PDLI2_RAT
ID PDLI2_RAT Reviewed; 349 AA.
AC Q6AYD6;
DT 07-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT 13-SEP-2004, sequence version 1.
DT 03-AUG-2022, entry version 126.
DE RecName: Full=PDZ and LIM domain protein 2;
GN Name=Pdlim2;
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], FUNCTION, SUBCELLULAR LOCATION, TISSUE
RP SPECIFICITY, AND INTERACTION WITH ACTN1; ACTN4; FLNA AND MYH9.
RC STRAIN=Wistar;
RX PubMed=15505042; DOI=10.1167/iovs.04-0721;
RA Torrado M., Senatorov V.V., Trivedi R., Fariss R.N., Tomarev S.I.;
RT "Pdlim2, a novel PDZ-LIM domain protein, interacts with alpha-actinins and
RT filamin A.";
RL Invest. Ophthalmol. Vis. Sci. 45:3955-3963(2004).
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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-199; SER-210 AND SER-263, AND
RP 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: 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 ECO:0000269|PubMed:15505042}.
CC -!- SUBUNIT: Interacts with alpha-actinins ACTN1 and ACTN4, FLNA and MYH9
CC (PubMed:15505042). Interacts (via LIM zinc-binding domain) with MKRN2
CC (By similarity). {ECO:0000250|UniProtKB:Q8R1G6,
CC ECO:0000269|PubMed:15505042}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:15505042}.
CC Cytoplasm, cytoskeleton {ECO:0000269|PubMed:15505042}. Note=Localizes
CC at the cytoskeleton. Colocalizes with beta-1 integrin (ITGB1) and
CC alpha-actinin but not with paxillin (PXN).
CC -!- TISSUE SPECIFICITY: Highly expressed in cornea and lung. Expressed at
CC intermediate level in sclera and combined tissues of the eye irido-
CC corneal angle. Specifically expressed in the corneal epithelial cells
CC but not in other corneal layers. {ECO:0000269|PubMed:15505042}.
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DR EMBL; AY531526; AAS99334.1; -; mRNA.
DR EMBL; BC079091; AAH79091.1; -; mRNA.
DR RefSeq; NP_001007623.1; NM_001007622.1.
DR RefSeq; XP_006252318.1; XM_006252256.3.
DR RefSeq; XP_006252319.1; XM_006252257.3.
DR RefSeq; XP_006252320.1; XM_006252258.2.
DR RefSeq; XP_006252321.1; XM_006252259.3.
DR RefSeq; XP_008769045.1; XM_008770823.2.
DR AlphaFoldDB; Q6AYD6; -.
DR SMR; Q6AYD6; -.
DR BioGRID; 253175; 5.
DR STRING; 10116.ENSRNOP00000011663; -.
DR iPTMnet; Q6AYD6; -.
DR PhosphoSitePlus; Q6AYD6; -.
DR PaxDb; Q6AYD6; -.
DR PRIDE; Q6AYD6; -.
DR Ensembl; ENSRNOT00000011663; ENSRNOP00000011663; ENSRNOG00000008543.
DR GeneID; 290354; -.
DR KEGG; rno:290354; -.
DR UCSC; RGD:1359203; rat.
DR CTD; 64236; -.
DR RGD; 1359203; Pdlim2.
DR eggNOG; KOG1703; Eukaryota.
DR GeneTree; ENSGT00940000160418; -.
DR HOGENOM; CLU_038114_1_1_1; -.
DR InParanoid; Q6AYD6; -.
DR OMA; HAVRIQE; -.
DR OrthoDB; 840552at2759; -.
DR PhylomeDB; Q6AYD6; -.
DR TreeFam; TF106408; -.
DR PRO; PR:Q6AYD6; -.
DR Proteomes; UP000002494; Chromosome 15.
DR Bgee; ENSRNOG00000008543; Expressed in esophagus and 19 other tissues.
DR Genevisible; Q6AYD6; RN.
DR GO; GO:0005912; C:adherens junction; IBA:GO_Central.
DR GO; GO:0031941; C:filamentous actin; IBA:GO_Central.
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:RGD.
DR GO; GO:0031005; F:filamin binding; IPI:RGD.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0051371; F:muscle alpha-actinin binding; IPI:RGD.
DR GO; GO:0032036; F:myosin heavy chain binding; IPI:RGD.
DR GO; GO:0031625; F:ubiquitin protein ligase binding; ISO:RGD.
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 Cytoplasm; Cytoskeleton; LIM domain; Metal-binding; Phosphoprotein;
KW Reference proteome; Zinc.
FT CHAIN 1..349
FT /note="PDZ and LIM domain protein 2"
FT /id="PRO_0000075865"
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 72..95
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 108..147
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 168..212
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 250..272
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 72..92
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 108..131
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 173..194
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 124
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96JY6"
FT MOD_RES 127
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8R1G6"
FT MOD_RES 129
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96JY6"
FT MOD_RES 134
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8R1G6"
FT MOD_RES 137
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96JY6"
FT MOD_RES 138
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q8R1G6"
FT MOD_RES 142
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q8R1G6"
FT MOD_RES 143
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8R1G6"
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:22673903"
FT MOD_RES 204
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8R1G6"
FT MOD_RES 205
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8R1G6"
FT MOD_RES 209
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8R1G6"
FT MOD_RES 210
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 263
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
SQ SEQUENCE 349 AA; 37580 MW; 39AE7B31979668D8 CRC64;
MALTVNVVGP APWGFRISGG RDFHTPIIVT KVTERGKAEA ADLRPGDIIV AINGESAESM
LHAEAQSKIR QSASPLRLQL DRSQTASPGQ INGEGSLDML ATRFQGSLRT HHNSQSSQRS
ACFSPASLSP RPDSPFSTPP PTSPIALSGE NVIGCSFQSL THSPGLAATH HLTYPGQPTS
QQAGHSSPSD STVRVLLHSP GRPSSPRLSS LDLEEDSEVF KMLQENRQGR AAPRQSSSFR
LLQEALEAEE RGGTPAFVPS SLSPKASLPT SRALATPPKL HTCEKCSVNI SNQAVRIQEG
RYRHPGCYTC ADCGLNLKMR GHFWVGNELY CEKHARQRYS MPGTLSSQA
