| LRRIQ3 | |||||||||||||||||||||||||||||||||||||||||||||||||||
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| Identifiers | |||||||||||||||||||||||||||||||||||||||||||||||||||
| Aliases | LRRIQ3 , LRRC44, leucine-rich repeats and IQ motif containing 3, leucine rich repeats and IQ motif containing 3 | ||||||||||||||||||||||||||||||||||||||||||||||||||
| External IDs | OMIM: 617957; MGI: 1921685; HomoloGene: 23668; GeneCards: LRRIQ3; OMA:LRRIQ3 - orthologs | ||||||||||||||||||||||||||||||||||||||||||||||||||
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| Wikidata | |||||||||||||||||||||||||||||||||||||||||||||||||||
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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]
LRRIQ3 is found on the minus strand of the end of the short arm of human chromosome 1 at 1p31.1. [7]
There are a total of 7 exons in the putative sequence of LRRIQ3. [7]
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]
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]
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]
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]
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.
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]
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]
| Genus and species | Common name | Divergence from Human Lineage (MYA) | Accession number | Sequence length (aa) | Sequence Identity to Human Protein | Sequence Similarity to Human Protein |
|---|---|---|---|---|---|---|
| Gorilla gorilla gorilla | Gorilla | 9.06 | XP_004026030.1 | 624 | 97% | 98% |
| Macaca mulatta | Rhesus monkey | 29.44 | XP_001097148.2 | 623 | 93% | 95% |
| Ursus maritimus | Polar bear | 96 | XP_008689049.1 | 625 | 76% | 87% |
| Felis catus | Domestic cat | 96 | XP_003990274.1 | 625 | 74% | 86% |
| Camelus ferus | Bactrian camel | 96 | XP_006178380.1 | 618 | 73% | 84% |
| Oryctolagus cuniculus | European rabbit | 90 | XP_002715603.1 | 622 | 71% | 83% |
| Bison bison bison | American bison | 96 | XP_010847739.1 | 625 | 70% | 82% |
| Trichechus manatus latirostris | Manatee | 105 | XP_004369192.1 | 623 | 70% | 82% |
| Loxodonta africana | African elephant | 105 | XP_003411181.1 | 625 | 68% | 80% |
| Condylura cristata | Star-nosed mole | 96 | XP_004679575.1 | 627 | 67% | 80% |
| Eptesicus fuscus | Big brown bat | 96 | XP_008137759.1 | 621 | 66% | 80% |
| Myotis davidii | Vesper bat | 96 | XP_006775977.1 | 618 | 65% | 79% |
| Rattus norvegicus | Norway rat | 90 | NP_001019478.1 | 633 | 62% | 77% |
| Mus Musculus | House mouse | 90 | NP_083214.2 | 633 | 63% | 76% |
| Sorex araneus | Common shrew | 96 | XP_004603704.1 | 612 | 55% | 73% |
| Chrysemys picta bellii | Painted turtle | 312 | XP_005285573.1 | 624 | 40% | 56% |
| Pogona vitticeps | Bearded dragon | 312 | XP_020650341.1 | 651 | 35% | 54% |
| Apteryx australis mantelli | Brown kiwi | 312 | XP_013800580.1 | 664 | 35% | 54% |
| Struthio camelus australis | Southern Ostrich | 312 | XP_009685099.1 | 628 | 34% | 51% |
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]
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