Hmdb loader

Showing Protein Ephrin type-A receptor 2 (HMDBP01246)

IdentificationBiological propertiesGene propertiesProtein propertiesExternal linksReferencesXMLShow 3 metabolites
Identification
HMDB Protein ID HMDBP01246
Secondary Accession Numbers
  • 6542
Name Ephrin type-A receptor 2
Synonyms
  1. Epithelial cell kinase
  2. Tyrosine-protein kinase receptor ECK
Gene Name EPHA2
Protein Type Enzyme
Biological Properties
General Function Involved in ephrin receptor activity
Specific Function Receptor for members of the ephrin-A family. Binds to ephrin-A1, -A3, -A4 and -A5. Plays an important role in angiogenesis and tumor neovascularization. The recruitement of VAV2, VAV3 and PI3-kinase p85 subunit by phosphorylated EPHA2 is critical for EFNA1-induced RAC1 GTPase activation and vascular endothelial cell migration and assembly. Induces apoptosis in a TP53/p53-independent, caspase-8-dependent manner
Pathways Not Available
Reactions Not Available
GO Classification
Component
integral to plasma membrane
membrane
cell part
membrane part
intrinsic to membrane
integral to membrane
Function
protein tyrosine kinase activity
transmembrane receptor protein tyrosine kinase activity
binding
catalytic activity
transferase activity
transferase activity, transferring phosphorus-containing groups
kinase activity
nucleoside binding
purine nucleoside binding
adenyl nucleotide binding
adenyl ribonucleotide binding
atp binding
ephrin receptor activity
protein binding
protein kinase activity
Process
phosphorus metabolic process
phosphate metabolic process
enzyme linked receptor protein signaling pathway
transmembrane receptor protein tyrosine kinase signaling pathway
metabolic process
ephrin receptor signaling pathway
cellular metabolic process
protein amino acid phosphorylation
signaling
signaling pathway
cell surface receptor linked signaling pathway
phosphorylation
Cellular Location
  1. Membrane
  2. Single-pass type I membrane protein
Gene Properties
Chromosome Location Chromosome:1
Locus 1p36
SNPs EPHA2
Gene Sequence 
>2931 bp
ATGGAGCTCCAGGCAGCCCGCGCCTGCTTCGCCCTGCTGTGGGGCTGTGCGCTGGCCGCG
GCCGCGGCGGCGCAGGGCAAGGAAGTGGTACTGCTGGACTTTGCTGCAGCTGGAGGGGAG
CTCGGCTGGCTCACACACCCGTATGGCAAAGGGTGGGACCTGATGCAGAACATCATGAAT
GACATGCCGATCTACATGTACTCCGTGTGCAACGTGATGTCTGGCGACCAGGACAACTGG
CTCCGCACCAACTGGGTGTACCGAGGAGAGGCTGAGCGTATCTTCATTGAGCTCAAGTTT
ACTGTACGTGACTGCAACAGCTTCCCTGGTGGCGCCAGCTCCTGCAAGGAGACTTTCAAC
CTCTACTATGCCGAGTCGGACCTGGACTACGGCACCAACTTCCAGAAGCGCCTGTTCACC
AAGATTGACACCATTGCGCCCGATGAGATCACCGTCAGCAGCGACTTCGAGGCACGCCAC
GTGAAGCTGAACGTGGAGGAGCGCTCCGTGGGGCCGCTCACCCGCAAAGGCTTCTACCTG
GCCTTCCAGGATATCGGTGCCTGTGTGGCGCTGCTCTCCGTCCGTGTCTACTACAAGAAG
TGCCCCGAGCTGCTGCAGGGCCTGGCCCACTTCCCTGAGACCATCGCCGGCTCTGATGCA
CCTTCCCTGGCCACTGTGGCCGGCACCTGTGTGGACCATGCCGTGGTGCCACCGGGGGGT
GAAGAGCCCCGTATGCACTGTGCAGTGGATGGCGAGTGGCTGGTGCCCATTGGGCAGTGC
CTGTGCCAGGCAGGCTACGAGAAGGTGGAGGATGCCTGCCAGGCCTGCTCGCCTGGATTT
TTTAAGTTTGAGGCATCTGAGAGCCCCTGCTTGGAGTGCCCTGAGCACACGCTGCCATCC
CCTGAGGGTGCCACCTCCTGCGAGTGTGAGGAAGGCTTCTTCCGGGCACCTCAGGACCCA
GCGTCGATGCCTTGCACACGACCCCCCTCCGCCCCACACTACCTCACAGCCGTGGGCATG
GGTGCCAAGGTGGAGCTGCGCTGGACGCCCCCTCAGGACAGCGGGGGCCGCGAGGACATT
GTCTACAGCGTCACCTGCGAACAGTGCTGGCCCGAGTCTGGGGAATGCGGGCCGTGTGAG
GCCAGTGTGCGCTACTCGGAGCCTCCTCACGGACTGACCCGCACCAGTGTGACAGTGAGC
GACCTGGAGCCCCACATGAACTACACCTTCACCGTGGAGGCCCGCAATGGCGTCTCAGGC
CTGGTAACCAGCCGCAGCTTCCGTACTGCCAGTGTCAGCATCAACCAGACAGAGCCCCCC
AAGGTGAGGCTGGAGGGCCGCAGCACCACCTCGCTTAGCGTCTCCTGGAGCATCCCCCCG
CCGCAGCAGAGCCGAGTGTGGAAGTACGAGGTCACTTACCGCAAGAAGGGAGACTCCAAC
AGCTACAATGTGCGCCGCACCGAGGGTTTCTCCGTGACCCTGGACGACCTGGCCCCAGAC
ACCACCTACCTGGTCCAGGTGCAGGCACTGACGCAGGAGGGCCAGGGGGCCGGCAGCAAG
GTGCACGAATTCCAGACGCTGTCCCCGGAGGGATCTGGCAACTTGGCGGTGATTGGCGGC
GTGGCTGTCGGTGTGGTCCTGCTTCTGGTGCTGGCAGGAGTTGGCTTCTTTATCCACCGC
AGGAGGAAGAACCAGCGTGCCCGCCAGTCCCCGGAGGACGTTTACTTCTCCAAGTCAGAA
CAACTGAAGCCCCTGAAGACATACGTGGACCCCCACACATATGAGGACCCCAACCAGGCT
GTGTTGAAGTTCACTACCGAGATCCATCCATCCTGTGTCACTCGGCAGAAGGTGATCGGA
GCAGGAGAGTTTGGGGAGGTGTACAAGGGCATGCTGAAGACATCCTCGGGGAAGAAGGAG
GTGCCGGTGGCCATCAAGACGCTGAAAGCCGGCTACACAGAGAAGCAGCGAGTGGACTTC
CTCGGCGAGGCCGGCATCATGGGCCAGTTCAGCCACCACAACATCATCCGCCTAGAGGGC
GTCATCTCCAAATACAAGCCCATGATGATCATCACTGAGTACATGGAGAATGGGGCCCTG
GACAAGTTCCTTCGGGAGAAGGATGGCGAGTTCAGCGTGCTGCAGCTGGTGGGCATGCTG
CGGGGCATCGCAGCTGGCATGAAGTACCTGGCCAACATGAACTATGTGCACCGTGACCTG
GCTGCCCGCAACATCCTCGTCAACAGCAACCTGGTCTGCAAGGTGTCTGACTTTGGCCTG
TCCCGCGTGCTGGAGGACGACCCCGAGGCCACCTACACCACCAGTGGCGGCAAGATCCCC
ATCCGCTGGACCGCCCCGGAGGCCATTTCCTACCGGAAGTTCACCTCTGCCAGCGACGTG
TGGAGCTTTGGCATTGTCATGTGGGAGGTGATGACCTATGGCGAGCGGCCCTACTGGGAG
TTGTCCAACCACGAGGTGATGAAAGCCATCAATGATGGCTTCCGGCTCCCCACACCCATG
GACTGCCCCTCCGCCATCTACCAGCTCATGATGCAGTGCTGGCAGCAGGAGCGTGCCCGC
CGCCCCAAGTTCGCTGACATCGTCAGCATCCTGGACAAGCTCATTCGTGCCCCTGACTCC
CTCAAGACCCTGGCTGACTTTGACCCCCGCGTGTCTATCCGGCTCCCCAGCACGAGCGGC
TCGGAGGGGGTGCCCTTCCGCACGGTGTCCGAGTGGCTGGAGTCCATCAAGATGCAGCAG
TATACGGAGCACTTCATGGCGGCCGGCTACACTGCCATCGAGAAGGTGGTGCAGATGACC
AACGACGACATCAAGAGGATTGGGGTGCGGCTGCCCGGCCACCAGAAGCGCATCGCCTAC
AGCCTGCTGGGACTCAAGGACCAGGTGAACACTGTGGGGATCCCCATCTGA
Protein Properties
Number of Residues 976
Molecular Weight 108265.6
Theoretical pI 6.14
Pfam Domain Function
Signals
  • 1-24
Transmembrane Regions
  • 535-558
Protein Sequence 
>Ephrin type-A receptor 2
MELQAARACFALLWGCALAAAAAAQGKEVVLLDFAAAGGELGWLTHPYGKGWDLMQNIMN
DMPIYMYSVCNVMSGDQDNWLRTNWVYRGEAERIFIELKFTVRDCNSFPGGASSCKETFN
LYYAESDLDYGTNFQKRLFTKIDTIAPDEITVSSDFEARHVKLNVEERSVGPLTRKGFYL
AFQDIGACVALLSVRVYYKKCPELLQGLAHFPETIAGSDAPSLATVAGTCVDHAVVPPGG
EEPRMHCAVDGEWLVPIGQCLCQAGYEKVEDACQACSPGFFKFEASESPCLECPEHTLPS
PEGATSCECEEGFFRAPQDPASMPCTRPPSAPHYLTAVGMGAKVELRWTPPQDSGGREDI
VYSVTCEQCWPESGECGPCEASVRYSEPPHGLTRTSVTVSDLEPHMNYTFTVEARNGVSG
LVTSRSFRTASVSINQTEPPKVRLEGRSTTSLSVSWSIPPPQQSRVWKYEVTYRKKGDSN
SYNVRRTEGFSVTLDDLAPDTTYLVQVQALTQEGQGAGSKVHEFQTLSPEGSGNLAVIGG
VAVGVVLLLVLAGVGFFIHRRRKNQRARQSPEDVYFSKSEQLKPLKTYVDPHTYEDPNQA
VLKFTTEIHPSCVTRQKVIGAGEFGEVYKGMLKTSSGKKEVPVAIKTLKAGYTEKQRVDF
LGEAGIMGQFSHHNIIRLEGVISKYKPMMIITEYMENGALDKFLREKDGEFSVLQLVGML
RGIAAGMKYLANMNYVHRDLAARNILVNSNLVCKVSDFGLSRVLEDDPEATYTTSGGKIP
IRWTAPEAISYRKFTSASDVWSFGIVMWEVMTYGERPYWELSNHEVMKAINDGFRLPTPM
DCPSAIYQLMMQCWQQERARRPKFADIVSILDKLIRAPDSLKTLADFDPRVSIRLPSTSG
SEGVPFRTVSEWLESIKMQQYTEHFMAAGYTAIEKVVQMTNDDIKRIGVRLPGHQKRIAY
SLLGLKDQVNTVGIPI
GenBank ID Protein 55665160
UniProtKB/Swiss-Prot ID P29317
UniProtKB/Swiss-Prot Entry Name EPHA2_HUMAN
PDB IDs
GenBank Gene ID AL451042
GeneCard ID EPHA2
GenAtlas ID EPHA2
HGNC ID HGNC:3386
References
General References
  1. Chen R, Jiang X, Sun D, Han G, Wang F, Ye M, Wang L, Zou H: Glycoproteomics analysis of human liver tissue by combination of multiple enzyme digestion and hydrazide chemistry. J Proteome Res. 2009 Feb;8(2):651-61. doi: 10.1021/pr8008012. [PubMed:19159218 ]
  2. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed:15489334 ]
  3. Gregory SG, Barlow KF, McLay KE, Kaul R, Swarbreck D, Dunham A, Scott CE, Howe KL, Woodfine K, Spencer CC, Jones MC, Gillson C, Searle S, Zhou Y, Kokocinski F, McDonald L, Evans R, Phillips K, Atkinson A, Cooper R, Jones C, Hall RE, Andrews TD, Lloyd C, Ainscough R, Almeida JP, Ambrose KD, Anderson F, Andrew RW, Ashwell RI, Aubin K, Babbage AK, Bagguley CL, Bailey J, Beasley H, Bethel G, Bird CP, Bray-Allen S, Brown JY, Brown AJ, Buckley D, Burton J, Bye J, Carder C, Chapman JC, Clark SY, Clarke G, Clee C, Cobley V, Collier RE, Corby N, Coville GJ, Davies J, Deadman R, Dunn M, Earthrowl M, Ellington AG, Errington H, Frankish A, Frankland J, French L, Garner P, Garnett J, Gay L, Ghori MR, Gibson R, Gilby LM, Gillett W, Glithero RJ, Grafham DV, Griffiths C, Griffiths-Jones S, Grocock R, Hammond S, Harrison ES, Hart E, Haugen E, Heath PD, Holmes S, Holt K, Howden PJ, Hunt AR, Hunt SE, Hunter G, Isherwood J, James R, Johnson C, Johnson D, Joy A, Kay M, Kershaw JK, Kibukawa M, Kimberley AM, King A, Knights AJ, Lad H, Laird G, Lawlor S, Leongamornlert DA, Lloyd DM, Loveland J, Lovell J, Lush MJ, Lyne R, Martin S, Mashreghi-Mohammadi M, Matthews L, Matthews NS, McLaren S, Milne S, Mistry S, Moore MJ, Nickerson T, O'Dell CN, Oliver K, Palmeiri A, Palmer SA, Parker A, Patel D, Pearce AV, Peck AI, Pelan S, Phelps K, Phillimore BJ, Plumb R, Rajan J, Raymond C, Rouse G, Saenphimmachak C, Sehra HK, Sheridan E, Shownkeen R, Sims S, Skuce CD, Smith M, Steward C, Subramanian S, Sycamore N, Tracey A, Tromans A, Van Helmond Z, Wall M, Wallis JM, White S, Whitehead SL, Wilkinson JE, Willey DL, Williams H, Wilming L, Wray PW, Wu Z, Coulson A, Vaudin M, Sulston JE, Durbin R, Hubbard T, Wooster R, Dunham I, Carter NP, McVean G, Ross MT, Harrow J, Olson MV, Beck S, Rogers J, Bentley DR, Banerjee R, Bryant SP, Burford DC, Burrill WD, Clegg SM, Dhami P, Dovey O, Faulkner LM, Gribble SM, Langford CF, Pandian RD, Porter KM, Prigmore E: The DNA sequence and biological annotation of human chromosome 1. Nature. 2006 May 18;441(7091):315-21. [PubMed:16710414 ]
  4. Dephoure N, Zhou C, Villen J, Beausoleil SA, Bakalarski CE, Elledge SJ, Gygi SP: A quantitative atlas of mitotic phosphorylation. Proc Natl Acad Sci U S A. 2008 Aug 5;105(31):10762-7. doi: 10.1073/pnas.0805139105. Epub 2008 Jul 31. [PubMed:18669648 ]
  5. Daub H, Olsen JV, Bairlein M, Gnad F, Oppermann FS, Korner R, Greff Z, Keri G, Stemmann O, Mann M: Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle. Mol Cell. 2008 Aug 8;31(3):438-48. doi: 10.1016/j.molcel.2008.07.007. [PubMed:18691976 ]
  6. Oppermann FS, Gnad F, Olsen JV, Hornberger R, Greff Z, Keri G, Mann M, Daub H: Large-scale proteomics analysis of the human kinome. Mol Cell Proteomics. 2009 Jul;8(7):1751-64. doi: 10.1074/mcp.M800588-MCP200. Epub 2009 Apr 15. [PubMed:19369195 ]
  7. Rikova K, Guo A, Zeng Q, Possemato A, Yu J, Haack H, Nardone J, Lee K, Reeves C, Li Y, Hu Y, Tan Z, Stokes M, Sullivan L, Mitchell J, Wetzel R, Macneill J, Ren JM, Yuan J, Bakalarski CE, Villen J, Kornhauser JM, Smith B, Li D, Zhou X, Gygi SP, Gu TL, Polakiewicz RD, Rush J, Comb MJ: Global survey of phosphotyrosine signaling identifies oncogenic kinases in lung cancer. Cell. 2007 Dec 14;131(6):1190-203. [PubMed:18083107 ]
  8. Zhang Y, Wolf-Yadlin A, Ross PL, Pappin DJ, Rush J, Lauffenburger DA, White FM: Time-resolved mass spectrometry of tyrosine phosphorylation sites in the epidermal growth factor receptor signaling network reveals dynamic modules. Mol Cell Proteomics. 2005 Sep;4(9):1240-50. Epub 2005 Jun 11. [PubMed:15951569 ]
  9. Heibeck TH, Ding SJ, Opresko LK, Zhao R, Schepmoes AA, Yang F, Tolmachev AV, Monroe ME, Camp DG 2nd, Smith RD, Wiley HS, Qian WJ: An extensive survey of tyrosine phosphorylation revealing new sites in human mammary epithelial cells. J Proteome Res. 2009 Aug;8(8):3852-61. doi: 10.1021/pr900044c. [PubMed:19534553 ]
  10. Wolf-Yadlin A, Hautaniemi S, Lauffenburger DA, White FM: Multiple reaction monitoring for robust quantitative proteomic analysis of cellular signaling networks. Proc Natl Acad Sci U S A. 2007 Apr 3;104(14):5860-5. Epub 2007 Mar 26. [PubMed:17389395 ]
  11. Greenman C, Stephens P, Smith R, Dalgliesh GL, Hunter C, Bignell G, Davies H, Teague J, Butler A, Stevens C, Edkins S, O'Meara S, Vastrik I, Schmidt EE, Avis T, Barthorpe S, Bhamra G, Buck G, Choudhury B, Clements J, Cole J, Dicks E, Forbes S, Gray K, Halliday K, Harrison R, Hills K, Hinton J, Jenkinson A, Jones D, Menzies A, Mironenko T, Perry J, Raine K, Richardson D, Shepherd R, Small A, Tofts C, Varian J, Webb T, West S, Widaa S, Yates A, Cahill DP, Louis DN, Goldstraw P, Nicholson AG, Brasseur F, Looijenga L, Weber BL, Chiew YE, DeFazio A, Greaves MF, Green AR, Campbell P, Birney E, Easton DF, Chenevix-Trench G, Tan MH, Khoo SK, Teh BT, Yuen ST, Leung SY, Wooster R, Futreal PA, Stratton MR: Patterns of somatic mutation in human cancer genomes. Nature. 2007 Mar 8;446(7132):153-8. [PubMed:17344846 ]
  12. Wissing J, Jansch L, Nimtz M, Dieterich G, Hornberger R, Keri G, Wehland J, Daub H: Proteomics analysis of protein kinases by target class-selective prefractionation and tandem mass spectrometry. Mol Cell Proteomics. 2007 Mar;6(3):537-47. Epub 2006 Dec 27. [PubMed:17192257 ]
  13. Lindberg RA, Hunter T: cDNA cloning and characterization of eck, an epithelial cell receptor protein-tyrosine kinase in the eph/elk family of protein kinases. Mol Cell Biol. 1990 Dec;10(12):6316-24. [PubMed:2174105 ]
  14. Liu DP, Wang Y, Koeffler HP, Xie D: Ephrin-A1 is a negative regulator in glioma through down-regulation of EphA2 and FAK. Int J Oncol. 2007 Apr;30(4):865-71. [PubMed:17332925 ]
  15. Zhuang G, Hunter S, Hwang Y, Chen J: Regulation of EphA2 receptor endocytosis by SHIP2 lipid phosphatase via phosphatidylinositol 3-Kinase-dependent Rac1 activation. J Biol Chem. 2007 Jan 26;282(4):2683-94. Epub 2006 Nov 29. [PubMed:17135240 ]
  16. Zhang G, Njauw CN, Park JM, Naruse C, Asano M, Tsao H: EphA2 is an essential mediator of UV radiation-induced apoptosis. Cancer Res. 2008 Mar 15;68(6):1691-6. doi: 10.1158/0008-5472.CAN-07-2372. [PubMed:18339848 ]
  17. Wykosky J, Palma E, Gibo DM, Ringler S, Turner CP, Debinski W: Soluble monomeric EphrinA1 is released from tumor cells and is a functional ligand for the EphA2 receptor. Oncogene. 2008 Dec 11;27(58):7260-73. doi: 10.1038/onc.2008.328. Epub 2008 Sep 15. [PubMed:18794797 ]
  18. Nowakowski J, Cronin CN, McRee DE, Knuth MW, Nelson CG, Pavletich NP, Rogers J, Sang BC, Scheibe DN, Swanson RV, Thompson DA: Structures of the cancer-related Aurora-A, FAK, and EphA2 protein kinases from nanovolume crystallography. Structure. 2002 Dec;10(12):1659-67. [PubMed:12467573 ]
  19. Himanen JP, Goldgur Y, Miao H, Myshkin E, Guo H, Buck M, Nguyen M, Rajashankar KR, Wang B, Nikolov DB: Ligand recognition by A-class Eph receptors: crystal structures of the EphA2 ligand-binding domain and the EphA2/ephrin-A1 complex. EMBO Rep. 2009 Jul;10(7):722-8. doi: 10.1038/embor.2009.91. Epub 2009 Jun 12. [PubMed:19525919 ]
  20. Shiels A, Bennett TM, Knopf HL, Maraini G, Li A, Jiao X, Hejtmancik JF: The EPHA2 gene is associated with cataracts linked to chromosome 1p. Mol Vis. 2008;14:2042-55. Epub 2008 Nov 12. [PubMed:19005574 ]
  21. Zhang T, Hua R, Xiao W, Burdon KP, Bhattacharya SS, Craig JE, Shang D, Zhao X, Mackey DA, Moore AT, Luo Y, Zhang J, Zhang X: Mutations of the EPHA2 receptor tyrosine kinase gene cause autosomal dominant congenital cataract. Hum Mutat. 2009 May;30(5):E603-11. doi: 10.1002/humu.20995. [PubMed:19306328 ]
  22. Jun G, Guo H, Klein BE, Klein R, Wang JJ, Mitchell P, Miao H, Lee KE, Joshi T, Buck M, Chugha P, Bardenstein D, Klein AP, Bailey-Wilson JE, Gong X, Spector TD, Andrew T, Hammond CJ, Elston RC, Iyengar SK, Wang B: EPHA2 is associated with age-related cortical cataract in mice and humans. PLoS Genet. 2009 Jul;5(7):e1000584. doi: 10.1371/journal.pgen.1000584. Epub 2009 Jul 31. [PubMed:19649315 ]