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PDZ and LIM domain protein 4 (LIM protein RIL) (Reversion-induced LIM protein)

 PDLI4_HUMAN             Reviewed;         330 AA.
P50479; B2R8U1; Q53Y39; Q96AT8; Q9BTW8; Q9Y292;
01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
23-JAN-2002, sequence version 2.
20-DEC-2017, entry version 157.
RecName: Full=PDZ and LIM domain protein 4;
AltName: Full=LIM protein RIL;
AltName: Full=Reversion-induced LIM protein;
Name=PDLIM4; Synonyms=RIL;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE (ISOFORM 1), AND VARIANTS CYS-142 AND CYS-259.
TISSUE=Lung;
Scharm B., Schaefer R.;
Submitted (OCT-1995) to the EMBL/GenBank/DDBJ databases.
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORMS 1 AND 2), AND TISSUE
SPECIFICITY (ISOFORM 2).
PubMed=9573374; DOI=10.1016/S0378-1119(98)00080-8;
Bashirova A.A., Markelov M.L., Shlykova T.V., Levshenkova E.V.,
Alibaeva R.A., Frolova E.I.;
"The human RIL gene: mapping to human chromosome 5q31.1, genomic
organization and alternative transcripts.";
Gene 210:239-245(1998).
[3]
NUCLEOTIDE SEQUENCE (ISOFORM 1).
Bashirova A.A., Markelov M.L., Levshenkova E.V., Shelkunova M.A.,
Frolova E.I.;
Submitted (MAY-1999) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
Phelan M., Farmer A.;
"Cloning of human full-length CDSs in BD Creator(TM) system donor
vector.";
Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2), AND VARIANT
GLY-118.
TISSUE=Bone marrow, and Brain;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[8]
INTERACTION WITH TRIP6, AND SUBCELLULAR LOCATION.
PubMed=10826496; DOI=10.1078/S0171-9335(04)70031-X;
Cuppen E., van Ham M., Wansink D.G., de Leeuw A., Wieringa B.,
Hendriks W.;
"The zyxin-related protein TRIP6 interacts with PDZ motifs in the
adaptor protein RIL and the protein tyrosine phosphatase PTP-BL.";
Eur. J. Cell Biol. 79:283-293(2000).
[9]
INVOLVEMENT IN BMD.
PubMed=12908099; DOI=10.1007/s10038-003-0035-1;
Omasu F., Ezura Y., Kajita M., Ishida R., Kodaira M., Yoshida H.,
Suzuki T., Hosoi T., Inoue S., Shiraki M., Orimo H., Emi M.;
"Association of genetic variation of the RIL gene, encoding a PDZ-LIM
domain protein and localized in 5q31.1, with low bone mineral density
in adult Japanese women.";
J. Hum. Genet. 48:342-345(2003).
[10]
FUNCTION, INTERACTION WITH PTPN13 AND SRC, AND SUBCELLULAR LOCATION.
PubMed=19307596; DOI=10.1083/jcb.200810155;
Zhang Y., Tu Y., Zhao J., Chen K., Wu C.;
"Reversion-induced LIM interaction with Src reveals a novel Src
inactivation cycle.";
J. Cell Biol. 184:785-792(2009).
[11]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19369195; DOI=10.1074/mcp.M800588-MCP200;
Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,
Mann M., Daub H.;
"Large-scale proteomics analysis of the human kinome.";
Mol. Cell. Proteomics 8:1751-1764(2009).
[12]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[13]
IDENTIFICATION BY MASS SPECTROMETRY (ISOFORM 2), FUNCTION (ISOFORMS 1
AND 2), INTERACTION WITH NQO1 (ISOFORMS 1 AND 2), SUBCELLULAR LOCATION
(ISOFORMS 1 AND 2), AND INDUCTION (ISOFORM 2).
PubMed=21636573; DOI=10.1074/jbc.M111.241554;
Guryanova O.A., Drazba J.A., Frolova E.I., Chumakov P.M.;
"Actin cytoskeleton remodeling by the alternatively spliced isoform of
PDLIM4/RIL protein.";
J. Biol. Chem. 286:26849-26859(2011).
[14]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-112, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21406692; DOI=10.1126/scisignal.2001570;
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
Blagoev B.;
"System-wide temporal characterization of the proteome and
phosphoproteome of human embryonic stem cell differentiation.";
Sci. Signal. 4:RS3-RS3(2011).
[15]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-112, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[16]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-112, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[17]
STRUCTURE BY NMR OF 1-81.
RIKEN structural genomics initiative (RSGI);
"Solution structure of PDZ domain of PDZ and LIM domain protein.";
Submitted (AUG-2007) to the PDB data bank.
[18]
X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) OF 1-85 BOUND TO C-TERMINAL
PEPTIDE OF ACTN1.
PubMed=20120020; DOI=10.1002/pro.349;
Elkins J.M., Gileadi C., Shrestha L., Phillips C., Wang J.,
Muniz J.R., Doyle D.A.;
"Unusual binding interactions in PDZ domain crystal structures help
explain binding mechanisms.";
Protein Sci. 19:731-741(2010).
[19]
X-RAY CRYSTALLOGRAPHY (2.10 ANGSTROMS) OF 1-84 BOUND TO PEPTIDE
LIGAND, SUBUNIT, AND DOMAIN.
PubMed=25158098; DOI=10.1016/j.jmb.2014.08.012;
Ernst A., Appleton B.A., Ivarsson Y., Zhang Y., Gfeller D.,
Wiesmann C., Sidhu S.S.;
"A structural portrait of the PDZ domain family.";
J. Mol. Biol. 426:3509-3519(2014).
-!- FUNCTION: Isoform 1: 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 (PubMed:19307596).
Involved in reorganization of the actin cytoskeleton
(PubMed:21636573). 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:0000269|PubMed:19307596, ECO:0000269|PubMed:21636573}.
-!- FUNCTION: Isoform 2: Involved in reorganization of the actin
cytoskeleton and in regulation of cell migration. In response to
oxidative stress, binds to NQO1, which stabilizes it and protects
it from ubiquitin-independent degradation by the core 20S
proteasome. Stabilized protein is able to heterodimerize with
isoform 1 changing the subcellular location of it from
cytoskeleton and nuclei to cytosol, leading to loss of isoforms 1
ability to induce formation of actin stress fibers. Counteracts
the effects produced by isoform 1 on organization of actin
cytoskeleton and cell motility to fine-tune actin cytoskeleton
rearrangement and to attenuate cell migration.
{ECO:0000269|PubMed:21636573}.
-!- SUBUNIT: Homodimer (PubMed:25158098). Interacts with PTPN13
(PubMed:19307596). Interacts (via C-terminus only or via combined
C-terminus and LIM domain, but not LIM domain only) with PTPN13
(via the second or fourth PDZ domains). Found in a complex with
PTPN13 and TRIP6 (By similarity). Interacts (via PDZ domain) with
ACTN1 and ACTN2 (via C-terminal SDL residues) (By similarity).
Interacts (via PDZ domain) with TRIP6 (via the second LIM domain
or via the third LIM domain plus C-terminus) (PubMed:10826496).
Interacts (via LIM domain) with GRIA1 (via C-terminus); this
interaction as well as the interaction with alpha-actinin is
required for their colocalization in early endosomes. Interacts
with PDLIM1 (By similarity). Forms (via LIM domain) a heterodimer
with PDLIM3 (By similarity). Interacts directly with SRC (via
kinase domain and to a lesser extent the SH2 domain)
(PubMed:19307596). Isoform 2 interacts with NQO1. NQO1-stabilized
isoform 2 heterodimerizes with isoform 1 (PubMed:21636573).
{ECO:0000250|UniProtKB:P36202, ECO:0000250|UniProtKB:P70271,
ECO:0000269|PubMed:10826496, ECO:0000269|PubMed:19307596,
ECO:0000269|PubMed:21636573, ECO:0000269|PubMed:25158098}.
-!- INTERACTION:
P48728-4:AMT; NbExp=4; IntAct=EBI-372861, EBI-14394829;
-!- SUBCELLULAR LOCATION: Isoform 1: Cytoplasm, cytoskeleton
{ECO:0000269|PubMed:21636573}. Nucleus
{ECO:0000269|PubMed:10826496, ECO:0000269|PubMed:21636573}.
Cytoplasm {ECO:0000269|PubMed:21636573}. Cytoplasm, perinuclear
region {ECO:0000269|PubMed:19307596}. Cell projection,
lamellipodium {ECO:0000269|PubMed:10826496}. 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}. Cell junction, 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 (PubMed:10826496). Colocalizes with TRIP6
at cell-cell contacts and lamellipodia (PubMed:10826496). 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 (PubMed:21636573). Colocalizes with SRC at the
perinuclear region, but not at focal adhesions (PubMed:19307596).
{ECO:0000250|UniProtKB:P36202, ECO:0000269|PubMed:10826496,
ECO:0000269|PubMed:19307596, ECO:0000269|PubMed:21636573}.
-!- SUBCELLULAR LOCATION: Isoform 2: Cytoplasm
{ECO:0000269|PubMed:21636573}. Note=Stains more diffusely in the
cytoplasm with thin fibers forming a dense mesh-like pattern.
{ECO:0000269|PubMed:21636573}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=P50479-1; Sequence=Displayed;
Name=2;
IsoId=P50479-2; Sequence=VSP_003124;
-!- TISSUE SPECIFICITY: Isoform 2 is found in brain.
{ECO:0000269|PubMed:9573374}.
-!- INDUCTION: Isoform 2 expression is up-regulated by UV irradiation
and to a lesser extent by oxidative stress.
{ECO:0000269|PubMed:21636573}.
-!- PTM: Phosphorylated on tyrosine residue(s). Can be
dephosphorylated by PTPN13. {ECO:0000250|UniProtKB:P70271}.
-!- POLYMORPHISM: Genetic variations in PDLIM4 may be correlated with
bone mineral density (BMD). Low BMD is a risk factor for
osteoporotic fracture. Osteoporosis is characterized by reduced
bone mineral density, disruption of bone microarchitecture, and
the alteration of the amount and variety of non-collagenous
proteins in bone. Osteoporotic bones are more at risk of fracture.
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EMBL; X93510; CAA63767.1; -; mRNA.
EMBL; AF153882; AAD38070.1; -; mRNA.
EMBL; AF154335; AAD34646.1; -; mRNA.
EMBL; U82997; AAC52072.1; -; Genomic_DNA.
EMBL; AK313508; BAG36288.1; -; mRNA.
EMBL; BT007019; AAP35665.1; -; mRNA.
EMBL; CH471062; EAW62349.1; -; Genomic_DNA.
EMBL; CH471062; EAW62351.1; -; Genomic_DNA.
EMBL; BC003096; AAH03096.1; -; mRNA.
EMBL; BC016765; AAH16765.1; -; mRNA.
CCDS; CCDS4152.1; -. [P50479-1]
CCDS; CCDS47261.1; -. [P50479-2]
RefSeq; NP_001124499.1; NM_001131027.1. [P50479-2]
RefSeq; NP_003678.2; NM_003687.3. [P50479-1]
UniGene; Hs.424312; -.
PDB; 2EEG; NMR; -; A=1-81.
PDB; 2V1W; X-ray; 1.90 A; A/B=1-85.
PDB; 4Q2O; X-ray; 2.10 A; A/B/C/D/E/F=1-84.
PDBsum; 2EEG; -.
PDBsum; 2V1W; -.
PDBsum; 4Q2O; -.
ProteinModelPortal; P50479; -.
SMR; P50479; -.
BioGrid; 114140; 4.
IntAct; P50479; 15.
MINT; MINT-1437771; -.
STRING; 9606.ENSP00000253754; -.
iPTMnet; P50479; -.
PhosphoSitePlus; P50479; -.
BioMuta; PDLIM4; -.
DMDM; 20141642; -.
EPD; P50479; -.
MaxQB; P50479; -.
PaxDb; P50479; -.
PeptideAtlas; P50479; -.
PRIDE; P50479; -.
DNASU; 8572; -.
Ensembl; ENST00000253754; ENSP00000253754; ENSG00000131435. [P50479-1]
Ensembl; ENST00000379018; ENSP00000368303; ENSG00000131435. [P50479-2]
GeneID; 8572; -.
KEGG; hsa:8572; -.
UCSC; uc003kwn.4; human. [P50479-1]
CTD; 8572; -.
DisGeNET; 8572; -.
EuPathDB; HostDB:ENSG00000131435.12; -.
GeneCards; PDLIM4; -.
HGNC; HGNC:16501; PDLIM4.
HPA; HPA011912; -.
MalaCards; PDLIM4; -.
MIM; 603422; gene.
neXtProt; NX_P50479; -.
OpenTargets; ENSG00000131435; -.
PharmGKB; PA134869796; -.
eggNOG; KOG1703; Eukaryota.
eggNOG; ENOG410XRD4; LUCA.
GeneTree; ENSGT00590000082980; -.
HOGENOM; HOG000290704; -.
HOVERGEN; HBG061371; -.
InParanoid; P50479; -.
OMA; HIDPEAQ; -.
OrthoDB; EOG091G0A6C; -.
PhylomeDB; P50479; -.
TreeFam; TF106408; -.
EvolutionaryTrace; P50479; -.
GeneWiki; PDLIM4; -.
GenomeRNAi; 8572; -.
PRO; PR:P50479; -.
Proteomes; UP000005640; Chromosome 5.
Bgee; ENSG00000131435; -.
CleanEx; HS_PDLIM4; -.
ExpressionAtlas; P50479; baseline and differential.
Genevisible; P50479; HS.
GO; GO:0030054; C:cell junction; IEA:UniProtKB-KW.
GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
GO; GO:0005856; C:cytoskeleton; IDA:UniProtKB.
GO; GO:0043197; C:dendritic spine; ISS:UniProtKB.
GO; GO:0031905; C:early endosome lumen; ISS:UniProtKB.
GO; GO:0031901; C:early endosome membrane; IEA:UniProtKB-SubCell.
GO; GO:0031941; C:filamentous actin; IDA:UniProtKB.
GO; GO:0030027; C:lamellipodium; IDA:UniProtKB.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:UniProtKB.
GO; GO:0045211; C:postsynaptic membrane; ISS:UniProtKB.
GO; GO:0034777; C:recycling endosome lumen; ISS:UniProtKB.
GO; GO:0055038; C:recycling endosome membrane; IEA:UniProtKB-SubCell.
GO; GO:0001725; C:stress fiber; IDA:UniProtKB.
GO; GO:0051393; F:alpha-actinin binding; IPI:UniProtKB.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0042803; F:protein homodimerization activity; IDA:UniProtKB.
GO; GO:0019903; F:protein phosphatase binding; IPI:UniProtKB.
GO; GO:0031532; P:actin cytoskeleton reorganization; IDA:UniProtKB.
GO; GO:0098976; P:excitatory chemical synaptic transmission; ISS:UniProtKB.
InterPro; IPR031847; DUF4749.
InterPro; IPR001478; PDZ.
InterPro; IPR036034; PDZ_sf.
InterPro; IPR001781; Znf_LIM.
Pfam; PF15936; DUF4749; 1.
Pfam; PF00412; LIM; 1.
Pfam; PF00595; PDZ; 1.
SMART; SM00132; LIM; 1.
SMART; SM00228; PDZ; 1.
SUPFAM; SSF50156; SSF50156; 1.
PROSITE; PS00478; LIM_DOMAIN_1; 1.
PROSITE; PS50023; LIM_DOMAIN_2; 1.
PROSITE; PS50106; PDZ; 1.
1: Evidence at protein level;
3D-structure; Alternative splicing; Cell junction; Cell projection;
Complete proteome; Cytoplasm; Cytoskeleton; Endosome; LIM domain;
Membrane; Metal-binding; Nucleus; Phosphoprotein; Polymorphism;
Reference proteome; Synapse; Synaptosome; Zinc.
CHAIN 1 330 PDZ and LIM domain protein 4.
/FTId=PRO_0000075873.
DOMAIN 1 84 PDZ. {ECO:0000244|PDB:4Q2O,
ECO:0000255|PROSITE-ProRule:PRU00143,
ECO:0000269|PubMed:25158098}.
DOMAIN 253 312 LIM zinc-binding. {ECO:0000255|PROSITE-
ProRule:PRU00125}.
MOD_RES 112 112 Phosphoserine.
{ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163,
ECO:0000244|PubMed:24275569}.
MOD_RES 116 116 Phosphoserine.
{ECO:0000250|UniProtKB:P70271}.
MOD_RES 120 120 Phosphoserine.
{ECO:0000250|UniProtKB:P70271}.
MOD_RES 135 135 Phosphoserine.
{ECO:0000250|UniProtKB:P36202}.
VAR_SEQ 225 330 DWPGPGGPRNLKPTASKLGAPLSGLQGLPECTRCGHGIVGT
IVKARDKLYHPECFMCSDCGLNLKQRGYFFLDERLYCESHA
KARVKPPEGYDVVAVYPNAKVELV -> APSSRHGTSSTIP
SASCAVTAA (in isoform 2).
{ECO:0000303|PubMed:15489334,
ECO:0000303|Ref.5}.
/FTId=VSP_003124.
VARIANT 118 118 R -> G (in dbSNP:rs17851430).
{ECO:0000269|PubMed:15489334}.
/FTId=VAR_035205.
VARIANT 142 142 R -> C (in dbSNP:rs1050805).
{ECO:0000269|Ref.1}.
/FTId=VAR_050167.
VARIANT 184 184 V -> I (in dbSNP:rs175218).
/FTId=VAR_035206.
VARIANT 259 259 G -> C (in dbSNP:rs4877).
{ECO:0000269|Ref.1}.
/FTId=VAR_035207.
CONFLICT 20 20 Missing (in Ref. 1; CAA63767).
{ECO:0000305}.
CONFLICT 39 39 A -> S (in Ref. 1; CAA63767).
{ECO:0000305}.
CONFLICT 139 139 Q -> K (in Ref. 1; CAA63767).
{ECO:0000305}.
CONFLICT 174 182 RGLPRSRDC -> EASRGAGS (in Ref. 1;
CAA63767). {ECO:0000305}.
CONFLICT 269 269 A -> E (in Ref. 1; CAA63767).
{ECO:0000305}.
STRAND 3 11 {ECO:0000244|PDB:2V1W}.
STRAND 15 20 {ECO:0000244|PDB:2V1W}.
HELIX 21 23 {ECO:0000244|PDB:2V1W}.
STRAND 25 32 {ECO:0000244|PDB:2V1W}.
STRAND 34 36 {ECO:0000244|PDB:2EEG}.
HELIX 37 40 {ECO:0000244|PDB:2V1W}.
STRAND 48 52 {ECO:0000244|PDB:2V1W}.
TURN 57 59 {ECO:0000244|PDB:2EEG}.
HELIX 62 70 {ECO:0000244|PDB:2V1W}.
STRAND 74 81 {ECO:0000244|PDB:2V1W}.
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


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