PDLI5_RAT
ID PDLI5_RAT Reviewed; 591 AA.
AC Q62920;
DT 24-MAY-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1999, sequence version 2.
DT 03-AUG-2022, entry version 160.
DE RecName: Full=PDZ and LIM domain protein 5;
DE AltName: Full=Enigma homolog {ECO:0000303|PubMed:8940095};
DE AltName: Full=Enigma-like PDZ and LIM domains protein {ECO:0000303|PubMed:8940095};
GN Name=Pdlim5; Synonyms=Enh {ECO:0000303|PubMed:8940095};
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] (ISOFORM 1), SUBCELLULAR LOCATION, INTERACTION
RP WITH PKC, AND TISSUE SPECIFICITY.
RC STRAIN=Sprague-Dawley; TISSUE=Brain;
RX PubMed=8940095; DOI=10.1074/jbc.271.49.31029;
RA Kuroda S., Tokunaga C., Kiyohara Y., Higuchi O., Konishi H., Mizuno K.,
RA Gill G.N., Kikkawa U.;
RT "Protein-protein interaction of zinc finger LIM domains with protein kinase
RT C.";
RL J. Biol. Chem. 271:31029-31032(1996).
RN [2]
RP INTERACTION WITH ACTIN AND ALPHA-ACTININ.
RX PubMed=10833443; DOI=10.1006/bbrc.2000.2787;
RA Nakagawa N., Hoshijima M., Oyasu M., Saito N., Tanizawa K., Kuroda S.;
RT "ENH, containing PDZ and LIM domains, heart/skeletal muscle-specific
RT protein, associates with cytoskeletal proteins through the PDZ domain.";
RL Biochem. Biophys. Res. Commun. 272:505-512(2000).
RN [3]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=16641100; DOI=10.1073/pnas.0600895103;
RA Hoffert J.D., Pisitkun T., Wang G., Shen R.-F., Knepper M.A.;
RT "Quantitative phosphoproteomics of vasopressin-sensitive renal cells:
RT regulation of aquaporin-2 phosphorylation at two sites.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:7159-7164(2006).
RN [4]
RP FUNCTION, SUBCELLULAR LOCATION, ALTERNATIVE SPLICING, AND TISSUE
RP SPECIFICITY.
RX PubMed=20097676; DOI=10.1093/cvr/cvq023;
RA Yamazaki T., Walchli S., Fujita T., Ryser S., Hoshijima M., Schlegel W.,
RA Kuroda S., Maturana A.D.;
RT "Splice variants of Enigma homolog, differentially expressed during heart
RT development, promote or prevent hypertrophy.";
RL Cardiovasc. Res. 86:374-382(2010).
RN [5]
RP FUNCTION, SUBCELLULAR LOCATION (ISOFORMS 1 AND 2), ALTERNATIVE SPLICING
RP (ISOFORMS 1 AND 2), INTERACTION WITH SIPA1L1, TISSUE SPECIFICITY, AND
RP DEVELOPMENTAL STAGE.
RX PubMed=19900557; DOI=10.1016/j.mcn.2009.10.009;
RA Herrick S., Evers D.M., Lee J.Y., Udagawa N., Pak D.T.;
RT "Postsynaptic PDLIM5/Enigma homolog binds SPAR and causes dendritic spine
RT shrinkage.";
RL Mol. Cell. Neurosci. 43:188-200(2010).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2; SER-228; SER-318 AND
RP SER-355, 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: May play an important role in the heart development by
CC scaffolding PKC to the Z-disk region (PubMed:8940095, PubMed:20097676).
CC May play a role in the regulation of cardiomyocyte expansion
CC (PubMed:20097676). Isoforms lacking the LIM domains may negatively
CC modulate the scaffolding activity of isoform 1 (PubMed:20097676).
CC Overexpression promotes the development of heart hypertrophy.
CC Contributes to the regulation of dendritic spine morphogenesis in
CC neurons (PubMed:20097676). May be required to restrain postsynaptic
CC growth of excitatory synapses. Isoform 1, but not isoform 2, expression
CC favors spine thinning and elongation (PubMed:19900557).
CC {ECO:0000269|PubMed:19900557, ECO:0000269|PubMed:20097676,
CC ECO:0000269|PubMed:8940095}.
CC -!- SUBUNIT: Interacts with various PKC isoforms through the LIM domains
CC (PubMed:8940095). Interacts with actin and alpha-actinin through the
CC PDZ domain (PubMed:10833443). Interacts (via LIM domains) with
CC SIPA1L1/SPAR; this interaction may occur preferentially with isoform 1
CC (PubMed:19900557). {ECO:0000269|PubMed:10833443,
CC ECO:0000269|PubMed:19900557, ECO:0000269|PubMed:8940095}.
CC -!- INTERACTION:
CC Q62920; P68403-1: Prkcb; NbExp=5; IntAct=EBI-918433, EBI-12559950;
CC -!- SUBCELLULAR LOCATION: [Isoform 1]: Postsynaptic density
CC {ECO:0000269|PubMed:19900557}. Presynapse
CC {ECO:0000269|PubMed:19900557}. Postsynapse
CC {ECO:0000269|PubMed:19900557}. Cytoplasm, cytosol
CC {ECO:0000269|PubMed:19900557}. Note=Detected both at presynaptic and
CC postsynaptic sites, exclusively at excitatory synapses, but not
CC inhibitory synapses, in hippocampal neurons.
CC {ECO:0000269|PubMed:19900557}.
CC -!- SUBCELLULAR LOCATION: [Isoform 2]: Postsynaptic density
CC {ECO:0000269|PubMed:19900557}. Presynapse
CC {ECO:0000269|PubMed:19900557}. Postsynapse
CC {ECO:0000269|PubMed:19900557}. Cytoplasm, cytosol
CC {ECO:0000269|PubMed:19900557}. Note=Detected both at presynaptic and
CC postsynaptic sites, exclusively at excitatory synapses, but not
CC inhibitory synapses, in hippocampal neurons.
CC {ECO:0000269|PubMed:19900557}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1; Synonyms=PDLIM5a {ECO:0000303|PubMed:19900557};
CC IsoId=Q62920-1; Sequence=Displayed;
CC Name=2; Synonyms=PDLIM5b {ECO:0000303|PubMed:19900557};
CC IsoId=Q62920-2; Sequence=VSP_058746;
CC -!- TISSUE SPECIFICITY: Detected in brain, in neurons, including in
CC hippocampal neurons, and glial cells (at protein level). Detected in
CC heart and skeletal muscle. {ECO:0000269|PubMed:19900557,
CC ECO:0000269|PubMed:20097676, ECO:0000269|PubMed:8940095}.
CC -!- DEVELOPMENTAL STAGE: In cultured hippocampal neurons, expression levels
CC of both isoform 1 and isoform 2 increases with in vitro development,
CC with prominent expression coinciding with the completion of
CC synaptogenesis and persisting through mature stages.
CC {ECO:0000269|PubMed:19900557}.
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DR EMBL; U48247; AAC72251.1; -; mRNA.
DR RefSeq; NP_445778.1; NM_053326.1. [Q62920-1]
DR RefSeq; XP_006233481.1; XM_006233419.3. [Q62920-2]
DR AlphaFoldDB; Q62920; -.
DR SMR; Q62920; -.
DR IntAct; Q62920; 4.
DR STRING; 10116.ENSRNOP00000022387; -.
DR iPTMnet; Q62920; -.
DR PhosphoSitePlus; Q62920; -.
DR jPOST; Q62920; -.
DR PaxDb; Q62920; -.
DR PRIDE; Q62920; -.
DR GeneID; 64353; -.
DR KEGG; rno:64353; -.
DR CTD; 10611; -.
DR RGD; 621076; Pdlim5.
DR VEuPathDB; HostDB:ENSRNOG00000016419; -.
DR eggNOG; KOG1703; Eukaryota.
DR HOGENOM; CLU_001357_8_1_1; -.
DR InParanoid; Q62920; -.
DR OMA; QDTFVQR; -.
DR OrthoDB; 1013114at2759; -.
DR PhylomeDB; Q62920; -.
DR PRO; PR:Q62920; -.
DR Proteomes; UP000002494; Chromosome 2.
DR Bgee; ENSRNOG00000016419; Expressed in quadriceps femoris and 19 other tissues.
DR Genevisible; Q62920; RN.
DR GO; GO:0005912; C:adherens junction; IBA:GO_Central.
DR GO; GO:0042995; C:cell projection; IEA:UniProtKB-KW.
DR GO; GO:0005829; C:cytosol; IDA:UniProtKB.
DR GO; GO:0031941; C:filamentous actin; IBA:GO_Central.
DR GO; GO:0016020; C:membrane; IDA:UniProtKB.
DR GO; GO:0014069; C:postsynaptic density; IDA:UniProtKB.
DR GO; GO:0098793; C:presynapse; IEA:UniProtKB-SubCell.
DR GO; GO:0001725; C:stress fiber; IBA:GO_Central.
DR GO; GO:0030018; C:Z disc; ISO:RGD.
DR GO; GO:0003779; F:actin binding; IDA:UniProtKB.
DR GO; GO:0042805; F:actinin binding; IDA: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:0005080; F:protein kinase C binding; IDA:UniProtKB.
DR GO; GO:0047485; F:protein N-terminus binding; IMP:RGD.
DR GO; GO:0030159; F:signaling receptor complex adaptor activity; NAS:UniProtKB.
DR GO; GO:0030036; P:actin cytoskeleton organization; IBA:GO_Central.
DR GO; GO:0061049; P:cell growth involved in cardiac muscle cell development; IGI:BHF-UCL.
DR GO; GO:0007507; P:heart development; IBA:GO_Central.
DR GO; GO:0061061; P:muscle structure development; IBA:GO_Central.
DR GO; GO:0061001; P:regulation of dendritic spine morphogenesis; IDA:UniProtKB.
DR GO; GO:0051963; P:regulation of synapse 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; 3.
DR Pfam; PF00595; PDZ; 1.
DR SMART; SM00132; LIM; 3.
DR SMART; SM00228; PDZ; 1.
DR SUPFAM; SSF50156; SSF50156; 1.
DR PROSITE; PS00478; LIM_DOMAIN_1; 2.
DR PROSITE; PS50023; LIM_DOMAIN_2; 3.
DR PROSITE; PS50106; PDZ; 1.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; Cell projection; Cytoplasm;
KW Isopeptide bond; LIM domain; Metal-binding; Phosphoprotein;
KW Reference proteome; Repeat; Synapse; Ubl conjugation; Zinc.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:Q96HC4"
FT CHAIN 2..591
FT /note="PDZ and LIM domain protein 5"
FT /id="PRO_0000075879"
FT DOMAIN 2..85
FT /note="PDZ"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00143"
FT DOMAIN 413..472
FT /note="LIM zinc-binding 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00125"
FT DOMAIN 472..531
FT /note="LIM zinc-binding 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00125"
FT DOMAIN 531..591
FT /note="LIM zinc-binding 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00125"
FT REGION 125..240
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 255..334
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 348..398
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 135..158
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 177..196
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 207..235
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 255..274
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 305..328
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 348..381
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0000250|UniProtKB:Q96HC4"
FT MOD_RES 2
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 89
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q8CI51"
FT MOD_RES 89
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q8CI51"
FT MOD_RES 111
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96HC4"
FT MOD_RES 134
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96HC4"
FT MOD_RES 137
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96HC4"
FT MOD_RES 228
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 260
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96HC4"
FT MOD_RES 313
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96HC4"
FT MOD_RES 318
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 346
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q8CI51"
FT MOD_RES 355
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 357
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96HC4"
FT CROSSLNK 89
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0000250|UniProtKB:Q96HC4"
FT VAR_SEQ 98..206
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:19900557"
FT /id="VSP_058746"
SQ SEQUENCE 591 AA; 63201 MW; 7B26FB9BE1680299 CRC64;
MSNYNVSLVG PAPWGFRLQG GKDFNMPLTI SSLKDGGKAS QAHVRIGDVV LSIDGISAQG
MTHLEAQNKI KACTGSLNMT LQRASAAAKS EPVAVQKGEP KEVVKPVPIT SPAVSKVTST
TNMAYNKVPR PFGSVSSPKV TSIPSPSSAF TPAHAATSSH ASPPPVAAVT PPPLSASGLH
ASANPSAAQC SSPPNTGKPA VHVPRQPTVT SVCSESAQEL AEGQRRGSQG DIKQQNGPPR
KHIVERNTEF YHIPTHSDAS KKRLIEDTED WRPRTGTTQS RSFRILAQIT GTEHLKESEN
DNAKKANSTP EPSQQSASPL SAAESLESPG SNRPVVAGLR SAAAFKPVGS TSVKSPSWQR
PNQAAPSTGR ISNSASSSGT GAPMKPAVGP PQPSDQDTLV QRAEHIPAGK RTPMCAHCNQ
AIRGPFLVAL GKSWHPEEFN CAHCKNTMAY IGFVEEKGAL YCELCYEKFF APECGRCQRK
ILGEVINALK QTWHVSCFVC VACGKPIRNN VFHLEDGEPY CETDYYALFG TICRGCEFPI
EAGDMFLEAL GSTWHDTCFV CSVCCESLEG QTFFSKKDKP LCKKHAHSVN F
