LOXL2_HUMAN
ID LOXL2_HUMAN Reviewed; 774 AA.
AC Q9Y4K0; B2R5Q0; Q53HV3; Q9BW70; Q9Y5Y8;
DT 27-APR-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 1.
DT 03-AUG-2022, entry version 195.
DE RecName: Full=Lysyl oxidase homolog 2;
DE EC=1.4.3.13 {ECO:0000269|PubMed:20306300, ECO:0000269|PubMed:20439985, ECO:0000269|PubMed:23319596, ECO:0000269|PubMed:29581294};
DE AltName: Full=Lysyl oxidase-like protein 2;
DE AltName: Full=Lysyl oxidase-related protein 2;
DE AltName: Full=Lysyl oxidase-related protein WS9-14;
DE Flags: Precursor;
GN Name=LOXL2;
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=9079631; DOI=10.1074/jbc.272.13.8157;
RA Saito H., Papaconstantinou J., Sato H., Goldstein S.;
RT "Regulation of a novel gene encoding a lysyl oxidase-related protein in
RT cellular adhesion and senescence.";
RL J. Biol. Chem. 272:8157-8160(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT LEU-570.
RC TISSUE=Adipose tissue;
RA Suzuki Y., Sugano S., Totoki Y., Toyoda A., Takeda T., Sakaki Y.,
RA Tanaka A., Yokoyama S.;
RL Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16421571; DOI=10.1038/nature04406;
RA Nusbaum C., Mikkelsen T.S., Zody M.C., Asakawa S., Taudien S., Garber M.,
RA Kodira C.D., Schueler M.G., Shimizu A., Whittaker C.A., Chang J.L.,
RA Cuomo C.A., Dewar K., FitzGerald M.G., Yang X., Allen N.R., Anderson S.,
RA Asakawa T., Blechschmidt K., Bloom T., Borowsky M.L., Butler J., Cook A.,
RA Corum B., DeArellano K., DeCaprio D., Dooley K.T., Dorris L. III,
RA Engels R., Gloeckner G., Hafez N., Hagopian D.S., Hall J.L., Ishikawa S.K.,
RA Jaffe D.B., Kamat A., Kudoh J., Lehmann R., Lokitsang T., Macdonald P.,
RA Major J.E., Matthews C.D., Mauceli E., Menzel U., Mihalev A.H.,
RA Minoshima S., Murayama Y., Naylor J.W., Nicol R., Nguyen C., O'Leary S.B.,
RA O'Neill K., Parker S.C.J., Polley A., Raymond C.K., Reichwald K.,
RA Rodriguez J., Sasaki T., Schilhabel M., Siddiqui R., Smith C.L.,
RA Sneddon T.P., Talamas J.A., Tenzin P., Topham K., Venkataraman V., Wen G.,
RA Yamazaki S., Young S.K., Zeng Q., Zimmer A.R., Rosenthal A., Birren B.W.,
RA Platzer M., Shimizu N., Lander E.S.;
RT "DNA sequence and analysis of human chromosome 8.";
RL Nature 439:331-335(2006).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT LEU-570.
RC TISSUE=Kidney;
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 [6]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 202-774, AND TISSUE SPECIFICITY.
RC TISSUE=Placenta, and Spleen;
RX PubMed=10212285; DOI=10.1074/jbc.274.18.12939;
RA Jourdan-Le Saux C., Tronecker H., Bogic L., Bryant-Greenwood G.D.,
RA Boyd C.D., Csiszar K.;
RT "The LOXL2 gene encodes a new lysyl oxidase-like protein and is expressed
RT at high levels in reproductive tissues.";
RL J. Biol. Chem. 274:12939-12944(1999).
RN [7]
RP FUNCTION, AND INTERACTION WITH SNAI1.
RX PubMed=16096638; DOI=10.1038/sj.emboj.7600781;
RA Peinado H., Del Carmen Iglesias-de la Cruz M., Olmeda D., Csiszar K.,
RA Fong K.S., Vega S., Nieto M.A., Cano A., Portillo F.;
RT "A molecular role for lysyl oxidase-like 2 enzyme in snail regulation and
RT tumor progression.";
RL EMBO J. 24:3446-3458(2005).
RN [8]
RP FUNCTION, AND INDUCTION.
RX PubMed=20026874; DOI=10.1074/jbc.m109.042424;
RA Schietke R., Warnecke C., Wacker I., Schodel J., Mole D.R., Campean V.,
RA Amann K., Goppelt-Struebe M., Behrens J., Eckardt K.U., Wiesener M.S.;
RT "The lysyl oxidases LOX and LOXL2 are necessary and sufficient to repress
RT E-cadherin in hypoxia: insights into cellular transformation processes
RT mediated by HIF-1.";
RL J. Biol. Chem. 285:6658-6669(2010).
RN [9]
RP CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND ACTIVITY REGULATION.
RX PubMed=20439985; DOI=10.1074/jbc.m109.094136;
RA Rodriguez H.M., Vaysberg M., Mikels A., McCauley S., Velayo A.C.,
RA Garcia C., Smith V.;
RT "Modulation of lysyl oxidase-like 2 enzymatic activity by an allosteric
RT antibody inhibitor.";
RL J. Biol. Chem. 285:20964-20974(2010).
RN [10]
RP ACTIVITY REGULATION.
RX PubMed=20818376; DOI=10.1038/nm.2208;
RA Barry-Hamilton V., Spangler R., Marshall D., McCauley S., Rodriguez H.M.,
RA Oyasu M., Mikels A., Vaysberg M., Ghermazien H., Wai C., Garcia C.A.,
RA Velayo A.C., Jorgensen B., Biermann D., Tsai D., Green J.,
RA Zaffryar-Eilot S., Holzer A., Ogg S., Thai D., Neufeld G.,
RA Van Vlasselaer P., Smith V.;
RT "Allosteric inhibition of lysyl oxidase-like-2 impedes the development of a
RT pathologic microenvironment.";
RL Nat. Med. 16:1009-1017(2010).
RN [11]
RP FUNCTION.
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 [12]
RP ROLE IN TUMOR PROGRESSION.
RX PubMed=21233336; DOI=10.1158/0008-5472.can-10-2868;
RA Barker H.E., Chang J., Cox T.R., Lang G., Bird D., Nicolau M., Evans H.R.,
RA Gartland A., Erler J.T.;
RT "LOXL2-mediated matrix remodeling in metastasis and mammary gland
RT involution.";
RL Cancer Res. 71:1561-1572(2011).
RN [13]
RP ROLE IN TUMOR PROGRESSION.
RX PubMed=21732535; DOI=10.1002/emmm.201100156;
RA Moreno-Bueno G., Salvador F., Martin A., Floristan A., Cuevas E.P.,
RA Santos V., Montes A., Morales S., Castilla M.A., Rojo-Sebastian A.,
RA Martinez A., Hardisson D., Csiszar K., Portillo F., Peinado H.,
RA Palacios J., Cano A.;
RT "Lysyl oxidase-like 2 (LOXL2), a new regulator of cell polarity required
RT for metastatic dissemination of basal-like breast carcinomas.";
RL EMBO Mol. Med. 3:528-544(2011).
RN [14]
RP FUNCTION, CATALYTIC ACTIVITY, AND ACTIVITY REGULATION.
RX PubMed=20306300; DOI=10.1007/s11033-010-0088-0;
RA Kim Y.M., Kim E.C., Kim Y.;
RT "The human lysyl oxidase-like 2 protein functions as an amine oxidase
RT toward collagen and elastin.";
RL Mol. Biol. Rep. 38:145-149(2011).
RN [15]
RP SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=22204712; DOI=10.1016/j.humpath.2011.07.027;
RA Li T.Y., Xu L.Y., Wu Z.Y., Liao L.D., Shen J.H., Xu X.E., Du Z.P., Zhao Q.,
RA Li E.M.;
RT "Reduced nuclear and ectopic cytoplasmic expression of lysyl oxidase-like 2
RT is associated with lymph node metastasis and poor prognosis in esophageal
RT squamous cell carcinoma.";
RL Hum. Pathol. 43:1068-1076(2012).
RN [16]
RP MUTAGENESIS OF TYR-689.
RX PubMed=22157764; DOI=10.1074/jbc.m111.261016;
RA Lugassy J., Zaffryar-Eilot S., Soueid S., Mordoviz A., Smith V.,
RA Kessler O., Neufeld G.;
RT "The enzymatic activity of lysyl oxidas-like-2 (LOXL2) is not required for
RT LOXL2-induced inhibition of keratinocyte differentiation.";
RL J. Biol. Chem. 287:3541-3549(2012).
RN [17]
RP CAUTION.
RX PubMed=22483618; DOI=10.1016/j.molcel.2012.03.002;
RA Herranz N., Dave N., Millanes-Romero A., Morey L., Diaz V.M.,
RA Lorenz-Fonfria V., Gutierrez-Gallego R., Jeronimo C., Di Croce L.,
RA Garcia de Herreros A., Peiro S.;
RT "Lysyl oxidase-like 2 deaminates lysine 4 in histone H3.";
RL Mol. Cell 46:369-376(2012).
RN [18]
RP INTERACTION WITH EFEMP2.
RX PubMed=27339457; DOI=10.1016/j.matbio.2016.06.003;
RA Sasaki T., Hanisch F.G., Deutzmann R., Sakai L.Y., Sakuma T., Miyamoto T.,
RA Yamamoto T., Hannappel E., Chu M.L., Lanig H., von der Mark K.;
RT "Functional consequence of fibulin-4 missense mutations associated with
RT vascular and skeletal abnormalities and cutis laxa.";
RL Matrix Biol. 56:132-149(2016).
RN [19]
RP RETRACTION NOTICE OF PUBMED:22483618.
RX PubMed=27392148; DOI=10.1016/j.molcel.2016.06.013;
RA Herranz N., Dave N., Millanes-Romero A., Morey L., Diaz V.M.,
RA Lorenz-Fonfria V., Gutierrez-Gallego R., Jeronimo C., Di Croce L.,
RA Garcia de Herreros A., Peiro S.;
RL Mol. Cell 63:180-180(2016).
RN [20]
RP CATALYTIC ACTIVITY, ACTIVITY REGULATION, BIOPHYSICOCHEMICAL PROPERTIES,
RP GLYCOSYLATION AT ASN-455 AND ASN-644, MUTAGENESIS OF ASN-455 AND ASN-644,
RP CROSS-LINK FORMATION, AND SUBCELLULAR LOCATION.
RX PubMed=23319596; DOI=10.1074/jbc.c112.421768;
RA Xu L., Go E.P., Finney J., Moon H., Lantz M., Rebecchi K., Desaire H.,
RA Mure M.;
RT "Post-translational modifications of recombinant human lysyl oxidase-like 2
RT (rhLOXL2) secreted from Drosophila S2 cells.";
RL J. Biol. Chem. 288:5357-5363(2013).
RN [21]
RP FUNCTION.
RX PubMed=24239292; DOI=10.1016/j.molcel.2013.10.015;
RA Millanes-Romero A., Herranz N., Perrera V., Iturbide A.,
RA Loubat-Casanovas J., Gil J., Jenuwein T., Garcia de Herreros A., Peiro S.;
RT "Regulation of heterochromatin transcription by Snail1/LOXL2 during
RT epithelial-to-mesenchymal transition.";
RL Mol. Cell 52:746-757(2013).
RN [22]
RP FUNCTION, SUBCELLULAR LOCATION, AND MUTAGENESIS OF 626-HIS--HIS-628.
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 [23]
RP FUNCTION, AND INTERACTION WITH TAF10.
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).
RN [24]
RP FUNCTION, SUBCELLULAR LOCATION, AND MUTAGENESIS OF 626-HIS--HIS-628.
RX PubMed=27735137; DOI=10.1111/febs.13922;
RA Herranz N., Dave N., Millanes-Romero A., Pascual-Reguant L., Morey L.,
RA Diaz V.M., Lorenz-Fonfria V., Gutierrez-Gallego R., Jeronimo C.,
RA Iturbide A., Di Croce L., Garcia de Herreros A., Peiro S.;
RT "Lysyl oxidase-like 2 (LOXL2) oxidizes trimethylated lysine 4 in histone
RT H3.";
RL FEBS J. 283:4263-4273(2016).
RN [25]
RP INTERACTION WITH HSPA5, AND SUBCELLULAR LOCATION.
RX PubMed=28332555; DOI=10.1038/srep44988;
RA Cuevas E.P., Eraso P., Mazon M.J., Santos V., Moreno-Bueno G., Cano A.,
RA Portillo F.;
RT "LOXL2 drives epithelial-mesenchymal transition via activation of IRE1-XBP1
RT signalling pathway.";
RL Sci. Rep. 7:44988-44988(2017).
RN [26] {ECO:0007744|PDB:5ZE3}
RP X-RAY CRYSTALLOGRAPHY (2.40 ANGSTROMS) OF 318-774 IN COMPLEX WITH ZINC AND
RP CALCIUM, CATALYTIC ACTIVITY, COFACTOR, GLYCOSYLATION AT ASN-644, DISULFIDE
RP BONDS, MUTAGENESIS OF HIS-626; HIS-628; HIS-630; LYS-653 AND TYR-689,
RP CROSS-LINK FORMATION, TOPAQUINONE FORMATION, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RX PubMed=29581294; DOI=10.1073/pnas.1720859115;
RA Zhang X., Wang Q., Wu J., Wang J., Shi Y., Liu M.;
RT "Crystal structure of human lysyl oxidase-like 2 (hLOXL2) in a precursor
RT state.";
RL Proc. Natl. Acad. Sci. U.S.A. 115:3828-3833(2018).
CC -!- FUNCTION: Mediates the post-translational oxidative deamination of
CC lysine residues on target proteins leading to the formation of
CC deaminated lysine (allysine) (PubMed:27735137). 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 (PubMed:27735137). 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) (PubMed:27735137). 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 (PubMed:25959397). 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 (By similarity). Involved in epithelial to
CC mesenchymal transition (EMT) via interaction with SNAI1 and
CC participates in repression of E-cadherin CDH1, probably by mediating
CC deamination of histone H3 (PubMed:16096638, PubMed:27735137,
CC PubMed:24414204). During EMT, involved with SNAI1 in negatively
CC regulating pericentromeric heterochromatin transcription
CC (PubMed:24239292). SNAI1 recruits LOXL2 to pericentromeric regions to
CC oxidize histone H3 and repress transcription which leads to release of
CC heterochromatin component CBX5/HP1A, enabling chromatin reorganization
CC and acquisition of mesenchymal traits (PubMed:24239292). Interacts with
CC the endoplasmic reticulum protein HSPA5 which activates the IRE1-XBP1
CC pathway of the unfolded protein response, leading to expression of
CC several transcription factors involved in EMT and subsequent EMT
CC induction (PubMed:28332555). Involved in E-cadherin repression
CC following hypoxia, a hallmark of EMT believed to amplify tumor
CC aggressiveness, suggesting that it may play a role in tumor progression
CC (PubMed:20026874). When secreted into the extracellular matrix,
CC promotes cross-linking of extracellular matrix proteins by mediating
CC oxidative deamination of peptidyl lysine residues in precursors to
CC fibrous collagen and elastin (PubMed:20306300). Acts as a regulator of
CC sprouting angiogenesis, probably via collagen IV scaffolding
CC (PubMed:21835952). Acts as a regulator of chondrocyte differentiation,
CC probably by regulating expression of factors that control chondrocyte
CC differentiation (By similarity). {ECO:0000250|UniProtKB:P58022,
CC ECO:0000269|PubMed:16096638, ECO:0000269|PubMed:20026874,
CC ECO:0000269|PubMed:20306300, ECO:0000269|PubMed:21835952,
CC ECO:0000269|PubMed:24239292, ECO:0000269|PubMed:24414204,
CC ECO:0000269|PubMed:25959397, ECO:0000269|PubMed:27735137}.
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:20306300, ECO:0000269|PubMed:20439985,
CC ECO:0000269|PubMed:23319596, ECO:0000269|PubMed:29581294};
CC -!- COFACTOR:
CC Name=Cu cation; Xref=ChEBI:CHEBI:23378;
CC Evidence={ECO:0000269|PubMed:29581294};
CC -!- COFACTOR:
CC Name=lysine tyrosylquinone residue; Xref=ChEBI:CHEBI:20489;
CC Evidence={ECO:0000269|PubMed:29581294};
CC Note=Contains 1 lysine tyrosylquinone. {ECO:0000250|UniProtKB:P33072};
CC -!- ACTIVITY REGULATION: According to some reports, it is inhibited by
CC beta-aminopropionitrile (BAPN) (PubMed:20439985 and PubMed:23319596).
CC According to another report, it is not inhibited by beta-
CC aminopropionitrile (BAPN) (PubMed:20306300). Specifically inhibited by
CC a mouse monoclonal antibody AB0023, inhibition occurs in a non-
CC competitive manner. {ECO:0000269|PubMed:20306300,
CC ECO:0000269|PubMed:20439985, ECO:0000269|PubMed:20818376,
CC ECO:0000269|PubMed:23319596}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=1.01 mM for 1,5-diaminopentane {ECO:0000269|PubMed:20439985,
CC ECO:0000269|PubMed:23319596};
CC KM=1.05 mM for spermine {ECO:0000269|PubMed:20439985,
CC ECO:0000269|PubMed:23319596};
CC KM=0.59 uM for tropoelastin (without the first three SRCR domains)
CC {ECO:0000269|PubMed:20439985, ECO:0000269|PubMed:23319596};
CC KM=0.62 uM for tropoelastin (without all four SRCR domains)
CC {ECO:0000269|PubMed:20439985, ECO:0000269|PubMed:23319596};
CC Note=kcat is 2.04 min(-1) with tropoelastin as substrate (without the
CC first three SRCR domains). kcat is 0.62 min(-1) with tropoelastin as
CC substrate (without all four SRCR domains).;
CC -!- SUBUNIT: Component of some chromatin repressor complex. Interacts with
CC SNAI1 (PubMed:16096638). Interacts with TAF10 (PubMed:25959397).
CC Interacts with HSPA5 (PubMed:28332555). Interacts with EFEMP2
CC (PubMed:27339457). {ECO:0000269|PubMed:16096638,
CC ECO:0000269|PubMed:25959397, ECO:0000269|PubMed:27339457,
CC ECO:0000269|PubMed:28332555}.
CC -!- INTERACTION:
CC Q9Y4K0; P15502-2: ELN; NbExp=2; IntAct=EBI-7172227, EBI-7882008;
CC Q9Y4K0; P02751: FN1; NbExp=2; IntAct=EBI-7172227, EBI-1220319;
CC Q9Y4K0; P49006: MARCKSL1; NbExp=4; IntAct=EBI-7172227, EBI-4289961;
CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
CC matrix, basement membrane {ECO:0000269|PubMed:23319596}. Nucleus
CC {ECO:0000269|PubMed:22204712, ECO:0000269|PubMed:24414204}. Chromosome
CC {ECO:0000269|PubMed:27735137}. Endoplasmic reticulum
CC {ECO:0000269|PubMed:28332555}. Note=Associated with chromatin
CC (PubMed:27735137). It is unclear how LOXL2 is nuclear as it contains a
CC signal sequence and has been shown to be secreted (PubMed:23319596).
CC However, a number of reports confirm its intracellular location and its
CC key role in transcription regulation (PubMed:22204712,
CC PubMed:22483618). {ECO:0000269|PubMed:22204712,
CC ECO:0000269|PubMed:23319596, ECO:0000269|PubMed:24414204,
CC ECO:0000269|PubMed:27735137}.
CC -!- TISSUE SPECIFICITY: Expressed in many tissues (PubMed:10212285).
CC Highest expression in reproductive tissues, placenta, uterus and
CC prostate (PubMed:10212285). In esophageal epithelium, expressed in the
CC basal, prickle and granular cell layers (PubMed:22204712). Up-regulated
CC in a number of cancers cells and tissues. {ECO:0000269|PubMed:10212285,
CC ECO:0000269|PubMed:22204712}.
CC -!- INDUCTION: Strongly induced in hypoxia. Direct transcriptional target
CC of HIF1A. {ECO:0000269|PubMed:20026874}.
CC -!- DOMAIN: The fourth SRCR domain plays an important role in optimizing
CC the catalytic activity of the lysyl-oxidase like (LOX) catalytic
CC domain.
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:0000269|PubMed:23319596,
CC ECO:0000269|PubMed:29581294}.
CC -!- PTM: N-glycosylated. N-glycosylation on Asn-455 and Asn-644 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:0000269|PubMed:23319596}.
CC -!- MISCELLANEOUS: Its overexpression in a number of cancers and its
CC ability to promote epithelial to mesenchymal transition suggest that
CC LOXL2 might play a role in tumor progression: expression is correlated
CC with metastasis and decreased survival in patients with aggressive
CC breast cancer (PubMed:21233336, PubMed:21732535). Allosteric inhibition
CC by AB0023 inhibits formation of the tumor microenvironment and reduces
CC metastatic tumor burden in xenograft models (PubMed:20818376,
CC PubMed:21732535). However, inhibiting the enzyme activity of LOXL2 may
CC not be sufficient, since inhibition of keratinocyte differentiation is
CC not prevented in mutants that lack enzyme activity nor by inhibition of
CC activity by the AB0023 antibody, thereby promoting development of
CC squamous cell carcinomas (PubMed:22157764).
CC {ECO:0000305|PubMed:20818376, ECO:0000305|PubMed:21233336,
CC ECO:0000305|PubMed:21732535, ECO:0000305|PubMed:22157764}.
CC -!- SIMILARITY: Belongs to the lysyl oxidase family. {ECO:0000305}.
CC -!- CAUTION: The original paper reporting the role of LOXL2 in deamination
CC of trimethylated 'Lys-4' of histone H3 was retracted due to
CC inappropriate manipulation of figure data (PubMed:22483618,
CC PubMed:27392148). However, this role was confirmed in a subsequent
CC publication (PubMed:27735137). {ECO:0000269|PubMed:27735137,
CC ECO:0000305|PubMed:22483618, ECO:0000305|PubMed:27392148}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAD34343.1; Type=Erroneous termination; Note=Extended C-terminus.; Evidence={ECO:0000305};
CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and
CC Haematology;
CC URL="http://atlasgeneticsoncology.org/Genes/LOXL2ID41192ch8p21.html";
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
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DR EMBL; U89942; AAB49697.1; -; mRNA.
DR EMBL; AK312266; BAG35197.1; -; mRNA.
DR EMBL; AK222477; BAD96197.1; -; mRNA.
DR EMBL; AC090197; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC000594; AAH00594.1; -; mRNA.
DR EMBL; AF117949; AAD34343.1; ALT_SEQ; mRNA.
DR CCDS; CCDS34864.1; -.
DR RefSeq; NP_002309.1; NM_002318.2.
DR PDB; 5ZE3; X-ray; 2.40 A; A/B=318-774.
DR PDBsum; 5ZE3; -.
DR AlphaFoldDB; Q9Y4K0; -.
DR SMR; Q9Y4K0; -.
DR BioGRID; 110201; 114.
DR IntAct; Q9Y4K0; 34.
DR MINT; Q9Y4K0; -.
DR STRING; 9606.ENSP00000373783; -.
DR BindingDB; Q9Y4K0; -.
DR ChEMBL; CHEMBL3714029; -.
DR GuidetoPHARMACOLOGY; 2853; -.
DR GlyConnect; 1480; 1 N-Linked glycan (1 site).
DR GlyGen; Q9Y4K0; 3 sites, 1 N-linked glycan (1 site).
DR iPTMnet; Q9Y4K0; -.
DR PhosphoSitePlus; Q9Y4K0; -.
DR BioMuta; LOXL2; -.
DR DMDM; 13878585; -.
DR EPD; Q9Y4K0; -.
DR jPOST; Q9Y4K0; -.
DR MassIVE; Q9Y4K0; -.
DR MaxQB; Q9Y4K0; -.
DR PaxDb; Q9Y4K0; -.
DR PeptideAtlas; Q9Y4K0; -.
DR PRIDE; Q9Y4K0; -.
DR ProteomicsDB; 86223; -.
DR ABCD; Q9Y4K0; 1 sequenced antibody.
DR Antibodypedia; 22758; 464 antibodies from 35 providers.
DR DNASU; 4017; -.
DR Ensembl; ENST00000389131.8; ENSP00000373783.3; ENSG00000134013.16.
DR GeneID; 4017; -.
DR KEGG; hsa:4017; -.
DR MANE-Select; ENST00000389131.8; ENSP00000373783.3; NM_002318.3; NP_002309.1.
DR UCSC; uc003xdh.2; human.
DR CTD; 4017; -.
DR DisGeNET; 4017; -.
DR GeneCards; LOXL2; -.
DR HGNC; HGNC:6666; LOXL2.
DR HPA; ENSG00000134013; Tissue enhanced (smooth).
DR MIM; 606663; gene.
DR neXtProt; NX_Q9Y4K0; -.
DR OpenTargets; ENSG00000134013; -.
DR PharmGKB; PA30429; -.
DR VEuPathDB; HostDB:ENSG00000134013; -.
DR eggNOG; ENOG502QSX8; Eukaryota.
DR GeneTree; ENSGT00940000155874; -.
DR HOGENOM; CLU_002555_3_0_1; -.
DR InParanoid; Q9Y4K0; -.
DR OMA; YCTGKEA; -.
DR OrthoDB; 815466at2759; -.
DR PhylomeDB; Q9Y4K0; -.
DR TreeFam; TF326061; -.
DR BRENDA; 1.4.3.13; 2681.
DR PathwayCommons; Q9Y4K0; -.
DR Reactome; R-HSA-1566948; Elastic fibre formation.
DR Reactome; R-HSA-2243919; Crosslinking of collagen fibrils.
DR SignaLink; Q9Y4K0; -.
DR SIGNOR; Q9Y4K0; -.
DR BioGRID-ORCS; 4017; 9 hits in 1074 CRISPR screens.
DR ChiTaRS; LOXL2; human.
DR GeneWiki; LOXL2; -.
DR GenomeRNAi; 4017; -.
DR Pharos; Q9Y4K0; Tchem.
DR PRO; PR:Q9Y4K0; -.
DR Proteomes; UP000005640; Chromosome 8.
DR RNAct; Q9Y4K0; protein.
DR Bgee; ENSG00000134013; Expressed in stromal cell of endometrium and 143 other tissues.
DR ExpressionAtlas; Q9Y4K0; baseline and differential.
DR Genevisible; Q9Y4K0; HS.
DR GO; GO:0005604; C:basement membrane; ISS:UniProtKB.
DR GO; GO:0000785; C:chromatin; IDA:UniProtKB.
DR GO; GO:0062023; C:collagen-containing extracellular matrix; HDA:BHF-UCL.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:UniProtKB.
DR GO; GO:0005615; C:extracellular space; IDA:UniProtKB.
DR GO; GO:0016020; C:membrane; IEA:InterPro.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0005509; F:calcium ion binding; IDA:UniProtKB.
DR GO; GO:0005507; F:copper ion binding; IDA:UniProtKB.
DR GO; GO:0009055; F:electron transfer activity; TAS:UniProtKB.
DR GO; GO:0070492; F:oligosaccharide binding; IDA:UniProtKB.
DR GO; GO:0004720; F:protein-lysine 6-oxidase activity; IDA:UniProtKB.
DR GO; GO:0005044; F:scavenger receptor activity; IEA:InterPro.
DR GO; GO:0007568; P:aging; TAS:ProtInc.
DR GO; GO:0007155; P:cell adhesion; TAS:ProtInc.
DR GO; GO:0030199; P:collagen fibril organization; IMP:UniProtKB.
DR GO; GO:0043542; P:endothelial cell migration; IMP:UniProtKB.
DR GO; GO:0001935; P:endothelial cell proliferation; IMP:UniProtKB.
DR GO; GO:0001837; P:epithelial to mesenchymal transition; IDA:UniProtKB.
DR GO; GO:0070828; P:heterochromatin organization; IMP:UniProtKB.
DR GO; GO:1902455; P:negative regulation of stem cell population maintenance; ISS:UniProtKB.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IDA:UniProtKB.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IDA:UniProtKB.
DR GO; GO:0018057; P:peptidyl-lysine oxidation; IDA:UniProtKB.
DR GO; GO:0032332; P:positive regulation of chondrocyte differentiation; ISS:UniProtKB.
DR GO; GO:0010718; P:positive regulation of epithelial to mesenchymal transition; IMP:UniProtKB.
DR GO; GO:0036211; P:protein modification process; IDA:UniProtKB.
DR GO; GO:0046688; P:response to copper ion; IDA:UniProtKB.
DR GO; GO:0001666; P:response to hypoxia; ISS:UniProtKB.
DR GO; GO:0002040; P:sprouting angiogenesis; IMP: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 3D-structure; Basement membrane; Calcium; Chromatin regulator; Chromosome;
KW Copper; Disulfide bond; Endoplasmic reticulum; Extracellular matrix;
KW Glycoprotein; LTQ; Metal-binding; Nucleus; Oxidoreductase;
KW Reference proteome; Repeat; Repressor; Secreted; Signal; TPQ;
KW Transcription; Transcription regulation.
FT SIGNAL 1..25
FT /evidence="ECO:0000255"
FT CHAIN 26..774
FT /note="Lysyl oxidase homolog 2"
FT /id="PRO_0000018532"
FT DOMAIN 58..159
FT /note="SRCR 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00196"
FT DOMAIN 188..302
FT /note="SRCR 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00196"
FT DOMAIN 326..425
FT /note="SRCR 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00196"
FT DOMAIN 435..544
FT /note="SRCR 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00196"
FT REGION 548..751
FT /note="Lysyl-oxidase like"
FT BINDING 549
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000305|PubMed:29581294"
FT BINDING 550
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000305|PubMed:29581294"
FT BINDING 626
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /evidence="ECO:0000305|PubMed:29581294"
FT BINDING 628
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /evidence="ECO:0000305|PubMed:29581294"
FT BINDING 630
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /evidence="ECO:0000305|PubMed:29581294"
FT BINDING 722
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000305|PubMed:29581294"
FT BINDING 724
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000305|PubMed:29581294"
FT BINDING 727
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000305|PubMed:29581294"
FT BINDING 728
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000305|PubMed:29581294"
FT MOD_RES 689
FT /note="2',4',5'-topaquinone"
FT /evidence="ECO:0000269|PubMed:29581294"
FT CARBOHYD 288
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 455
FT /note="N-linked (GlcNAc...) (complex) asparagine"
FT /evidence="ECO:0000269|PubMed:23319596"
FT CARBOHYD 644
FT /note="N-linked (GlcNAc...) (complex) asparagine"
FT /evidence="ECO:0000269|PubMed:23319596,
FT ECO:0000269|PubMed:29581294, ECO:0007744|PDB:5ZE3"
FT DISULFID 84..148
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00196"
FT DISULFID 97..158
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00196"
FT DISULFID 128..138
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00196"
FT DISULFID 218..291
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00196"
FT DISULFID 231..301
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00196"
FT DISULFID 265..275
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00196"
FT DISULFID 351..414
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00196"
FT DISULFID 364..424
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00196,
FT ECO:0000269|PubMed:29581294, ECO:0007744|PDB:5ZE3"
FT DISULFID 395..405
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00196,
FT ECO:0000269|PubMed:29581294, ECO:0007744|PDB:5ZE3"
FT DISULFID 464..530
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00196,
FT ECO:0000269|PubMed:29581294, ECO:0007744|PDB:5ZE3"
FT DISULFID 477..543
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00196,
FT ECO:0000269|PubMed:29581294, ECO:0007744|PDB:5ZE3"
FT DISULFID 511..521
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00196,
FT ECO:0000269|PubMed:29581294, ECO:0007744|PDB:5ZE3"
FT DISULFID 573..625
FT /evidence="ECO:0000269|PubMed:29581294,
FT ECO:0007744|PDB:5ZE3"
FT DISULFID 579..695
FT /evidence="ECO:0000269|PubMed:29581294,
FT ECO:0007744|PDB:5ZE3"
FT DISULFID 657..673
FT /evidence="ECO:0000269|PubMed:29581294,
FT ECO:0007744|PDB:5ZE3"
FT DISULFID 663..685
FT /evidence="ECO:0000269|PubMed:29581294,
FT ECO:0007744|PDB:5ZE3"
FT DISULFID 732..746
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00196,
FT ECO:0000269|PubMed:29581294, ECO:0007744|PDB:5ZE3"
FT CROSSLNK 653..689
FT /note="Lysine tyrosylquinone (Lys-Tyr)"
FT /evidence="ECO:0000269|PubMed:23319596,
FT ECO:0000269|PubMed:29581294"
FT VARIANT 359
FT /note="S -> W (in dbSNP:rs4602894)"
FT /id="VAR_050010"
FT VARIANT 570
FT /note="M -> L (in dbSNP:rs1063582)"
FT /evidence="ECO:0000269|PubMed:15489334, ECO:0000269|Ref.3"
FT /id="VAR_024527"
FT MUTAGEN 455
FT /note="N->Q: Inhibits secretion."
FT /evidence="ECO:0000269|PubMed:23319596"
FT MUTAGEN 626..628
FT /note="HRH->ARA: Abolishes oxidase activity and oxidation
FT of trimethylated 'Lys-4' of histone H3 but does not affect
FT secretion, interaction with SNAI1, binding to the CDH1
FT promoter, repression of CDH1 transcription or ability to
FT induce EMT."
FT /evidence="ECO:0000269|PubMed:24414204,
FT ECO:0000269|PubMed:27735137"
FT MUTAGEN 626
FT /note="H->A: Loss of enzyme activity."
FT /evidence="ECO:0000269|PubMed:29581294"
FT MUTAGEN 628
FT /note="H->A: Loss of enzyme activity."
FT /evidence="ECO:0000269|PubMed:29581294"
FT MUTAGEN 630
FT /note="H->A: Loss of enzyme activity."
FT /evidence="ECO:0000269|PubMed:29581294"
FT MUTAGEN 644
FT /note="N->Q: Inhibits secretion."
FT /evidence="ECO:0000269|PubMed:23319596"
FT MUTAGEN 653
FT /note="K->A: Loss of enzyme activity."
FT /evidence="ECO:0000269|PubMed:29581294"
FT MUTAGEN 689
FT /note="Y->A: Loss of enzyme activity."
FT /evidence="ECO:0000269|PubMed:29581294"
FT MUTAGEN 689
FT /note="Y->F: Does not affect ability to inhibit
FT keratinocyte differentiation."
FT /evidence="ECO:0000269|PubMed:22157764"
FT CONFLICT 184
FT /note="E -> K (in Ref. 2; BAG35197)"
FT /evidence="ECO:0000305"
FT CONFLICT 239
FT /note="E -> G (in Ref. 3; BAD96197)"
FT /evidence="ECO:0000305"
FT CONFLICT 295
FT /note="L -> Q (in Ref. 6; AAD34343)"
FT /evidence="ECO:0000305"
FT CONFLICT 536
FT /note="Q -> R (in Ref. 2; BAG35197)"
FT /evidence="ECO:0000305"
FT CONFLICT 652
FT /note="H -> Q (in Ref. 6; AAD34343)"
FT /evidence="ECO:0000305"
FT CONFLICT 746
FT /note="C -> S (in Ref. 6; AAD34343)"
FT /evidence="ECO:0000305"
FT STRAND 325..333
FT /evidence="ECO:0007829|PDB:5ZE3"
FT STRAND 336..343
FT /evidence="ECO:0007829|PDB:5ZE3"
FT STRAND 346..351
FT /evidence="ECO:0007829|PDB:5ZE3"
FT HELIX 357..366
FT /evidence="ECO:0007829|PDB:5ZE3"
FT STRAND 372..376
FT /evidence="ECO:0007829|PDB:5ZE3"
FT TURN 378..381
FT /evidence="ECO:0007829|PDB:5ZE3"
FT STRAND 388..390
FT /evidence="ECO:0007829|PDB:5ZE3"
FT STRAND 404..406
FT /evidence="ECO:0007829|PDB:5ZE3"
FT STRAND 421..424
FT /evidence="ECO:0007829|PDB:5ZE3"
FT STRAND 434..441
FT /evidence="ECO:0007829|PDB:5ZE3"
FT STRAND 445..454
FT /evidence="ECO:0007829|PDB:5ZE3"
FT STRAND 457..463
FT /evidence="ECO:0007829|PDB:5ZE3"
FT HELIX 470..480
FT /evidence="ECO:0007829|PDB:5ZE3"
FT STRAND 484..490
FT /evidence="ECO:0007829|PDB:5ZE3"
FT STRAND 504..506
FT /evidence="ECO:0007829|PDB:5ZE3"
FT HELIX 518..520
FT /evidence="ECO:0007829|PDB:5ZE3"
FT HELIX 534..536
FT /evidence="ECO:0007829|PDB:5ZE3"
FT STRAND 540..545
FT /evidence="ECO:0007829|PDB:5ZE3"
FT STRAND 550..552
FT /evidence="ECO:0007829|PDB:5ZE3"
FT HELIX 554..559
FT /evidence="ECO:0007829|PDB:5ZE3"
FT STRAND 562..567
FT /evidence="ECO:0007829|PDB:5ZE3"
FT HELIX 568..570
FT /evidence="ECO:0007829|PDB:5ZE3"
FT HELIX 572..576
FT /evidence="ECO:0007829|PDB:5ZE3"
FT HELIX 582..586
FT /evidence="ECO:0007829|PDB:5ZE3"
FT TURN 589..591
FT /evidence="ECO:0007829|PDB:5ZE3"
FT STRAND 593..598
FT /evidence="ECO:0007829|PDB:5ZE3"
FT STRAND 601..605
FT /evidence="ECO:0007829|PDB:5ZE3"
FT STRAND 607..609
FT /evidence="ECO:0007829|PDB:5ZE3"
FT HELIX 617..619
FT /evidence="ECO:0007829|PDB:5ZE3"
FT STRAND 621..623
FT /evidence="ECO:0007829|PDB:5ZE3"
FT TURN 624..627
FT /evidence="ECO:0007829|PDB:5ZE3"
FT STRAND 628..641
FT /evidence="ECO:0007829|PDB:5ZE3"
FT STRAND 645..649
FT /evidence="ECO:0007829|PDB:5ZE3"
FT STRAND 652..656
FT /evidence="ECO:0007829|PDB:5ZE3"
FT STRAND 661..664
FT /evidence="ECO:0007829|PDB:5ZE3"
FT TURN 674..676
FT /evidence="ECO:0007829|PDB:5ZE3"
FT STRAND 685..689
FT /evidence="ECO:0007829|PDB:5ZE3"
FT STRAND 697..699
FT /evidence="ECO:0007829|PDB:5ZE3"
FT STRAND 705..715
FT /evidence="ECO:0007829|PDB:5ZE3"
FT STRAND 728..736
FT /evidence="ECO:0007829|PDB:5ZE3"
FT STRAND 741..748
FT /evidence="ECO:0007829|PDB:5ZE3"
FT HELIX 754..759
FT /evidence="ECO:0007829|PDB:5ZE3"
SQ SEQUENCE 774 AA; 86725 MW; 9DF5D25D4824BCCD CRC64;
MERPLCSHLC SCLAMLALLS PLSLAQYDSW PHYPEYFQQP APEYHQPQAP ANVAKIQLRL
AGQKRKHSEG RVEVYYDGQW GTVCDDDFSI HAAHVVCREL GYVEAKSWTA SSSYGKGEGP
IWLDNLHCTG NEATLAACTS NGWGVTDCKH TEDVGVVCSD KRIPGFKFDN SLINQIENLN
IQVEDIRIRA ILSTYRKRTP VMEGYVEVKE GKTWKQICDK HWTAKNSRVV CGMFGFPGER
TYNTKVYKMF ASRRKQRYWP FSMDCTGTEA HISSCKLGPQ VSLDPMKNVT CENGLPAVVS
CVPGQVFSPD GPSRFRKAYK PEQPLVRLRG GAYIGEGRVE VLKNGEWGTV CDDKWDLVSA
SVVCRELGFG SAKEAVTGSR LGQGIGPIHL NEIQCTGNEK SIIDCKFNAE SQGCNHEEDA
GVRCNTPAMG LQKKLRLNGG RNPYEGRVEV LVERNGSLVW GMVCGQNWGI VEAMVVCRQL
GLGFASNAFQ ETWYWHGDVN SNKVVMSGVK CSGTELSLAH CRHDGEDVAC PQGGVQYGAG
VACSETAPDL VLNAEMVQQT TYLEDRPMFM LQCAMEENCL SASAAQTDPT TGYRRLLRFS
SQIHNNGQSD FRPKNGRHAW IWHDCHRHYH SMEVFTHYDL LNLNGTKVAE GHKASFCLED
TECEGDIQKN YECANFGDQG ITMGCWDMYR HDIDCQWVDI TDVPPGDYLF QVVINPNFEV
AESDYSNNIM KCRSRYDGHR IWMYNCHIGG SFSEETEKKF EHFSGLLNNQ LSPQ
