PDLI7_HUMAN
ID PDLI7_HUMAN Reviewed; 457 AA.
AC Q9NR12; Q14250; Q5XG82; Q6NVZ5; Q96C91; Q9BXB8; Q9BXB9;
DT 06-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 185.
DE RecName: Full=PDZ and LIM domain protein 7;
DE AltName: Full=LIM mineralization protein;
DE Short=LMP;
DE AltName: Full=Protein enigma;
GN Name=PDLIM7; Synonyms=ENIGMA;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND INTERACTION WITH INSR.
RX PubMed=7929196; DOI=10.1016/s0021-9258(17)31502-8;
RA Wu R.-Y., Gill G.N.;
RT "LIM domain recognition of a tyrosine-containing tight turn.";
RL J. Biol. Chem. 269:25085-25090(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2 AND 3), FUNCTION, TISSUE
RP SPECIFICITY, AND ALTERNATIVE SPLICING.
RC TISSUE=Heart;
RX PubMed=11874232; DOI=10.1359/jbmr.2002.17.3.406;
RA Liu Y., Hair G.A., Boden S.D., Viggeswarapu M., Titus L.;
RT "Overexpressed LIM mineralization proteins do not require LIM domains to
RT induce bone.";
RL J. Bone Miner. Res. 17:406-414(2002).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC TISSUE=Neuroepithelium;
RA Borrello M.G., Billaud M., Mercalli E., Ghizzoni S., Bidaud C.;
RT "Enigma sequence and interaction with Ret.";
RL Submitted (MAY-2000) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 4; 5 AND 6).
RC TISSUE=Brain, Kidney, Mammary gland, and Uterus;
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 [5]
RP PROTEIN SEQUENCE OF 6-17; 94-103 AND 246-258, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RC TISSUE=Platelet;
RA Bienvenut W.V., Claeys D.;
RL Submitted (NOV-2005) to UniProtKB.
RN [6]
RP INTERACTION WITH PKC.
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 [7]
RP SUBCELLULAR LOCATION, AND INTERACTION WITH RET AND SHC1.
RX PubMed=9528800; DOI=10.1128/mcb.18.4.2298;
RA Durick K., Gill G.N., Taylor S.S.;
RT "Shc and Enigma are both required for mitogenic signaling by Ret/ptc2.";
RL Mol. Cell. Biol. 18:2298-2308(1998).
RN [8]
RP INTERACTION WITH TPM2, AND MUTAGENESIS OF 15-GLY-PHE-16 AND HIS-63.
RX PubMed=10359609; DOI=10.1091/mbc.10.6.1973;
RA Guy P.M., Kenny D.A., Gill G.N.;
RT "The PDZ domain of the LIM protein enigma binds to beta-tropomyosin.";
RL Mol. Biol. Cell 10:1973-1984(1999).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-247, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [10]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [11]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [12]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-78 AND SER-111, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [14]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [15]
RP METHYLATION [LARGE SCALE ANALYSIS] AT ARG-103, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Colon carcinoma;
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 [16]
RP X-RAY CRYSTALLOGRAPHY (1.11 ANGSTROMS) OF 1-84.
RG Structural genomics consortium (SGC);
RT "Structure of the PDZ domain of human PDLIM7 bound to a C-terminal
RT extension from human beta-tropomyosin.";
RL Submitted (FEB-2009) to the PDB data bank.
RN [17]
RP VARIANT [LARGE SCALE ANALYSIS] ASN-450.
RX PubMed=16959974; DOI=10.1126/science.1133427;
RA Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D.,
RA Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P.,
RA Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V.,
RA Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H.,
RA Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W.,
RA Velculescu V.E.;
RT "The consensus coding sequences of human breast and colorectal cancers.";
RL Science 314:268-274(2006).
CC -!- FUNCTION: May function as a scaffold on which the coordinated assembly
CC of proteins can occur. May play a role as an adapter that, via its PDZ
CC domain, localizes LIM-binding proteins to actin filaments of both
CC skeletal muscle and nonmuscle tissues. Involved in both of the two
CC fundamental mechanisms of bone formation, direct bone formation (e.g.
CC embryonic flat bones mandible and cranium), and endochondral bone
CC formation (e.g. embryonic long bone development). Plays a role during
CC fracture repair. Involved in BMP6 signaling pathway (By similarity).
CC {ECO:0000250, ECO:0000269|PubMed:11874232, ECO:0000269|PubMed:7929196}.
CC -!- SUBUNIT: Binds via its LIM zinc-binding 3 domain (LIM 3) to endocytic
CC codes of INSR, but not with those of IGF1R, LDLR, TFRC, or EGFR.
CC Interacts with various PKC isoforms through the LIM zinc-binding
CC domains. Binds to RET in a phosphorylation-independent manner via its
CC LIM zinc-binding domain 2 (LIM 2). Probably part of a complex with SHC
CC and the RET dimer. Interacts with TPM2. Interacts with TBX4 and TBX5
CC (By similarity). {ECO:0000250}.
CC -!- INTERACTION:
CC Q9NR12; Q9NYB9-2: ABI2; NbExp=3; IntAct=EBI-350517, EBI-11096309;
CC Q9NR12; O95817: BAG3; NbExp=5; IntAct=EBI-350517, EBI-747185;
CC Q9NR12; Q8NEC5: CATSPER1; NbExp=5; IntAct=EBI-350517, EBI-744545;
CC Q9NR12; P26196: DDX6; NbExp=3; IntAct=EBI-350517, EBI-351257;
CC Q9NR12; Q8NFT8: DNER; NbExp=3; IntAct=EBI-350517, EBI-2682727;
CC Q9NR12; Q9H0I2: ENKD1; NbExp=6; IntAct=EBI-350517, EBI-744099;
CC Q9NR12; Q7L5A3: FAM214B; NbExp=3; IntAct=EBI-350517, EBI-745689;
CC Q9NR12; Q8NEG0: FAM71C; NbExp=3; IntAct=EBI-350517, EBI-752049;
CC Q9NR12; Q86YD7: FAM90A1; NbExp=3; IntAct=EBI-350517, EBI-6658203;
CC Q9NR12; O43559: FRS3; NbExp=3; IntAct=EBI-350517, EBI-725515;
CC Q9NR12; P55040: GEM; NbExp=5; IntAct=EBI-350517, EBI-744104;
CC Q9NR12; Q9NWQ4-1: GPATCH2L; NbExp=3; IntAct=EBI-350517, EBI-11959863;
CC Q9NR12; Q9UBP5: HEY2; NbExp=3; IntAct=EBI-350517, EBI-750630;
CC Q9NR12; P52597: HNRNPF; NbExp=5; IntAct=EBI-350517, EBI-352986;
CC Q9NR12; O75031: HSF2BP; NbExp=3; IntAct=EBI-350517, EBI-7116203;
CC Q9NR12; Q9UBY9: HSPB7; NbExp=3; IntAct=EBI-350517, EBI-739361;
CC Q9NR12; Q14005-2: IL16; NbExp=3; IntAct=EBI-350517, EBI-17178971;
CC Q9NR12; A4QPB0: IQGAP1; NbExp=3; IntAct=EBI-350517, EBI-9512851;
CC Q9NR12; Q63ZY3: KANK2; NbExp=3; IntAct=EBI-350517, EBI-2556193;
CC Q9NR12; Q8NFP7: NUDT10; NbExp=3; IntAct=EBI-350517, EBI-726826;
CC Q9NR12; Q7L8S5: OTUD6A; NbExp=3; IntAct=EBI-350517, EBI-11960139;
CC Q9NR12; Q9HBI0: PARVG; NbExp=3; IntAct=EBI-350517, EBI-3921217;
CC Q9NR12; O43189: PHF1; NbExp=4; IntAct=EBI-350517, EBI-530034;
CC Q9NR12; Q13526: PIN1; NbExp=3; IntAct=EBI-350517, EBI-714158;
CC Q9NR12; Q494U1-3: PLEKHN1; NbExp=3; IntAct=EBI-350517, EBI-12014286;
CC Q9NR12; Q0VAM2-3: RASGEF1B; NbExp=3; IntAct=EBI-350517, EBI-12013954;
CC Q9NR12; Q9BUL9: RPP25; NbExp=3; IntAct=EBI-350517, EBI-366570;
CC Q9NR12; Q9BWG6: SCNM1; NbExp=3; IntAct=EBI-350517, EBI-748391;
CC Q9NR12; Q8ND83: SLAIN1; NbExp=3; IntAct=EBI-350517, EBI-10269374;
CC Q9NR12; Q9Y242: TCF19; NbExp=3; IntAct=EBI-350517, EBI-7413767;
CC Q9NR12; O14787-2: TNPO2; NbExp=3; IntAct=EBI-350517, EBI-12076664;
CC Q9NR12; Q99816: TSG101; NbExp=10; IntAct=EBI-350517, EBI-346882;
CC Q9NR12; Q3SY00: TSGA10IP; NbExp=3; IntAct=EBI-350517, EBI-10241197;
CC Q9NR12; Q9NRR5: UBQLN4; NbExp=2; IntAct=EBI-350517, EBI-711226;
CC Q9NR12; O00308: WWP2; NbExp=6; IntAct=EBI-350517, EBI-743923;
CC Q9NR12; P46937: YAP1; NbExp=2; IntAct=EBI-350517, EBI-1044059;
CC Q9NR12; P09022: Hoxa1; Xeno; NbExp=3; IntAct=EBI-350517, EBI-3957603;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Cytoplasm, cytoskeleton
CC {ECO:0000250}. Note=Colocalizes with RET to the cell periphery and in
CC some cytoskeletal components. Colocalizes with TPM2 near the Z line in
CC muscle. Colocalizes with TBX4 and TBX5 to actin filaments (By
CC similarity). {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=6;
CC Name=1; Synonyms=LMP-1;
CC IsoId=Q9NR12-1; Sequence=Displayed;
CC Name=2; Synonyms=LMP-2;
CC IsoId=Q9NR12-2; Sequence=VSP_016509;
CC Name=3; Synonyms=LMP-3;
CC IsoId=Q9NR12-3; Sequence=VSP_016510, VSP_016513;
CC Name=4;
CC IsoId=Q9NR12-4; Sequence=VSP_016511, VSP_016516;
CC Name=5;
CC IsoId=Q9NR12-5; Sequence=VSP_016514;
CC Name=6;
CC IsoId=Q9NR12-6; Sequence=VSP_016512, VSP_016515;
CC -!- TISSUE SPECIFICITY: Isoform 1 and isoform 2 are expressed ubiquitously,
CC however, isoform 2 predominates in skeletal muscle, isoform 1 is more
CC abundant in lung, spleen, leukocytes and fetal liver.
CC {ECO:0000269|PubMed:11874232}.
CC -!- DOMAIN: The LIM zinc-binding 2 (LIM 2) domain interacts with TBX4.
CC {ECO:0000250}.
CC -!- DOMAIN: The LIM zinc-binding 3 (LIM 3) domain provides the structural
CC basis for recognition of tyrosine-containing tight turn structures.
CC This domain is necessary and sufficient for interaction with TBX5 (By
CC similarity). {ECO:0000250}.
CC -!- DOMAIN: Anchored to cell periphery via its N-terminal PDZ domain.
CC -!- MISCELLANEOUS: [Isoform 2]: Did not induce bone induction.
CC {ECO:0000305}.
CC -!- MISCELLANEOUS: [Isoform 3]: Same activity as isoform 1 in bone nodule
CC induction. {ECO:0000305}.
CC -!- MISCELLANEOUS: [Isoform 5]: May be produced at very low levels due to a
CC premature stop codon in the mRNA, leading to nonsense-mediated mRNA
CC decay. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAC37565.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; L35240; AAC37565.1; ALT_FRAME; Genomic_DNA.
DR EMBL; AF345904; AAK30567.1; -; mRNA.
DR EMBL; AF345905; AAK30568.1; -; mRNA.
DR EMBL; AF345906; AAK30569.1; -; mRNA.
DR EMBL; AF265209; AAF76152.1; -; mRNA.
DR EMBL; BC001093; AAH01093.1; -; mRNA.
DR EMBL; BC014521; AAH14521.1; -; mRNA.
DR EMBL; BC067806; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; BC084575; AAH84575.1; -; mRNA.
DR CCDS; CCDS4422.1; -. [Q9NR12-1]
DR CCDS; CCDS4423.1; -. [Q9NR12-2]
DR CCDS; CCDS4424.1; -. [Q9NR12-6]
DR PIR; A55050; A55050.
DR RefSeq; NP_005442.2; NM_005451.4. [Q9NR12-1]
DR RefSeq; NP_976227.1; NM_203352.2. [Q9NR12-2]
DR RefSeq; NP_998801.1; NM_213636.2. [Q9NR12-6]
DR PDB; 2Q3G; X-ray; 1.11 A; A/B=1-84.
DR PDBsum; 2Q3G; -.
DR AlphaFoldDB; Q9NR12; -.
DR SMR; Q9NR12; -.
DR BioGRID; 114682; 229.
DR IntAct; Q9NR12; 193.
DR MINT; Q9NR12; -.
DR STRING; 9606.ENSP00000348099; -.
DR GlyConnect; 2908; 1 O-Linked glycan (1 site). [Q9NR12-4]
DR GlyGen; Q9NR12; 2 sites, 2 O-linked glycans (2 sites).
DR iPTMnet; Q9NR12; -.
DR MetOSite; Q9NR12; -.
DR PhosphoSitePlus; Q9NR12; -.
DR SwissPalm; Q9NR12; -.
DR BioMuta; PDLIM7; -.
DR DMDM; 74752914; -.
DR CPTAC; CPTAC-107; -.
DR CPTAC; CPTAC-108; -.
DR EPD; Q9NR12; -.
DR jPOST; Q9NR12; -.
DR MassIVE; Q9NR12; -.
DR MaxQB; Q9NR12; -.
DR PaxDb; Q9NR12; -.
DR PeptideAtlas; Q9NR12; -.
DR PRIDE; Q9NR12; -.
DR ProteomicsDB; 82244; -. [Q9NR12-1]
DR ProteomicsDB; 82245; -. [Q9NR12-2]
DR ProteomicsDB; 82246; -. [Q9NR12-3]
DR ProteomicsDB; 82247; -. [Q9NR12-4]
DR ProteomicsDB; 82248; -. [Q9NR12-5]
DR ProteomicsDB; 82249; -. [Q9NR12-6]
DR Antibodypedia; 17442; 150 antibodies from 23 providers.
DR DNASU; 9260; -.
DR Ensembl; ENST00000355572.6; ENSP00000347776.2; ENSG00000196923.14. [Q9NR12-6]
DR Ensembl; ENST00000355841.7; ENSP00000348099.2; ENSG00000196923.14. [Q9NR12-1]
DR Ensembl; ENST00000359895.6; ENSP00000352964.2; ENSG00000196923.14. [Q9NR12-2]
DR Ensembl; ENST00000393551.5; ENSP00000377182.1; ENSG00000196923.14. [Q9NR12-4]
DR Ensembl; ENST00000486828.6; ENSP00000439157.1; ENSG00000196923.14. [Q9NR12-5]
DR Ensembl; ENST00000493815.5; ENSP00000431236.1; ENSG00000196923.14. [Q9NR12-3]
DR GeneID; 9260; -.
DR KEGG; hsa:9260; -.
DR MANE-Select; ENST00000355841.7; ENSP00000348099.2; NM_005451.5; NP_005442.2.
DR UCSC; uc003mhb.3; human. [Q9NR12-1]
DR CTD; 9260; -.
DR DisGeNET; 9260; -.
DR GeneCards; PDLIM7; -.
DR HGNC; HGNC:22958; PDLIM7.
DR HPA; ENSG00000196923; Tissue enhanced (endometrium, skeletal muscle).
DR MIM; 605903; gene.
DR neXtProt; NX_Q9NR12; -.
DR OpenTargets; ENSG00000196923; -.
DR PharmGKB; PA128394546; -.
DR VEuPathDB; HostDB:ENSG00000196923; -.
DR eggNOG; KOG1703; Eukaryota.
DR GeneTree; ENSGT00940000159626; -.
DR HOGENOM; CLU_001357_8_1_1; -.
DR InParanoid; Q9NR12; -.
DR OMA; ACKVPIR; -.
DR OrthoDB; 1013114at2759; -.
DR PhylomeDB; Q9NR12; -.
DR TreeFam; TF106408; -.
DR PathwayCommons; Q9NR12; -.
DR Reactome; R-HSA-8853659; RET signaling.
DR SignaLink; Q9NR12; -.
DR BioGRID-ORCS; 9260; 23 hits in 1079 CRISPR screens.
DR ChiTaRS; PDLIM7; human.
DR EvolutionaryTrace; Q9NR12; -.
DR GeneWiki; PDLIM7; -.
DR GenomeRNAi; 9260; -.
DR Pharos; Q9NR12; Tbio.
DR PRO; PR:Q9NR12; -.
DR Proteomes; UP000005640; Chromosome 5.
DR RNAct; Q9NR12; protein.
DR Bgee; ENSG00000196923; Expressed in body of uterus and 157 other tissues.
DR ExpressionAtlas; Q9NR12; baseline and differential.
DR Genevisible; Q9NR12; HS.
DR GO; GO:0015629; C:actin cytoskeleton; IDA:HPA.
DR GO; GO:0005912; C:adherens junction; IDA:BHF-UCL.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0031941; C:filamentous actin; IBA:GO_Central.
DR GO; GO:0005925; C:focal adhesion; IDA:HPA.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0001726; C:ruffle; IEA:Ensembl.
DR GO; GO:0001725; C:stress fiber; 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:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0051371; F:muscle alpha-actinin binding; IBA:GO_Central.
DR GO; GO:0030036; P:actin cytoskeleton organization; IBA:GO_Central.
DR GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR GO; GO:0007507; P:heart development; IBA:GO_Central.
DR GO; GO:0061061; P:muscle structure development; IBA:GO_Central.
DR GO; GO:0001503; P:ossification; IEA:UniProtKB-KW.
DR GO; GO:0045669; P:positive regulation of osteoblast differentiation; IEA:Ensembl.
DR GO; GO:0006898; P:receptor-mediated endocytosis; TAS:ProtInc.
DR Gene3D; 2.30.42.10; -; 1.
DR InterPro; IPR001478; PDZ.
DR InterPro; IPR036034; PDZ_sf.
DR InterPro; IPR001781; Znf_LIM.
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 3D-structure; Alternative splicing; Cytoplasm; Cytoskeleton;
KW Developmental protein; Differentiation; Direct protein sequencing;
KW LIM domain; Metal-binding; Methylation; Osteogenesis; Phosphoprotein;
KW Reference proteome; Repeat; Zinc.
FT CHAIN 1..457
FT /note="PDZ and LIM domain protein 7"
FT /id="PRO_0000075881"
FT DOMAIN 1..85
FT /note="PDZ"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00143"
FT DOMAIN 280..338
FT /note="LIM zinc-binding 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00125"
FT DOMAIN 339..398
FT /note="LIM zinc-binding 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00125"
FT DOMAIN 399..457
FT /note="LIM zinc-binding 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00125"
FT REGION 82..142
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 176..226
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 239..258
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 178..192
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 204..223
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 240..258
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 78
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 103
FT /note="Asymmetric dimethylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 111
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 247
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT VAR_SEQ 94..133
FT /note="ASAPAADPPRYTFAPSVSLNKTARPFGAPPPADSAPQQNG -> VQTPDK
FT (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:11874232"
FT /id="VSP_016509"
FT VAR_SEQ 134..153
FT /note="QPLRPLVPDASKQRLMENTE -> CRPLTNSRSDRWSQMPASSG (in
FT isoform 3)"
FT /evidence="ECO:0000303|PubMed:11874232"
FT /id="VSP_016510"
FT VAR_SEQ 154..457
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:11874232"
FT /id="VSP_016513"
FT VAR_SEQ 191..287
FT /note="SQVPRTEAPAPASSTPQEPWPGPTAPSPTSRPPWAVDPAFAERYAPDKTSTV
FT LTRHSQPATPTPLQSRTSIVQAAAGGVPGGGSNNGKTPVCHQCHK -> RPYRPQPYQP
FT PALGCGPCVCRALCPGQNEHSADPAQPAGHAHAAAEPHLHCAGSCRRGARRGQQQRQDS
FT RVSPVPQGHPGPLPGGAGPRVPPGGVCV (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_016511"
FT VAR_SEQ 191..222
FT /note="SQVPRTEAPAPASSTPQEPWPGPTAPSPTSRP -> REKYVLELQSPRYTRL
FT RDWHHQRSAHVLNVQS (in isoform 6)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_016512"
FT VAR_SEQ 192..457
FT /note="Missing (in isoform 5)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_016514"
FT VAR_SEQ 223..457
FT /note="Missing (in isoform 6)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_016515"
FT VAR_SEQ 288..457
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_016516"
FT VARIANT 326
FT /note="A -> T (in dbSNP:rs2306764)"
FT /id="VAR_050168"
FT VARIANT 450
FT /note="K -> N (in a breast cancer sample; somatic
FT mutation)"
FT /evidence="ECO:0000269|PubMed:16959974"
FT /id="VAR_036193"
FT MUTAGEN 15..16
FT /note="GF->AA: Loss of binding to TPM2."
FT /evidence="ECO:0000269|PubMed:10359609"
FT MUTAGEN 63
FT /note="H->A: Loss of binding to TPM2."
FT /evidence="ECO:0000269|PubMed:10359609"
FT CONFLICT 138
FT /note="P -> Q (in Ref. 4; BC067806)"
FT /evidence="ECO:0000305"
FT STRAND 1..12
FT /evidence="ECO:0007829|PDB:2Q3G"
FT STRAND 16..21
FT /evidence="ECO:0007829|PDB:2Q3G"
FT HELIX 22..24
FT /evidence="ECO:0007829|PDB:2Q3G"
FT STRAND 26..33
FT /evidence="ECO:0007829|PDB:2Q3G"
FT HELIX 38..41
FT /evidence="ECO:0007829|PDB:2Q3G"
FT STRAND 49..53
FT /evidence="ECO:0007829|PDB:2Q3G"
FT HELIX 58..60
FT /evidence="ECO:0007829|PDB:2Q3G"
FT HELIX 63..71
FT /evidence="ECO:0007829|PDB:2Q3G"
FT STRAND 76..84
FT /evidence="ECO:0007829|PDB:2Q3G"
SQ SEQUENCE 457 AA; 49845 MW; AA37F9E8E987D990 CRC64;
MDSFKVVLEG PAPWGFRLQG GKDFNVPLSI SRLTPGGKAA QAGVAVGDWV LSIDGENAGS
LTHIEAQNKI RACGERLSLG LSRAQPVQSK PQKASAPAAD PPRYTFAPSV SLNKTARPFG
APPPADSAPQ QNGQPLRPLV PDASKQRLME NTEDWRPRPG TGQSRSFRIL AHLTGTEFMQ
DPDEEHLKKS SQVPRTEAPA PASSTPQEPW PGPTAPSPTS RPPWAVDPAF AERYAPDKTS
TVLTRHSQPA TPTPLQSRTS IVQAAAGGVP GGGSNNGKTP VCHQCHKVIR GRYLVALGHA
YHPEEFVCSQ CGKVLEEGGF FEEKGAIFCP PCYDVRYAPS CAKCKKKITG EIMHALKMTW
HVHCFTCAAC KTPIRNRAFY MEEGVPYCER DYEKMFGTKC HGCDFKIDAG DRFLEALGFS
WHDTCFVCAI CQINLEGKTF YSKKDRPLCK SHAFSHV
