PDLI3_MOUSE
ID PDLI3_MOUSE Reviewed; 316 AA.
AC O70209;
DT 06-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1998, sequence version 1.
DT 03-AUG-2022, entry version 154.
DE RecName: Full=PDZ and LIM domain protein 3;
DE AltName: Full=Actinin-associated LIM protein;
DE AltName: Full=Alpha-actinin-2-associated LIM protein;
GN Name=Pdlim3;
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 [MRNA], AND DEVELOPMENTAL STAGE.
RC TISSUE=Skeletal muscle;
RX PubMed=9334352; DOI=10.1083/jcb.139.2.507;
RA Xia H., Winokur S.T., Kuo W.-L., Altherr M.R., Bredt D.S.;
RT "Actinin-associated LIM protein: identification of a domain interaction
RT between PDZ and spectrin-like repeat motifs.";
RL J. Cell Biol. 139:507-515(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Wolffian duct;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Brain;
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 [4]
RP INTERACTION WITH PDLIM4.
RX PubMed=15663004; DOI=10.1007/s11033-005-1407-8;
RA van den Berk L.C., van Ham M.A., te Lindert M.M., Walma T., Aelen J.,
RA Vuister G.W., Hendriks W.J.;
RT "The interaction of PTP-BL PDZ domains with RIL: an enigmatic role for the
RT RIL LIM domain.";
RL Mol. Biol. Rep. 31:203-215(2004).
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brown adipose tissue, Heart, Lung, 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 [6]
RP METHYLATION [LARGE SCALE ANALYSIS] AT ARG-164, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, and Embryo;
RX PubMed=24129315; DOI=10.1074/mcp.o113.027870;
RA Guo A., Gu H., Zhou J., Mulhern D., Wang Y., Lee K.A., Yang V., Aguiar M.,
RA Kornhauser J., Jia X., Ren J., Beausoleil S.A., Silva J.C., Vemulapalli V.,
RA Bedford M.T., Comb M.J.;
RT "Immunoaffinity enrichment and mass spectrometry analysis of protein
RT methylation.";
RL Mol. Cell. Proteomics 13:372-387(2014).
RN [7]
RP STRUCTURE BY NMR OF 4-93 AND 226-301 IN COMPLEX WITH ZINC IONS.
RG RIKEN structural genomics initiative (RSGI);
RT "Solution structure of PDZ and LIM domains of mouse alpha-actinin-2
RT associated LIM protein.";
RL Submitted (MAY-2004) to the PDB data bank.
CC -!- FUNCTION: May play a role in the organization of actin filament arrays
CC within muscle cells. {ECO:0000250}.
CC -!- SUBUNIT: Interacts with ACTN2 (By similarity). Forms a heterodimer with
CC PDLIM4 (via LIM domain) (PubMed:15663004).
CC {ECO:0000250|UniProtKB:Q66HS7, ECO:0000269|PubMed:15663004}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, myofibril, sarcomere, Z line
CC {ECO:0000250}. Note=Localizes to myofiber Z-lines. {ECO:0000250}.
CC -!- DEVELOPMENTAL STAGE: At 15 dpc highly expressed in skeletal muscle and
CC heart. {ECO:0000269|PubMed:9334352}.
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DR EMBL; AF002283; AAC16673.1; -; mRNA.
DR EMBL; AK078421; BAC37266.1; -; mRNA.
DR EMBL; BC070418; AAH70418.1; -; mRNA.
DR CCDS; CCDS22281.1; -.
DR RefSeq; NP_058078.1; NM_016798.3.
DR PDB; 1V5L; NMR; -; A=4-93.
DR PDB; 1X64; NMR; -; A=226-301.
DR PDBsum; 1V5L; -.
DR PDBsum; 1X64; -.
DR AlphaFoldDB; O70209; -.
DR SMR; O70209; -.
DR STRING; 10090.ENSMUSP00000034053; -.
DR iPTMnet; O70209; -.
DR PhosphoSitePlus; O70209; -.
DR REPRODUCTION-2DPAGE; IPI00116347; -.
DR MaxQB; O70209; -.
DR PaxDb; O70209; -.
DR PeptideAtlas; O70209; -.
DR PRIDE; O70209; -.
DR ProteomicsDB; 289337; -.
DR Antibodypedia; 1500; 188 antibodies from 24 providers.
DR DNASU; 53318; -.
DR Ensembl; ENSMUST00000034053; ENSMUSP00000034053; ENSMUSG00000031636.
DR GeneID; 53318; -.
DR KEGG; mmu:53318; -.
DR UCSC; uc009lpl.1; mouse.
DR CTD; 27295; -.
DR MGI; MGI:1859274; Pdlim3.
DR VEuPathDB; HostDB:ENSMUSG00000031636; -.
DR eggNOG; KOG1703; Eukaryota.
DR GeneTree; ENSGT00940000156741; -.
DR HOGENOM; CLU_038114_1_1_1; -.
DR InParanoid; O70209; -.
DR PhylomeDB; O70209; -.
DR TreeFam; TF106408; -.
DR BioGRID-ORCS; 53318; 2 hits in 72 CRISPR screens.
DR ChiTaRS; Pdlim3; mouse.
DR EvolutionaryTrace; O70209; -.
DR PRO; PR:O70209; -.
DR Proteomes; UP000000589; Chromosome 8.
DR RNAct; O70209; protein.
DR Bgee; ENSMUSG00000031636; Expressed in tarsal region and 168 other tissues.
DR ExpressionAtlas; O70209; baseline and differential.
DR Genevisible; O70209; MM.
DR GO; GO:0015629; C:actin cytoskeleton; IPI:MGI.
DR GO; GO:0005912; C:adherens junction; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0031941; C:filamentous actin; IBA:GO_Central.
DR GO; GO:0001725; C:stress fiber; IBA:GO_Central.
DR GO; GO:0030018; C:Z disc; ISO:MGI.
DR GO; GO:0003779; F:actin binding; IBA:GO_Central.
DR GO; GO:0042805; F:actinin binding; ISO:MGI.
DR GO; GO:0008092; F:cytoskeletal protein binding; IPI:MGI.
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:0008307; F:structural constituent of muscle; IDA:MGI.
DR GO; GO:0030036; P:actin cytoskeleton organization; IBA:GO_Central.
DR GO; GO:0007015; P:actin filament organization; IDA:MGI.
DR GO; GO:0007507; P:heart development; IMP:MGI.
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; IPR006643; Zasp-like_motif.
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 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 3D-structure; Cytoplasm; LIM domain; Metal-binding; Methylation;
KW Phosphoprotein; Reference proteome; Zinc.
FT CHAIN 1..316
FT /note="PDZ and LIM domain protein 3"
FT /id="PRO_0000075868"
FT DOMAIN 1..84
FT /note="PDZ"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00143"
FT DOMAIN 244..303
FT /note="LIM zinc-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00125"
FT MOD_RES 18
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q66HS7"
FT MOD_RES 93
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q53GG5"
FT MOD_RES 164
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT STRAND 6..11
FT /evidence="ECO:0007829|PDB:1V5L"
FT STRAND 18..20
FT /evidence="ECO:0007829|PDB:1V5L"
FT TURN 21..24
FT /evidence="ECO:0007829|PDB:1V5L"
FT STRAND 25..28
FT /evidence="ECO:0007829|PDB:1V5L"
FT STRAND 34..36
FT /evidence="ECO:0007829|PDB:1V5L"
FT HELIX 39..41
FT /evidence="ECO:0007829|PDB:1V5L"
FT STRAND 48..52
FT /evidence="ECO:0007829|PDB:1V5L"
FT HELIX 62..69
FT /evidence="ECO:0007829|PDB:1V5L"
FT STRAND 74..77
FT /evidence="ECO:0007829|PDB:1V5L"
FT TURN 84..87
FT /evidence="ECO:0007829|PDB:1V5L"
FT TURN 247..249
FT /evidence="ECO:0007829|PDB:1X64"
FT STRAND 258..262
FT /evidence="ECO:0007829|PDB:1X64"
FT TURN 267..269
FT /evidence="ECO:0007829|PDB:1X64"
FT STRAND 273..275
FT /evidence="ECO:0007829|PDB:1X64"
FT TURN 279..281
FT /evidence="ECO:0007829|PDB:1X64"
FT STRAND 285..287
FT /evidence="ECO:0007829|PDB:1X64"
FT STRAND 290..292
FT /evidence="ECO:0007829|PDB:1X64"
FT HELIX 294..300
FT /evidence="ECO:0007829|PDB:1X64"
SQ SEQUENCE 316 AA; 34300 MW; E59916D0BC430B6F CRC64;
MPQNVVLPGP APWGFRLSGG IDFNQPLVIT RITPGSKAAA ANLCPGDVIL AIDGFGTESM
THADAQDRIK AASYQLCLKI DRAETRLWSP QVSEDGKAHP FKINLEAEPQ EFKPIGTAHN
RRAQPFVAAA NIDDKRQVVS ASYNSPIGLY STSNIQDALH GQLRGLIPGS LQNEPTASVP
PQSDVYRMLH DNRDDPAAPR QSGSFRVLQD LVNDGPDDRP AGTRSVRAPV TKVHGGAGSA
QRMPLCDKCG SGIVGAVVKA RDKYRHPECF VCADCNLNLK QKGYFFVEGE LYCETHARAR
TRPPEGYDTV TLYPKA
