PDLI4_HUMAN
ID PDLI4_HUMAN Reviewed; 330 AA.
AC P50479; B2R8U1; Q53Y39; Q96AT8; Q9BTW8; Q9Y292;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2002, sequence version 2.
DT 03-AUG-2022, entry version 187.
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 Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE (ISOFORM 1), AND VARIANTS CYS-142 AND CYS-259.
RC TISSUE=Lung;
RA Scharm B., Schaefer R.;
RL Submitted (OCT-1995) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORMS 1 AND 2), AND TISSUE
RP SPECIFICITY (ISOFORM 2).
RX PubMed=9573374; DOI=10.1016/s0378-1119(98)00080-8;
RA Bashirova A.A., Markelov M.L., Shlykova T.V., Levshenkova E.V.,
RA Alibaeva R.A., Frolova E.I.;
RT "The human RIL gene: mapping to human chromosome 5q31.1, genomic
RT organization and alternative transcripts.";
RL Gene 210:239-245(1998).
RN [3]
RP NUCLEOTIDE SEQUENCE (ISOFORM 1).
RA Bashirova A.A., Markelov M.L., Levshenkova E.V., Shelkunova M.A.,
RA Frolova E.I.;
RL Submitted (MAY-1999) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RA Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
RA Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
RA Phelan M., Farmer A.;
RT "Cloning of human full-length CDSs in BD Creator(TM) system donor vector.";
RL Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2), AND VARIANT
RP GLY-118.
RC TISSUE=Bone marrow, and Brain;
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 [8]
RP INTERACTION WITH TRIP6, AND SUBCELLULAR LOCATION.
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 [9]
RP INVOLVEMENT IN BMD.
RX PubMed=12908099; DOI=10.1007/s10038-003-0035-1;
RA Omasu F., Ezura Y., Kajita M., Ishida R., Kodaira M., Yoshida H.,
RA Suzuki T., Hosoi T., Inoue S., Shiraki M., Orimo H., Emi M.;
RT "Association of genetic variation of the RIL gene, encoding a PDZ-LIM
RT domain protein and localized in 5q31.1, with low bone mineral density in
RT adult Japanese women.";
RL J. Hum. Genet. 48:342-345(2003).
RN [10]
RP FUNCTION, INTERACTION WITH PTPN13 AND SRC, AND SUBCELLULAR LOCATION.
RX PubMed=19307596; DOI=10.1083/jcb.200810155;
RA Zhang Y., Tu Y., Zhao J., Chen K., Wu C.;
RT "Reversion-induced LIM interaction with Src reveals a novel Src
RT inactivation cycle.";
RL J. Cell Biol. 184:785-792(2009).
RN [11]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19369195; DOI=10.1074/mcp.m800588-mcp200;
RA Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,
RA Mann M., Daub H.;
RT "Large-scale proteomics analysis of the human kinome.";
RL Mol. Cell. Proteomics 8:1751-1764(2009).
RN [12]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [13]
RP IDENTIFICATION BY MASS SPECTROMETRY (ISOFORM 2), FUNCTION (ISOFORMS 1 AND
RP 2), INTERACTION WITH NQO1 (ISOFORMS 1 AND 2), SUBCELLULAR LOCATION
RP (ISOFORMS 1 AND 2), AND INDUCTION (ISOFORM 2).
RX PubMed=21636573; DOI=10.1074/jbc.m111.241554;
RA Guryanova O.A., Drazba J.A., Frolova E.I., Chumakov P.M.;
RT "Actin cytoskeleton remodeling by the alternatively spliced isoform of
RT PDLIM4/RIL protein.";
RL J. Biol. Chem. 286:26849-26859(2011).
RN [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-112, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT "System-wide temporal characterization of the proteome and phosphoproteome
RT of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [15]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-112, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [16]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-112, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [17]
RP STRUCTURE BY NMR OF 1-81.
RG RIKEN structural genomics initiative (RSGI);
RT "Solution structure of PDZ domain of PDZ and LIM domain protein.";
RL Submitted (AUG-2007) to the PDB data bank.
RN [18]
RP X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) OF 1-85 BOUND TO C-TERMINAL PEPTIDE
RP OF ACTN1.
RX PubMed=20120020; DOI=10.1002/pro.349;
RA Elkins J.M., Gileadi C., Shrestha L., Phillips C., Wang J., Muniz J.R.,
RA Doyle D.A.;
RT "Unusual binding interactions in PDZ domain crystal structures help explain
RT binding mechanisms.";
RL Protein Sci. 19:731-741(2010).
RN [19]
RP X-RAY CRYSTALLOGRAPHY (2.10 ANGSTROMS) OF 1-84 BOUND TO PEPTIDE LIGAND,
RP SUBUNIT, AND DOMAIN.
RX PubMed=25158098; DOI=10.1016/j.jmb.2014.08.012;
RA Ernst A., Appleton B.A., Ivarsson Y., Zhang Y., Gfeller D., Wiesmann C.,
RA Sidhu S.S.;
RT "A structural portrait of the PDZ domain family.";
RL J. Mol. Biol. 426:3509-3519(2014).
CC -!- FUNCTION: [Isoform 1]: Suppresses SRC activation by recognizing and
CC binding to active SRC and facilitating PTPN13-mediated
CC dephosphorylation of SRC 'Tyr-419' leading to its inactivation.
CC Inactivated SRC dissociates from this protein allowing the initiation
CC of a new SRC inactivation cycle (PubMed:19307596). Involved in
CC reorganization of the actin cytoskeleton (PubMed:21636573). In
CC 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:0000269|PubMed:19307596, ECO:0000269|PubMed:21636573}.
CC -!- FUNCTION: [Isoform 2]: Involved in reorganization of the actin
CC cytoskeleton and in regulation of cell migration. In response to
CC oxidative stress, binds to NQO1, which stabilizes it and protects it
CC from ubiquitin-independent degradation by the core 20S proteasome.
CC Stabilized protein is able to heterodimerize with isoform 1 changing
CC the subcellular location of it from cytoskeleton and nuclei to cytosol,
CC leading to loss of isoforms 1 ability to induce formation of actin
CC stress fibers. Counteracts the effects produced by isoform 1 on
CC organization of actin cytoskeleton and cell motility to fine-tune actin
CC cytoskeleton rearrangement and to attenuate cell migration.
CC {ECO:0000269|PubMed:21636573}.
CC -!- SUBUNIT: Homodimer (PubMed:25158098). Interacts with PTPN13
CC (PubMed:19307596). Interacts (via C-terminus only or via combined C-
CC terminus and LIM domain, but not LIM domain only) with PTPN13 (via the
CC second or fourth PDZ domains). Found in a complex with PTPN13 and TRIP6
CC (By similarity). 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 (By similarity). Interacts directly with SRC
CC (via kinase domain and to a lesser extent the SH2 domain)
CC (PubMed:19307596). Isoform 2 interacts with NQO1. NQO1-stabilized
CC isoform 2 heterodimerizes with isoform 1 (PubMed:21636573).
CC {ECO:0000250|UniProtKB:P36202, ECO:0000250|UniProtKB:P70271,
CC ECO:0000269|PubMed:10826496, ECO:0000269|PubMed:19307596,
CC ECO:0000269|PubMed:21636573, ECO:0000269|PubMed:25158098}.
CC -!- INTERACTION:
CC P50479; P12814: ACTN1; NbExp=3; IntAct=EBI-372861, EBI-351710;
CC P50479; P48728-4: AMT; NbExp=5; IntAct=EBI-372861, EBI-14394829;
CC P50479; Q8WU58: FAM222B; NbExp=3; IntAct=EBI-372861, EBI-2807642;
CC P50479; O00560: SDCBP; NbExp=3; IntAct=EBI-372861, EBI-727004;
CC -!- SUBCELLULAR LOCATION: [Isoform 1]: Cytoplasm, cytoskeleton
CC {ECO:0000269|PubMed:21636573}. Nucleus {ECO:0000269|PubMed:10826496,
CC ECO:0000269|PubMed:21636573}. Cytoplasm {ECO:0000269|PubMed:21636573}.
CC Cytoplasm, perinuclear region {ECO:0000269|PubMed:19307596}. Cell
CC projection, lamellipodium {ECO:0000269|PubMed:10826496}. Cell
CC projection, dendritic spine {ECO:0000250|UniProtKB:P36202}. Early
CC endosome membrane {ECO:0000250|UniProtKB:P36202}; Peripheral membrane
CC protein {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}. Synapse, synaptosome
CC {ECO:0000250|UniProtKB:P36202}. Note=Localizes to actin stress fibers
CC in nonmuscle cells. Colocalizes with GRIA1 in early endosomes. Enriched
CC in numerous but not all spine-like structures along dendritic branches.
CC Colocalizes with actin and enriched at sites containing larger amounts
CC of actin and alpha-actinin. Targeted efficiently to spines via its PDZ
CC domain-mediated interaction with the alpha-actinin/actin cytoskeletal
CC complex. Localizes to synaptosomes in brain (By similarity).
CC Colocalizes with F-actin (PubMed:10826496). Colocalizes with TRIP6 at
CC cell-cell contacts and lamellipodia (PubMed:10826496). 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 (PubMed:21636573). Colocalizes with SRC at the perinuclear
CC region, but not at focal adhesions (PubMed:19307596).
CC {ECO:0000250|UniProtKB:P36202, ECO:0000269|PubMed:10826496,
CC ECO:0000269|PubMed:19307596, ECO:0000269|PubMed:21636573}.
CC -!- SUBCELLULAR LOCATION: [Isoform 2]: Cytoplasm
CC {ECO:0000269|PubMed:21636573}. Note=Stains more diffusely in the
CC cytoplasm with thin fibers forming a dense mesh-like pattern.
CC {ECO:0000269|PubMed:21636573}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=P50479-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P50479-2; Sequence=VSP_003124;
CC -!- TISSUE SPECIFICITY: [Isoform 2]: Found in brain.
CC {ECO:0000269|PubMed:9573374}.
CC -!- INDUCTION: [Isoform 2]: Expression is up-regulated by UV irradiation
CC and to a lesser extent by oxidative stress.
CC {ECO:0000269|PubMed:21636573}.
CC -!- PTM: Phosphorylated on tyrosine residue(s). Can be dephosphorylated by
CC PTPN13. {ECO:0000250|UniProtKB:P70271}.
CC -!- POLYMORPHISM: Genetic variations in PDLIM4 may be correlated with bone
CC mineral density (BMD). Low BMD is a risk factor for osteoporotic
CC fracture. Osteoporosis is characterized by reduced bone mineral
CC density, disruption of bone microarchitecture, and the alteration of
CC the amount and variety of non-collagenous proteins in bone.
CC Osteoporotic bones are more at risk of fracture.
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DR EMBL; X93510; CAA63767.1; -; mRNA.
DR EMBL; AF153882; AAD38070.1; -; mRNA.
DR EMBL; AF154335; AAD34646.1; -; mRNA.
DR EMBL; U82997; AAC52072.1; -; Genomic_DNA.
DR EMBL; AK313508; BAG36288.1; -; mRNA.
DR EMBL; BT007019; AAP35665.1; -; mRNA.
DR EMBL; CH471062; EAW62349.1; -; Genomic_DNA.
DR EMBL; CH471062; EAW62351.1; -; Genomic_DNA.
DR EMBL; BC003096; AAH03096.1; -; mRNA.
DR EMBL; BC016765; AAH16765.1; -; mRNA.
DR CCDS; CCDS4152.1; -. [P50479-1]
DR CCDS; CCDS47261.1; -. [P50479-2]
DR RefSeq; NP_001124499.1; NM_001131027.1. [P50479-2]
DR RefSeq; NP_003678.2; NM_003687.3. [P50479-1]
DR PDB; 2EEG; NMR; -; A=1-81.
DR PDB; 2V1W; X-ray; 1.90 A; A/B=1-85.
DR PDB; 4Q2O; X-ray; 2.10 A; A/B/C/D/E/F=1-84.
DR PDBsum; 2EEG; -.
DR PDBsum; 2V1W; -.
DR PDBsum; 4Q2O; -.
DR AlphaFoldDB; P50479; -.
DR SMR; P50479; -.
DR BioGRID; 114140; 21.
DR IntAct; P50479; 28.
DR MINT; P50479; -.
DR STRING; 9606.ENSP00000253754; -.
DR GlyGen; P50479; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; P50479; -.
DR PhosphoSitePlus; P50479; -.
DR BioMuta; PDLIM4; -.
DR DMDM; 20141642; -.
DR EPD; P50479; -.
DR jPOST; P50479; -.
DR MassIVE; P50479; -.
DR MaxQB; P50479; -.
DR PaxDb; P50479; -.
DR PeptideAtlas; P50479; -.
DR PRIDE; P50479; -.
DR ProteomicsDB; 56232; -. [P50479-1]
DR ProteomicsDB; 56233; -. [P50479-2]
DR Antibodypedia; 2128; 205 antibodies from 28 providers.
DR DNASU; 8572; -.
DR Ensembl; ENST00000253754.8; ENSP00000253754.3; ENSG00000131435.13. [P50479-1]
DR Ensembl; ENST00000379018.7; ENSP00000368303.3; ENSG00000131435.13. [P50479-2]
DR GeneID; 8572; -.
DR KEGG; hsa:8572; -.
DR MANE-Select; ENST00000253754.8; ENSP00000253754.3; NM_003687.4; NP_003678.2.
DR UCSC; uc003kwn.4; human. [P50479-1]
DR CTD; 8572; -.
DR DisGeNET; 8572; -.
DR GeneCards; PDLIM4; -.
DR HGNC; HGNC:16501; PDLIM4.
DR HPA; ENSG00000131435; Low tissue specificity.
DR MalaCards; PDLIM4; -.
DR MIM; 603422; gene.
DR neXtProt; NX_P50479; -.
DR OpenTargets; ENSG00000131435; -.
DR PharmGKB; PA134869796; -.
DR VEuPathDB; HostDB:ENSG00000131435; -.
DR eggNOG; KOG1703; Eukaryota.
DR GeneTree; ENSGT00940000159536; -.
DR HOGENOM; CLU_038114_1_1_1; -.
DR InParanoid; P50479; -.
DR OMA; QYNNPTR; -.
DR OrthoDB; 840552at2759; -.
DR PhylomeDB; P50479; -.
DR TreeFam; TF106408; -.
DR PathwayCommons; P50479; -.
DR SignaLink; P50479; -.
DR BioGRID-ORCS; 8572; 8 hits in 1075 CRISPR screens.
DR ChiTaRS; PDLIM4; human.
DR EvolutionaryTrace; P50479; -.
DR GeneWiki; PDLIM4; -.
DR GenomeRNAi; 8572; -.
DR Pharos; P50479; Tbio.
DR PRO; PR:P50479; -.
DR Proteomes; UP000005640; Chromosome 5.
DR RNAct; P50479; protein.
DR Bgee; ENSG00000131435; Expressed in lower esophagus muscularis layer and 168 other tissues.
DR ExpressionAtlas; P50479; baseline and differential.
DR Genevisible; P50479; HS.
DR GO; GO:0005912; C:adherens junction; IBA:GO_Central.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005856; C:cytoskeleton; IDA:UniProtKB.
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; IDA:UniProtKB.
DR GO; GO:0030027; C:lamellipodium; IDA:UniProtKB.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:UniProtKB.
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; 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: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; IDA:UniProtKB.
DR GO; GO:0019903; F:protein phosphatase binding; IPI:UniProtKB.
DR GO; GO:0030036; P:actin cytoskeleton organization; IBA:GO_Central.
DR GO; GO:0031532; P:actin cytoskeleton reorganization; IDA:UniProtKB.
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 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 3D-structure; Alternative splicing; Cell projection; Cytoplasm;
KW Cytoskeleton; Endosome; LIM domain; Membrane; Metal-binding; Nucleus;
KW Phosphoprotein; Reference proteome; Synapse; Synaptosome; Zinc.
FT CHAIN 1..330
FT /note="PDZ and LIM domain protein 4"
FT /id="PRO_0000075873"
FT DOMAIN 1..84
FT /note="PDZ"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00143,
FT ECO:0000269|PubMed:25158098, ECO:0007744|PDB:4Q2O"
FT DOMAIN 253..312
FT /note="LIM zinc-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00125"
FT REGION 104..180
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 151..165
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 112
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569"
FT MOD_RES 116
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P70271"
FT MOD_RES 120
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P70271"
FT MOD_RES 135
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P36202"
FT VAR_SEQ 225..330
FT /note="DWPGPGGPRNLKPTASKLGAPLSGLQGLPECTRCGHGIVGTIVKARDKLYHP
FT ECFMCSDCGLNLKQRGYFFLDERLYCESHAKARVKPPEGYDVVAVYPNAKVELV -> A
FT PSSRHGTSSTIPSASCAVTAA (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334, ECO:0000303|Ref.5"
FT /id="VSP_003124"
FT VARIANT 118
FT /note="R -> G (in dbSNP:rs17851430)"
FT /evidence="ECO:0000269|PubMed:15489334"
FT /id="VAR_035205"
FT VARIANT 142
FT /note="R -> C (in dbSNP:rs1050805)"
FT /evidence="ECO:0000269|Ref.1"
FT /id="VAR_050167"
FT VARIANT 184
FT /note="V -> I (in dbSNP:rs175218)"
FT /id="VAR_035206"
FT VARIANT 259
FT /note="G -> C (in dbSNP:rs4877)"
FT /evidence="ECO:0000269|Ref.1"
FT /id="VAR_035207"
FT CONFLICT 20
FT /note="Missing (in Ref. 1; CAA63767)"
FT /evidence="ECO:0000305"
FT CONFLICT 39
FT /note="A -> S (in Ref. 1; CAA63767)"
FT /evidence="ECO:0000305"
FT CONFLICT 139
FT /note="Q -> K (in Ref. 1; CAA63767)"
FT /evidence="ECO:0000305"
FT CONFLICT 174..182
FT /note="RGLPRSRDC -> EASRGAGS (in Ref. 1; CAA63767)"
FT /evidence="ECO:0000305"
FT CONFLICT 269
FT /note="A -> E (in Ref. 1; CAA63767)"
FT /evidence="ECO:0000305"
FT STRAND 3..11
FT /evidence="ECO:0007829|PDB:2V1W"
FT STRAND 15..20
FT /evidence="ECO:0007829|PDB:2V1W"
FT HELIX 21..23
FT /evidence="ECO:0007829|PDB:2V1W"
FT STRAND 25..32
FT /evidence="ECO:0007829|PDB:2V1W"
FT STRAND 34..36
FT /evidence="ECO:0007829|PDB:2EEG"
FT HELIX 37..40
FT /evidence="ECO:0007829|PDB:2V1W"
FT STRAND 48..52
FT /evidence="ECO:0007829|PDB:2V1W"
FT TURN 57..59
FT /evidence="ECO:0007829|PDB:2EEG"
FT HELIX 62..70
FT /evidence="ECO:0007829|PDB:2V1W"
FT STRAND 74..81
FT /evidence="ECO:0007829|PDB:2V1W"
SQ SEQUENCE 330 AA; 35398 MW; 68FCA8FD93700E7B CRC64;
MPHSVTLRGP SPWGFRLVGG RDFSAPLTIS RVHAGSKAAL AALCPGDLIQ AINGESTELM
THLEAQNRIK GCHDHLTLSV SRPEGRSWPS APDDSKAQAH RIHIDPEIQD GSPTTSRRPS
GTGTGPEDGR PSLGSPYGQP PRFPVPHNGS SEATLPAQMS TLHVSPPPSA DPARGLPRSR
DCRVDLGSEV YRMLREPAEP VAAEPKQSGS FRYLQGMLEA GEGGDWPGPG GPRNLKPTAS
KLGAPLSGLQ GLPECTRCGH GIVGTIVKAR DKLYHPECFM CSDCGLNLKQ RGYFFLDERL
YCESHAKARV KPPEGYDVVA VYPNAKVELV
