PDLI2_MOUSE
ID PDLI2_MOUSE Reviewed; 349 AA.
AC Q8R1G6;
DT 07-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 1.
DT 03-AUG-2022, entry version 150.
DE RecName: Full=PDZ and LIM domain protein 2;
DE AltName: Full=PDZ-LIM protein mystique;
GN Name=Pdlim2;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=FVB/N; TISSUE=Colon;
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 [2]
RP TISSUE SPECIFICITY, AND INDUCTION.
RX PubMed=15659642; DOI=10.1091/mbc.e04-12-1052;
RA Loughran G., Healy N., Kiely P.A., Huigsloot M., Kedersha N.L.,
RA O'connor R.;
RT "Mystique is a new IGF-I regulated PDZ-LIM domain protein that promotes
RT cell attachment and migration and suppresses anchorage independent
RT growth.";
RL Mol. Biol. Cell 16:1811-1822(2005).
RN [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-199 AND SER-205, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic fibroblast;
RX PubMed=19131326; DOI=10.1074/mcp.m800451-mcp200;
RA Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.;
RT "Large scale localization of protein phosphorylation by use of electron
RT capture dissociation mass spectrometry.";
RL Mol. Cell. Proteomics 8:904-912(2009).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-124; SER-127; SER-129;
RP SER-134; SER-137; THR-138; THR-142; SER-143; SER-204 AND SER-209, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Kidney, Lung, Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [5]
RP INTERACTION WITH MKRN2.
RX PubMed=28378844; DOI=10.1038/srep46097;
RA Shin C., Ito Y., Ichikawa S., Tokunaga M., Sakata-Sogawa K., Tanaka T.;
RT "MKRN2 is a novel ubiquitin E3 ligase for the p65 subunit of NF-kappaB and
RT negatively regulates inflammatory responses.";
RL Sci. Rep. 7:46097-46097(2017).
RN [6]
RP STRUCTURE BY NMR OF 3-83.
RG RIKEN structural genomics initiative (RSGI);
RT "Solution structure of the PDZ domain of PDZ and LIM domain 2.";
RL Submitted (FEB-2004) to the PDB data bank.
CC -!- FUNCTION: Probable adapter protein located at the actin cytoskeleton
CC that promotes cell attachment. Necessary for the migratory capacity of
CC epithelial cells. Overexpression enhances cell adhesion to collagen and
CC fibronectin and suppresses anchorage independent growth. May contribute
CC to tumor cell migratory capacity (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Interacts with alpha-actinins ACTN1 and ACTN4, FLNA and MYH9
CC (By similarity). Interacts (via LIM zinc-binding domain) with MKRN2
CC (PubMed:28378844). {ECO:0000250|UniProtKB:Q6AYD6,
CC ECO:0000269|PubMed:28378844}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Cytoplasm, cytoskeleton.
CC Note=Localizes at the cytoskeleton. Colocalizes with beta-1 integrin
CC (ITGB1) and alpha-actinin but not with paxillin (PXN) (By similarity).
CC {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=1;
CC Comment=A number of isoforms are produced.;
CC Name=1;
CC IsoId=Q8R1G6-1; Sequence=Displayed;
CC -!- TISSUE SPECIFICITY: Highly expressed in lung. Expressed at intermediate
CC level in kidney, testis and spleen. Weakly expressed in heart and
CC brain. {ECO:0000269|PubMed:15659642}.
CC -!- INDUCTION: Regulated by IGF-1. {ECO:0000269|PubMed:15659642}.
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DR EMBL; BC024556; AAH24556.1; -; mRNA.
DR CCDS; CCDS27248.1; -. [Q8R1G6-1]
DR RefSeq; NP_001240665.1; NM_001253736.1. [Q8R1G6-1]
DR RefSeq; NP_666090.1; NM_145978.2. [Q8R1G6-1]
DR RefSeq; XP_011243308.1; XM_011245006.2.
DR PDB; 1VB7; NMR; -; A=3-83.
DR PDBsum; 1VB7; -.
DR AlphaFoldDB; Q8R1G6; -.
DR SMR; Q8R1G6; -.
DR BioGRID; 229389; 3.
DR IntAct; Q8R1G6; 1.
DR MINT; Q8R1G6; -.
DR STRING; 10090.ENSMUSP00000116200; -.
DR iPTMnet; Q8R1G6; -.
DR PhosphoSitePlus; Q8R1G6; -.
DR EPD; Q8R1G6; -.
DR jPOST; Q8R1G6; -.
DR MaxQB; Q8R1G6; -.
DR PaxDb; Q8R1G6; -.
DR PeptideAtlas; Q8R1G6; -.
DR PRIDE; Q8R1G6; -.
DR ProteomicsDB; 288085; -. [Q8R1G6-1]
DR Antibodypedia; 999; 265 antibodies from 27 providers.
DR DNASU; 213019; -.
DR Ensembl; ENSMUST00000022681; ENSMUSP00000022681; ENSMUSG00000022090. [Q8R1G6-1]
DR Ensembl; ENSMUST00000153735; ENSMUSP00000116200; ENSMUSG00000022090. [Q8R1G6-1]
DR GeneID; 213019; -.
DR KEGG; mmu:213019; -.
DR UCSC; uc007uni.1; mouse. [Q8R1G6-1]
DR CTD; 64236; -.
DR MGI; MGI:2384850; Pdlim2.
DR VEuPathDB; HostDB:ENSMUSG00000022090; -.
DR eggNOG; KOG1703; Eukaryota.
DR GeneTree; ENSGT00940000160418; -.
DR HOGENOM; CLU_038114_1_1_1; -.
DR InParanoid; Q8R1G6; -.
DR OMA; HAVRIQE; -.
DR OrthoDB; 840552at2759; -.
DR PhylomeDB; Q8R1G6; -.
DR TreeFam; TF106408; -.
DR BioGRID-ORCS; 213019; 1 hit in 72 CRISPR screens.
DR ChiTaRS; Pdlim2; mouse.
DR EvolutionaryTrace; Q8R1G6; -.
DR PRO; PR:Q8R1G6; -.
DR Proteomes; UP000000589; Chromosome 14.
DR RNAct; Q8R1G6; protein.
DR Bgee; ENSMUSG00000022090; Expressed in esophagus and 203 other tissues.
DR ExpressionAtlas; Q8R1G6; baseline and differential.
DR Genevisible; Q8R1G6; MM.
DR GO; GO:0005912; C:adherens junction; IBA:GO_Central.
DR GO; GO:0030864; C:cortical actin cytoskeleton; ISO:MGI.
DR GO; GO:0031941; C:filamentous actin; IBA:GO_Central.
DR GO; GO:0001725; C:stress fiber; ISO:MGI.
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; ISO:MGI.
DR GO; GO:0031005; F:filamin binding; ISO:MGI.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0051371; F:muscle alpha-actinin binding; ISO:MGI.
DR GO; GO:0032036; F:myosin heavy chain binding; ISO:MGI.
DR GO; GO:0031625; F:ubiquitin protein ligase binding; IPI:UniProtKB.
DR GO; GO:0030036; P:actin cytoskeleton organization; IBA:GO_Central.
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; Cytoplasm; Cytoskeleton; LIM domain;
KW Metal-binding; Phosphoprotein; Reference proteome; Zinc.
FT CHAIN 1..349
FT /note="PDZ and LIM domain protein 2"
FT /id="PRO_0000075864"
FT DOMAIN 1..84
FT /note="PDZ"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00143"
FT DOMAIN 281..341
FT /note="LIM zinc-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00125"
FT REGION 74..147
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 169..212
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 74..98
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 107..131
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 175..193
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 124
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 127
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 129
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 134
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 137
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 138
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 142
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 143
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 163
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96JY6"
FT MOD_RES 199
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19131326"
FT MOD_RES 204
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 205
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19131326"
FT MOD_RES 209
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 210
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6AYD6"
FT MOD_RES 263
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6AYD6"
FT STRAND 3..7
FT /evidence="ECO:0007829|PDB:1VB7"
FT STRAND 9..11
FT /evidence="ECO:0007829|PDB:1VB7"
FT STRAND 18..20
FT /evidence="ECO:0007829|PDB:1VB7"
FT TURN 21..24
FT /evidence="ECO:0007829|PDB:1VB7"
FT STRAND 25..28
FT /evidence="ECO:0007829|PDB:1VB7"
FT HELIX 38..41
FT /evidence="ECO:0007829|PDB:1VB7"
FT STRAND 48..52
FT /evidence="ECO:0007829|PDB:1VB7"
FT HELIX 62..70
FT /evidence="ECO:0007829|PDB:1VB7"
FT STRAND 74..81
FT /evidence="ECO:0007829|PDB:1VB7"
SQ SEQUENCE 349 AA; 37703 MW; 9809D7F1AF2BD907 CRC64;
MALTVDVAGP APWGFRISGG RDFHTPIIVT KVTERGKAEA ADLRPGDIIV AINGQSAENM
LHAEAQSKIR QSASPLRLQL DRSQTASPGQ TNGEGSLEVL ATRFQGSLRT HRDSQSSQRS
ACFSPVSLSP RPCSPFSTPP PTSPVALSKE DMIGCSFQSL THSPGLAAAH HLTYPGHPTS
QQAGHSSPSD SAVRVLLHSP GRPSSPRFSS LDLEEDSEVF KMLQENRQGR AAPRQSSSFR
LLQEALEAEE RGGTPAFVPS SLSSQASLPT SRALATPPKL HTCEKCSVNI SNQAVRIQEG
RYRHPGCYTC ADCGLNLKMR GHFWVGNELY CEKHARQRYS MPGTLNSRA
