LOXL2_MOUSE
ID LOXL2_MOUSE Reviewed; 776 AA.
AC P58022; Q8BRE6; Q8BS86; Q8C4K0; Q9JJ39;
DT 27-APR-2001, integrated into UniProtKB/Swiss-Prot.
DT 22-NOV-2005, sequence version 2.
DT 03-AUG-2022, entry version 166.
DE RecName: Full=Lysyl oxidase homolog 2;
DE EC=1.4.3.13 {ECO:0000250|UniProtKB:Q9Y4K0};
DE AltName: Full=Lysyl oxidase-like protein 2;
DE Flags: Precursor;
GN Name=Loxl2;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC STRAIN=C57BL/6J; TISSUE=Embryo, and Head;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 558-776 (ISOFORM 1).
RX PubMed=10842102; DOI=10.1016/s0945-053x(00)00061-5;
RA Jourdan-Le Saux C., Le Saux O., Gleyzal C., Sommer P., Csiszar K.;
RT "The mouse lysyl oxidase-like 2 gene (mLOXL2) maps to chromosome 14 and is
RT highly expressed in skin, lung and thymus.";
RL Matrix Biol. 19:179-183(2000).
RN [3]
RP INDUCTION.
RX PubMed=21835952; DOI=10.1182/blood-2010-10-313296;
RA Bignon M., Pichol-Thievend C., Hardouin J., Malbouyres M., Brechot N.,
RA Nasciutti L., Barret A., Teillon J., Guillon E., Etienne E., Caron M.,
RA Joubert-Caron R., Monnot C., Ruggiero F., Muller L., Germain S.;
RT "Lysyl oxidase-like protein-2 regulates sprouting angiogenesis and type IV
RT collagen assembly in the endothelial basement membrane.";
RL Blood 118:3979-3989(2011).
RN [4]
RP FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=21071451; DOI=10.1074/jbc.m110.155622;
RA Iftikhar M., Hurtado P., Bais M.V., Wigner N., Stephens D.N.,
RA Gerstenfeld L.C., Trackman P.C.;
RT "Lysyl oxidase-like-2 (LOXL2) is a major isoform in chondrocytes and is
RT critically required for differentiation.";
RL J. Biol. Chem. 286:909-918(2011).
RN [5]
RP MUTAGENESIS OF 547-ALA--ILE-667.
RX PubMed=24414204; DOI=10.1242/bio.20146841;
RA Cuevas E.P., Moreno-Bueno G., Canesin G., Santos V., Portillo F., Cano A.;
RT "LOXL2 catalytically inactive mutants mediate epithelial-to-mesenchymal
RT transition.";
RL Biol. Open 3:129-137(2014).
RN [6]
RP FUNCTION.
RX PubMed=25959397; DOI=10.1016/j.molcel.2015.04.012;
RA Iturbide A., Pascual-Reguant L., Fargas L., Cebria J.P., Alsina B.,
RA Garcia de Herreros A., Peiro S.;
RT "LOXL2 oxidizes methylated TAF10 and controls TFIID-dependent genes during
RT neural progenitor differentiation.";
RL Mol. Cell 58:755-766(2015).
CC -!- FUNCTION: Mediates the post-translational oxidative deamination of
CC lysine residues on target proteins leading to the formation of
CC deaminated lysine (allysine) (By similarity). Acts as a transcription
CC corepressor and specifically mediates deamination of trimethylated
CC 'Lys-4' of histone H3 (H3K4me3), a specific tag for epigenetic
CC transcriptional activation (By similarity). Shows no activity against
CC histone H3 when it is trimethylated on 'Lys-9' (H3K9me3) or 'Lys-27'
CC (H3K27me3) or when 'Lys-4' is monomethylated (H3K4me1) or dimethylated
CC (H3K4me2) (By similarity). Also mediates deamination of methylated
CC TAF10, a member of the transcription factor IID (TFIID) complex, which
CC induces release of TAF10 from promoters, leading to inhibition of
CC TFIID-dependent transcription (By similarity). LOXL2-mediated
CC deamination of TAF10 results in transcriptional repression of genes
CC required for embryonic stem cell pluripotency including POU5F1/OCT4,
CC NANOG, KLF4 and SOX2 (PubMed:25959397). Involved in epithelial to
CC mesenchymal transition (EMT) via interaction with SNAI1 and
CC participates in repression of E-cadherin, probably by mediating
CC deamination of histone H3 (By similarity). During EMT, involved with
CC SNAI1 in negatively regulating pericentromeric heterochromatin
CC transcription (By similarity). SNAI1 recruits LOXL2 to pericentromeric
CC regions to oxidize histone H3 and repress transcription which leads to
CC release of heterochromatin component CBX5/HP1A, enabling chromatin
CC reorganization and acquisition of mesenchymal traits (By similarity).
CC Interacts with the endoplasmic reticulum protein HSPA5 which activates
CC the IRE1-XBP1 pathway of the unfolded protein response, leading to
CC expression of several transcription factors involved in EMT and
CC subsequent EMT induction (By similarity). When secreted into the
CC extracellular matrix, promotes cross-linking of extracellular matrix
CC proteins by mediating oxidative deamination of peptidyl lysine residues
CC in precursors to fibrous collagen and elastin (By similarity). Acts as
CC a regulator of sprouting angiogenesis, probably via collagen IV
CC scaffolding (By similarity). Acts as a regulator of chondrocyte
CC differentiation, probably by regulating expression of factors that
CC control chondrocyte differentiation (PubMed:21071451).
CC {ECO:0000250|UniProtKB:Q9Y4K0, ECO:0000269|PubMed:21071451,
CC ECO:0000269|PubMed:25959397}.
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:0000250|UniProtKB:Q9Y4K0};
CC -!- COFACTOR:
CC Name=Cu cation; Xref=ChEBI:CHEBI:23378;
CC Evidence={ECO:0000250|UniProtKB:Q9Y4K0};
CC -!- COFACTOR:
CC Name=lysine tyrosylquinone residue; Xref=ChEBI:CHEBI:20489;
CC Evidence={ECO:0000250|UniProtKB:Q9Y4K0};
CC Note=Contains 1 lysine tyrosylquinone. {ECO:0000250|UniProtKB:P33072,
CC ECO:0000250|UniProtKB:Q9Y4K0};
CC -!- ACTIVITY REGULATION: Specifically inhibited by a mouse monoclonal
CC antibody AB0023, inhibition occurs in a non-competitive manner.
CC {ECO:0000250|UniProtKB:Q9Y4K0}.
CC -!- SUBUNIT: Component of some chromatin repressor complex. Interacts with
CC SNAI1. Interacts with TAF10. Interacts with HSPA5. Interacts with
CC EFEMP2 (By similarity). {ECO:0000250|UniProtKB:Q9Y4K0}.
CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
CC matrix, basement membrane {ECO:0000250|UniProtKB:Q9Y4K0}. Nucleus
CC {ECO:0000250|UniProtKB:Q9Y4K0}. Chromosome
CC {ECO:0000250|UniProtKB:Q9Y4K0}. Endoplasmic reticulum
CC {ECO:0000250|UniProtKB:Q9Y4K0}. Note=Associated with chromatin. It is
CC unclear how LOXL2 is nuclear as it contains a signal sequence and has
CC been shown to be secreted. However, a number of reports confirm its
CC intracellular location and its key role in transcription regulation.
CC {ECO:0000250|UniProtKB:Q9Y4K0}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=P58022-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P58022-2; Sequence=VSP_016231, VSP_016232;
CC -!- TISSUE SPECIFICITY: Ubiquitous. Highest expression in skin, lung and
CC thymus. Present in chondrocytes: mainly expressed by chondrocytes in
CC healing fractures and in epiphyseal growth plates (at protein level).
CC {ECO:0000269|PubMed:21071451}.
CC -!- INDUCTION: Strongly induced in hypoxia. {ECO:0000269|PubMed:21835952}.
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:Q9Y4K0}.
CC -!- PTM: N-glycosylated. N-glycosylation on Asn-458 and Asn-646 may be
CC essential for proper folding and secretion; may be composed of a
CC fucosylated carbohydrates attached to a trimannose N-linked glycan
CC core. {ECO:0000250|UniProtKB:Q9Y4K0}.
CC -!- SIMILARITY: Belongs to the lysyl oxidase family. {ECO:0000305}.
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DR EMBL; AK034957; BAC28894.1; -; mRNA.
DR EMBL; AK045019; BAC32186.1; -; mRNA.
DR EMBL; AK081898; BAC38364.1; -; mRNA.
DR EMBL; AK145323; BAE26367.1; -; mRNA.
DR EMBL; AK159386; BAE35041.1; -; mRNA.
DR EMBL; AF117951; AAF29046.1; -; mRNA.
DR CCDS; CCDS27241.1; -. [P58022-1]
DR RefSeq; NP_201582.2; NM_033325.2. [P58022-1]
DR RefSeq; XP_006519810.1; XM_006519747.2. [P58022-1]
DR AlphaFoldDB; P58022; -.
DR SMR; P58022; -.
DR BioGRID; 220507; 4.
DR IntAct; P58022; 1.
DR MINT; P58022; -.
DR STRING; 10090.ENSMUSP00000022660; -.
DR BindingDB; P58022; -.
DR ChEMBL; CHEMBL4105831; -.
DR GlyGen; P58022; 4 sites.
DR PhosphoSitePlus; P58022; -.
DR MaxQB; P58022; -.
DR PaxDb; P58022; -.
DR PeptideAtlas; P58022; -.
DR PRIDE; P58022; -.
DR ProteomicsDB; 286231; -. [P58022-1]
DR ProteomicsDB; 287256; -. [P58022-2]
DR Antibodypedia; 22758; 464 antibodies from 35 providers.
DR DNASU; 94352; -.
DR Ensembl; ENSMUST00000022660; ENSMUSP00000022660; ENSMUSG00000034205. [P58022-1]
DR Ensembl; ENSMUST00000100420; ENSMUSP00000097987; ENSMUSG00000034205. [P58022-1]
DR GeneID; 94352; -.
DR KEGG; mmu:94352; -.
DR UCSC; uc007umn.3; mouse. [P58022-1]
DR CTD; 4017; -.
DR MGI; MGI:2137913; Loxl2.
DR VEuPathDB; HostDB:ENSMUSG00000034205; -.
DR eggNOG; ENOG502QSX8; Eukaryota.
DR GeneTree; ENSGT00940000155874; -.
DR HOGENOM; CLU_002555_3_0_1; -.
DR InParanoid; P58022; -.
DR OMA; YCTGKEA; -.
DR OrthoDB; 815466at2759; -.
DR PhylomeDB; P58022; -.
DR TreeFam; TF326061; -.
DR Reactome; R-MMU-1566948; Elastic fibre formation.
DR Reactome; R-MMU-2243919; Crosslinking of collagen fibrils.
DR BioGRID-ORCS; 94352; 1 hit in 74 CRISPR screens.
DR ChiTaRS; Loxl2; mouse.
DR PRO; PR:P58022; -.
DR Proteomes; UP000000589; Chromosome 14.
DR RNAct; P58022; protein.
DR Bgee; ENSMUSG00000034205; Expressed in vault of skull and 159 other tissues.
DR Genevisible; P58022; MM.
DR GO; GO:0005604; C:basement membrane; ISS:UniProtKB.
DR GO; GO:0000785; C:chromatin; ISS:UniProtKB.
DR GO; GO:0062023; C:collagen-containing extracellular matrix; HDA:BHF-UCL.
DR GO; GO:0005783; C:endoplasmic reticulum; ISS:UniProtKB.
DR GO; GO:0005615; C:extracellular space; HDA:BHF-UCL.
DR GO; GO:0016020; C:membrane; IEA:InterPro.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0005509; F:calcium ion binding; ISS:UniProtKB.
DR GO; GO:0005507; F:copper ion binding; ISS:UniProtKB.
DR GO; GO:0070492; F:oligosaccharide binding; ISS:UniProtKB.
DR GO; GO:0004720; F:protein-lysine 6-oxidase activity; ISS:UniProtKB.
DR GO; GO:0005044; F:scavenger receptor activity; IEA:InterPro.
DR GO; GO:0030199; P:collagen fibril organization; ISS:UniProtKB.
DR GO; GO:0043542; P:endothelial cell migration; ISS:UniProtKB.
DR GO; GO:0001935; P:endothelial cell proliferation; ISS:UniProtKB.
DR GO; GO:0001837; P:epithelial to mesenchymal transition; ISS:UniProtKB.
DR GO; GO:0070828; P:heterochromatin organization; ISS:UniProtKB.
DR GO; GO:1902455; P:negative regulation of stem cell population maintenance; IDA:UniProtKB.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; ISS:UniProtKB.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; ISS:UniProtKB.
DR GO; GO:0018057; P:peptidyl-lysine oxidation; ISS:UniProtKB.
DR GO; GO:0032332; P:positive regulation of chondrocyte differentiation; IMP:UniProtKB.
DR GO; GO:0010718; P:positive regulation of epithelial to mesenchymal transition; ISS:UniProtKB.
DR GO; GO:0036211; P:protein modification process; ISS:UniProtKB.
DR GO; GO:0046688; P:response to copper ion; ISS:UniProtKB.
DR GO; GO:0001666; P:response to hypoxia; IDA:UniProtKB.
DR GO; GO:0002040; P:sprouting angiogenesis; ISS:UniProtKB.
DR Gene3D; 3.10.250.10; -; 4.
DR InterPro; IPR001695; Lysyl_oxidase.
DR InterPro; IPR019828; Lysyl_oxidase_CS.
DR InterPro; IPR001190; SRCR.
DR InterPro; IPR017448; SRCR-like_dom.
DR InterPro; IPR036772; SRCR-like_dom_sf.
DR Pfam; PF01186; Lysyl_oxidase; 1.
DR Pfam; PF00530; SRCR; 4.
DR PRINTS; PR00074; LYSYLOXIDASE.
DR PRINTS; PR00258; SPERACTRCPTR.
DR SMART; SM00202; SR; 4.
DR SUPFAM; SSF56487; SSF56487; 4.
DR PROSITE; PS00926; LYSYL_OXIDASE; 1.
DR PROSITE; PS00420; SRCR_1; 2.
DR PROSITE; PS50287; SRCR_2; 4.
PE 1: Evidence at protein level;
KW Alternative splicing; Basement membrane; Calcium; Chromatin regulator;
KW Chromosome; Copper; Disulfide bond; Endoplasmic reticulum;
KW Extracellular matrix; Glycoprotein; LTQ; Metal-binding; Nucleus;
KW Oxidoreductase; Reference proteome; Repeat; Repressor; Secreted; Signal;
KW TPQ; Transcription; Transcription regulation.
FT SIGNAL 1..25
FT /evidence="ECO:0000255"
FT CHAIN 26..776
FT /note="Lysyl oxidase homolog 2"
FT /id="PRO_0000042854"
FT DOMAIN 61..162
FT /note="SRCR 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00196"
FT DOMAIN 191..305
FT /note="SRCR 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00196"
FT DOMAIN 329..428
FT /note="SRCR 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00196"
FT DOMAIN 438..546
FT /note="SRCR 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00196"
FT REGION 550..753
FT /note="Lysyl-oxidase like"
FT /evidence="ECO:0000250"
FT BINDING 551
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:Q9Y4K0"
FT BINDING 552
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:Q9Y4K0"
FT BINDING 628
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /evidence="ECO:0000250|UniProtKB:Q9Y4K0"
FT BINDING 630
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /evidence="ECO:0000250|UniProtKB:Q9Y4K0"
FT BINDING 632
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /evidence="ECO:0000250|UniProtKB:Q9Y4K0"
FT BINDING 724
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:Q9Y4K0"
FT BINDING 726
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:Q9Y4K0"
FT BINDING 729
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:Q9Y4K0"
FT BINDING 730
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:Q9Y4K0"
FT MOD_RES 691
FT /note="2',4',5'-topaquinone"
FT /evidence="ECO:0000250|UniProtKB:P33072"
FT CARBOHYD 267
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 291
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 458
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 646
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 87..151
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00196"
FT DISULFID 100..161
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00196"
FT DISULFID 131..141
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00196"
FT DISULFID 221..294
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00196"
FT DISULFID 234..304
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00196"
FT DISULFID 268..278
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00196"
FT DISULFID 354..417
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00196"
FT DISULFID 367..427
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00196"
FT DISULFID 398..408
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00196"
FT DISULFID 467..532
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00196"
FT DISULFID 480..545
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00196"
FT DISULFID 514..524
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00196"
FT DISULFID 575..627
FT /evidence="ECO:0000250|UniProtKB:Q9Y4K0"
FT DISULFID 581..697
FT /evidence="ECO:0000250|UniProtKB:Q9Y4K0"
FT DISULFID 659..675
FT /evidence="ECO:0000250|UniProtKB:Q9Y4K0"
FT DISULFID 665..687
FT /evidence="ECO:0000250|UniProtKB:Q9Y4K0"
FT DISULFID 734..748
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00196"
FT CROSSLNK 655..691
FT /note="Lysine tyrosylquinone (Lys-Tyr)"
FT /evidence="ECO:0000250|UniProtKB:P33072"
FT VAR_SEQ 714..727
FT /note="VVINPNYEVPESDF -> PSNRVLVRAGQTPY (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_016231"
FT VAR_SEQ 728..776
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_016232"
FT MUTAGEN 547..667
FT /note="Missing: Abolishes oxidase activity and secretion
FT but does not affect binding to the CDH1 promoter,
FT repression of CDH1 transcription, interaction with SNAI1,
FT binding to the CDH1 promoter, repression of CDH1
FT transcription or ability to induce EMT."
FT /evidence="ECO:0000269|PubMed:24414204"
FT CONFLICT 320
FT /note="K -> E (in Ref. 1; BAC32186)"
FT /evidence="ECO:0000305"
FT CONFLICT 558..560
FT /note="IVQ -> HEE (in Ref. 2; AAF29046)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 776 AA; 87003 MW; 9DE55C6F37DE5EEF CRC64;
MELHFGSCLS GCLALLVLLP SLSLAQYEGW PYQLQYPEYF QQPAPEHHQR QVPSDVVKIQ
VRLAGQKRKH NEGRVEVYYE GQWGTVCDDD FSIHAAHVVC RQVGYVEAKS WAASSSYGPG
EGPIWLDNIY CTGKESTLAS CSSNGWGVTD CKHTEDVGVV CSEKRIPGFK FDNSLINQIE
SLNIQVEDIR IRPILSAFRH RKPVTEGYVE VKEGKAWKQI CNKHWTAKNS HVVCGMFGFP
AEKTYNPKAY KTFASRRKLR YWKFSMNCTG TEAHISSCKL GPSVTRDPVK NATCENGQPA
VVSCVPSQIF SPDGPSRFRK AYKPEQPLVR LRGGAQVGEG RVEVLKNGEW GTICDDKWDL
VSASVVCREL GFGTAKEAIT GSRLGQGIGP IHLNEVQCTG TEKSIIDCKF NTESQGCNHE
EDAGVRCNIP IMGFQKKVRL NGGRNPYEGR VEVLTERNGS LVWGTVCGQN WGIVEAMVVC
RQLGLGFASN AFQETWYWHG NIFANNVVMS GVKCSGTELS LAHCRHDEEV ACPEGGVRFG
AGVACSETAP DLVLNAEIVQ QTAYLEDRPM SLLQCAMEEN CLSASAVHTD PTRGHRRLLR
FSSQIHNNGQ SDFRPKNGRH AWIWHDCHRH YHSMEVFTYY DLLSLNGTKV AEGHKASFCL
EDTECEGDIQ KSYECANFGE QGITMGCWDM YRHDIDCQWI DITDVPPGDY LFQVVINPNY
EVPESDFSNN IMKCRSRYDG YRIWMYNCHV GGAFSEETEQ KFEHFSGLLN NQLSVQ
