LYOX_HUMAN
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 03-AUG-2022, entry version 204.
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="http://atlasgeneticsoncology.org/Genes/LOXID41191ch5q23.html";
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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; 51.
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 GlyGen; P28300; 7 sites, 15 N-linked glycans (4 sites), 1 O-linked glycan (2 sites).
DR iPTMnet; P28300; -.
DR PhosphoSitePlus; P28300; -.
DR BioMuta; LOX; -.
DR EPD; P28300; -.
DR jPOST; P28300; -.
DR MassIVE; P28300; -.
DR MaxQB; P28300; -.
DR PaxDb; P28300; -.
DR PeptideAtlas; P28300; -.
DR PRIDE; P28300; -.
DR ProteomicsDB; 54461; -.
DR Antibodypedia; 25606; 855 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 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; 330091at2759; -.
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 1083 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 154 other tissues.
DR ExpressionAtlas; P28300; baseline and differential.
DR Genevisible; P28300; HS.
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:0005634; C:nucleus; IEA:Ensembl.
DR GO; GO:0005518; F:collagen binding; IDA:UniProtKB.
DR GO; GO:0005507; F:copper ion binding; TAS:ProtInc.
DR GO; GO:0004720; F:protein-lysine 6-oxidase activity; IDA:UniProtKB.
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:0035791; P:platelet-derived growth factor receptor-beta signaling pathway; IEA:Ensembl.
DR GO; GO:0043491; P:protein kinase B signaling; 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:1900120; P:regulation of receptor binding; 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 GO; GO:0042060; P:wound healing; IEA:Ensembl.
DR InterPro; IPR001695; Lysyl_oxidase.
DR InterPro; IPR019828; Lysyl_oxidase_CS.
DR Pfam; PF01186; Lysyl_oxidase; 1.
DR PRINTS; PR00074; LYSYLOXIDASE.
DR PROSITE; PS00926; LYSYL_OXIDASE; 1.
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; unknown pathological significance;
FT dbSNP:rs752839330)"
FT /evidence="ECO:0000269|PubMed:26838787"
FT /id="VAR_077534"
FT VARIANT 154
FT /note="L -> F (in AAT10; unknown pathological 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; unknown pathological significance;
FT 8% 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 186-F-F-
FT 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
