ID LYOX_HUMAN Reviewed; 417 AA. AC P28300; B2R5Q3; Q5FWF0; DT 01-DEC-1992, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-1993, sequence version 2. DT 27-MAR-2024, entry version 213. DE RecName: Full=Protein-lysine 6-oxidase; DE EC=1.4.3.13 {ECO:0000269|PubMed:26838787, ECO:0000269|PubMed:31152061}; DE AltName: Full=Lysyl oxidase; DE Contains: DE RecName: Full=Protein-lysine 6-oxidase, long form {ECO:0000305|PubMed:31152061}; DE Contains: DE RecName: Full=Protein-lysine 6-oxidase, short form {ECO:0000305|PubMed:31152061}; DE Flags: Precursor; GN Name=LOX; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; OC Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RX PubMed=1685472; DOI=10.1016/0888-7543(91)90057-l; RA Haemaelaeinen E.-R., Jones T.A., Sheer D., Taskinen K., Pihlajaniemi T., RA Kivirikko K.I.; RT "Molecular cloning of human lysyl oxidase and assignment of the gene to RT chromosome 5q23.3-31.2."; RL Genomics 11:508-516(1991). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA]. RC TISSUE=Skin; RX PubMed=1357535; DOI=10.1016/s0934-8832(11)80067-3; RA Mariani T.J., Trackman P.C., Kagan H.M., Eddy R.L., Shows T.B., Boyd C.D., RA Deak S.B.; RT "The complete derived amino acid sequence of human lysyl oxidase and RT assignment of the gene to chromosome 5 (extensive sequence homology with RT the murine ras recision gene)."; RL Matrix 12:242-248(1992). RN [3] RP NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY. RX PubMed=7706256; DOI=10.1074/jbc.270.13.7176; RA Kim Y., Boyd C.D., Csiszar K.; RT "A new gene with sequence and structural similarity to the gene encoding RT human lysyl oxidase."; RL J. Biol. Chem. 270:7176-7182(1995). RN [4] RP NUCLEOTIDE SEQUENCE [MRNA]. RX PubMed=10391127; DOI=10.1023/a:1006913122261; RA Contente S., Kenyon K., Sriraman P., Subramanyan S., Friedman R.M.; RT "Epigenetic inhibition of lysyl oxidase transcription after transformation RT by ras oncogene."; RL Mol. Cell. Biochem. 194:79-91(1999). RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT GLN-158. RX PubMed=14702039; DOI=10.1038/ng1285; RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S., RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., RA Isogai T., Sugano S.; RT "Complete sequencing and characterization of 21,243 full-length human RT cDNAs."; RL Nat. Genet. 36:40-45(2004). RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Lung; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA project: RT the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [7] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-213. RX PubMed=7902322; DOI=10.1006/geno.1993.1369; RA Haemaelaeinen E.-R., Kemppainen R., Pihlajaniemi T., Kivirikko K.I.; RT "Structure of the human lysyl oxidase gene."; RL Genomics 17:544-548(1993). RN [8] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 55-216. RC TISSUE=Blood; RX PubMed=1352776; DOI=10.1016/s0021-9258(19)49723-8; RA Svinarich D.M., Twomey T.A., Macauley S.P., Krebs C.J., Yang T.P., RA Krawetz S.A.; RT "Characterization of the human lysyl oxidase gene locus."; RL J. Biol. Chem. 267:14382-14387(1992). RN [9] RP INTERACTION WITH EFEMP2. RX PubMed=19570982; DOI=10.1074/jbc.m109.019364; RA Choudhury R., McGovern A., Ridley C., Cain S.A., Baldwin A., Wang M.C., RA Guo C., Mironov A. Jr., Drymoussi Z., Trump D., Shuttleworth A., RA Baldock C., Kielty C.M.; RT "Differential regulation of elastic fiber formation by fibulin-4 and -5."; RL J. Biol. Chem. 284:24553-24567(2009). RN [10] RP INTERACTION WITH EFEMP2. RX PubMed=19855011; DOI=10.1073/pnas.0908268106; RA Horiguchi M., Inoue T., Ohbayashi T., Hirai M., Noda K., Marmorstein L.Y., RA Yabe D., Takagi K., Akama T.O., Kita T., Kimura T., Nakamura T.; RT "Fibulin-4 conducts proper elastogenesis via interaction with cross-linking RT enzyme lysyl oxidase."; RL Proc. Natl. Acad. Sci. U.S.A. 106:19029-19034(2009). RN [11] RP INTERACTION WITH MFAP4. RX PubMed=26601954; DOI=10.1074/jbc.m115.681775; RA Pilecki B., Holm A.T., Schlosser A., Moeller J.B., Wohl A.P., Zuk A.V., RA Heumueller S.E., Wallis R., Moestrup S.K., Sengle G., Holmskov U., RA Sorensen G.L.; RT "Characterization of microfibrillar-associated protein 4 (MFAP4) as a RT tropoelastin- and fibrillin-binding protein involved in elastic fiber RT formation."; RL J. Biol. Chem. 291:1103-1114(2016). RN [12] RP IDENTIFICATION BY MASS SPECTROMETRY, CATALYTIC ACTIVITY, SUBCELLULAR RP LOCATION, PROTEOLYTIC CLEAVAGE, SULFATION AT TYR-187, AND MUTAGENESIS OF RP 183-TYR-TYR-184; 186-TYR-TYR-187 AND TYR-190. RX PubMed=31152061; DOI=10.1074/jbc.ra119.007806; RA Rosell-Garcia T., Paradela A., Bravo G., Dupont L., Bekhouche M., RA Colige A., Rodriguez-Pascual F.; RT "Differential cleavage of lysyl oxidase by the metalloproteinases BMP1 and RT ADAMTS2/14 regulates collagen binding through a tyrosine sulfate domain."; RL J. Biol. Chem. 294:11087-11100(2019). RN [13] RP VARIANT GLN-158. RX PubMed=8100215; DOI=10.1006/geno.1993.1203; RA Csiszar K., Mariani T.J., Gosin J.S., Deak S.B., Boyd C.D.; RT "A restriction fragment length polymorphism results in a nonconservative RT amino acid substitution encoded within the first exon of the human lysyl RT oxidase gene."; RL Genomics 16:401-406(1993). RN [14] RP VARIANTS AAT10 THR-79; PHE-154; ILE-248; PRO-267; ILE-280 AND ARG-348, RP CHARACTERIZATION OF VARIANTS AAT10 THR-79; PHE-154; ILE-248; PRO-267; RP ARG-280 AND ARG-348, INVOLVEMENT IN AAT10, FUNCTION, AND CATALYTIC RP ACTIVITY. RX PubMed=26838787; DOI=10.1161/circresaha.115.307130; RG University of Washington Center for Mendelian Genomics; RA Guo D.C., Regalado E.S., Gong L., Duan X., Santos-Cortez R.L., Arnaud P., RA Ren Z., Cai B., Hostetler E.M., Moran R., Liang D., Estrera A., Safi H.J., RA Leal S.M., Bamshad M.J., Shendure J., Nickerson D.A., Jondeau G., RA Boileau C., Milewicz D.M.; RT "LOX mutations predispose to thoracic aortic aneurysms and dissections."; RL Circ. Res. 118:928-934(2016). RN [15] RP VARIANT AAT10 ARG-298, AND CHARACTERIZATION OF VARIANT AAT10 ARG-298. RX PubMed=27432961; DOI=10.1073/pnas.1601442113; RG Brigham Genomic Medicine; RA Lee V.S., Halabi C.M., Hoffman E.P., Carmichael N., Leshchiner I., RA Lian C.G., Bierhals A.J., Vuzman D., Mecham R.P., Frank N.Y., RA Stitziel N.O.; RT "Loss of function mutation in LOX causes thoracic aortic aneurysm and RT dissection in humans."; RL Proc. Natl. Acad. Sci. U.S.A. 113:8759-8764(2016). CC -!- FUNCTION: Responsible for the post-translational oxidative deamination CC of peptidyl lysine residues in precursors to fibrous collagen and CC elastin (PubMed:26838787). Regulator of Ras expression. May play a role CC in tumor suppression. Plays a role in the aortic wall architecture (By CC similarity). {ECO:0000250|UniProtKB:P28301, CC ECO:0000269|PubMed:26838787}. CC -!- CATALYTIC ACTIVITY: CC Reaction=H2O + L-lysyl-[protein] + O2 = (S)-2-amino-6-oxohexanoyl- CC [protein] + H2O2 + NH4(+); Xref=Rhea:RHEA:24544, Rhea:RHEA-COMP:9752, CC Rhea:RHEA-COMP:12448, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379, CC ChEBI:CHEBI:16240, ChEBI:CHEBI:28938, ChEBI:CHEBI:29969, CC ChEBI:CHEBI:131803; EC=1.4.3.13; CC Evidence={ECO:0000269|PubMed:26838787, ECO:0000269|PubMed:31152061}; CC -!- COFACTOR: CC Name=Cu cation; Xref=ChEBI:CHEBI:23378; CC Evidence={ECO:0000250|UniProtKB:P16636}; CC -!- COFACTOR: CC Name=lysine tyrosylquinone residue; Xref=ChEBI:CHEBI:20489; CC Evidence={ECO:0000250|UniProtKB:P33072}; CC Note=Contains 1 lysine tyrosylquinone. {ECO:0000250|UniProtKB:P33072}; CC -!- SUBUNIT: Interacts with MFAP4 (PubMed:26601954). Interacts (via CC propeptide) with EFEMP2; this interaction is strong and facilitates CC formation of ternary complexes with ELN during elastic fiber assembly; CC this interaction limits interaction of EFEMP2 with FBLN5 CC (PubMed:19855011). {ECO:0000269|PubMed:19855011, CC ECO:0000269|PubMed:26601954}. CC -!- INTERACTION: CC P28300; O95967: EFEMP2; NbExp=7; IntAct=EBI-3893481, EBI-743414; CC P28300; P15502: ELN; NbExp=2; IntAct=EBI-3893481, EBI-1222108; CC P28300; Q9UBX5: FBLN5; NbExp=2; IntAct=EBI-3893481, EBI-947897; CC P28300; P35555: FBN1; NbExp=2; IntAct=EBI-3893481, EBI-2505934; CC P28300; Q15262: PTPRK; NbExp=4; IntAct=EBI-3893481, EBI-474052; CC PRO_0000018520; Q07507: DPT; NbExp=2; IntAct=EBI-20724846, EBI-719535; CC PRO_0000018520; PRO_0000007541 [P01133]: EGF; NbExp=2; IntAct=EBI-20724846, EBI-9076336; CC PRO_0000018520; P02751: FN1; NbExp=2; IntAct=EBI-20724846, EBI-1220319; CC PRO_0000018520; PRO_0000390479 [P02751]: FN1; NbExp=3; IntAct=EBI-20724846, EBI-15482592; CC PRO_0000018520; P00747: PLG; NbExp=2; IntAct=EBI-20724846, EBI-999394; CC PRO_0000018520; P21980: TGM2; NbExp=3; IntAct=EBI-20724846, EBI-727668; CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:31152061}. Secreted, CC extracellular space. CC -!- TISSUE SPECIFICITY: Heart, placenta, skeletal muscle, kidney, lung and CC pancreas. {ECO:0000269|PubMed:7706256}. CC -!- PTM: The lysine tyrosylquinone cross-link (LTQ) is generated by CC condensation of the epsilon-amino group of a lysine with a topaquinone CC produced by oxidation of tyrosine. {ECO:0000250|UniProtKB:P33072}. CC -!- PTM: Proteolytically cleaved by BMP1 which removes the propeptide CC (PubMed:31152061). Also proteolytically cleaved by ADAMTS2 and CC ADAMTS14, but not by ADAMTS3, at an additional cleavage site downstream CC of the BMP1 cleavage site (PubMed:31152061). The propeptide plays a CC role in directing the deposition of this enzyme to elastic fibers, via CC interaction with tropoelastin (By similarity). Cleavage by BMP1 to CC remove the propeptide does not increase enzymatic activity but CC increases binding to collagen (PubMed:31152061). Cleavage by ADAMTS2 CC produces a form with reduced collagen-binding activity CC (PubMed:31152061). {ECO:0000250|UniProtKB:P28301, CC ECO:0000269|PubMed:31152061}. CC -!- PTM: Sulfated at Tyr-187 and also at either Tyr-183 or Tyr-184 which CC enhances binding to collagen. {ECO:0000269|PubMed:31152061}. CC -!- DISEASE: Aortic aneurysm, familial thoracic 10 (AAT10) [MIM:617168]: A CC form of thoracic aortic aneurysm, a disease characterized by permanent CC dilation of the thoracic aorta usually due to degenerative changes in CC the aortic wall. It is primarily associated with a characteristic CC histologic appearance known as 'medial necrosis' or 'Erdheim cystic CC medial necrosis' in which there is degeneration and fragmentation of CC elastic fibers, loss of smooth muscle cells, and an accumulation of CC basophilic ground substance. {ECO:0000269|PubMed:26838787, CC ECO:0000269|PubMed:27432961}. Note=The disease is caused by variants CC affecting the gene represented in this entry. CC -!- SIMILARITY: Belongs to the lysyl oxidase family. {ECO:0000305}. CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and CC Haematology; CC URL="https://atlasgeneticsoncology.org/gene/41191/LOX"; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; S78694; AAB21243.1; -; mRNA. DR EMBL; M94054; AAA59525.1; -; mRNA. DR EMBL; S45875; AAB23549.1; -; mRNA. DR EMBL; AF039291; AAD02130.1; -; mRNA. DR EMBL; AK312269; BAG35200.1; -; mRNA. DR EMBL; BC074820; AAH74820.1; -; mRNA. DR EMBL; BC074872; AAH74872.1; -; mRNA. DR EMBL; BC089436; AAH89436.1; -; mRNA. DR EMBL; L16895; AAA16870.1; -; Genomic_DNA. DR EMBL; M84150; AAA59541.1; -; Genomic_DNA. DR CCDS; CCDS4129.1; -. DR PIR; A47529; OXHUL. DR RefSeq; NP_002308.2; NM_002317.6. DR AlphaFoldDB; P28300; -. DR SMR; P28300; -. DR BioGRID; 110199; 53. DR DIP; DIP-49007N; -. DR IntAct; P28300; 59. DR MINT; P28300; -. DR STRING; 9606.ENSP00000231004; -. DR BindingDB; P28300; -. DR ChEMBL; CHEMBL2249; -. DR DrugBank; DB09130; Copper. DR DrugBank; DB06778; Cupric sulfate. DR GuidetoPHARMACOLOGY; 3097; -. DR GlyConnect; 816; 13 N-Linked glycans (4 sites). DR GlyCosmos; P28300; 6 sites, 16 glycans. DR GlyGen; P28300; 14 sites, 15 N-linked glycans (4 sites), 3 O-linked glycans (9 sites). DR iPTMnet; P28300; -. DR PhosphoSitePlus; P28300; -. DR BioMuta; LOX; -. DR EPD; P28300; -. DR jPOST; P28300; -. DR MassIVE; P28300; -. DR MaxQB; P28300; -. DR PaxDb; 9606-ENSP00000231004; -. DR PeptideAtlas; P28300; -. DR ProteomicsDB; 54461; -. DR Pumba; P28300; -. DR Antibodypedia; 25606; 947 antibodies from 35 providers. DR DNASU; 4015; -. DR Ensembl; ENST00000231004.5; ENSP00000231004.4; ENSG00000113083.15. DR GeneID; 4015; -. DR KEGG; hsa:4015; -. DR MANE-Select; ENST00000231004.5; ENSP00000231004.4; NM_002317.7; NP_002308.2. DR UCSC; uc003ksu.4; human. DR AGR; HGNC:6664; -. DR CTD; 4015; -. DR DisGeNET; 4015; -. DR GeneCards; LOX; -. DR GeneReviews; LOX; -. DR HGNC; HGNC:6664; LOX. DR HPA; ENSG00000113083; Tissue enhanced (adipose). DR MalaCards; LOX; -. DR MIM; 153455; gene. DR MIM; 617168; phenotype. DR neXtProt; NX_P28300; -. DR OpenTargets; ENSG00000113083; -. DR Orphanet; 91387; Familial thoracic aortic aneurysm and aortic dissection. DR PharmGKB; PA30427; -. DR VEuPathDB; HostDB:ENSG00000113083; -. DR eggNOG; ENOG502QWQR; Eukaryota. DR GeneTree; ENSGT00940000154779; -. DR HOGENOM; CLU_002555_2_1_1; -. DR InParanoid; P28300; -. DR OMA; GCHMSTY; -. DR OrthoDB; 3035117at2759; -. DR PhylomeDB; P28300; -. DR TreeFam; TF326061; -. DR BRENDA; 1.4.3.13; 2681. DR PathwayCommons; P28300; -. DR Reactome; R-HSA-1566948; Elastic fibre formation. DR Reactome; R-HSA-2243919; Crosslinking of collagen fibrils. DR SignaLink; P28300; -. DR SIGNOR; P28300; -. DR BioGRID-ORCS; 4015; 17 hits in 1161 CRISPR screens. DR ChiTaRS; LOX; human. DR GeneWiki; Lysyl_oxidase; -. DR GenomeRNAi; 4015; -. DR Pharos; P28300; Tchem. DR PRO; PR:P28300; -. DR Proteomes; UP000005640; Chromosome 5. DR RNAct; P28300; Protein. DR Bgee; ENSG00000113083; Expressed in stromal cell of endometrium and 156 other cell types or tissues. DR ExpressionAtlas; P28300; baseline and differential. DR GO; GO:0005581; C:collagen trimer; IEA:Ensembl. DR GO; GO:0062023; C:collagen-containing extracellular matrix; IBA:GO_Central. DR GO; GO:0005576; C:extracellular region; ISS:UniProtKB. DR GO; GO:0005615; C:extracellular space; IDA:UniProtKB. DR GO; GO:0005518; F:collagen binding; IDA:UniProtKB. DR GO; GO:0005507; F:copper ion binding; TAS:ProtInc. DR GO; GO:0060090; F:molecular adaptor activity; IPI:DisProt. DR GO; GO:0004720; F:protein-lysine 6-oxidase activity; IDA:UniProtKB. DR GO; GO:0036094; F:small molecule binding; IPI:DisProt. DR GO; GO:0035905; P:ascending aorta development; IEA:Ensembl. DR GO; GO:0048514; P:blood vessel morphogenesis; ISS:UniProtKB. DR GO; GO:0030282; P:bone mineralization; IEA:Ensembl. DR GO; GO:0060326; P:cell chemotaxis; IEA:Ensembl. DR GO; GO:1990869; P:cellular response to chemokine; IEA:Ensembl. DR GO; GO:0030199; P:collagen fibril organization; IBA:GO_Central. DR GO; GO:0061448; P:connective tissue development; IEA:Ensembl. DR GO; GO:0035906; P:descending aorta development; IEA:Ensembl. DR GO; GO:0071897; P:DNA biosynthetic process; IEA:Ensembl. DR GO; GO:0048251; P:elastic fiber assembly; IEA:Ensembl. DR GO; GO:0007507; P:heart development; IEA:Ensembl. DR GO; GO:0030324; P:lung development; IEA:Ensembl. DR GO; GO:0046716; P:muscle cell cellular homeostasis; IEA:Ensembl. DR GO; GO:0055001; P:muscle cell development; IEA:Ensembl. DR GO; GO:0001649; P:osteoblast differentiation; IEA:Ensembl. DR GO; GO:0018057; P:peptidyl-lysine oxidation; IDA:UniProtKB. DR GO; GO:0043491; P:phosphatidylinositol 3-kinase/protein kinase B signal transduction; IEA:Ensembl. DR GO; GO:0035791; P:platelet-derived growth factor receptor-beta signaling pathway; IEA:Ensembl. DR GO; GO:0036211; P:protein modification process; TAS:ProtInc. DR GO; GO:0042981; P:regulation of apoptotic process; IEA:Ensembl. DR GO; GO:1903010; P:regulation of bone development; IEA:Ensembl. DR GO; GO:0010468; P:regulation of gene expression; IEA:Ensembl. DR GO; GO:0045652; P:regulation of megakaryocyte differentiation; IEA:Ensembl. DR GO; GO:2000586; P:regulation of platelet-derived growth factor receptor-beta signaling pathway; IEA:Ensembl. DR GO; GO:0001932; P:regulation of protein phosphorylation; IEA:Ensembl. DR GO; GO:0016202; P:regulation of striated muscle tissue development; IEA:Ensembl. DR GO; GO:0017015; P:regulation of transforming growth factor beta receptor signaling pathway; IEA:Ensembl. DR GO; GO:0048545; P:response to steroid hormone; IEA:Ensembl. DR GO; GO:0009410; P:response to xenobiotic stimulus; IEA:Ensembl. DR InterPro; IPR001695; Lysyl_oxidase. DR InterPro; IPR019828; Lysyl_oxidase_CS. DR PANTHER; PTHR45817; LYSYL OXIDASE-LIKE-RELATED; 1. DR PANTHER; PTHR45817:SF6; PROTEIN-LYSINE 6-OXIDASE; 1. DR Pfam; PF01186; Lysyl_oxidase; 1. DR PRINTS; PR00074; LYSYLOXIDASE. DR PROSITE; PS00926; LYSYL_OXIDASE; 1. DR Genevisible; P28300; HS. PE 1: Evidence at protein level; KW Aortic aneurysm; Copper; Disease variant; Disulfide bond; Glycoprotein; KW LTQ; Metal-binding; Oxidoreductase; Reference proteome; Secreted; Signal; KW Sulfation; TPQ. FT SIGNAL 1..21 FT /evidence="ECO:0000250|UniProtKB:P16636" FT PROPEP 22..168 FT /note="Removed by BMP1" FT /evidence="ECO:0000250|UniProtKB:P16636" FT /id="PRO_0000018520" FT CHAIN 169..417 FT /note="Protein-lysine 6-oxidase, long form" FT /evidence="ECO:0000250|UniProtKB:P16636" FT /id="PRO_0000018521" FT CHAIN 219..417 FT /note="Protein-lysine 6-oxidase, short form" FT /evidence="ECO:0000269|PubMed:31152061" FT /id="PRO_0000447885" FT REGION 64..89 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 137..174 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 213..417 FT /note="Lysyl-oxidase like" FT BINDING 292 FT /ligand="Cu cation" FT /ligand_id="ChEBI:CHEBI:23378" FT /evidence="ECO:0000255" FT BINDING 294 FT /ligand="Cu cation" FT /ligand_id="ChEBI:CHEBI:23378" FT /evidence="ECO:0000255" FT BINDING 296 FT /ligand="Cu cation" FT /ligand_id="ChEBI:CHEBI:23378" FT /evidence="ECO:0000255" FT SITE 218..219 FT /note="Cleavage; by ADAMTS2 and ADAMTS14" FT /evidence="ECO:0000269|PubMed:31152061" FT MOD_RES 187 FT /note="Sulfotyrosine" FT /evidence="ECO:0000269|PubMed:31152061" FT MOD_RES 355 FT /note="2',4',5'-topaquinone" FT /evidence="ECO:0000250|UniProtKB:P33072" FT CARBOHYD 81 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 97 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 144 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT DISULFID 238..244 FT /evidence="ECO:0000250|UniProtKB:P33072" FT DISULFID 291..340 FT /evidence="ECO:0000250|UniProtKB:P33072" FT DISULFID 324..330 FT /evidence="ECO:0000250|UniProtKB:P33072" FT DISULFID 351..361 FT /evidence="ECO:0000250|UniProtKB:P33072" FT DISULFID 398..412 FT /evidence="ECO:0000250|UniProtKB:P33072" FT CROSSLNK 320..355 FT /note="Lysine tyrosylquinone (Lys-Tyr)" FT /evidence="ECO:0000250|UniProtKB:P33072" FT VARIANT 79 FT /note="A -> T (in AAT10; uncertain significance; FT dbSNP:rs752839330)" FT /evidence="ECO:0000269|PubMed:26838787" FT /id="VAR_077534" FT VARIANT 154 FT /note="L -> F (in AAT10; uncertain significance; FT dbSNP:rs767855588)" FT /evidence="ECO:0000269|PubMed:26838787" FT /id="VAR_077535" FT VARIANT 158 FT /note="R -> Q (in dbSNP:rs1800449)" FT /evidence="ECO:0000269|PubMed:14702039, FT ECO:0000269|PubMed:8100215" FT /id="VAR_004282" FT VARIANT 248 FT /note="T -> I (in AAT10; uncertain significance; 8% FT decrease of lysyl oxidase activity; dbSNP:rs1561420103)" FT /evidence="ECO:0000269|PubMed:26838787" FT /id="VAR_077536" FT VARIANT 267 FT /note="Q -> P (in AAT10; dbSNP:rs886040967)" FT /evidence="ECO:0000269|PubMed:26838787" FT /id="VAR_077537" FT VARIANT 280 FT /note="S -> I (in AAT10; 50% decrease of lysyl oxidase FT activity; dbSNP:rs886040965)" FT /evidence="ECO:0000269|PubMed:26838787" FT /id="VAR_077538" FT VARIANT 298 FT /note="M -> R (in AAT10; dbSNP:rs876657852)" FT /evidence="ECO:0000269|PubMed:27432961" FT /id="VAR_077539" FT VARIANT 348 FT /note="S -> R (in AAT10; 21% decrease of lysyl oxidase FT activity; dbSNP:rs1561417568)" FT /evidence="ECO:0000269|PubMed:26838787" FT /id="VAR_077540" FT MUTAGEN 183..184 FT /note="YY->FF: Abolishes sulfation and reduces binding to FT collagen; when associated with 186-F-F-187 and F-190." FT /evidence="ECO:0000269|PubMed:31152061" FT MUTAGEN 186..187 FT /note="YY->FF: Abolishes sulfation and reduces binding to FT collagen; when associated with 183-F-F-184 and F-190." FT /evidence="ECO:0000269|PubMed:31152061" FT MUTAGEN 190 FT /note="Y->F: Abolishes sulfation and reduces binding to FT collagen; when associated with 183-F-F-184 and FT 186-F-F-187." FT /evidence="ECO:0000269|PubMed:31152061" FT CONFLICT 30 FT /note="Q -> H (in Ref. 3)" FT /evidence="ECO:0000305" FT CONFLICT 31 FT /note="P -> A (in Ref. 3)" FT /evidence="ECO:0000305" FT CONFLICT 95 FT /note="R -> A (in Ref. 3)" FT /evidence="ECO:0000305" FT CONFLICT 102 FT /note="A -> G (in Ref. 1; AAB21243)" FT /evidence="ECO:0000305" FT CONFLICT 137 FT /note="A -> R (in Ref. 2; AAA59525/AAB23549)" FT /evidence="ECO:0000305" FT CONFLICT 139 FT /note="A -> P (in Ref. 1; AAB21243)" FT /evidence="ECO:0000305" FT CONFLICT 304..305 FT /note="YD -> LY (in Ref. 1; AAB21243)" FT /evidence="ECO:0000305" FT CONFLICT 315 FT /note="V -> W (in Ref. 1; AAB21243)" FT /evidence="ECO:0000305" SQ SEQUENCE 417 AA; 46944 MW; 6412A78443E03F04 CRC64; MRFAWTVLLL GPLQLCALVH CAPPAAGQQQ PPREPPAAPG AWRQQIQWEN NGQVFSLLSL GSQYQPQRRR DPGAAVPGAA NASAQQPRTP ILLIRDNRTA AARTRTAGSS GVTAGRPRPT ARHWFQAGYS TSRAREAGAS RAENQTAPGE VPALSNLRPP SRVDGMVGDD PYNPYKYSDD NPYYNYYDTY ERPRPGGRYR PGYGTGYFQY GLPDLVADPY YIQASTYVQK MSMYNLRCAA EENCLASTAY RADVRDYDHR VLLRFPQRVK NQGTSDFLPS RPRYSWEWHS CHQHYHSMDE FSHYDLLDAN TQRRVAEGHK ASFCLEDTSC DYGYHRRFAC TAHTQGLSPG CYDTYGADID CQWIDITDVK PGNYILKVSV NPSYLVPESD YTNNVVRCDI RYTGHHAYAS GCTISPY //