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4-aminobutyrate aminotransferase, mitochondrial (EC 2.6.1.19) ((S)-3-amino-2-methylpropionate transaminase) (EC 2.6.1.22) (GABA aminotransferase) (GABA-AT) (Gamma-amino-N-butyrate transaminase) (GABA transaminase) (GABA-T) (L-AIBAT)

 GABT_HUMAN              Reviewed;         500 AA.
P80404; A8K386; Q16260; Q8N5W2; Q96BG2; Q99800;
01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
07-JUN-2004, sequence version 3.
25-OCT-2017, entry version 171.
RecName: Full=4-aminobutyrate aminotransferase, mitochondrial;
EC=2.6.1.19;
AltName: Full=(S)-3-amino-2-methylpropionate transaminase;
EC=2.6.1.22;
AltName: Full=GABA aminotransferase;
Short=GABA-AT;
AltName: Full=Gamma-amino-N-butyrate transaminase;
Short=GABA transaminase;
Short=GABA-T;
AltName: Full=L-AIBAT;
Flags: Precursor;
Name=ABAT; Synonyms=GABAT;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Brain;
PubMed=7721088; DOI=10.1016/0378-1119(94)00858-P;
Osei Y.D., Churchich J.E.;
"Screening and sequence determination of a cDNA encoding the human
brain 4-aminobutyrate aminotransferase.";
Gene 155:185-187(1995).
[2]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Pancreatic islet;
Medina-Kauwe L.K., Gibson K.M., Nyhan W.L., Tobin A.J.;
Submitted (NOV-1996) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Brain;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT ARG-56.
TISSUE=Brain, and Eye;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[5]
NUCLEOTIDE SEQUENCE [MRNA] OF 36-485, AND PARTIAL PROTEIN SEQUENCE.
TISSUE=Liver;
PubMed=7851425; DOI=10.1111/j.1432-1033.1995.tb20412.x;
de Biase D., Barra D., Simmaco M., John R.A., Bossa F.;
"Primary structure and tissue distribution of human 4-aminobutyrate
aminotransferase.";
Eur. J. Biochem. 227:476-480(1995).
[6]
SUBUNIT, INTERCHAIN DISULFIDE BOND, AND MUTAGENESIS OF CYS-321.
PubMed=15528998;
Yoon C.S., Kim D.W., Jang S.H., Lee B.R., Choi H.S., Choi S.H.,
Kim S.Y., An J.J., Kwon O.S., Kang T.C., Won M.H., Cho S.W., Lee K.S.,
Park J., Eum W.S., Choi S.Y.;
"Cysteine-321 of human brain GABA transaminase is involved in
intersubunit cross-linking.";
Mol. Cells 18:214-219(2004).
[7]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[8]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[9]
VARIANT GABATD LYS-220.
PubMed=10407778; DOI=10.1023/A:1005500122231;
Medina-Kauwe L.K., Tobin A.J., De Meirleir L., Jaeken J., Jakobs C.,
Nyhan W.L., Gibson K.M.;
"4-aminobutyrate aminotransferase (GABA-transaminase) deficiency.";
J. Inherit. Metab. Dis. 22:414-427(1999).
-!- FUNCTION: Catalyzes the conversion of gamma-aminobutyrate and L-
beta-aminoisobutyrate to succinate semialdehyde and methylmalonate
semialdehyde, respectively. Can also convert delta-aminovalerate
and beta-alanine.
-!- CATALYTIC ACTIVITY: 4-aminobutanoate + 2-oxoglutarate = succinate
semialdehyde + L-glutamate.
-!- CATALYTIC ACTIVITY: (S)-3-amino-2-methylpropanoate + 2-
oxoglutarate = 2-methyl-3-oxopropanoate + L-glutamate.
-!- COFACTOR:
Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
Evidence={ECO:0000250|UniProtKB:P80147};
Name=[2Fe-2S] cluster; Xref=ChEBI:CHEBI:49601;
Evidence={ECO:0000250|UniProtKB:P80147};
Note=Binds 1 [2Fe-2S] cluster per homodimer.
{ECO:0000250|UniProtKB:P80147};
-!- SUBUNIT: Homodimer; disulfide-linked.
{ECO:0000269|PubMed:15528998}.
-!- SUBCELLULAR LOCATION: Mitochondrion matrix.
-!- TISSUE SPECIFICITY: Liver > pancreas > brain > kidney > heart >
placenta.
-!- DISEASE: GABA transaminase deficiency (GABATD) [MIM:613163]: An
enzymatic deficiency resulting in psychomotor retardation,
hypotonia, hyperreflexia, lethargy, refractory seizures, and EEG
abnormalities. {ECO:0000269|PubMed:10407778}. Note=The disease is
caused by mutations affecting the gene represented in this entry.
-!- SIMILARITY: Belongs to the class-III pyridoxal-phosphate-dependent
aminotransferase family. {ECO:0000305}.
-!- WEB RESOURCE: Name=SHMPD; Note=The Singapore human mutation and
polymorphism database;
URL="http://shmpd.bii.a-star.edu.sg/gene.php?genestart=A&genename=ABAT+%40+GABAT";
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EMBL; L32961; AAA74449.1; -; mRNA.
EMBL; U80226; AAB38510.1; -; mRNA.
EMBL; AK290501; BAF83190.1; -; mRNA.
EMBL; BC015628; AAH15628.1; -; mRNA.
EMBL; BC031413; AAH31413.1; -; mRNA.
EMBL; S75578; AAD14176.1; -; mRNA.
CCDS; CCDS10534.1; -.
PIR; JC4022; JC4022.
PIR; S67470; S67470.
RefSeq; NP_000654.2; NM_000663.4.
RefSeq; NP_001120920.1; NM_001127448.1.
RefSeq; NP_065737.2; NM_020686.5.
RefSeq; XP_011520702.1; XM_011522400.2.
RefSeq; XP_011520703.1; XM_011522401.2.
UniGene; Hs.336768; -.
ProteinModelPortal; P80404; -.
SMR; P80404; -.
BioGrid; 106536; 37.
IntAct; P80404; 2.
STRING; 9606.ENSP00000268251; -.
BindingDB; P80404; -.
ChEMBL; CHEMBL2044; -.
DrugBank; DB01699; (4e)-4-Aminohex-4-Enoic Acid.
DrugBank; DB04235; 4-Amino Hexanoic Acid.
DrugBank; DB00160; L-Alanine.
DrugBank; DB00142; L-Glutamic Acid.
DrugBank; DB00780; Phenelzine.
DrugBank; DB00114; Pyridoxal Phosphate.
DrugBank; DB00119; Pyruvic acid.
DrugBank; DB00313; Valproic Acid.
DrugBank; DB01080; Vigabatrin.
GuidetoPHARMACOLOGY; 2464; -.
iPTMnet; P80404; -.
PhosphoSitePlus; P80404; -.
SwissPalm; P80404; -.
BioMuta; ABAT; -.
DMDM; 48429239; -.
EPD; P80404; -.
PaxDb; P80404; -.
PeptideAtlas; P80404; -.
PRIDE; P80404; -.
DNASU; 18; -.
Ensembl; ENST00000268251; ENSP00000268251; ENSG00000183044.
Ensembl; ENST00000396600; ENSP00000379845; ENSG00000183044.
Ensembl; ENST00000425191; ENSP00000411916; ENSG00000183044.
GeneID; 18; -.
KEGG; hsa:18; -.
CTD; 18; -.
DisGeNET; 18; -.
EuPathDB; HostDB:ENSG00000183044.11; -.
GeneCards; ABAT; -.
HGNC; HGNC:23; ABAT.
HPA; HPA041528; -.
HPA; HPA041690; -.
MalaCards; ABAT; -.
MIM; 137150; gene.
MIM; 613163; phenotype.
neXtProt; NX_P80404; -.
OpenTargets; ENSG00000183044; -.
Orphanet; 2066; Gamma-aminobutyric acid transaminase deficiency.
PharmGKB; PA24372; -.
eggNOG; KOG1405; Eukaryota.
eggNOG; COG0160; LUCA.
GeneTree; ENSGT00550000074885; -.
HOVERGEN; HBG000634; -.
InParanoid; P80404; -.
KO; K13524; -.
PhylomeDB; P80404; -.
TreeFam; TF105021; -.
BioCyc; MetaCyc:HS02477-MONOMER; -.
Reactome; R-HSA-916853; Degradation of GABA.
SABIO-RK; P80404; -.
ChiTaRS; ABAT; human.
GenomeRNAi; 18; -.
PRO; PR:P80404; -.
Proteomes; UP000005640; Chromosome 16.
Bgee; ENSG00000183044; -.
CleanEx; HS_ABAT; -.
ExpressionAtlas; P80404; baseline and differential.
Genevisible; P80404; HS.
GO; GO:0032144; C:4-aminobutyrate transaminase complex; IDA:UniProtKB.
GO; GO:0070062; C:extracellular exosome; IDA:UniProtKB.
GO; GO:0005759; C:mitochondrial matrix; TAS:Reactome.
GO; GO:0005739; C:mitochondrion; IDA:LIFEdb.
GO; GO:0043005; C:neuron projection; IEA:Ensembl.
GO; GO:0047298; F:(S)-3-amino-2-methylpropionate transaminase activity; IEA:UniProtKB-EC.
GO; GO:0003867; F:4-aminobutyrate transaminase activity; TAS:Reactome.
GO; GO:0034386; F:4-aminobutyrate:2-oxoglutarate transaminase activity; IEA:UniProtKB-EC.
GO; GO:0051536; F:iron-sulfur cluster binding; IEA:UniProtKB-KW.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0042803; F:protein homodimerization activity; IPI:UniProtKB.
GO; GO:0030170; F:pyridoxal phosphate binding; IDA:UniProtKB.
GO; GO:0032145; F:succinate-semialdehyde dehydrogenase binding; ISS:UniProtKB.
GO; GO:0007568; P:aging; IEA:Ensembl.
GO; GO:0048148; P:behavioral response to cocaine; ISS:UniProtKB.
GO; GO:0021549; P:cerebellum development; IEA:Ensembl.
GO; GO:0007620; P:copulation; IEA:Ensembl.
GO; GO:0035640; P:exploration behavior; IEA:Ensembl.
GO; GO:0009449; P:gamma-aminobutyric acid biosynthetic process; IEA:Ensembl.
GO; GO:0009450; P:gamma-aminobutyric acid catabolic process; NAS:UniProtKB.
GO; GO:0007626; P:locomotory behavior; IEA:Ensembl.
GO; GO:0045776; P:negative regulation of blood pressure; IEA:Ensembl.
GO; GO:0033602; P:negative regulation of dopamine secretion; IEA:Ensembl.
GO; GO:0014053; P:negative regulation of gamma-aminobutyric acid secretion; IEA:Ensembl.
GO; GO:0090331; P:negative regulation of platelet aggregation; IEA:Ensembl.
GO; GO:0042135; P:neurotransmitter catabolic process; NAS:UniProtKB.
GO; GO:1904450; P:positive regulation of aspartate secretion; IEA:Ensembl.
GO; GO:0045964; P:positive regulation of dopamine metabolic process; IEA:Ensembl.
GO; GO:0031652; P:positive regulation of heat generation; IEA:Ensembl.
GO; GO:0097151; P:positive regulation of inhibitory postsynaptic potential; IEA:Ensembl.
GO; GO:0032024; P:positive regulation of insulin secretion; IEA:Ensembl.
GO; GO:1902722; P:positive regulation of prolactin secretion; IEA:Ensembl.
GO; GO:0070474; P:positive regulation of uterine smooth muscle contraction; IEA:Ensembl.
GO; GO:0042493; P:response to drug; IEA:Ensembl.
GO; GO:0045471; P:response to ethanol; IEA:Ensembl.
GO; GO:0001666; P:response to hypoxia; IEA:Ensembl.
GO; GO:0010039; P:response to iron ion; IEA:Ensembl.
GO; GO:0035094; P:response to nicotine; IEA:Ensembl.
CDD; cd00610; OAT_like; 1.
Gene3D; 3.40.640.10; -; 1.
Gene3D; 3.90.1150.10; -; 1.
InterPro; IPR004631; 4NH2But_aminotransferase_euk.
InterPro; IPR005814; Aminotrans_3.
InterPro; IPR015424; PyrdxlP-dep_Trfase.
InterPro; IPR015421; PyrdxlP-dep_Trfase_major_sub1.
InterPro; IPR015422; PyrdxlP-dep_Trfase_sub2.
Pfam; PF00202; Aminotran_3; 1.
PIRSF; PIRSF000521; Transaminase_4ab_Lys_Orn; 1.
SUPFAM; SSF53383; SSF53383; 1.
TIGRFAMs; TIGR00699; GABAtrns_euk; 1.
PROSITE; PS00600; AA_TRANSFER_CLASS_3; 1.
1: Evidence at protein level;
Acetylation; Aminotransferase; Complete proteome;
Direct protein sequencing; Disease mutation; Disulfide bond; Iron;
Iron-sulfur; Metal-binding; Mitochondrion;
Neurotransmitter degradation; Polymorphism; Pyridoxal phosphate;
Reference proteome; Transferase; Transit peptide.
TRANSIT 1 28 Mitochondrion.
CHAIN 29 500 4-aminobutyrate aminotransferase,
mitochondrial.
/FTId=PRO_0000001249.
REGION 164 165 Pyridoxal phosphate binding.
{ECO:0000250|UniProtKB:P80147}.
METAL 163 163 Iron-sulfur (2Fe-2S); shared with dimeric
partner. {ECO:0000250|UniProtKB:P80147}.
METAL 166 166 Iron-sulfur (2Fe-2S); shared with dimeric
partner. {ECO:0000250|UniProtKB:P80147}.
BINDING 220 220 Substrate.
{ECO:0000250|UniProtKB:P80147}.
BINDING 381 381 Pyridoxal phosphate; shared with dimeric
partner. {ECO:0000250|UniProtKB:P80147}.
MOD_RES 231 231 N6-succinyllysine.
{ECO:0000250|UniProtKB:P61922}.
MOD_RES 252 252 N6-acetyllysine; alternate.
{ECO:0000250|UniProtKB:P61922}.
MOD_RES 252 252 N6-succinyllysine; alternate.
{ECO:0000250|UniProtKB:P61922}.
MOD_RES 279 279 N6-acetyllysine.
{ECO:0000250|UniProtKB:P61922}.
MOD_RES 318 318 N6-acetyllysine.
{ECO:0000250|UniProtKB:P61922}.
MOD_RES 357 357 N6-(pyridoxal phosphate)lysine.
{ECO:0000250|UniProtKB:P80147}.
MOD_RES 413 413 N6-acetyllysine; alternate.
{ECO:0000250|UniProtKB:P61922}.
MOD_RES 413 413 N6-succinyllysine; alternate.
{ECO:0000250|UniProtKB:P61922}.
MOD_RES 452 452 N6-acetyllysine.
{ECO:0000250|UniProtKB:P61922}.
MOD_RES 470 470 N6-acetyllysine.
{ECO:0000250|UniProtKB:P61922}.
DISULFID 321 321 Interchain.
VARIANT 56 56 Q -> R (in dbSNP:rs1731017).
{ECO:0000269|PubMed:15489334}.
/FTId=VAR_018979.
VARIANT 220 220 R -> K (in GABATD; 25% reduction in
activity; dbSNP:rs121434578).
{ECO:0000269|PubMed:10407778}.
/FTId=VAR_008883.
MUTAGEN 321 321 C->M,S,A,G,K: Loss of activity.
{ECO:0000269|PubMed:15528998}.
CONFLICT 17 17 S -> T (in Ref. 1; AAA74449).
{ECO:0000305}.
CONFLICT 109 109 H -> D (in Ref. 1; AAA74449).
{ECO:0000305}.
CONFLICT 113 113 L -> V (in Ref. 1; AAA74449).
{ECO:0000305}.
CONFLICT 132 132 G -> E (in Ref. 1; AAA74449).
{ECO:0000305}.
CONFLICT 155 171 MSQLITMACGSCSNENA -> CPSSSPWPACPAPMKTT
(in Ref. 2; AAB38510). {ECO:0000305}.
CONFLICT 191 191 Q -> K (in Ref. 1; AAA74449).
{ECO:0000305}.
CONFLICT 204 204 G -> W (in Ref. 1; AAA74449).
{ECO:0000305}.
CONFLICT 216 216 A -> S (in Ref. 1; AAA74449).
{ECO:0000305}.
CONFLICT 247 247 P -> T (in Ref. 2; AAB38510).
{ECO:0000305}.
CONFLICT 268 268 R -> G (in Ref. 1; AAA74449).
{ECO:0000305}.
CONFLICT 320 320 G -> C (in Ref. 1; AAA74449).
{ECO:0000305}.
CONFLICT 366 366 H -> L (in Ref. 1; AAA74449).
{ECO:0000305}.
SEQUENCE 500 AA; 56439 MW; F990B0B6B77BD3F5 CRC64;
MASMLLAQRL ACSFQHSYRL LVPGSRHISQ AAAKVDVEFD YDGPLMKTEV PGPRSQELMK
QLNIIQNAEA VHFFCNYEES RGNYLVDVDG NRMLDLYSQI SSVPIGYSHP ALLKLIQQPQ
NASMFVNRPA LGILPPENFV EKLRQSLLSV APKGMSQLIT MACGSCSNEN ALKTIFMWYR
SKERGQRGFS QEELETCMIN QAPGCPDYSI LSFMGAFHGR TMGCLATTHS KAIHKIDIPS
FDWPIAPFPR LKYPLEEFVK ENQQEEARCL EEVEDLIVKY RKKKKTVAGI IVEPIQSEGG
DNHASDDFFR KLRDIARKHG CAFLVDEVQT GGGCTGKFWA HEHWGLDDPA DVMTFSKKMM
TGGFFHKEEF RPNAPYRIFN TWLGDPSKNL LLAEVINIIK REDLLNNAAH AGKALLTGLL
DLQARYPQFI SRVRGRGTFC SFDTPDDSIR NKLILIARNK GVVLGGCGDK SIRFRPTLVF
RDHHAHLFLN IFSDILADFK


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E0207h ELISA kit AAT1,Alanine aminotransferase 1,ALT1,Glutamate pyruvate transaminase 1,Glutamic--alanine transaminase 1,Glutamic--pyruvic transaminase 1,GPT,GPT 1,GPT1,Homo sapiens,Human 96T
U0207h CLIA AAT1,Alanine aminotransferase 1,ALT1,Glutamate pyruvate transaminase 1,Glutamic--alanine transaminase 1,Glutamic--pyruvic transaminase 1,GPT,GPT 1,GPT1,Homo sapiens,Human 96T
E0207r ELISA Aat1,Alanine aminotransferase 1,ALT1,Glutamate pyruvate transaminase 1,Glutamic--alanine transaminase 1,Glutamic--pyruvic transaminase 1,Gpt,GPT 1,Gpt1,Rat,Rattus norvegicus 96T
E0207r ELISA kit Aat1,Alanine aminotransferase 1,ALT1,Glutamate pyruvate transaminase 1,Glutamic--alanine transaminase 1,Glutamic--pyruvic transaminase 1,Gpt,GPT 1,Gpt1,Rat,Rattus norvegicus 96T
U0207r CLIA Aat1,Alanine aminotransferase 1,ALT1,Glutamate pyruvate transaminase 1,Glutamic--alanine transaminase 1,Glutamic--pyruvic transaminase 1,Gpt,GPT 1,Gpt1,Rat,Rattus norvegicus 96T
GABA-101AP GABA Beta 1 WB control: PC-GABA Host: Rabbit Affinity purifed 100-150ul


 

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