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LRRIQ3
Protein-coding gene in the species Homo sapiens From Wikipedia, the free encyclopedia
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LRRIQ3 (Leucine-rich repeats and IQ motif containing 3), which is also known as LRRC44, is a protein that in humans is encoded by the LRRIQ3 gene.[5] It is predominantly expressed in the testes, and is linked to a number of diseases.[6]
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Gene
Locus
LRRIQ3 is found on the minus strand of the end of the short arm of human chromosome 1 at 1p31.1.[7]
Overall Structure
There are a total of 7 exons in the putative sequence of LRRIQ3.[7]
mRNA
Expression
LRRIQ3 is expressed as 2 primary isoforms, which produce proteins of length 624 amino acids and 464 amino acids respectively.[7] It is expressed at low levels in human and brown rat tissues,[8][9] with highest expression levels in testes tissue. There are relatively high expression levels in T cells, the epididymis, the kidney, and a number of glands.[10]
Protein
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General Characteristics and Compositional Features
Human protein LRRIQ3 Isoform 1 consists of 624 amino acids, and has a molecular weight of 73.7 kDa. The isoelectric point of LRRIQ3 is 9.73, which suggests that LRRIQ3 is basic at normal physiological pH (~7.4).[11] Additionally, there is strong evidence that human LRRIQ3 localizes to the plasma membrane from antibody staining.[12] LRRIQ3 is rich in lysine residues, with a total of 82 lysines. It is also slightly low on glycines.[13]
Domains and Motifs
In total, there are 4 conserved domains within LRRIQ3: 3 leucine-rich repeats and 1 IQ calmodulin-binding motif.[13] Leucine-rich repeats are typically involved in protein-protein interactions, and form a characteristic α/β horseshoe fold.[14][15] An IQ motif provides a binding site for calmodulin (CaM) or CaM-like proteins.[16]
Secondary and Tertiary Structure
LRRIQ3 is predicted to be mostly alpha-helical in structure, including a long alpha-helical C-terminal domain. It is also predicted to function as a monomer.[17][18][19][20]

Post-translational Modifications
LRRIQ3 is predicted to undergo many post-translational modifications. These include O-GlcNAcylation, SUMOylation, ubiquitination, and phosphorylation.[22][23] LRRIQ3 is predicted to have 4 well conserved SUMOylation sites and 1 well conserved ubiquitination site.[22] A representation of these post-translational modifications is shown in the figure below.

Protein Interactions
There is evidence that LRRIQ3 interacts with a number of proteins from two-hybrid assays and affinity chromatography. The proteins LRRIQ3 interact with include LYN, NCK2, GNB4, and ABL1.[25][26] These proteins are associated with cell signalling, cytoskeletal reorganization, and cell differentiation, as well as others.[27][28][29][30]
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Homology and evolution
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Paralogs and Orthologs
No paralogs exists for LRRIQ3 in humans.[6] However, there are a number of orthologs, as reported by BLAST, some of which are listed below.[31] The number of years since divergence from the human protein, listed in "million of years ago (MYA)" below, were calculated using TimeTree.[32]
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Clinical significance
LRRIQ3 is linked to a number of cancers. RNA-seq experiments have shown that LRRIQ3 is severely down-regulated (Log2-fold changes between -3.4 and -4.2) in a number of disease states, including pancreatic cancer, colorectal cancer, and breast cancer.[33][34][35]
References
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