPMRMV EGSTMMNAAM YSVEITVEKD
KVTGETRVLS SATVLPREHP PQGIKVYEDE TKVVHAVDGT AENGIHPLSS SEVDELIHKA
DEVTLSEAGS AAAPETRGPS EEVVRTTPSR REITGVQAQP GEATSGPPGI QPGQEPPVTM
IFMGYQNVED EAETQKVLGL QDTITAELVV IEDAAEPKEP APPNGSAAEP LATEGSREEN
QVGPEAPASD PQDLDMKKQR CKCCSIM
