LOXL4

LOXL4
Identifiers
Aliases	LOXL4 , LOXC, lysyl oxidase like 4
External IDs	OMIM: 607318 MGI: 1914823 HomoloGene: 12977 GeneCards: LOXL4
Gene location (Human) Chr. Chromosome 10 (human) [1] Band 10q24.2 Start 98,247,690 bp [1] End 98,268,194 bp [1]
Gene location (Mouse) Chr. Chromosome 19 (mouse) [2] Band 19|19 C3 Start 42,582,421 bp [2] End 42,601,252 bp [2]
RNA expression pattern Bgee Human Mouse (ortholog) Top expressed in tibia islet of Langerhans tibialis anterior muscle pancreatic epithelial cell pancreatic ductal cell stromal cell of endometrium parotid gland minor salivary gland Achilles tendon ascending aorta Top expressed in dermal bone calvaria maxilla mandible molar rib ascending aorta aortic valve clavicle fossa More reference expression data BioGPS More reference expression data
Gene ontology Molecular function scavenger receptor activity oxidoreductase activity copper ion binding protein binding oxidoreductase activity, acting on the CH-NH2 group of donors, oxygen as acceptor metal ion binding protein-lysine 6-oxidase activity Cellular component extracellular region receptor complex extracellular exosome membrane extracellular space Biological process receptor-mediated endocytosis peptidyl-lysine oxidation collagen fibril organization vesicle-mediated transport endocytosis Sources:Amigo / QuickGO
Orthologs Species Human Mouse Entrez 84171 67573 Ensembl ENSG00000138131 ENSMUSG00000025185 UniProt Q96JB6 Q924C6 RefSeq (mRNA) NM_032211 NM_001164311 NM_053083 RefSeq (protein) NP_115587 NP_001157783 NP_444313 Location (UCSC) Chr 10: 98.25 – 98.27 Mb Chr 19: 42.58 – 42.6 Mb PubMed search [3] [4]
Wikidata
View/Edit Human View/Edit Mouse

Lysyl oxidase homolog 4 is an enzyme that in humans is encoded by the LOXL4 gene. ^{[5] [6]}

This gene encodes a member of the lysyl oxidase gene family. The prototypic member of the family is essential to the biogenesis of connective tissue, encoding an extracellular copper-dependent amine oxidase that catalyses the first step in the formation of crosslinks in collagens and elastin. A highly conserved amino acid sequence at the C-terminus end appears to be sufficient for amine oxidase activity, suggesting that each family member may retain this function. The N-terminus is poorly conserved and may impart additional roles in developmental regulation, senescence, tumor suppression, cell growth control, and chemotaxis to each member of the family. ^[6]

See also

• LOXL1
• LOXL2
• LOXL3

References

1. GRCh38: Ensembl release 89: ENSG00000138131 - Ensembl, May 2017
2. GRCm38: Ensembl release 89: ENSMUSG00000025185 - Ensembl, May 2017
3. "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
4. "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
5. Ito H, Akiyama H, Iguchi H, Iyama K, Miyamoto M, Ohsawa K, Nakamura T (Jun 2001). "Molecular cloning and biological activity of a novel lysyl oxidase-related gene expressed in cartilage". J Biol Chem. 276 (26): 24023–9. doi: 10.1074/jbc.M100861200 . PMID   11292829.
6. "Entrez Gene: LOXL4 lysyl oxidase-like 4".

Further reading

• Molnar J, Fong KS, He QP, et al. (2003). "Structural and functional diversity of lysyl oxidase and the LOX-like proteins". Biochim. Biophys. Acta. 1647 (1–2): 220–4. doi:10.1016/s1570-9639(03)00053-0. PMID   12686136.
• Asuncion L, Fogelgren B, Fong KS, et al. (2002). "A novel human lysyl oxidase-like gene (LOXL4) on chromosome 10q24 has an altered scavenger receptor cysteine rich domain". Matrix Biol. 20 (7): 487–91. doi:10.1016/S0945-053X(01)00161-5. PMID   11691588.
• Mäki JM, Tikkanen H, Kivirikko KI (2002). "Cloning and characterization of a fifth human lysyl oxidase isoenzyme: the third member of the lysyl oxidase-related subfamily with four scavenger receptor cysteine-rich domains". Matrix Biol. 20 (7): 493–6. doi:10.1016/S0945-053X(01)00157-3. PMID   11691589.
• Strausberg RL, Feingold EA, Grouse LH, et al. (2003). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899–903. Bibcode:2002PNAS...9916899M. doi: 10.1073/pnas.242603899 . PMC   139241 . PMID   12477932.
• Holtmeier C, Görögh T, Beier U, et al. (2003). "Overexpression of a novel lysyl oxidase-like gene in human head and neck squamous cell carcinomas". Anticancer Res. 23 (3B): 2585–91. PMID   12894545.
• Kim MS, Kim SS, Jung ST, et al. (2004). "Expression and purification of enzymatically active forms of the human lysyl oxidase-like protein 4". J. Biol. Chem. 278 (52): 52071–4. doi: 10.1074/jbc.M308856200 . PMID   14551188.
• Ota T, Suzuki Y, Nishikawa T, et al. (2004). "Complete sequencing and characterization of 21,243 full-length human cDNAs". Nat. Genet. 36 (1): 40–5. doi: 10.1038/ng1285 . PMID   14702039.
• Gerhard DS, Wagner L, Feingold EA, et al. (2004). "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)". Genome Res. 14 (10B): 2121–7. doi:10.1101/gr.2596504. PMC   528928 . PMID   15489334.
• Rual JF, Venkatesan K, Hao T, et al. (2005). "Towards a proteome-scale map of the human protein-protein interaction network". Nature. 437 (7062): 1173–8. Bibcode:2005Natur.437.1173R. doi:10.1038/nature04209. PMID   16189514. S2CID   4427026.
• Olsen JV, Blagoev B, Gnad F, et al. (2006). "Global, in vivo, and site-specific phosphorylation dynamics in signaling networks". Cell. 127 (3): 635–48. doi: 10.1016/j.cell.2006.09.026 . PMID   17081983. S2CID   7827573.
• Shieh TM, Lin SC, Liu CJ, et al. (2007). "Association of expression aberrances and genetic polymorphisms of lysyl oxidase with areca-associated oral tumorigenesis". Clin. Cancer Res. 13 (15 Pt 1): 4378–85. doi: 10.1158/1078-0432.CCR-06-2685 . PMID   17671119.