LRRIQ3

LRRIQ3 is found on the minus strand of the end of the short arm of human chromosome 1 at 1p31.1.{{Cite web|url=https://www.ncbi.nlm.nih.gov/gene/127255|title=LRRIQ3 leucine rich repeats and IQ motif containing 3 [Homo sapiens (human)] - Gene - NCBI|website=www.ncbi.nlm.nih.gov|access-date=2018-04-30}}

There are a total of 7 exons in the putative sequence of LRRIQ3.

LRRIQ3 is expressed as 2 primary isoforms, which produce proteins of length 624 amino acids and 464 amino acids respectively. It is expressed at low levels in human and brown rat tissues,{{Cite web|url=https://pax-db.org/protein/2120177|title=Lrriq3 protein abundance in PaxDb|website=pax-db.org|language=en|access-date=2018-04-30}}{{Cite web|url=https://pax-db.org/protein/1853050|title=LRRIQ3 protein abundance in PaxDb|website=pax-db.org|language=en|access-date=2018-04-30}} 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.{{Cite web|url=https://www.ncbi.nlm.nih.gov/geo/tools/profileGraph.cgi?ID=GDS3834:3169|title=GDS3834 / 3169|website=www.ncbi.nlm.nih.gov|access-date=2018-05-06}}

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).{{Cite web|url=https://web.expasy.org/compute_pi/|title=ExPASy - Compute pI/Mw tool|website=web.expasy.org|language=en-US|access-date=2018-04-30}} Additionally, there is strong evidence that human LRRIQ3 localizes to the plasma membrane from antibody staining.{{Cite web|url=https://www.proteinatlas.org/ENSG00000162620-LRRIQ3/cell|title=Cell atlas - LRRIQ3 - The Human Protein Atlas|website=www.proteinatlas.org|access-date=2018-04-30}} LRRIQ3 is rich in lysine residues, with a total of 82 lysines. It is also slightly low on glycines.{{Cite web|url=https://www.ebi.ac.uk/Tools/seqstats/saps/|title=SAPS < Sequence Statistics < EMBL-EBI|last=EMBL-EBI|website=www.ebi.ac.uk|language=en|access-date=2018-04-30}}

In total, there are 4 conserved domains within LRRIQ3: 3 leucine-rich repeats and 1 IQ calmodulin-binding motif. Leucine-rich repeats are typically involved in protein-protein interactions, and form a characteristic α/β horseshoe fold.{{cite journal | vauthors = Kobe B, Deisenhofer J | title = The leucine-rich repeat: a versatile binding motif | journal = Trends Biochem. Sci. | volume = 19 | issue = 10 | pages = 415–21 | date = October 1994 | pmid = 7817399 | issn = 0968-0004| doi = 10.1016/0968-0004(94)90090-6 }}{{cite journal | vauthors = Enkhbayar P, Kamiya M, Osaki M, Matsumoto T, Matsushima N | title = Structural principles of leucine-rich repeat (LRR) proteins | journal = Proteins | volume = 54 | issue = 3 | pages = 394–403 | date = February 2004 | pmid = 14747988 |issn = 1097-0134 | doi = 10.1002/prot.10605 | s2cid = 19951452 }} An IQ motif provides a binding site for calmodulin (CaM) or CaM-like proteins.{{cite journal | vauthors = Rhoads AR, Friedberg F | title = Sequence motifs for calmodulin recognition | journal = FASEB J. | volume = 11 | issue = 5 | pages = 331–40 | date = April 1997 | pmid = 9141499 | issn = 0892-6638| doi = 10.1096/fasebj.11.5.9141499 | doi-access = free | s2cid = 1877645 }}

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.{{cite journal | vauthors = Rost B | title = Review: protein secondary structure prediction continues to rise | journal = J. Struct. Biol. | volume = 134 | issue = 2–3 | pages = 204–18 | date = 2001 | pmid = 11551180 | issn = 1047-8477| doi = 10.1006/jsbi.2001.4336 | citeseerx = 10.1.1.8.8169 }}{{cite journal | vauthors = Ouali M, King RD | title = Cascaded multiple classifiers for secondary structure prediction | journal = Protein Sci. | volume = 9 | issue = 6 | pages = 1162–76 | date = June 2000 | pmid = 10892809 | pmc = 2144653 |issn = 0961-8368 | doi = 10.1110/ps.9.6.1162 }}{{cite journal | vauthors = Cuff JA, Barton GJ | title = Application of multiple sequence alignment profiles to improve protein secondary structure prediction | journal = Proteins | volume = 40 | issue = 3 | pages = 502–11 | date = August 2000 | pmid = 10861942 | issn=0887-3585 | doi = 10.1002/1097-0134(20000815)40:3<502::AID-PROT170>3.0.CO;2-Q | s2cid = 855816 }}{{cite journal | vauthors = Jones DT | title = Protein secondary structure prediction based on position-specific scoring matrices | journal = J. Mol. Biol. | volume = 292 | issue = 2 | pages = 195–202 | date = September 1999 | pmid = 10493868 |issn = 0022-2836| doi = 10.1006/jmbi.1999.3091 | s2cid = 15506630 }}File:LRRIQ3_I-TASSER_Model.png{{cite journal | vauthors = Yang J, Yan R, Roy A, Xu D, Poisson J, Zhang Y | title = The I-TASSER Suite: protein structure and function prediction | journal = Nat. Methods | volume = 12 | issue = 1 | pages = 7–8 | date = January 2015 | pmid = 25549265 | pmc = 4428668 |issn = 1548-7091| doi = 10.1038/nmeth.3213 }} for LRRIQ3. The 3 leucine-rich repeats are shown in red, salmon, and magenta respectively. The IQ calmodulin-binding domain is shown in green.|292x292px]]

LRRIQ3 is predicted to undergo many post-translational modifications. These include O-GlcNAcylation, SUMOylation, ubiquitination, and phosphorylation.{{cite journal | vauthors = Pagni M, Ioannidis V, Cerutti L, Zahn-Zabal M, Jongeneel CV, Falquet L | title = MyHits: a new interactive resource for protein annotation and domain identification | journal = Nucleic Acids Res. | volume = 32 | issue = Web Server issue | pages = W332–5 | date = July 2004 | pmid = 15215405 | pmc = 441617 |issn = 0305-1048| doi = 10.1093/nar/gkh479 }}{{cite journal | vauthors = de Castro E, Sigrist CJ, Gattiker A, Bulliard V, Langendijk-Genevaux PS, Gasteiger E, Bairoch A, Hulo N | title = ScanProsite: detection of PROSITE signature matches and ProRule-associated functional and structural residues in proteins | journal = Nucleic Acids Res. | volume = 34 | issue = Web Server issue | pages = W362–5 | date = July 2006 | pmid = 16845026 |issn = 1362-4962| pmc = 1538847 | doi = 10.1093/nar/gkl124 }} LRRIQ3 is predicted to have 4 well conserved SUMOylation sites and 1 well conserved ubiquitination site. A representation of these post-translational modifications is shown in the figure below.

File:LRRIQ3_Domains_and_Motifs.png

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.{{Cite web|url=https://mentha.uniroma2.it/result.php#LRRIQ3|title=Results - mentha: the interactome browser|website=mentha.uniroma2.it|access-date=2018-04-30}}{{Cite web|url=https://www.uniprot.org/uniprot/A6PVS8|title=LRRIQ3 - Leucine-rich repeat and IQ domain-containing protein 3 - Homo sapiens (Human) - LRRIQ3 gene & protein|website=www.uniprot.org|language=en|access-date=2018-04-30}} These proteins are associated with cell signalling, cytoskeletal reorganization, and cell differentiation, as well as others.{{cite journal | vauthors = Harder KW, Parsons LM, Armes J, Evans N, Kountouri N, Clark R, Quilici C, Grail D, Hodgson GS, Dunn AR, Hibbs ML | title = Gain- and loss-of-function Lyn mutant mice define a critical inhibitory role for Lyn in the myeloid lineage | journal = Immunity | volume = 15 | issue = 4 | pages = 603–15 | date = October 2001 | pmid = 11672542 |issn = 1074-7613 | doi = 10.1016/s1074-7613(01)00208-4| doi-access = free }}{{cite journal | vauthors = Downes GB, Gautam N | title = The G protein subunit gene families | journal = Genomics | volume = 62 | issue = 3 | pages = 544–52 | date = December 1999 | pmid = 10644457 |issn=0888-7543| doi = 10.1006/geno.1999.5992}}{{cite journal | vauthors = Tu Y, Li F, Wu C | title = Nck-2, a novel Src homology2/3-containing adaptor protein that interacts with the LIM-only protein PINCH and components of growth factor receptor kinase-signaling pathways | journal = Mol. Biol. Cell | volume = 9 | issue = 12 | pages = 3367–82 | date = December 1998 | pmid = 9843575 | pmc = 25640 |issn = 1059-1524 | doi = 10.1091/mbc.9.12.3367 }}{{cite journal | vauthors = Era T | title = Bcr-Abl is a "molecular switch" for the decision for growth and differentiation in hematopoietic stem cells | journal = Int. J. Hematol. | volume = 76 | issue = 1 | pages = 35–43 | date = July 2002 | pmid = 12138893 | doi = 10.1007/BF02982716 | s2cid = 10269867 }}

No paralogs exists for LRRIQ3 in humans. However, there are a number of orthologs, as reported by BLAST, some of which are listed below.{{cite journal | vauthors = Altschul SF, Gish W, Miller W, Myers EW, Lipman DJ | title = Basic local alignment search tool | journal = J. Mol. Biol. | volume = 215 | issue = 3 | pages = 403–10 | date = October 1990 | pmid = 2231712 | issn = 0022-2836|doi = 10.1016/S0022-2836(05)80360-2 | s2cid = 14441902 }} The number of years since divergence from the human protein, listed in "million of years ago (MYA)" below, were calculated using TimeTree.{{Cite web|url=http://www.timetree.org/|title=TimeTree :: The Timescale of Life|website=www.timetree.org|access-date=2018-05-06}}

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.{{Cite web|url=https://www.proteinatlas.org/ENSG00000162620-LRRIQ3/tissue|title=Tissue expression of LRRIQ3 - Summary - The Human Protein Atlas|website=www.proteinatlas.org|access-date=2018-05-06}}{{Cite web|url=https://www.ebi.ac.uk/gxa/search?geneQuery=%5B%7B%22value%22:%22LRRIQ3%22%7D%5D&organism=&conditionQuery=%5B%5D&bs=%7B%22homo%20sapiens%22:%5B%22ORGANISM_PART%22%5D,%22bos%20taurus%22:%5B%22ORGANISM_PART%22%5D,%22equus%20caballus%22:%5B%22ORGANISM_PART%22%5D,%22macaca%20mulatta%22:%5B%22ORGANISM_PART%22%5D,%22mus%20musculus%22:%5B%22ORGANISM_PART%22%5D,%22ovis%20aries%22:%5B%22ORGANISM_PART%22%5D,%22papio%20anubis%22:%5B%22ORGANISM_PART%22%5D,%22rattus%20norvegicus%22:%5B%22ORGANISM_PART%22%5D,%22sus%20scrofa%22:%5B%22ORGANISM_PART%22%5D%7D&ds=%7B%22kingdom%22:%5B%22animals%22%5D%7D#differential|title=Search results < Expression Atlas < EMBL-EBI|last=github.com/gxa/atlas/graphs/contributors|first=EMBL-EBI Expression Atlas development team|website=www.ebi.ac.uk|language=en|access-date=2018-04-30}}{{Cite web|url=https://www.ebi.ac.uk/gxa/experiments/E-GEOD-68086|title=Experiment < Expression Atlas < EMBL-EBI|last=github.com/gxa/atlas/graphs/contributors|first=EMBL-EBI Expression Atlas development team|website=www.ebi.ac.uk|language=en|access-date=2018-05-06}}

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Category:Proteins

Category:Genes on human chromosome 1