PDLI1_RAT
ID PDLI1_RAT Reviewed; 327 AA.
AC P52944; Q6IN45;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 4.
DT 03-AUG-2022, entry version 156.
DE RecName: Full=PDZ and LIM domain protein 1;
DE AltName: Full=C-terminal LIM domain protein 1;
DE AltName: Full=Elfin;
DE AltName: Full=LIM domain protein CLP-36;
GN Name=Pdlim1; Synonyms=Clim1, Clp36;
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].
RC STRAIN=Sprague-Dawley; TISSUE=Liver;
RX PubMed=8522188; DOI=10.1016/0378-1119(95)00542-e;
RA Wang H., Harrison-Shostak D.C., Lemasters J.J., Herman B.;
RT "Cloning of a rat cDNA encoding a novel LIM domain protein with high
RT homology to rat RIL.";
RL Gene 165:267-271(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Lung;
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 [3]
RP FUNCTION, INTERACTION WITH ACTN1 AND PDLIM4, AND SUBCELLULAR LOCATION.
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 [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-90, AND IDENTIFICATION BY
RP 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: Cytoskeletal protein that may act as an adapter that brings
CC other proteins (like kinases) to the cytoskeleton (By similarity).
CC Involved in assembly, disassembly and directioning of stress fibers in
CC fibroblasts. Required for the localization of ACTN1 and PALLD to stress
CC fibers. Required for cell migration and in maintaining cell polarity of
CC fibroblasts (PubMed:22659164). {ECO:0000250|UniProtKB:O00151,
CC ECO:0000269|PubMed:22659164}.
CC -!- SUBUNIT: Interacts with ACTN1 (PubMed:22659164). Interacts with ACTN2
CC and ACTN4 (By similarity). Interacts with PDLIM4 (PubMed:22659164).
CC {ECO:0000250|UniProtKB:O00151, ECO:0000269|PubMed:22659164}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:22659164}.
CC Cytoplasm, cytoskeleton {ECO:0000269|PubMed:22659164}. Cytoplasm,
CC myofibril, sarcomere, Z line {ECO:0000250|UniProtKB:O00151}.
CC Note=Associates with actin stress fibers.
CC {ECO:0000269|PubMed:22659164}.
CC -!- TISSUE SPECIFICITY: Expressed most abundantly in heart, lung and liver,
CC moderately in spleen and skeletal muscle, and at extremely low levels
CC (if at all) in testis and brain tissues.
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DR EMBL; U23769; AAA92046.1; -; mRNA.
DR EMBL; BC072465; AAH72465.1; -; mRNA.
DR PIR; JC4385; JC4385.
DR RefSeq; NP_059061.1; NM_017365.2.
DR AlphaFoldDB; P52944; -.
DR SMR; P52944; -.
DR CORUM; P52944; -.
DR IntAct; P52944; 1.
DR STRING; 10116.ENSRNOP00000022000; -.
DR iPTMnet; P52944; -.
DR PhosphoSitePlus; P52944; -.
DR jPOST; P52944; -.
DR PaxDb; P52944; -.
DR PRIDE; P52944; -.
DR Ensembl; ENSRNOT00000022000; ENSRNOP00000022000; ENSRNOG00000016166.
DR GeneID; 54133; -.
DR KEGG; rno:54133; -.
DR UCSC; RGD:68324; rat.
DR CTD; 9124; -.
DR RGD; 68324; Pdlim1.
DR eggNOG; KOG1703; Eukaryota.
DR GeneTree; ENSGT00940000155525; -.
DR HOGENOM; CLU_038114_1_1_1; -.
DR InParanoid; P52944; -.
DR OMA; EPQEVKH; -.
DR OrthoDB; 840552at2759; -.
DR PhylomeDB; P52944; -.
DR TreeFam; TF106408; -.
DR PRO; PR:P52944; -.
DR Proteomes; UP000002494; Chromosome 1.
DR Bgee; ENSRNOG00000016166; Expressed in jejunum and 20 other tissues.
DR Genevisible; P52944; RN.
DR GO; GO:0015629; C:actin cytoskeleton; IDA:UniProtKB.
DR GO; GO:0005912; C:adherens junction; IBA:GO_Central.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005856; C:cytoskeleton; ISO:RGD.
DR GO; GO:0031941; C:filamentous actin; IBA:GO_Central.
DR GO; GO:0001725; C:stress fiber; IDA:UniProtKB.
DR GO; GO:0005667; C:transcription regulator complex; ISO:RGD.
DR GO; GO:0030018; C:Z disc; IDA:UniProtKB.
DR GO; GO:0003779; F:actin 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:0003713; F:transcription coactivator activity; ISO:RGD.
DR GO; GO:0030036; P:actin cytoskeleton organization; IMP:UniProtKB.
DR GO; GO:0030950; P:establishment or maintenance of actin cytoskeleton polarity; IMP:UniProtKB.
DR GO; GO:0010761; P:fibroblast migration; IMP:UniProtKB.
DR GO; GO:0007507; P:heart development; IBA:GO_Central.
DR GO; GO:0030011; P:maintenance of cell polarity; IMP:UniProtKB.
DR GO; GO:0061061; P:muscle structure development; IBA:GO_Central.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; ISO:RGD.
DR GO; GO:0001666; P:response to hypoxia; IEP:RGD.
DR GO; GO:0043149; P:stress fiber assembly; IMP:UniProtKB.
DR Gene3D; 2.30.42.10; -; 1.
DR InterPro; IPR031847; DUF4749.
DR InterPro; IPR028537; PDLIM1.
DR InterPro; IPR001478; PDZ.
DR InterPro; IPR036034; PDZ_sf.
DR InterPro; IPR006643; Zasp-like_motif.
DR InterPro; IPR001781; Znf_LIM.
DR PANTHER; PTHR24214:SF5; PTHR24214:SF5; 1.
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 SMART; SM00735; ZM; 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 Acetylation; Cytoplasm; Cytoskeleton; LIM domain; Metal-binding;
KW Phosphoprotein; Reference proteome; Zinc.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:O00151"
FT CHAIN 2..327
FT /note="PDZ and LIM domain protein 1"
FT /id="PRO_0000075861"
FT DOMAIN 3..85
FT /note="PDZ"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00143"
FT DOMAIN 256..315
FT /note="LIM zinc-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00125"
FT REGION 161..186
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 161..180
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 258
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 261
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 278
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 281
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 284
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 287
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 305
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 308
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT MOD_RES 2
FT /note="N-acetylthreonine"
FT /evidence="ECO:0000250|UniProtKB:O00151"
FT MOD_RES 90
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 130
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O00151"
FT MOD_RES 142
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:O00151"
FT MOD_RES 314
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:O00151"
FT MOD_RES 319
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:O00151"
FT CONFLICT 277
FT /note="R -> P (in Ref. 1; AAA92046)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 327 AA; 35584 MW; 4C3B5CDA296544D1 CRC64;
MTTQQIVLQG PGPWGFRLVG GKDFEQPLAI SRVTPGSKAA IANLCIGDLI TAIDGEDTSS
MTHLEAQNKI KGCVDNMTLT VSRSEQKIWS PLVTEEGKRH PYKMNLASEP QEVLHIGSAH
NRSAMPFTAS PAPGTRVITN QYNSPTGLYS SENISNFNNA VESKTSASGE EANSRPSAQP
HPSGGLIIDK ESEVYKMLQE KQELNEPPKQ STSFLVLQEI LESDGKGDPN KPSGFRSVKA
PVTKVAASVG NAQKLPICDK CGTGIVGVFV KLRDHHRHPE CYVCTDCGIN LKQKGHFFVG
DQIYCEKHAR ERVTPPEGYD VVTVFPK
