Pdlim4
entrez
30794
canonical
uniprot
P70271
canonical
ensembl
ENSMUSG00000020388
resolver
ensp
ENSMUSP00000018755
resolver
ensp
ENSMUSP00000090797
resolver
ensp
ENSMUSP00000298828
resolver
ensp
ENSMUSP00000298830
resolver
enst
ENSMUST00000018755
resolver
enst
ENSMUST00000093109
resolver
genesymbol
Pdlim4
resolver
genesymbol_syn
Ril
resolver
uniprot
Q5SWV2
resolver
uniprot
Q5SWV3
resolver
uniprot
Q8K0W4
resolver
uniprot_entry
PDLI4_MOUSE
resolver
uniprot_entry
Q5SWV3_MOUSE
resolver
uniprot_sec
Q5SWV2
resolver
uniprot_sec
Q8K0W4
resolver
amino_acid_sequence
MTHSVTLRGPSPWGFRLVGGRDFSAPLTISRVHAGSKAALAALCPGDLIQAINGESTELMTHLEAQNRIKGCHDHLTLSVSRPENKNWPSAPDDKAQAHRIHIDPESQDCSPATSRRSSVSGISLEDNRSGLGSPYGQPPRLPVPHNGSSNEATLPAQMSALHVSPPTSADTARVLPRNRDCRVDLGSEVYRMLREPAEPTASEPKQSGSFRYLQGMLEAGEGGDRPGSGGPRNLKPAASKLGAPLSGLQGLPECTRCGHGIVGTIVKARDKLYHPECFMCSDCGLNLKQRGYFFLDERLYCENHAKARVKPPEGYDVVAVYPNAKVELV
uniprot
proteins
function
FUNCTION: Suppresses SRC activation by recognizing and binding to active SRC and facilitating PTPN13-mediated dephosphorylation of SRC 'Tyr-419' leading to its inactivation. Inactivated SRC dissociates from this protein allowing the initiation of a new SRC inactivation cycle. Involved in reorganization of the actin cytoskeleton (By similarity). In nonmuscle cells, binds to ACTN1 (alpha-actinin-1), increases the affinity of ACTN1 to F-actin (filamentous actin), and promotes formation of actin stress fibers. Involved in regulation of the synaptic AMPA receptor transport in dendritic spines of hippocampal pyramidal neurons directing the receptors toward an insertion at the postsynaptic membrane. Links endosomal surface-internalized GRIA1-containing AMPA receptors to the alpha-actinin/actin cytoskeleton. Increases AMPA receptor-mediated excitatory postsynaptic currents in neurons (By similarity). {ECO:0000250|UniProtKB:P36202, ECO:0000250|UniProtKB:P50479}.
uniprot
proteins
mass_dalton
35556
uniprot
proteins
mutagenesis
MUTAGEN 261; /note="G->A: No loss of interaction with PTPN13 (via PDZ domains); when associated with A-263."; /evidence="ECO:0000269|PubMed:15663004"; MUTAGEN 263; /note="V->A: No loss of interaction with PTPN13 (via PDZ domains); when associated with A-261."; /evidence="ECO:0000269|PubMed:15663004"; MUTAGEN 264; /note="G->A: No loss of interaction with PTPN13 (via PDZ domains); when associated with A-266."; /evidence="ECO:0000269|PubMed:15663004"; MUTAGEN 265; /note="T->A: No loss of interaction with PTPN13 (via PDZ domains); when associated with A-267."; /evidence="ECO:0000269|PubMed:15663004"; MUTAGEN 266; /note="I->A: No loss of interaction with PTPN13 (via PDZ domains); when associated with A-264."; /evidence="ECO:0000269|PubMed:15663004"; MUTAGEN 267; /note="V->A: No loss of interaction with PTPN13 (via PDZ domains); when associated with A-265."; /evidence="ECO:0000269|PubMed:15663004"; MUTAGEN 272; /note="K->A: No loss of interaction with PTPN13 (via PDZ domains); when associated with A-274."; /evidence="ECO:0000269|PubMed:15663004"; MUTAGEN 274; /note="Y->A: No loss of interaction with PTPN13 (via PDZ domains); when associated with A-272."; /evidence="ECO:0000269|PubMed:15663004"; MUTAGEN 276; /note="P->A: No loss of interaction with PTPN13 (via PDZ domains); when associated with A-277."; /evidence="ECO:0000269|PubMed:15663004"; MUTAGEN 277; /note="E->A: No loss of interaction with PTPN13 (via PDZ domains); when associated with A-276."; /evidence="ECO:0000269|PubMed:15663004"; MUTAGEN 280; /note="M->A: No loss of interaction with PTPN13 (via PDZ domains)."; /evidence="ECO:0000269|PubMed:15663004"; MUTAGEN 286; /note="L->A: No loss of interaction with PTPN13 (via PDZ domains); when associated with A-288."; /evidence="ECO:0000269|PubMed:15663004"; MUTAGEN 287; /note="N->A: No loss of interaction with PTPN13 (via PDZ domains)."; /evidence="ECO:0000269|PubMed:15663004"; MUTAGEN 288; /note="L->A: No loss of interaction with PTPN13 (via PDZ domains); when associated with A-286."; /evidence="ECO:0000269|PubMed:15663004"; MUTAGEN 291; /note="R->A: No loss of interaction with PTPN13 (via PDZ domains); when associated with A-292."; /evidence="ECO:0000269|PubMed:15663004"; MUTAGEN 292; /note="G->A: No loss of interaction with PTPN13 (via PDZ domains); when associated with A-291."; /evidence="ECO:0000269|PubMed:15663004"; MUTAGEN 294; /note="F->A: No loss of interaction with PTPN13 (via PDZ domains); when associated with A-295."; /evidence="ECO:0000269|PubMed:15663004"; MUTAGEN 295; /note="F->A: No loss of interaction with PTPN13 (via PDZ domains); when associated with A-294."; /evidence="ECO:0000269|PubMed:15663004"; MUTAGEN 299; /note="R->A: No loss of interaction with PTPN13 (via PDZ domains); when associated with A-301."; /evidence="ECO:0000269|PubMed:15663004"; MUTAGEN 301; /note="Y->A: No loss of interaction with PTPN13 (via PDZ domains); when associated with A-299."; /evidence="ECO:0000269|PubMed:15663004"; MUTAGEN 326..330; /note="Missing: Interaction with TRIP6."; /evidence="ECO:0000269|PubMed:10826496
uniprot
proteins
post_translational_modification
PTM: Phosphorylated on tyrosine residue(s). Can be dephosphorylated by PTPN13. {ECO:0000269|PubMed:9487134}.
uniprot
proteins
pubmed
10826496
uniprot
proteins
pubmed
14729062
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
15663004
uniprot
proteins
pubmed
16452087
uniprot
proteins
pubmed
17242355
uniprot
proteins
pubmed
19468303
uniprot
proteins
pubmed
21183079
uniprot
proteins
pubmed
9487134
uniprot
proteins
sequence_length
330
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000250|UniProtKB:P36202}. Cell projection, dendritic spine {ECO:0000250|UniProtKB:P36202}. Early endosome membrane {ECO:0000250|UniProtKB:P36202}; Peripheral membrane protein {ECO:0000250|UniProtKB:P36202}; Cytoplasmic side {ECO:0000250|UniProtKB:P36202}. Recycling endosome membrane {ECO:0000250|UniProtKB:P36202}; Peripheral membrane protein {ECO:0000250|UniProtKB:P36202}; Cytoplasmic side {ECO:0000250|UniProtKB:P36202}. Nucleus {ECO:0000250|UniProtKB:P50479}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:P50479}. Cell projection, lamellipodium {ECO:0000250|UniProtKB:P50479}. Synapse, synaptosome {ECO:0000250|UniProtKB:P36202}. Note=Localizes to actin stress fibers in nonmuscle cells. Colocalizes with GRIA1 in early endosomes. Enriched in numerous but not all spine-like structures along dendritic branches. Colocalizes with actin and enriched at sites containing larger amounts of actin and alpha-actinin. Targeted efficiently to spines via its PDZ domain-mediated interaction with the alpha-actinin/actin cytoskeletal complex. Localizes to synaptosomes in brain (By similarity). Colocalizes with F-actin. Colocalizes with TRIP6 at cell-cell contacts and lamellipodia. In the cytoplasm, displays a fibrillar pattern with characteristic thick fibers and occasional clusters. Colocalizes with the actin stress fibers. Oxidative stress induces redistribution from cytoskeleton to cytosol. Colocalizes with SRC at the perinuclear region, but not at focal adhesions (By similarity). {ECO:0000250|UniProtKB:P36202, ECO:0000250|UniProtKB:P50479}.
uniprot
proteins