PDLI4_MOUSE
ID PDLI4_MOUSE Reviewed; 330 AA.
AC P70271; Q5SWV2; Q8K0W4;
DT 15-MAR-2004, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 3.
DT 03-AUG-2022, entry version 159.
DE RecName: Full=PDZ and LIM domain protein 4;
DE AltName: Full=LIM protein RIL;
DE AltName: Full=Reversion-induced LIM protein;
GN Name=Pdlim4; Synonyms=Ril;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], PHOSPHORYLATION, AND INTERACTION WITH PTPN13.
RC STRAIN=BALB/cJ; TISSUE=Brain;
RX PubMed=9487134; DOI=10.1091/mbc.9.3.671;
RA Cuppen E., Gerrits H., Pepers B., Wieringa B., Hendriks W.;
RT "PDZ motifs in PTP-BL and RIL bind to internal protein segments in the LIM
RT domain protein RIL.";
RL Mol. Biol. Cell 9:671-683(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
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 [4]
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 [5]
RP INTERACTION WITH TRIP6 AND PTPN13, AND MUTAGENESIS OF 326-VAL--VAL-330.
RX PubMed=10826496; DOI=10.1078/s0171-9335(04)70031-x;
RA Cuppen E., van Ham M., Wansink D.G., de Leeuw A., Wieringa B., Hendriks W.;
RT "The zyxin-related protein TRIP6 interacts with PDZ motifs in the adaptor
RT protein RIL and the protein tyrosine phosphatase PTP-BL.";
RL Eur. J. Cell Biol. 79:283-293(2000).
RN [6]
RP TISSUE SPECIFICITY.
RX PubMed=14729062; DOI=10.1016/j.yexcr.2003.09.004;
RA Vallenius T., Scharm B., Vesikansa A., Luukko K., Schaefer R.,
RA Maekelae T.P.;
RT "The PDZ-LIM protein RIL modulates actin stress fiber turnover and enhances
RT the association of alpha-actinin with F-actin.";
RL Exp. Cell Res. 293:117-128(2004).
RN [7]
RP INTERACTION WITH PDLIM3 AND PTPN13, AND MUTAGENESIS OF GLY-261; VAL-263;
RP GLY-264; THR-265; ILE-266; VAL-267; LYS-272; TYR-274; PRO-276; GLU-277;
RP MET-280; LEU-286; ASN-287; LEU-288; ARG-291; GLY-292; PHE-294; PHE-295;
RP ARG-299 AND TYR-301.
RX PubMed=15663004; DOI=10.1007/s11033-005-1407-8;
RA van den Berk L.C., van Ham M.A., te Lindert M.M., Walma T., Aelen J.,
RA Vuister G.W., Hendriks W.J.;
RT "The interaction of PTP-BL PDZ domains with RIL: an enigmatic role for the
RT RIL LIM domain.";
RL Mol. Biol. Rep. 31:203-215(2004).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-111, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
RX PubMed=16452087; DOI=10.1074/mcp.t500041-mcp200;
RA Trinidad J.C., Specht C.G., Thalhammer A., Schoepfer R., Burlingame A.L.;
RT "Comprehensive identification of phosphorylation sites in postsynaptic
RT density preparations.";
RL Mol. Cell. Proteomics 5:914-922(2006).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-111, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT "Large-scale phosphorylation analysis of mouse liver.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-107; SER-111; SER-115;
RP SER-118; SER-119 AND SER-124, AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: Suppresses SRC activation by recognizing and binding to
CC active SRC and facilitating PTPN13-mediated dephosphorylation of SRC
CC 'Tyr-419' leading to its inactivation. Inactivated SRC dissociates from
CC this protein allowing the initiation of a new SRC inactivation cycle.
CC Involved in reorganization of the actin cytoskeleton (By similarity).
CC In nonmuscle cells, binds to ACTN1 (alpha-actinin-1), increases the
CC affinity of ACTN1 to F-actin (filamentous actin), and promotes
CC formation of actin stress fibers. Involved in regulation of the
CC synaptic AMPA receptor transport in dendritic spines of hippocampal
CC pyramidal neurons directing the receptors toward an insertion at the
CC postsynaptic membrane. Links endosomal surface-internalized GRIA1-
CC containing AMPA receptors to the alpha-actinin/actin cytoskeleton.
CC Increases AMPA receptor-mediated excitatory postsynaptic currents in
CC neurons (By similarity). {ECO:0000250|UniProtKB:P36202,
CC ECO:0000250|UniProtKB:P50479}.
CC -!- SUBUNIT: Homodimer (By similarity). Interacts (via C-terminus only or
CC via combined C-terminus and LIM domain, but not LIM domain only) with
CC PTPN13 (via the second or fourth PDZ domains) (PubMed:9487134,
CC PubMed:15663004). Found in a complex with PTPN13 and TRIP6
CC (PubMed:10826496). Interacts (via PDZ domain) with ACTN1 and ACTN2 (via
CC C-terminal SDL residues) (By similarity). Interacts (via PDZ domain)
CC with TRIP6 (via the second LIM domain or via the third LIM domain plus
CC C-terminus) (PubMed:10826496). Interacts (via LIM domain) with GRIA1
CC (via C-terminus); this interaction as well as the interaction with
CC alpha-actinin is required for their colocalization in early endosomes.
CC Interacts with PDLIM1 (By similarity). Forms (via LIM domain) a
CC heterodimer with PDLIM3 (PubMed:15663004). Interacts directly with SRC
CC (via kinase domain and to a lesser extent the SH2 domain) (By
CC similarity). {ECO:0000250|UniProtKB:P36202,
CC ECO:0000250|UniProtKB:P50479, ECO:0000269|PubMed:10826496,
CC ECO:0000269|PubMed:15663004, ECO:0000269|PubMed:9487134}.
CC -!- INTERACTION:
CC P70271; Q9Z1Y4: Trip6; NbExp=2; IntAct=EBI-7288319, EBI-643879;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton
CC {ECO:0000250|UniProtKB:P36202}. Cell projection, dendritic spine
CC {ECO:0000250|UniProtKB:P36202}. Early endosome membrane
CC {ECO:0000250|UniProtKB:P36202}; Peripheral membrane protein
CC {ECO:0000250|UniProtKB:P36202}; Cytoplasmic side
CC {ECO:0000250|UniProtKB:P36202}. Recycling endosome membrane
CC {ECO:0000250|UniProtKB:P36202}; Peripheral membrane protein
CC {ECO:0000250|UniProtKB:P36202}; Cytoplasmic side
CC {ECO:0000250|UniProtKB:P36202}. Nucleus {ECO:0000250|UniProtKB:P50479}.
CC Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:P50479}. Cell
CC projection, lamellipodium {ECO:0000250|UniProtKB:P50479}. Synapse,
CC synaptosome {ECO:0000250|UniProtKB:P36202}. Note=Localizes to actin
CC stress fibers in nonmuscle cells. Colocalizes with GRIA1 in early
CC endosomes. Enriched in numerous but not all spine-like structures along
CC dendritic branches. Colocalizes with actin and enriched at sites
CC containing larger amounts of actin and alpha-actinin. Targeted
CC efficiently to spines via its PDZ domain-mediated interaction with the
CC alpha-actinin/actin cytoskeletal complex. Localizes to synaptosomes in
CC brain (By similarity). Colocalizes with F-actin. Colocalizes with TRIP6
CC at cell-cell contacts and lamellipodia. In the cytoplasm, displays a
CC fibrillar pattern with characteristic thick fibers and occasional
CC clusters. Colocalizes with the actin stress fibers. Oxidative stress
CC induces redistribution from cytoskeleton to cytosol. Colocalizes with
CC SRC at the perinuclear region, but not at focal adhesions (By
CC similarity). {ECO:0000250|UniProtKB:P36202,
CC ECO:0000250|UniProtKB:P50479}.
CC -!- TISSUE SPECIFICITY: Expressed in several non-muscle tissues including
CC lung, brain, ovary and uterus, and especially in epithelial cells at 14
CC dpc. In the uterus, high expression in the glandular epithelium, but
CC absent in the simple columnar epithelium lining the uterus cavity.
CC {ECO:0000269|PubMed:14729062}.
CC -!- PTM: Phosphorylated on tyrosine residue(s). Can be dephosphorylated by
CC PTPN13. {ECO:0000269|PubMed:9487134}.
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DR EMBL; Y08361; CAA69648.1; -; mRNA.
DR EMBL; AL596444; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH466575; EDL33550.1; -; Genomic_DNA.
DR EMBL; BC030068; AAH30068.1; -; mRNA.
DR CCDS; CCDS24690.1; -.
DR RefSeq; NP_062290.2; NM_019417.3.
DR AlphaFoldDB; P70271; -.
DR SMR; P70271; -.
DR BioGRID; 205965; 9.
DR IntAct; P70271; 6.
DR MINT; P70271; -.
DR STRING; 10090.ENSMUSP00000018755; -.
DR iPTMnet; P70271; -.
DR PhosphoSitePlus; P70271; -.
DR EPD; P70271; -.
DR jPOST; P70271; -.
DR MaxQB; P70271; -.
DR PaxDb; P70271; -.
DR PeptideAtlas; P70271; -.
DR PRIDE; P70271; -.
DR ProteomicsDB; 288086; -.
DR Antibodypedia; 2128; 205 antibodies from 28 providers.
DR DNASU; 30794; -.
DR Ensembl; ENSMUST00000018755; ENSMUSP00000018755; ENSMUSG00000020388.
DR GeneID; 30794; -.
DR KEGG; mmu:30794; -.
DR UCSC; uc007ixf.2; mouse.
DR CTD; 8572; -.
DR MGI; MGI:1353470; Pdlim4.
DR VEuPathDB; HostDB:ENSMUSG00000020388; -.
DR eggNOG; KOG1703; Eukaryota.
DR GeneTree; ENSGT00940000159536; -.
DR HOGENOM; CLU_038114_1_1_1; -.
DR InParanoid; P70271; -.
DR OMA; QYNNPTR; -.
DR OrthoDB; 840552at2759; -.
DR PhylomeDB; P70271; -.
DR TreeFam; TF106408; -.
DR BioGRID-ORCS; 30794; 4 hits in 73 CRISPR screens.
DR PRO; PR:P70271; -.
DR Proteomes; UP000000589; Chromosome 11.
DR RNAct; P70271; protein.
DR Bgee; ENSMUSG00000020388; Expressed in lip and 225 other tissues.
DR ExpressionAtlas; P70271; baseline and differential.
DR Genevisible; P70271; MM.
DR GO; GO:0015629; C:actin cytoskeleton; ISO:MGI.
DR GO; GO:0005912; C:adherens junction; IBA:GO_Central.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0005856; C:cytoskeleton; ISO:MGI.
DR GO; GO:0043197; C:dendritic spine; ISS:UniProtKB.
DR GO; GO:0031905; C:early endosome lumen; ISS:UniProtKB.
DR GO; GO:0031901; C:early endosome membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0031941; C:filamentous actin; ISO:MGI.
DR GO; GO:0030027; C:lamellipodium; ISO:MGI.
DR GO; GO:0005634; C:nucleus; ISO:MGI.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; ISO:MGI.
DR GO; GO:0045211; C:postsynaptic membrane; ISS:UniProtKB.
DR GO; GO:0034777; C:recycling endosome lumen; ISS:UniProtKB.
DR GO; GO:0055038; C:recycling endosome membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0001725; C:stress fiber; ISO:MGI.
DR GO; GO:0030018; C:Z disc; IBA:GO_Central.
DR GO; GO:0003779; F:actin binding; IBA:GO_Central.
DR GO; GO:0042805; F:actinin binding; ISO:MGI.
DR GO; GO:0051393; F:alpha-actinin binding; ISO:MGI.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0051371; F:muscle alpha-actinin binding; IBA:GO_Central.
DR GO; GO:0042803; F:protein homodimerization activity; ISO:MGI.
DR GO; GO:0019903; F:protein phosphatase binding; IPI:UniProtKB.
DR GO; GO:0030036; P:actin cytoskeleton organization; ISO:MGI.
DR GO; GO:0031532; P:actin cytoskeleton reorganization; ISO:MGI.
DR GO; GO:0098976; P:excitatory chemical synaptic transmission; ISS:UniProtKB.
DR GO; GO:0007507; P:heart development; IBA:GO_Central.
DR GO; GO:0061061; P:muscle structure development; IBA:GO_Central.
DR GO; GO:0051496; P:positive regulation of stress fiber assembly; ISO:MGI.
DR Gene3D; 2.30.42.10; -; 1.
DR InterPro; IPR031847; DUF4749.
DR InterPro; IPR001478; PDZ.
DR InterPro; IPR036034; PDZ_sf.
DR InterPro; IPR001781; Znf_LIM.
DR Pfam; PF15936; DUF4749; 1.
DR Pfam; PF00412; LIM; 1.
DR Pfam; PF00595; PDZ; 1.
DR SMART; SM00132; LIM; 1.
DR SMART; SM00228; PDZ; 1.
DR SUPFAM; SSF50156; SSF50156; 1.
DR PROSITE; PS00478; LIM_DOMAIN_1; 1.
DR PROSITE; PS50023; LIM_DOMAIN_2; 1.
DR PROSITE; PS50106; PDZ; 1.
PE 1: Evidence at protein level;
KW Cell projection; Cytoplasm; Cytoskeleton; Endosome; LIM domain; Membrane;
KW Metal-binding; Nucleus; Phosphoprotein; Reference proteome; Synapse;
KW Synaptosome; Zinc.
FT CHAIN 1..330
FT /note="PDZ and LIM domain protein 4"
FT /id="PRO_0000075874"
FT DOMAIN 1..84
FT /note="PDZ"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00143"
FT DOMAIN 255..305
FT /note="LIM zinc-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00125"
FT REGION 104..153
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 219..242
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 108..128
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 107
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 111
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:16452087,
FT ECO:0007744|PubMed:17242355, ECO:0007744|PubMed:21183079"
FT MOD_RES 115
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 118
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 119
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 124
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 134
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P36202"
FT MUTAGEN 261
FT /note="G->A: No loss of interaction with PTPN13 (via PDZ
FT domains); when associated with A-263."
FT /evidence="ECO:0000269|PubMed:15663004"
FT MUTAGEN 263
FT /note="V->A: No loss of interaction with PTPN13 (via PDZ
FT domains); when associated with A-261."
FT /evidence="ECO:0000269|PubMed:15663004"
FT MUTAGEN 264
FT /note="G->A: No loss of interaction with PTPN13 (via PDZ
FT domains); when associated with A-266."
FT /evidence="ECO:0000269|PubMed:15663004"
FT MUTAGEN 265
FT /note="T->A: No loss of interaction with PTPN13 (via PDZ
FT domains); when associated with A-267."
FT /evidence="ECO:0000269|PubMed:15663004"
FT MUTAGEN 266
FT /note="I->A: No loss of interaction with PTPN13 (via PDZ
FT domains); when associated with A-264."
FT /evidence="ECO:0000269|PubMed:15663004"
FT MUTAGEN 267
FT /note="V->A: No loss of interaction with PTPN13 (via PDZ
FT domains); when associated with A-265."
FT /evidence="ECO:0000269|PubMed:15663004"
FT MUTAGEN 272
FT /note="K->A: No loss of interaction with PTPN13 (via PDZ
FT domains); when associated with A-274."
FT /evidence="ECO:0000269|PubMed:15663004"
FT MUTAGEN 274
FT /note="Y->A: No loss of interaction with PTPN13 (via PDZ
FT domains); when associated with A-272."
FT /evidence="ECO:0000269|PubMed:15663004"
FT MUTAGEN 276
FT /note="P->A: No loss of interaction with PTPN13 (via PDZ
FT domains); when associated with A-277."
FT /evidence="ECO:0000269|PubMed:15663004"
FT MUTAGEN 277
FT /note="E->A: No loss of interaction with PTPN13 (via PDZ
FT domains); when associated with A-276."
FT /evidence="ECO:0000269|PubMed:15663004"
FT MUTAGEN 280
FT /note="M->A: No loss of interaction with PTPN13 (via PDZ
FT domains)."
FT /evidence="ECO:0000269|PubMed:15663004"
FT MUTAGEN 286
FT /note="L->A: No loss of interaction with PTPN13 (via PDZ
FT domains); when associated with A-288."
FT /evidence="ECO:0000269|PubMed:15663004"
FT MUTAGEN 287
FT /note="N->A: No loss of interaction with PTPN13 (via PDZ
FT domains)."
FT /evidence="ECO:0000269|PubMed:15663004"
FT MUTAGEN 288
FT /note="L->A: No loss of interaction with PTPN13 (via PDZ
FT domains); when associated with A-286."
FT /evidence="ECO:0000269|PubMed:15663004"
FT MUTAGEN 291
FT /note="R->A: No loss of interaction with PTPN13 (via PDZ
FT domains); when associated with A-292."
FT /evidence="ECO:0000269|PubMed:15663004"
FT MUTAGEN 292
FT /note="G->A: No loss of interaction with PTPN13 (via PDZ
FT domains); when associated with A-291."
FT /evidence="ECO:0000269|PubMed:15663004"
FT MUTAGEN 294
FT /note="F->A: No loss of interaction with PTPN13 (via PDZ
FT domains); when associated with A-295."
FT /evidence="ECO:0000269|PubMed:15663004"
FT MUTAGEN 295
FT /note="F->A: No loss of interaction with PTPN13 (via PDZ
FT domains); when associated with A-294."
FT /evidence="ECO:0000269|PubMed:15663004"
FT MUTAGEN 299
FT /note="R->A: No loss of interaction with PTPN13 (via PDZ
FT domains); when associated with A-301."
FT /evidence="ECO:0000269|PubMed:15663004"
FT MUTAGEN 301
FT /note="Y->A: No loss of interaction with PTPN13 (via PDZ
FT domains); when associated with A-299."
FT /evidence="ECO:0000269|PubMed:15663004"
FT MUTAGEN 326..330
FT /note="Missing: Interaction with TRIP6."
FT /evidence="ECO:0000269|PubMed:10826496"
FT CONFLICT 25
FT /note="A -> L (in Ref. 1; CAA69648)"
FT /evidence="ECO:0000305"
FT CONFLICT 91
FT /note="A -> S (in Ref. 1; CAA69648)"
FT /evidence="ECO:0000305"
FT CONFLICT 107
FT /note="S -> F (in Ref. 1; CAA69648)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 330 AA; 35556 MW; BB3421541BFC086E CRC64;
MTHSVTLRGP SPWGFRLVGG RDFSAPLTIS RVHAGSKAAL AALCPGDLIQ AINGESTELM
THLEAQNRIK GCHDHLTLSV SRPENKNWPS APDDKAQAHR IHIDPESQDC SPATSRRSSV
SGISLEDNRS GLGSPYGQPP RLPVPHNGSS NEATLPAQMS ALHVSPPTSA DTARVLPRNR
DCRVDLGSEV YRMLREPAEP TASEPKQSGS FRYLQGMLEA GEGGDRPGSG GPRNLKPAAS
KLGAPLSGLQ GLPECTRCGH GIVGTIVKAR DKLYHPECFM CSDCGLNLKQ RGYFFLDERL
YCENHAKARV KPPEGYDVVA VYPNAKVELV
