Human Gene PDLIM7 (uc003mhd.1) Description and Page Index
Description: Homo sapiens PDZ and LIM domain 7 (enigma) (PDLIM7), transcript variant 1, mRNA. RefSeq Summary (NM_005451): The protein encoded by this gene is representative of a family of proteins composed of conserved PDZ and LIM domains. LIM domains are proposed to function in protein-protein recognition in a variety of contexts including gene transcription and development and in cytoskeletal interaction. The LIM domains of this protein bind to protein kinases, whereas the PDZ domain binds to actin filaments. The gene product is involved in the assembly of an actin filament-associated complex essential for transmission of ret/ptc2 mitogenic signaling. The biological function is likely to be that of an adapter, with the PDZ domain localizing the LIM-binding proteins to actin filaments of both skeletal muscle and nonmuscle tissues. Alternative splicing of this gene results in multiple transcript variants. [provided by RefSeq, Jul 2008]. Transcript (Including UTRs) Position: hg19 chr5:176,910,395-176,924,602 Size: 14,208 Total Exon Count: 14 Strand: - Coding Region Position: hg19 chr5:176,910,645-176,918,101 Size: 7,457 Coding Exon Count: 8
ID:PDLI7_HUMAN DESCRIPTION: RecName: Full=PDZ and LIM domain protein 7; AltName: Full=LIM mineralization protein; Short=LMP; AltName: Full=Protein enigma; FUNCTION: May function as a scaffold on which the coordinated assembly of proteins can occur. May play a role as an adapter that, via its PDZ domain, localizes LIM-binding proteins to actin filaments of both skeletal muscle and nonmuscle tissues. Involved in both of the two fundamental mechanisms of bone formation, direct bone formation e.g (embryonic flat bones mandible and cranium), and endochondral bone formation e.g (embryonic long bone development). Plays a role during fracture repair. Involved in BMP6 signaling pathway (By similarity). SUBUNIT: Binds via its LIM zinc-binding 3 domain (LIM 3) to endocytic codes of INSR, but not with those of IGF1R, LDLR, TFRC, or EGFR. Interacts with various PKC isoforms through the LIM zinc- binding domains. Binds to RET in a phosphorylation-independent manner via its LIM zinc-binding domain 2 (LIM 2). Probably part of a complex with SHC and the RET dimer. Interacts with TPM2. Interacts with TBX4 and TBX5 (By similarity). INTERACTION: Q9NRR5:UBQLN4; NbExp=2; IntAct=EBI-350517, EBI-711226; SUBCELLULAR LOCATION: Cytoplasm (By similarity). Cytoplasm, cytoskeleton (By similarity). Note=Colocalizes with RET to the cell periphery and in some cytoskeletal components. Colocalizes with TPM2 near the Z line in muscle. Co-localizes with TBX4 and TBX5 to actin filaments (By similarity). TISSUE SPECIFICITY: Isoform 1 and isoform 2 are expressed ubiquitously, however, isoform 2 predominates in skeletal muscle, isoform 1 is more abundant in lung, spleen, leukocytes and fetal liver. DOMAIN: The LIM zinc-binding 2 (LIM 2) domain interacts with TBX4 (By similarity). DOMAIN: The LIM zinc-binding 3 (LIM 3) domain provides the structural basis for recognition of tyrosine-containing tight turn structures. This domain is necessary and sufficient for interaction with TBX5 (By similarity). DOMAIN: Anchored to cell periphery via its N-terminal PDZ domain. SIMILARITY: Contains 3 LIM zinc-binding domains. SIMILARITY: Contains 1 PDZ (DHR) domain. SEQUENCE CAUTION: Sequence=AAC37565.1; Type=Frameshift; Positions=103, 128, 161, 183, 195, 245;
The RNAfold program from the Vienna RNA Package is used to perform the secondary structure predictions and folding calculations. The estimated folding energy is in kcal/mol. The more negative the energy, the more secondary structure the RNA is likely to have.
ModBase Predicted Comparative 3D Structure on Q9NR12
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Orthologous Genes in Other Species
Orthologies between human, mouse, and rat are computed by taking the best BLASTP hit, and filtering out non-syntenic hits. For more distant species reciprocal-best BLASTP hits are used. Note that the absence of an ortholog in the table below may reflect incomplete annotations in the other species rather than a true absence of the orthologous gene.