PDLI4_CHICK
ID PDLI4_CHICK Reviewed; 330 AA.
AC Q9PW72;
DT 21-FEB-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 120.
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 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].
RC STRAIN=White leghorn;
RX PubMed=10918612; DOI=10.1038/sj.onc.1203691;
RA Fu S.-L., Waha A., Vogt P.K.;
RT "Identification and characterization of genes upregulated in cells
RT transformed by v-Jun.";
RL Oncogene 19:3537-3545(2000).
RN [2]
RP INTERACTION WITH ACTN1.
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).
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: Interacts (via LIM domain) with PTPN13 (By similarity).
CC Interacts (via PDZ domain) with ACTN1 (PubMed:14729062).
CC {ECO:0000250|UniProtKB:P70271, ECO:0000269|PubMed:14729062}.
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}.
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DR EMBL; AF167295; AAD46655.1; -; mRNA.
DR RefSeq; NP_990170.1; NM_204839.2.
DR AlphaFoldDB; Q9PW72; -.
DR SMR; Q9PW72; -.
DR STRING; 9031.ENSGALP00000042746; -.
DR PaxDb; Q9PW72; -.
DR GeneID; 395643; -.
DR KEGG; gga:395643; -.
DR CTD; 8572; -.
DR VEuPathDB; HostDB:geneid_395643; -.
DR eggNOG; KOG1703; Eukaryota.
DR HOGENOM; CLU_038114_1_1_1; -.
DR InParanoid; Q9PW72; -.
DR OrthoDB; 840552at2759; -.
DR PhylomeDB; Q9PW72; -.
DR TreeFam; TF106408; -.
DR PRO; PR:Q9PW72; -.
DR Proteomes; UP000000539; Unplaced.
DR GO; GO:0005912; C:adherens junction; IBA:GO_Central.
DR GO; GO:0005737; C:cytoplasm; IDA:AgBase.
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; IBA:GO_Central.
DR GO; GO:0030027; C:lamellipodium; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:UniProtKB-SubCell.
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; IBA:GO_Central.
DR GO; GO:0030018; C:Z disc; IBA:GO_Central.
DR GO; GO:0003779; F:actin binding; IBA:GO_Central.
DR GO; GO:0051015; F:actin filament binding; IDA:AgBase.
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:0030036; P:actin cytoskeleton organization; IBA:GO_Central.
DR GO; GO:0098976; P:excitatory chemical synaptic transmission; ISS:UniProtKB.
DR GO; GO:0007507; P:heart development; IBA:GO_Central.
DR GO; GO:0060173; P:limb development; IDA:AgBase.
DR GO; GO:0061061; P:muscle structure development; IBA:GO_Central.
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; Reference proteome; Synapse; Synaptosome; Zinc.
FT CHAIN 1..330
FT /note="PDZ and LIM domain protein 4"
FT /id="PRO_0000075876"
FT DOMAIN 8..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 106..152
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 163..182
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 135..149
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 163..177
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 330 AA; 35839 MW; 2C0E0B404301E404 CRC64;
MPHSVALRGP SPWGFRLVGG KDFSTPLTIS RINPGSKAAL ANLCPGDIIL AINGESTEAM
THLEAQNKIK ACVEQLLLSV SRAEERSWSP PILEDGKAQA YRINIEPEPQ DNGPAVGKRP
MPHAAGGSPV DSRPALSLQH PQPSRPHASS SADAALPLQL SGLHISPSQS TDPLKSLPRN
RNGIDVESDV YKMLQDYERP ASEPKQSGSF RYLQGMLEAG ENGEKLDRLS NPRSIKPAGP
KLGAAMSGLQ MLPECTRCGN GIVGTIVKAR DKLYHPECFM CDDCGLNLKQ RGYFFIEEQL
YCETHAKERV KPPEGYDVVA VYPNAKVELV
