PALM_CHICK
ID PALM_CHICK Reviewed; 386 AA.
AC Q9YGL6; Q9YGL4; Q9YGL5;
DT 30-AUG-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 03-AUG-2022, entry version 105.
DE RecName: Full=Paralemmin-1;
DE AltName: Full=Paralemmin;
DE Flags: Precursor;
GN Name=PALM;
OS Gallus gallus (Chicken).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Phasianinae; Gallus.
OX NCBI_TaxID=9031;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2 AND 3), SUBCELLULAR LOCATION, AND
RP TISSUE SPECIFICITY.
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 SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RX PubMed=12874826; DOI=10.1002/jcb.10574;
RA Bagchi M., Katar M., Lo W.K., Maisel H.;
RT "Paralemmin of the lens.";
RL J. Cell. Biochem. 89:917-921(2003).
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 (By similarity).
CC {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 {ECO:0000250}; Lipid-anchor
CC {ECO:0000250}. Cell projection, axon {ECO:0000250}. Cell projection,
CC dendrite {ECO:0000250}. Cell projection, dendritic spine {ECO:0000250}.
CC Basolateral cell membrane {ECO:0000250}; Lipid-anchor {ECO:0000250}.
CC Apicolateral cell membrane {ECO:0000250}; Lipid-anchor {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q9YGL6-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9YGL6-2; Sequence=VSP_003920;
CC Name=3;
CC IsoId=Q9YGL6-3; Sequence=VSP_003921;
CC -!- TISSUE SPECIFICITY: Expressed in the lens (at protein level). Highly
CC expressed in forebrain and cerebellum with lower expression in adrenal
CC gland and heart. Expression weak or undetectable in other tissues.
CC {ECO:0000269|PubMed:12874826, ECO:0000269|PubMed:9813098}.
CC -!- PTM: Phosphorylated. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the paralemmin family. {ECO:0000305}.
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DR EMBL; Y14769; CAB37358.1; -; mRNA.
DR EMBL; Y14769; CAB37359.1; -; mRNA.
DR EMBL; Y14769; CAB37360.1; -; mRNA.
DR AlphaFoldDB; Q9YGL6; -.
DR SMR; Q9YGL6; -.
DR STRING; 9031.ENSGALP00000002858; -.
DR PaxDb; Q9YGL6; -.
DR VEuPathDB; HostDB:geneid_101750199; -.
DR eggNOG; ENOG502QQ2W; Eukaryota.
DR InParanoid; Q9YGL6; -.
DR PhylomeDB; Q9YGL6; -.
DR Proteomes; UP000000539; 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:0005737; C:cytoplasm; ISS:AgBase.
DR GO; GO:0043197; C:dendritic spine; IEA:UniProtKB-SubCell.
DR GO; GO:0030175; C:filopodium; ISS:AgBase.
DR GO; GO:0031527; C:filopodium membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005622; C:intracellular anatomical structure; IDA:AgBase.
DR GO; GO:0044306; C:neuron projection terminus; IDA:AgBase.
DR GO; GO:0044309; C:neuron spine; ISS:AgBase.
DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR GO; GO:0014069; C:postsynaptic density; ISS:AgBase.
DR GO; GO:0097060; C:synaptic membrane; IDA:AgBase.
DR GO; GO:0031750; F:D3 dopamine receptor binding; ISS:AgBase.
DR GO; GO:0071257; P:cellular response to electrical stimulus; ISS:AgBase.
DR GO; GO:0007010; P:cytoskeleton organization; ISS:AgBase.
DR GO; GO:0007194; P:negative regulation of adenylate cyclase activity; ISS:AgBase.
DR GO; GO:0060999; P:positive regulation of dendritic spine development; ISS:AgBase.
DR GO; GO:0051491; P:positive regulation of filopodium assembly; ISS:AgBase.
DR GO; GO:0008104; P:protein localization; ISS:AgBase.
DR GO; GO:0072659; P:protein localization to plasma membrane; ISS:AgBase.
DR GO; GO:0008360; P:regulation of cell shape; ISS:AgBase.
DR GO; GO:0060074; P:synapse maturation; ISS:AgBase.
DR InterPro; IPR004965; Paralemmin.
DR Pfam; PF03285; Paralemmin; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cell membrane; Cell projection; Cell shape;
KW Coiled coil; Lipoprotein; Membrane; Methylation; Palmitate; Phosphoprotein;
KW Prenylation; Reference proteome; Synapse.
FT CHAIN 1..383
FT /note="Paralemmin-1"
FT /id="PRO_0000058217"
FT PROPEP 384..386
FT /note="Removed in mature form"
FT /evidence="ECO:0000255"
FT /id="PRO_0000396692"
FT REGION 21..40
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 51..149
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 240..290
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 321..378
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 4..115
FT /evidence="ECO:0000255"
FT COMPBIAS 63..96
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 246..261
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 383
FT /note="Cysteine methyl ester"
FT /evidence="ECO:0000255"
FT LIPID 380
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000255"
FT LIPID 382
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000255"
FT LIPID 383
FT /note="S-farnesyl cysteine"
FT /evidence="ECO:0000255"
FT VAR_SEQ 138..202
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:9813098"
FT /id="VSP_003920"
FT VAR_SEQ 159..202
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:9813098"
FT /id="VSP_003921"
SQ SEQUENCE 386 AA; 42125 MW; 137ACF03C387DBF2 CRC64;
MEAVEANTLQ QERLQAIAEK RKRQTEIENK RRQLEDDRRQ LQHLKSKALR ERWLLEGAPS
SASEEDEAMK KQMQEDEVKT KELEETIQRL ERELESLENS SSVTSTKENL AEAAAPAKEE
KKENIPSVQK SPLGTAIAEK KVSSSPMKAV QGTDMMKAAM YSVEITVEKD RVTGETKVLS
STTLLPQNHC VQGIKVYEDE LKVVHAVSAE DGALQNGAQP LSSSEVDELL HKADEVTLGE
ATASGDAPGS ATSSQKATPR REITGLQAKP RENSTEGAEP SREQPVTMIF MGYQNVEDEN
ETKKVLGLEG TIKAELVVIE DAESKAEPEG KDHAPPNGTA LEPAAAPLQG DEVPGGQKPG
TNATEAKEAE PDMDAKKQRC KCCTVM
