Protein-lysine 6-oxidase
Details
- Name
- Protein-lysine 6-oxidase
- Synonyms
- 1.4.3.13
- Lysyl oxidase
- Gene Name
- LOX
- Organism
- Humans
- Amino acid sequence
>lcl|BSEQ0049444|Protein-lysine 6-oxidase MRFAWTVLLLGPLQLCALVHCAPPAAGQQQPPREPPAAPGAWRQQIQWENNGQVFSLLSL GSQYQPQRRRDPGAAVPGAANASAQQPRTPILLIRDNRTAAARTRTAGSSGVTAGRPRPT ARHWFQAGYSTSRAREAGASRAENQTAPGEVPALSNLRPPSRVDGMVGDDPYNPYKYSDD NPYYNYYDTYERPRPGGRYRPGYGTGYFQYGLPDLVADPYYIQASTYVQKMSMYNLRCAA EENCLASTAYRADVRDYDHRVLLRFPQRVKNQGTSDFLPSRPRYSWEWHSCHQHYHSMDE FSHYDLLDANTQRRVAEGHKASFCLEDTSCDYGYHRRFACTAHTQGLSPGCYDTYGADID CQWIDITDVKPGNYILKVSVNPSYLVPESDYTNNVVRCDIRYTGHHAYASGCTISPY
- Number of residues
- 417
- Molecular Weight
- 46943.67
- Theoretical pI
- Not Available
- GO Classification
- Functionscopper ion binding / protein-lysine 6-oxidase activityProcessesaorta development / blood vessel morphogenesis / cellular protein modification process / collagen fibril organization / elastic fiber assembly / extracellular matrix organization / heart development / lung development / response to drug / response to steroid hormone / wound healingComponentscollagen trimer / extracellular region / extracellular space / nucleus / proteinaceous extracellular matrix
- General Function
- Protein-lysine 6-oxidase activity
- Specific Function
- Responsible for the post-translational oxidative deamination of peptidyl lysine residues in precursors to fibrous collagen and elastin (PubMed:26838787). Regulator of Ras expression. May play a role in tumor suppression. Plays a role in the aortic wall architecture (By similarity).
- Pfam Domain Function
- Lysyl_oxidase (PF01186)
- Transmembrane Regions
- Not Available
- Cellular Location
- Secreted
- Gene sequence
>lcl|BSEQ0049445|Protein-lysine 6-oxidase (LOX) ATGCGCTTCGCCTGGACCGTGCTCCTGCTCGGGCCTTTGCAGCTCTGCGCGCTAGTGCAC TGCGCCCCTCCCGCCGCCGGCCAACAGCAGCCCCCGCGCGAGCCGCCGGCGGCTCCGGGC GCCTGGCGCCAGCAGATCCAATGGGAGAACAACGGGCAGGTGTTCAGCTTGCTGAGCCTG GGCTCACAGTACCAGCCTCAGCGCCGCCGGGACCCGGGCGCCGCCGTCCCTGGTGCAGCC AACGCCTCCGCCCAGCAGCCCCGCACTCCGATCCTGCTGATCCGCGACAACCGCACCGCC GCGGCGCGAACGCGGACGGCCGGCTCATCTGGAGTCACCGCTGGCCGCCCCAGGCCCACC GCCCGTCACTGGTTCCAAGCTGGCTACTCGACATCTAGAGCCCGCGAAGCTGGCGCCTCG CGCGCGGAGAACCAGACAGCGCCGGGAGAAGTTCCTGCGCTCAGTAACCTGCGGCCGCCC AGCCGCGTGGACGGCATGGTGGGCGACGACCCTTACAACCCCTACAAGTACTCTGACGAC AACCCTTATTACAACTACTACGATACTTATGAAAGGCCCAGACCTGGGGGCAGGTACCGG CCCGGATACGGCACTGGCTACTTCCAGTACGGTCTCCCAGACCTGGTGGCCGACCCCTAC TACATCCAGGCGTCCACGTACGTGCAGAAGATGTCCATGTACAACCTGAGATGCGCGGCG GAGGAAAACTGTCTGGCCAGTACAGCATACAGGGCAGATGTCAGAGATTATGATCACAGG GTGCTGCTCAGATTTCCCCAAAGAGTGAAAAACCAAGGGACATCAGATTTCTTACCCAGC CGACCAAGATATTCCTGGGAATGGCACAGTTGTCATCAACATTACCACAGTATGGATGAG TTTAGCCACTATGACCTGCTTGATGCCAACACCCAGAGGAGAGTGGCTGAAGGCCACAAA GCAAGTTTCTGTCTTGAAGACACATCCTGTGACTATGGCTACCACAGGCGATTTGCATGT ACTGCACACACACAGGGATTGAGTCCTGGCTGTTATGATACCTATGGTGCAGACATAGAC TGCCAGTGGATTGATATTACAGATGTAAAACCTGGAAACTATATCCTAAAGGTCAGTGTA AACCCCAGCTACCTGGTTCCTGAATCTGACTATACCAACAATGTTGTGCGCTGTGACATT CGCTACACAGGACATCATGCGTATGCCTCAGGCTGCACAATTTCACCGTATTAG
- Chromosome Location
- Not Available
- Locus
- Not Available
- External Identifiers
Resource Link UniProtKB ID P28300 UniProtKB Entry Name LYOX_HUMAN HGNC ID HGNC:6664 - General References
- Hamalainen ER, Jones TA, Sheer D, Taskinen K, Pihlajaniemi T, Kivirikko KI: Molecular cloning of human lysyl oxidase and assignment of the gene to chromosome 5q23.3-31.2. Genomics. 1991 Nov;11(3):508-16. [Article]
- Mariani TJ, Trackman PC, Kagan HM, Eddy RL, Shows TB, Boyd CD, Deak SB: The complete derived amino acid sequence of human lysyl oxidase and assignment of the gene to chromosome 5 (extensive sequence homology with the murine ras recision gene). Matrix. 1992 Jun;12(3):242-8. [Article]
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- Hamalainen ER, Kemppainen R, Pihlajaniemi T, Kivirikko KI: Structure of the human lysyl oxidase gene. Genomics. 1993 Sep;17(3):544-8. [Article]
- Svinarich DM, Twomey TA, Macauley SP, Krebs CJ, Yang TP, Krawetz SA: Characterization of the human lysyl oxidase gene locus. J Biol Chem. 1992 Jul 15;267(20):14382-7. [Article]
- Pilecki B, Holm AT, Schlosser A, Moeller JB, Wohl AP, Zuk AV, Heumuller SE, Wallis R, Moestrup SK, Sengle G, Holmskov U, Sorensen GL: Characterization of Microfibrillar-associated Protein 4 (MFAP4) as a Tropoelastin- and Fibrillin-binding Protein Involved in Elastic Fiber Formation. J Biol Chem. 2016 Jan 15;291(3):1103-14. doi: 10.1074/jbc.M115.681775. Epub 2015 Nov 24. [Article]
- Csiszar K, Mariani TJ, Gosin JS, Deak SB, Boyd CD: A restriction fragment length polymorphism results in a nonconservative amino acid substitution encoded within the first exon of the human lysyl oxidase gene. Genomics. 1993 May;16(2):401-6. [Article]
- Guo DC, Regalado ES, Gong L, Duan X, Santos-Cortez RL, Arnaud P, Ren Z, Cai B, Hostetler EM, Moran R, Liang D, Estrera A, Safi HJ, Leal SM, Bamshad MJ, Shendure J, Nickerson DA, Jondeau G, Boileau C, Milewicz DM: LOX Mutations Predispose to Thoracic Aortic Aneurysms and Dissections. Circ Res. 2016 Mar 18;118(6):928-34. doi: 10.1161/CIRCRESAHA.115.307130. Epub 2016 Jan 12. [Article]
- Lee VS, Halabi CM, Hoffman EP, Carmichael N, Leshchiner I, Lian CG, Bierhals AJ, Vuzman D, Mecham RP, Frank NY, Stitziel NO: Loss of function mutation in LOX causes thoracic aortic aneurysm and dissection in humans. Proc Natl Acad Sci U S A. 2016 Aug 2;113(31):8759-64. doi: 10.1073/pnas.1601442113. Epub 2016 Jul 18. [Article]