PALM_HUMAN
ID PALM_HUMAN Reviewed; 387 AA.
AC O75781; O43359; O95673; Q92559; Q9UPJ4; Q9UQS2; Q9UQS3;
DT 30-AUG-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 2.
DT 03-AUG-2022, entry version 173.
DE RecName: Full=Paralemmin-1;
DE AltName: Full=Paralemmin;
DE Flags: Precursor;
GN Name=PALM; Synonyms=KIAA0270;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORMS 1 AND 2), AND VARIANT
RP ALA-107.
RC TISSUE=Blood;
RX PubMed=9615234; DOI=10.1006/geno.1998.5276;
RA Burwinkel B., Miglierini G., Jenne D.E., Gilbert D.J., Copeland N.G.,
RA Jenkins N.A., Ring H.Z., Francke U., Kilimann M.W.;
RT "Structure of the human paralemmin gene (PALM), mapping to human chromosome
RT 19p13.3 and mouse chromosome 10, and exclusion of coding mutations in
RT grizzled, mocha, jittery, and hesitant mice.";
RL Genomics 49:462-466(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2).
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15057824; DOI=10.1038/nature02399;
RA Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J., Lamerdin J.E.,
RA Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M., Aerts A.,
RA Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E., Caenepeel S.,
RA Carrano A.V., Caoile C., Chan Y.M., Christensen M., Cleland C.A.,
RA Copeland A., Dalin E., Dehal P., Denys M., Detter J.C., Escobar J.,
RA Flowers D., Fotopulos D., Garcia C., Georgescu A.M., Glavina T., Gomez M.,
RA Gonzales E., Groza M., Hammon N., Hawkins T., Haydu L., Ho I., Huang W.,
RA Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Larionov V.,
RA Leem S.-H., Lopez F., Lou Y., Lowry S., Malfatti S., Martinez D.,
RA McCready P.M., Medina C., Morgan J., Nelson K., Nolan M., Ovcharenko I.,
RA Pitluck S., Pollard M., Popkie A.P., Predki P., Quan G., Ramirez L.,
RA Rash S., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A.,
RA She X., Smith D., Slezak T., Solovyev V., Thayer N., Tice H., Tsai M.,
RA Ustaszewska A., Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J.,
RA Dubchak I., Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E.,
RA Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M.,
RA Rubin E.M., Lucas S.M.;
RT "The DNA sequence and biology of human chromosome 19.";
RL Nature 428:529-535(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Brain;
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 43-387 (ISOFORM 1).
RC TISSUE=Brain;
RX PubMed=9039502; DOI=10.1093/dnares/3.5.321;
RA Nagase T., Seki N., Ishikawa K., Ohira M., Kawarabayasi Y., Ohara O.,
RA Tanaka A., Kotani H., Miyajima N., Nomura N.;
RT "Prediction of the coding sequences of unidentified human genes. VI. The
RT coding sequences of 80 new genes (KIAA0201-KIAA0280) deduced by analysis of
RT cDNA clones from cell line KG-1 and brain.";
RL DNA Res. 3:321-329(1996).
RN [6]
RP FUNCTION, SUBCELLULAR LOCATION, AND MUTAGENESIS OF 381-CYS--CYS-383.
RX PubMed=14978216; DOI=10.1091/mbc.e03-07-0493;
RA Gauthier-Campbell C., Bredt D.S., Murphy T.H., El-Husseini A.;
RT "Regulation of dendritic branching and filopodia formation in hippocampal
RT neurons by specific acylated protein motifs.";
RL Mol. Biol. Cell 15:2205-2217(2004).
RN [7]
RP INTERACTION WITH DRD3.
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 [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-141; THR-145 AND SER-162, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-116; SER-124; THR-141 AND
RP THR-145, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [11]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22223895; DOI=10.1074/mcp.m111.015131;
RA Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T.,
RA Giglione C.;
RT "Comparative large-scale characterisation of plant vs. mammal proteins
RT reveals similar and idiosyncratic N-alpha acetylation features.";
RL Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
RN [12]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-116; SER-124; THR-141 AND
RP THR-145, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
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:14978216}.
CC -!- SUBUNIT: Interacts with dopamine receptor DRD3.
CC {ECO:0000269|PubMed:16386234}.
CC -!- INTERACTION:
CC O75781; G5E9A7: DMWD; NbExp=3; IntAct=EBI-6448827, EBI-10976677;
CC O75781; Q7Z699: SPRED1; NbExp=3; IntAct=EBI-6448827, EBI-5235340;
CC O75781-2; P28799: GRN; NbExp=3; IntAct=EBI-16399860, EBI-747754;
CC O75781-2; D3DTS7: PMP22; NbExp=3; IntAct=EBI-16399860, EBI-25882629;
CC O75781-2; P02766: TTR; NbExp=3; IntAct=EBI-16399860, EBI-711909;
CC O75781-2; O76024: WFS1; NbExp=3; IntAct=EBI-16399860, EBI-720609;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:14978216};
CC Lipid-anchor {ECO:0000269|PubMed:14978216}; Cytoplasmic side
CC {ECO:0000269|PubMed:14978216}. Cell projection, filopodium membrane
CC {ECO:0000269|PubMed:14978216}; Lipid-anchor
CC {ECO:0000269|PubMed:14978216}. Cell projection, axon {ECO:0000250}.
CC Cell projection, dendrite {ECO:0000250}. Cell projection, dendritic
CC spine {ECO:0000250}. Basolateral cell membrane {ECO:0000250}; Lipid-
CC anchor {ECO:0000250}. Apicolateral cell membrane {ECO:0000250}; Lipid-
CC anchor {ECO:0000250}. Note=Translocation to the plasma membrane is
CC enhanced upon stimulation of neuronal activity.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1; Synonyms=Paralemmin-L;
CC IsoId=O75781-1; Sequence=Displayed;
CC Name=2; Synonyms=Paralemmin-S;
CC IsoId=O75781-2; Sequence=VSP_003918;
CC -!- TISSUE SPECIFICITY: Widely expressed with highest expression in brain
CC and testis and intermediate expression in heart and adrenal gland.
CC -!- SIMILARITY: Belongs to the paralemmin family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; Y16270; CAA76151.1; -; Genomic_DNA.
DR EMBL; Y16271; CAA76151.1; JOINED; Genomic_DNA.
DR EMBL; Y16272; CAA76151.1; JOINED; Genomic_DNA.
DR EMBL; Y16273; CAA76151.1; JOINED; Genomic_DNA.
DR EMBL; Y16274; CAA76151.1; JOINED; Genomic_DNA.
DR EMBL; Y16275; CAA76151.1; JOINED; Genomic_DNA.
DR EMBL; Y16276; CAA76151.1; JOINED; Genomic_DNA.
DR EMBL; Y16277; CAA76151.1; JOINED; Genomic_DNA.
DR EMBL; Y16278; CAA76152.1; -; mRNA.
DR EMBL; Y14770; CAB37400.1; -; mRNA.
DR EMBL; Y14770; CAB37401.1; -; mRNA.
DR EMBL; BC032449; AAH32449.1; -; mRNA.
DR EMBL; AC004030; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC005763; AAC62429.1; -; Genomic_DNA.
DR EMBL; D87460; BAA13400.1; -; mRNA.
DR CCDS; CCDS32857.1; -. [O75781-1]
DR CCDS; CCDS32858.1; -. [O75781-2]
DR PIR; T00635; T00635.
DR RefSeq; NP_001035224.1; NM_001040134.1. [O75781-2]
DR RefSeq; NP_002570.2; NM_002579.2. [O75781-1]
DR AlphaFoldDB; O75781; -.
DR BioGRID; 111100; 91.
DR IntAct; O75781; 35.
DR MINT; O75781; -.
DR STRING; 9606.ENSP00000341911; -.
DR iPTMnet; O75781; -.
DR PhosphoSitePlus; O75781; -.
DR SwissPalm; O75781; -.
DR BioMuta; PALM; -.
DR EPD; O75781; -.
DR jPOST; O75781; -.
DR MassIVE; O75781; -.
DR MaxQB; O75781; -.
DR PaxDb; O75781; -.
DR PeptideAtlas; O75781; -.
DR PRIDE; O75781; -.
DR ProteomicsDB; 50191; -. [O75781-1]
DR ProteomicsDB; 50192; -. [O75781-2]
DR Antibodypedia; 22365; 97 antibodies from 20 providers.
DR DNASU; 5064; -.
DR Ensembl; ENST00000264560.11; ENSP00000264560.7; ENSG00000099864.18. [O75781-2]
DR Ensembl; ENST00000338448.10; ENSP00000341911.4; ENSG00000099864.18. [O75781-1]
DR GeneID; 5064; -.
DR KEGG; hsa:5064; -.
DR MANE-Select; ENST00000338448.10; ENSP00000341911.4; NM_002579.3; NP_002570.2.
DR UCSC; uc002lpm.2; human. [O75781-1]
DR CTD; 5064; -.
DR DisGeNET; 5064; -.
DR GeneCards; PALM; -.
DR HGNC; HGNC:8594; PALM.
DR HPA; ENSG00000099864; Tissue enhanced (brain).
DR MIM; 608134; gene.
DR neXtProt; NX_O75781; -.
DR OpenTargets; ENSG00000099864; -.
DR PharmGKB; PA32923; -.
DR VEuPathDB; HostDB:ENSG00000099864; -.
DR eggNOG; ENOG502QQ2W; Eukaryota.
DR GeneTree; ENSGT00940000160580; -.
DR HOGENOM; CLU_038333_2_0_1; -.
DR InParanoid; O75781; -.
DR OMA; VDGSTMM; -.
DR OrthoDB; 944013at2759; -.
DR PhylomeDB; O75781; -.
DR TreeFam; TF105402; -.
DR PathwayCommons; O75781; -.
DR SignaLink; O75781; -.
DR BioGRID-ORCS; 5064; 31 hits in 1078 CRISPR screens.
DR ChiTaRS; PALM; human.
DR GeneWiki; PALM; -.
DR GenomeRNAi; 5064; -.
DR Pharos; O75781; Tbio.
DR PRO; PR:O75781; -.
DR Proteomes; UP000005640; Chromosome 19.
DR RNAct; O75781; protein.
DR Bgee; ENSG00000099864; Expressed in amygdala and 149 other tissues.
DR ExpressionAtlas; O75781; baseline and differential.
DR Genevisible; O75781; HS.
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:0031410; C:cytoplasmic vesicle; TAS:ProtInc.
DR GO; GO:0043197; C:dendritic spine; IEA:UniProtKB-SubCell.
DR GO; GO:0031527; C:filopodium membrane; IDA:UniProtKB.
DR GO; GO:0031235; C:intrinsic component of the cytoplasmic side of the plasma membrane; TAS:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR GO; GO:0014069; C:postsynaptic density; IEA:Ensembl.
DR GO; GO:0031750; F:D3 dopamine receptor binding; IEA:Ensembl.
DR GO; GO:0007193; P:adenylate cyclase-inhibiting G protein-coupled receptor signaling pathway; IEA:Ensembl.
DR GO; GO:0071257; P:cellular response to electrical stimulus; IEA:Ensembl.
DR GO; GO:0007010; P:cytoskeleton organization; IEA:Ensembl.
DR GO; GO:0007194; P:negative regulation of adenylate cyclase activity; IBA:GO_Central.
DR GO; GO:0060160; P:negative regulation of dopamine receptor signaling pathway; IDA:UniProtKB.
DR GO; GO:0051491; P:positive regulation of filopodium assembly; IDA:UniProtKB.
DR GO; GO:0072659; P:protein localization to plasma membrane; IEA:Ensembl.
DR GO; GO:0008360; P:regulation of cell shape; IEA:UniProtKB-KW.
DR GO; GO:0060074; P:synapse maturation; IEA:Ensembl.
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; Lipoprotein; Membrane; Methylation; Palmitate;
KW Phosphoprotein; Prenylation; Reference proteome; Synapse.
FT CHAIN 1..384
FT /note="Paralemmin-1"
FT /id="PRO_0000058218"
FT PROPEP 385..387
FT /note="Removed in mature form"
FT /evidence="ECO:0000255"
FT /id="PRO_0000396689"
FT REGION 31..160
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 247..296
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 335..378
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 9..101
FT /evidence="ECO:0000255"
FT COMPBIAS 31..53
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 64..100
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 135..159
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0007744|PubMed:22223895,
FT ECO:0007744|PubMed:22814378"
FT MOD_RES 116
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 124
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 141
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163"
FT MOD_RES 145
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163"
FT MOD_RES 162
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 243
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9Z0P4"
FT MOD_RES 245
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 367
FT /note="Phosphothreonine"
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"
FT VAR_SEQ 168..211
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:9615234,
FT ECO:0000303|PubMed:9813098"
FT /id="VSP_003918"
FT VARIANT 107
FT /note="T -> A (in dbSNP:rs1050457)"
FT /evidence="ECO:0000269|PubMed:9615234"
FT /id="VAR_053803"
FT MUTAGEN 381..383
FT /note="CKC->SKS: Inhibits axonal and dendritic filopodia
FT formation and reduces axonal and dendritic branching."
FT /evidence="ECO:0000269|PubMed:14978216"
SQ SEQUENCE 387 AA; 42076 MW; 46D455D5D12C3135 CRC64;
MEVLAAETTS QQERLQAIAE KRKRQAEIEN KRRQLEDERR QLQHLKSKAL RERWLLEGTP
SSASEGDEDL RRQMQDDEQK TRLLEDSVSR LEKEIEVLER GDSAPATAKE NAAAPSPVRA
PAPSPAKEER KTEVVMNSQQ TPVGTPKDKR VSNTPLRTVD GSPMMKAAMY SVEITVEKDK
VTGETRVLSS TTLLPRQPLP LGIKVYEDET KVVHAVDGTA ENGIHPLSSS EVDELIHKAD
EVTLSEAGST AGAAETRGAV EGAARTTPSR REITGVQAQP GEATSGPPGI QPGQEPPVTM
IFMGYQNVED EAETKKVLGL QDTITAELVV IEDAAEPKEP APPNGSAAEP PTEAASREEN
QAGPEATTSD PQDLDMKKHR CKCCSIM
