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 27-MAR-2024, entry version 194. 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; Q7L5A3: ATOSB; NbExp=3; IntAct=EBI-350517, EBI-745689; 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; Q86YD7: FAM90A1; NbExp=3; IntAct=EBI-350517, EBI-6658203; CC Q9NR12; O43559: FRS3; NbExp=3; IntAct=EBI-350517, EBI-725515; CC Q9NR12; Q8NEG0: GARIN6; NbExp=3; IntAct=EBI-350517, EBI-752049; 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; 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}; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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 PDB; 7RM8; NMR; -; A=1-84. DR PDBsum; 2Q3G; -. DR PDBsum; 7RM8; -. DR AlphaFoldDB; Q9NR12; -. DR SMR; Q9NR12; -. DR BioGRID; 114682; 268. DR IntAct; Q9NR12; 195. DR MINT; Q9NR12; -. DR STRING; 9606.ENSP00000348099; -. DR GlyConnect; 2908; 1 O-GlcNAc glycan (1 site). [Q9NR12-4] DR GlyCosmos; Q9NR12; 2 sites, 2 glycans. DR GlyGen; Q9NR12; 11 sites, 3 O-linked glycans (11 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; 9606-ENSP00000348099; -. DR PeptideAtlas; 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 Pumba; Q9NR12; -. DR Antibodypedia; 17442; 180 antibodies from 24 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 AGR; HGNC:22958; -. DR CTD; 9260; -. DR DisGeNET; 9260; -. DR GeneCards; PDLIM7; -. DR HGNC; HGNC:22958; PDLIM7. DR HPA; ENSG00000196923; Tissue enhanced (intestine, 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; ACSKIIR; -. DR OrthoDB; 370973at2759; -. 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 1149 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 159 other cell types or tissues. DR ExpressionAtlas; Q9NR12; baseline and differential. 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:0006898; P:receptor-mediated endocytosis; TAS:ProtInc. DR CDD; cd09452; LIM1_Enigma; 1. DR CDD; cd09456; LIM2_Enigma; 1. DR CDD; cd09458; LIM3_Enigma; 1. DR CDD; cd00992; PDZ_signaling; 1. DR Gene3D; 2.30.42.10; -; 1. DR Gene3D; 2.10.110.10; Cysteine Rich Protein; 3. DR InterPro; IPR001478; PDZ. DR InterPro; IPR036034; PDZ_sf. DR InterPro; IPR001781; Znf_LIM. DR PANTHER; PTHR24214:SF0; PDZ AND LIM DOMAIN PROTEIN 7; 1. DR PANTHER; PTHR24214; PDZ AND LIM DOMAIN PROTEIN ZASP; 1. DR Pfam; PF00412; LIM; 3. DR Pfam; PF00595; PDZ; 1. DR SMART; SM00132; LIM; 3. DR SMART; SM00228; PDZ; 1. DR SUPFAM; SSF57716; Glucocorticoid receptor-like (DNA-binding domain); 4. DR SUPFAM; SSF50156; PDZ domain-like; 1. DR PROSITE; PS00478; LIM_DOMAIN_1; 2. DR PROSITE; PS50023; LIM_DOMAIN_2; 3. DR PROSITE; PS50106; PDZ; 1. DR Genevisible; Q9NR12; HS. 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 //