PDLI4_RAT
ID PDLI4_RAT Reviewed; 330 AA.
AC P36202;
DT 01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 2.
DT 03-AUG-2022, entry version 126.
DE RecName: Full=PDZ and LIM domain protein 4;
DE AltName: Full=H-REV18;
DE AltName: Full=LIM protein RIL;
DE AltName: Full=RIT-18;
DE AltName: Full=Reversion-induced LIM protein {ECO:0000303|PubMed:7824279};
GN Name=Pdlim4; Synonyms=Ril {ECO:0000303|PubMed:7824279};
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RC STRAIN=Sprague-Dawley; TISSUE=Liver;
RX PubMed=7824279;
RA Kiess M., Scharm B., Aguzzi A., Hajnal A., Klemenz R.,
RA Schwarte-Waldhoff I., Schaefer R.;
RT "Expression of ril, a novel LIM domain gene, is down-regulated in Hras-
RT transformed cells and restored in phenotypic revertants.";
RL Oncogene 10:61-68(1995).
RN [2]
RP FUNCTION, INTERACTION WITH ACTN1, AND SUBCELLULAR LOCATION.
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 [3]
RP FUNCTION, INTERACTION WITH ACTN2 AND GRIA1, AND SUBCELLULAR LOCATION.
RX PubMed=15456832; DOI=10.1523/jneurosci.2100-04.2004;
RA Schulz T.W., Nakagawa T., Licznerski P., Pawlak V., Kolleker A., Rozov A.,
RA Kim J., Dittgen T., Koehr G., Sheng M., Seeburg P.H., Osten P.;
RT "Actin/alpha-actinin-dependent transport of AMPA receptors in dendritic
RT spines: role of the PDZ-LIM protein RIL.";
RL J. Neurosci. 24:8584-8594(2004).
RN [4]
RP FUNCTION, INTERACTION WITH PDLIM1, SUBCELLULAR LOCATION, AND TISSUE
RP SPECIFICITY.
RX PubMed=22659164; DOI=10.1016/j.yexcr.2012.05.006;
RA Miyazaki K., Ohno K., Tamura N., Sasaki T., Sato K.;
RT "CLP36 and RIL recruit alpha-actinin-1 to stress fibers and differentially
RT regulate stress fiber dynamics in F2408 fibroblasts.";
RL Exp. Cell Res. 318:1716-1725(2012).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-111; SER-119; SER-124 AND
RP SER-134, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
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 (By similarity). Involved in reorganization of the actin cytoskeleton.
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 (PubMed:14729062, PubMed:22659164).
CC Involved in regulation of the synaptic AMPA receptor transport in
CC dendritic spines of hippocampal pyramidal neurons directing the
CC receptors toward an insertion at the postsynaptic membrane. Links
CC endosomal surface-internalized GRIA1-containing AMPA receptors to the
CC alpha-actinin/actin cytoskeleton. Increases AMPA receptor-mediated
CC excitatory postsynaptic currents in neurons (PubMed:15456832).
CC {ECO:0000250|UniProtKB:P50479, ECO:0000269|PubMed:14729062,
CC ECO:0000269|PubMed:15456832, ECO:0000269|PubMed:22659164}.
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). Found in a complex with
CC PTPN13 and TRIP6 (By similarity). Interacts (via PDZ domain) with ACTN1
CC and ACTN2 (via C-terminal SDL residues) (PubMed:14729062,
CC PubMed:15456832). Interacts (via PDZ domain) with TRIP6 (via the second
CC LIM domain or via the third LIM domain plus C-terminus) (By
CC similarity). Interacts (via LIM domain) with GRIA1 (via C-terminus);
CC this interaction as well as the interaction with alpha-actinin is
CC required for their colocalization in early endosomes (PubMed:15456832).
CC Interacts with PDLIM1 (PubMed:22659164). Forms (via LIM domain) a
CC heterodimer with PDLIM3 (By similarity). Interacts directly with SRC
CC (via kinase domain and to a lesser extent the SH2 domain) (By
CC similarity). {ECO:0000250|UniProtKB:P50479,
CC ECO:0000250|UniProtKB:P70271, ECO:0000269|PubMed:14729062,
CC ECO:0000269|PubMed:15456832, ECO:0000269|PubMed:22659164}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton
CC {ECO:0000269|PubMed:14729062, ECO:0000269|PubMed:15456832,
CC ECO:0000269|PubMed:22659164}. Cell projection, dendritic spine
CC {ECO:0000269|PubMed:15456832}. Early endosome membrane
CC {ECO:0000269|PubMed:15456832}; Peripheral membrane protein
CC {ECO:0000305}; Cytoplasmic side {ECO:0000305}. Recycling endosome
CC membrane {ECO:0000269|PubMed:15456832}; Peripheral membrane protein
CC {ECO:0000305}; Cytoplasmic side {ECO:0000305}. Nucleus
CC {ECO:0000250|UniProtKB:P50479}. Cytoplasm, perinuclear region
CC {ECO:0000250|UniProtKB:P50479}. Cell projection, lamellipodium
CC {ECO:0000250|UniProtKB:P50479}. Synapse, synaptosome
CC {ECO:0000269|PubMed:15456832}. Note=Localizes to actin stress fibers in
CC nonmuscle cells (PubMed:14729062, PubMed:22659164). Colocalizes with
CC GRIA1 in early endosomes. Enriched in numerous but not all spine-like
CC structures along dendritic branches. Colocalizes with actin and
CC enriched at sites containing larger amounts of actin and alpha-actinin.
CC Targeted efficiently to spines via its PDZ domain-mediated interaction
CC with the alpha-actinin/actin cytoskeletal complex. Localizes to
CC synaptosomes in brain (PubMed:15456832). Colocalizes with F-actin.
CC Colocalizes with TRIP6 at cell-cell contacts and lamellipodia. In the
CC cytoplasm, displays a fibrillar pattern with characteristic thick
CC fibers and occasional clusters. Colocalizes with the actin stress
CC fibers. Oxidative stress induces redistribution from cytoskeleton to
CC cytosol. Colocalizes with SRC at the perinuclear region, but not at
CC focal adhesions (By similarity). {ECO:0000250|UniProtKB:P50479,
CC ECO:0000269|PubMed:14729062, ECO:0000269|PubMed:15456832,
CC ECO:0000269|PubMed:22659164}.
CC -!- TISSUE SPECIFICITY: Detected in several tissues, most prominent in
CC brain and heart of adults (PubMed:7824279). Expressed in embryonic
CC fibroblasts (PubMed:22659164). {ECO:0000269|PubMed:22659164,
CC ECO:0000269|PubMed:7824279}.
CC -!- PTM: Phosphorylated on tyrosine residue(s). Can be dephosphorylated by
CC PTPN13. {ECO:0000250|UniProtKB:P70271}.
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; X76454; CAA53992.1; -; mRNA.
DR PIR; S71828; S71828.
DR RefSeq; NP_058758.1; NM_017062.2.
DR AlphaFoldDB; P36202; -.
DR SMR; P36202; -.
DR IntAct; P36202; 2.
DR STRING; 10116.ENSRNOP00000064261; -.
DR iPTMnet; P36202; -.
DR PhosphoSitePlus; P36202; -.
DR PaxDb; P36202; -.
DR PRIDE; P36202; -.
DR GeneID; 24915; -.
DR KEGG; rno:24915; -.
DR CTD; 8572; -.
DR RGD; 3575; Pdlim4.
DR eggNOG; KOG1703; Eukaryota.
DR InParanoid; P36202; -.
DR OrthoDB; 840552at2759; -.
DR PhylomeDB; P36202; -.
DR PRO; PR:P36202; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0015629; C:actin cytoskeleton; IPI:UniProtKB.
DR GO; GO:0005912; C:adherens junction; IBA:GO_Central.
DR GO; GO:0005737; C:cytoplasm; ISO:RGD.
DR GO; GO:0005856; C:cytoskeleton; ISO:RGD.
DR GO; GO:0043197; C:dendritic spine; IDA:UniProtKB.
DR GO; GO:0031905; C:early endosome lumen; IDA:UniProtKB.
DR GO; GO:0031901; C:early endosome membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0031941; C:filamentous actin; ISO:RGD.
DR GO; GO:0030027; C:lamellipodium; ISO:RGD.
DR GO; GO:0005634; C:nucleus; ISO:RGD.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; ISO:RGD.
DR GO; GO:0045211; C:postsynaptic membrane; IDA:UniProtKB.
DR GO; GO:0034777; C:recycling endosome lumen; IDA:UniProtKB.
DR GO; GO:0055038; C:recycling endosome membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0001725; C:stress fiber; IDA:UniProtKB.
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; IPI:RGD.
DR GO; GO:0051393; F:alpha-actinin binding; IPI:UniProtKB.
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:RGD.
DR GO; GO:0019903; F:protein phosphatase binding; ISO:RGD.
DR GO; GO:0030036; P:actin cytoskeleton organization; IDA:RGD.
DR GO; GO:0031532; P:actin cytoskeleton reorganization; ISO:RGD.
DR GO; GO:0098976; P:excitatory chemical synaptic transmission; IDA: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; IDA:UniProtKB.
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_0000075875"
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..154
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 219..239
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 111..128
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 111
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 115
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P70271"
FT MOD_RES 118
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P70271"
FT MOD_RES 119
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 124
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 134
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
SQ SEQUENCE 330 AA; 35521 MW; 84BEB1E629ADA584 CRC64;
MTHAVTLRGP SPWGFRLVGG RDFSAPLTIS RVHAGSKAAL AALCPGDSIQ AINGESTELM
THLEAQNRIK GCHDHLTLSV SRPENKNWPS SPNDKAQAHR IHIDPEAQDG SPATSRRSSI
SGISLEDNRS GLGSPYGQPP RLPVPHNGSS NEVTLPSQMS ALHVSPPPSA DTPRILPRNR
DCRVDLGSEV YRMLREPAEP AASEPKQSGS FRYLQGMLEA GEGGDRPGSG GSRNLKPAAS
KLGAPLSGLQ GLPECTRCGH GIVGTIVKAR DKLYHPECFM CSDCGLNLKQ RGYFFLDERL
YCENHAKARV KPPEGYDVVA VYPNAKVELV
