OAT_HUMAN
ID OAT_HUMAN Reviewed; 439 AA.
AC P04181; D3DRF0; Q16068; Q16069; Q68CS0; Q6IAV9; Q9UD03;
DT 20-MAR-1987, integrated into UniProtKB/Swiss-Prot.
DT 20-MAR-1987, sequence version 1.
DT 03-AUG-2022, entry version 234.
DE RecName: Full=Ornithine aminotransferase, mitochondrial;
DE EC=2.6.1.13 {ECO:0000269|PubMed:1737786, ECO:0000269|PubMed:23076989};
DE AltName: Full=Ornithine delta-aminotransferase;
DE AltName: Full=Ornithine--oxo-acid aminotransferase;
DE Contains:
DE RecName: Full=Ornithine aminotransferase, hepatic form;
DE Contains:
DE RecName: Full=Ornithine aminotransferase, renal form;
DE Flags: Precursor;
GN Name=OAT;
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] (ISOFORM 1).
RX PubMed=3456579; DOI=10.1073/pnas.83.5.1203;
RA Inana G., Totsuka S., Redmond M., Dougherty T., Nagle J., Shiono T.,
RA Ohura T., Kominami E., Katunuma N.;
RT "Molecular cloning of human ornithine aminotransferase mRNA.";
RL Proc. Natl. Acad. Sci. U.S.A. 83:1203-1207(1986).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC TISSUE=Liver;
RX PubMed=3816496; DOI=10.1089/dna.1.1986.5.493;
RA Ramesh V., Shaffer M.M., Allaire J.M., Shih V.E., Gusella J.F.;
RT "Investigation of gyrate atrophy using a cDNA clone for human ornithine
RT aminotransferase.";
RL DNA 5:493-501(1986).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), PROTEIN SEQUENCE OF 36-40, AND
RP PROTEOLYTIC PROCESSING.
RC TISSUE=Kidney;
RX PubMed=2507357; DOI=10.1016/0014-5793(89)81110-x;
RA Kobayashi T., Nishii M., Takagi Y., Titani T., Matsuzawa T.;
RT "Molecular cloning and nucleotide sequence analysis of mRNA for human
RT kidney ornithine aminotransferase. An examination of ornithine
RT aminotransferase isozymes between liver and kidney.";
RL FEBS Lett. 255:300-304(1989).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORM 1).
RX PubMed=3170546; DOI=10.1016/s0021-9258(18)68219-5;
RA Mitchell G.A., Looney J.E., Brody L.C., Steel G., Suchanek M.,
RA Engelhardt J.F., Willard H.F., Valle D.;
RT "Human ornithine-delta-aminotransferase. cDNA cloning and analysis of the
RT structural gene.";
RL J. Biol. Chem. 263:14288-14295(1988).
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC TISSUE=Placenta;
RX PubMed=2373169; DOI=10.1016/0014-4835(90)90126-f;
RA Zintz C.B., Inana G.;
RT "Analysis of the human ornithine aminotransferase gene family.";
RL Exp. Eye Res. 50:759-770(1990).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Brain, Brain cortex, and Subthalamic nucleus;
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 [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RA Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
RT "Cloning of human full open reading frames in Gateway(TM) system entry
RT vector (pDONR201).";
RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Brain cortex;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [9]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15164054; DOI=10.1038/nature02462;
RA Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L.,
RA Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K.,
RA Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L.,
RA Taylor A., Battles J., Bird C.P., Ainscough R., Almeida J.P.,
RA Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J.,
RA Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J., Brown J.Y.,
RA Burford D.C., Burrill W., Burton J., Cahill P., Camire D., Carter N.P.,
RA Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S., Corby N.,
RA Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L., Frankish A.,
RA Frankland J.A., Garner P., Garnett J., Gribble S., Griffiths C.,
RA Grocock R., Gustafson E., Hammond S., Harley J.L., Hart E., Heath P.D.,
RA Ho T.P., Hopkins B., Horne J., Howden P.J., Huckle E., Hynds C.,
RA Johnson C., Johnson D., Kana A., Kay M., Kimberley A.M., Kershaw J.K.,
RA Kokkinaki M., Laird G.K., Lawlor S., Lee H.M., Leongamornlert D.A.,
RA Laird G., Lloyd C., Lloyd D.M., Loveland J., Lovell J., McLaren S.,
RA McLay K.E., McMurray A., Mashreghi-Mohammadi M., Matthews L., Milne S.,
RA Nickerson T., Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V.,
RA Peck A.I., Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A.,
RA Ross M.T., Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M.,
RA Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W., Tracey A.,
RA Tromans A., Tsolas J., Wall M., Walsh J., Wang H., Weinstock K., West A.P.,
RA Willey D.L., Whitehead S.L., Wilming L., Wray P.W., Young L., Chen Y.,
RA Lovering R.C., Moschonas N.K., Siebert R., Fechtel K., Bentley D.,
RA Durbin R.M., Hubbard T., Doucette-Stamm L., Beck S., Smith D.R., Rogers J.;
RT "The DNA sequence and comparative analysis of human chromosome 10.";
RL Nature 429:375-381(2004).
RN [10]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [11]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Placenta, and Uterus;
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 [12]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 50-58 AND 328-336 (ISOFORM 1).
RX PubMed=1682785;
RA Ramesh V., Gusella J.F., Shih V.E.;
RT "Molecular pathology of gyrate atrophy of the choroid and retina due to
RT ornithine aminotransferase deficiency.";
RL Mol. Biol. Med. 8:81-93(1991).
RN [13]
RP PARTIAL PROTEIN SEQUENCE, PYRIDOXAL PHOSPHATE AT LYS-292, AND PROTEOLYTIC
RP PROCESSING.
RX PubMed=3754226; DOI=10.1016/0014-5793(86)81219-4;
RA Simmaco M., John R.A., Barra D., Bossa F.;
RT "The primary structure of ornithine aminotransferase. Identification of
RT active-site sequence and site of post-translational proteolysis.";
RL FEBS Lett. 199:39-42(1986).
RN [14]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [15]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [16]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25944712; DOI=10.1002/pmic.201400617;
RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT "N-terminome analysis of the human mitochondrial proteome.";
RL Proteomics 15:2519-2524(2015).
RN [17]
RP X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS).
RX PubMed=9309222; DOI=10.1016/s0969-2126(97)00258-x;
RA Shah S.A., Shen B.W., Brunger A.T.;
RT "Human ornithine aminotransferase complexed with L-canaline and gabaculine:
RT structural basis for substrate recognition.";
RL Structure 5:1067-1075(1997).
RN [18]
RP X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS), AND COFACTOR.
RX PubMed=9514741; DOI=10.1006/jmbi.1997.1583;
RA Shen B.W., Hennig M., Hohenester E., Jansonius J.N., Schirmer T.;
RT "Crystal structure of human recombinant ornithine aminotransferase.";
RL J. Mol. Biol. 277:81-102(1998).
RN [19]
RP X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS).
RX PubMed=9878407; DOI=10.1006/jmbi.1998.2289;
RA Storici P., Capitani G., Mueller R., Schirmer T., Jansonius J.N.;
RT "Crystal structure of human ornithine aminotransferase complexed with the
RT highly specific and potent inhibitor 5-fluoromethylornithine.";
RL J. Mol. Biol. 285:297-309(1999).
RN [20]
RP VARIANTS HOGA LYS-54 AND MET-332.
RX PubMed=3375240; DOI=10.1073/pnas.85.11.3777;
RA Ramesh V., McClatchey A.I., Ramesh N., Benoit L.A., Berson E.L., Shih V.E.,
RA Gusella J.F.;
RT "Molecular basis of ornithine aminotransferase deficiency in B-6-responsive
RT and -nonresponsive forms of gyrate atrophy.";
RL Proc. Natl. Acad. Sci. U.S.A. 85:3777-3780(1988).
RN [21]
RP VARIANT HOGA TYR-319.
RX PubMed=2793865; DOI=10.1016/s0021-9258(18)71513-5;
RA Inana G., Chambers C., Hotta Y., Inouye L., Filpula D., Pulford S.,
RA Shiono T.;
RT "Point mutation affecting processing of the ornithine aminotransferase
RT precursor protein in gyrate atrophy.";
RL J. Biol. Chem. 264:17432-17436(1989).
RN [22]
RP VARIANTS HOGA THR-180; LEU-241; PRO-250; ASP-353 AND ARG-394.
RX PubMed=1612597; DOI=10.1016/0888-7543(92)90258-t;
RA Michaud J., Brody L.C., Steel G., Fontaine G., Martin L.S., Valle D.,
RA Mitchell G.;
RT "Strand-separating conformational polymorphism analysis: efficacy of
RT detection of point mutations in the human ornithine delta-aminotransferase
RT gene.";
RL Genomics 13:389-394(1992).
RN [23]
RP VARIANTS HOGA HIS-55; LYS-89; PHE-93; LEU-154; THR-180; ALA-184 DEL;
RP LEU-241; CYS-245; PRO-250; ILE-267; LYS-271; ASP-353; ALA-375; ARG-394;
RP PRO-402 AND LEU-417, VARIANT PHE-437, CHARACTERIZATION OF VARIANTS HOGA
RP HIS-55; LYS-89; PHE-93; LEU-154; THR-180; ALA-184 DEL; LEU-241; CYS-245;
RP PRO-250; ILE-267; LYS-271; ASP-353; ALA-375; ARG-394; PRO-402 AND LEU-417,
RP CHARACTERIZATION OF VARIANT PRO-270, FUNCTION, CATALYTIC ACTIVITY, AND
RP PATHWAY.
RX PubMed=1737786; DOI=10.1016/s0021-9258(19)50731-1;
RA Brody L.C., Mitchell G.A., Obie C., Michaud J., Steel G., Fontaine G.,
RA Robert M.-F., Sipila I., Kaiser-Kupfer M., Valle D.;
RT "Ornithine delta-aminotransferase mutations in gyrate atrophy. Allelic
RT heterogeneity and functional consequences.";
RL J. Biol. Chem. 267:3302-3307(1992).
RN [24]
RP VARIANT HOGA VAL-226.
RX PubMed=7887415;
RA Michaud J., Thompson G.N., Brody L.C., Steel G., Obie C., Fontaine G.,
RA Schappert K., Keith C.G., Valle D., Mitchell G.A.;
RT "Pyridoxine-responsive gyrate atrophy of the choroid and retina: clinical
RT and biochemical correlates of the mutation A226V.";
RL Am. J. Hum. Genet. 56:616-622(1995).
RN [25]
RP VARIANT HOGA GLU-90.
RX PubMed=7668253;
RA Kobayashi T., Ogawa H., Kasahara M., Shiozawa Z., Matsuzawa T.;
RT "A single amino acid substitution within the mature sequence of ornithine
RT aminotransferase obstructs mitochondrial entry of the precursor.";
RL Am. J. Hum. Genet. 57:284-291(1995).
RN [26]
RP VARIANTS HOGA ASP-51; ARG-104; GLN-199; LYS-318; MET-332; TYR-394; LEU-417;
RP ASN-436 AND PHE-437, CHARACTERIZATION OF ASP-51; ARG-104; GLN-199; VAL-226;
RP LYS-318; MET-332; TYR-394; LEU-402; LEU-417; ASN-436 AND PHE-437, FUNCTION,
RP CATALYTIC ACTIVITY, PATHWAY, SUBUNIT, AND SUBCELLULAR LOCATION.
RX PubMed=23076989; DOI=10.1002/humu.22233;
RA Doimo M., Desbats M.A., Baldoin M.C., Lenzini E., Basso G., Murphy E.,
RA Graziano C., Seri M., Burlina A., Sartori G., Trevisson E., Salviati L.;
RT "Functional analysis of missense mutations of OAT, causing gyrate atrophy
RT of choroid and retina.";
RL Hum. Mutat. 34:229-236(2013).
CC -!- FUNCTION: Catalyzes the reversible interconversion of L-ornithine and
CC 2-oxoglutarate to L-glutamate semialdehyde and L-glutamate.
CC {ECO:0000269|PubMed:1737786, ECO:0000269|PubMed:23076989}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2-oxoglutarate + L-ornithine = L-glutamate + L-glutamate 5-
CC semialdehyde; Xref=Rhea:RHEA:25160, ChEBI:CHEBI:16810,
CC ChEBI:CHEBI:29985, ChEBI:CHEBI:46911, ChEBI:CHEBI:58066; EC=2.6.1.13;
CC Evidence={ECO:0000269|PubMed:1737786, ECO:0000269|PubMed:23076989};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:25161;
CC Evidence={ECO:0000305|PubMed:1737786};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:25162;
CC Evidence={ECO:0000305|PubMed:1737786};
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000269|PubMed:9514741};
CC -!- PATHWAY: Amino-acid biosynthesis; L-proline biosynthesis; L-glutamate
CC 5-semialdehyde from L-ornithine: step 1/1. {ECO:0000305|PubMed:1737786,
CC ECO:0000305|PubMed:23076989}.
CC -!- SUBUNIT: Homohexamer. {ECO:0000269|PubMed:23076989}.
CC -!- INTERACTION:
CC P04181; P05067: APP; NbExp=3; IntAct=EBI-721662, EBI-77613;
CC -!- SUBCELLULAR LOCATION: Mitochondrion matrix
CC {ECO:0000269|PubMed:23076989}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=P04181-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P04181-2; Sequence=VSP_043085;
CC -!- DISEASE: Hyperornithinemia with gyrate atrophy of choroid and retina
CC (HOGA) [MIM:258870]: A disorder clinically characterized by a triad of
CC progressive chorioretinal degeneration, early cataract formation, and
CC type II muscle fiber atrophy. Characteristic chorioretinal atrophy with
CC progressive constriction of the visual fields leads to blindness at the
CC latest during the sixth decade of life. Patients generally have normal
CC intelligence. {ECO:0000269|PubMed:1612597, ECO:0000269|PubMed:1737786,
CC ECO:0000269|PubMed:23076989, ECO:0000269|PubMed:2793865,
CC ECO:0000269|PubMed:3375240, ECO:0000269|PubMed:7668253,
CC ECO:0000269|PubMed:7887415}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- SIMILARITY: Belongs to the class-III pyridoxal-phosphate-dependent
CC aminotransferase family. {ECO:0000305}.
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DR EMBL; M12267; AAA59956.1; -; mRNA.
DR EMBL; M14963; AAA59959.1; -; mRNA.
DR EMBL; Y07511; CAA68809.1; -; mRNA.
DR EMBL; M23204; AAA36386.1; -; mRNA.
DR EMBL; M23205; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; M88760; AAA59958.1; ALT_SEQ; Genomic_DNA.
DR EMBL; M29927; AAA59957.1; -; Genomic_DNA.
DR EMBL; M29919; AAA59957.1; JOINED; Genomic_DNA.
DR EMBL; M29920; AAA59957.1; JOINED; Genomic_DNA.
DR EMBL; M29921; AAA59957.1; JOINED; Genomic_DNA.
DR EMBL; M29922; AAA59957.1; JOINED; Genomic_DNA.
DR EMBL; M29923; AAA59957.1; JOINED; Genomic_DNA.
DR EMBL; M29924; AAA59957.1; JOINED; Genomic_DNA.
DR EMBL; M29925; AAA59957.1; JOINED; Genomic_DNA.
DR EMBL; M29926; AAA59957.1; JOINED; Genomic_DNA.
DR EMBL; AK296032; BAH12241.1; -; mRNA.
DR EMBL; AK312561; BAG35458.1; -; mRNA.
DR EMBL; AK315947; BAH14318.1; -; mRNA.
DR EMBL; CR457045; CAG33326.1; -; mRNA.
DR EMBL; CR749808; CAH18668.1; -; mRNA.
DR EMBL; AL445237; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471066; EAW49271.1; -; Genomic_DNA.
DR EMBL; CH471066; EAW49272.1; -; Genomic_DNA.
DR EMBL; BC000964; AAH00964.1; -; mRNA.
DR EMBL; BC016928; AAH16928.1; -; mRNA.
DR EMBL; S66418; AAB20298.1; -; mRNA.
DR EMBL; S66421; AAB20297.1; -; mRNA.
DR CCDS; CCDS53586.1; -. [P04181-2]
DR CCDS; CCDS7639.1; -. [P04181-1]
DR PIR; A30806; XNHUO.
DR PIR; I55360; I55360.
DR RefSeq; NP_000265.1; NM_000274.3. [P04181-1]
DR RefSeq; NP_001165285.1; NM_001171814.1. [P04181-2]
DR RefSeq; NP_001309894.1; NM_001322965.1. [P04181-1]
DR RefSeq; NP_001309895.1; NM_001322966.1. [P04181-1]
DR RefSeq; NP_001309896.1; NM_001322967.1. [P04181-1]
DR RefSeq; NP_001309897.1; NM_001322968.1. [P04181-1]
DR RefSeq; NP_001309898.1; NM_001322969.1. [P04181-1]
DR RefSeq; NP_001309899.1; NM_001322970.1. [P04181-1]
DR RefSeq; NP_001309900.1; NM_001322971.1.
DR PDB; 1GBN; X-ray; 2.30 A; A/B/C=38-439.
DR PDB; 1OAT; X-ray; 2.50 A; A/B/C=1-439.
DR PDB; 2BYJ; X-ray; 3.02 A; A/B/C=1-439.
DR PDB; 2BYL; X-ray; 2.15 A; A/B/C=1-439.
DR PDB; 2CAN; X-ray; 2.30 A; A/B/C=38-439.
DR PDB; 2OAT; X-ray; 1.95 A; A/B/C=1-439.
DR PDB; 5VWO; X-ray; 1.77 A; A/B/C=36-439.
DR PDB; 6HX7; X-ray; 1.80 A; A/B/C=26-439.
DR PDB; 6OIA; X-ray; 1.78 A; A/B/C=36-439.
DR PDB; 6V8C; X-ray; 1.90 A; A/B/C=36-439.
DR PDB; 6V8D; X-ray; 2.25 A; A/B/C=36-439.
DR PDB; 7JX9; X-ray; 1.96 A; A/B/C=36-439.
DR PDB; 7LK0; X-ray; 1.96 A; A/B/C=36-439.
DR PDB; 7LK1; X-ray; 1.79 A; A/B/C=36-439.
DR PDB; 7LNM; X-ray; 2.00 A; B/C/E/F/I/J=36-439.
DR PDB; 7LOM; X-ray; 2.10 A; A/B/C=36-439.
DR PDB; 7LON; X-ray; 1.95 A; A/B/C=36-439.
DR PDB; 7TED; X-ray; 2.63 A; A/B/C/D/E/F/G/H/I=36-439.
DR PDB; 7TEV; X-ray; 1.91 A; A/B/C=36-439.
DR PDB; 7TFP; X-ray; 2.71 A; A/B/C=36-439.
DR PDBsum; 1GBN; -.
DR PDBsum; 1OAT; -.
DR PDBsum; 2BYJ; -.
DR PDBsum; 2BYL; -.
DR PDBsum; 2CAN; -.
DR PDBsum; 2OAT; -.
DR PDBsum; 5VWO; -.
DR PDBsum; 6HX7; -.
DR PDBsum; 6OIA; -.
DR PDBsum; 6V8C; -.
DR PDBsum; 6V8D; -.
DR PDBsum; 7JX9; -.
DR PDBsum; 7LK0; -.
DR PDBsum; 7LK1; -.
DR PDBsum; 7LNM; -.
DR PDBsum; 7LOM; -.
DR PDBsum; 7LON; -.
DR PDBsum; 7TED; -.
DR PDBsum; 7TEV; -.
DR PDBsum; 7TFP; -.
DR AlphaFoldDB; P04181; -.
DR SMR; P04181; -.
DR BioGRID; 110996; 150.
DR IntAct; P04181; 40.
DR MINT; P04181; -.
DR STRING; 9606.ENSP00000357838; -.
DR BindingDB; P04181; -.
DR ChEMBL; CHEMBL5954; -.
DR DrugBank; DB02821; Canaline.
DR DrugBank; DB02054; Gabaculine.
DR DrugBank; DB00129; Ornithine.
DR DrugBank; DB00114; Pyridoxal phosphate.
DR CarbonylDB; P04181; -.
DR GlyGen; P04181; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; P04181; -.
DR MetOSite; P04181; -.
DR PhosphoSitePlus; P04181; -.
DR SwissPalm; P04181; -.
DR BioMuta; OAT; -.
DR DMDM; 129018; -.
DR REPRODUCTION-2DPAGE; IPI00022334; -.
DR EPD; P04181; -.
DR jPOST; P04181; -.
DR MassIVE; P04181; -.
DR MaxQB; P04181; -.
DR PaxDb; P04181; -.
DR PeptideAtlas; P04181; -.
DR PRIDE; P04181; -.
DR ProteomicsDB; 51672; -. [P04181-1]
DR ProteomicsDB; 51673; -. [P04181-2]
DR Antibodypedia; 32371; 256 antibodies from 32 providers.
DR DNASU; 4942; -.
DR Ensembl; ENST00000368845.6; ENSP00000357838.5; ENSG00000065154.12. [P04181-1]
DR Ensembl; ENST00000539214.5; ENSP00000439042.1; ENSG00000065154.12. [P04181-2]
DR GeneID; 4942; -.
DR KEGG; hsa:4942; -.
DR MANE-Select; ENST00000368845.6; ENSP00000357838.5; NM_000274.4; NP_000265.1.
DR UCSC; uc001lhp.4; human. [P04181-1]
DR CTD; 4942; -.
DR DisGeNET; 4942; -.
DR GeneCards; OAT; -.
DR HGNC; HGNC:8091; OAT.
DR HPA; ENSG00000065154; Tissue enhanced (intestine).
DR MalaCards; OAT; -.
DR MIM; 258870; phenotype.
DR MIM; 613349; gene.
DR neXtProt; NX_P04181; -.
DR OpenTargets; ENSG00000065154; -.
DR Orphanet; 414; Gyrate atrophy of choroid and retina.
DR PharmGKB; PA31880; -.
DR VEuPathDB; HostDB:ENSG00000065154; -.
DR eggNOG; KOG1402; Eukaryota.
DR GeneTree; ENSGT00630000089895; -.
DR HOGENOM; CLU_016922_10_3_1; -.
DR InParanoid; P04181; -.
DR OMA; DVFPRFA; -.
DR PhylomeDB; P04181; -.
DR TreeFam; TF105720; -.
DR BioCyc; MetaCyc:HS00832-MON; -.
DR BRENDA; 2.6.1.13; 2681.
DR PathwayCommons; P04181; -.
DR Reactome; R-HSA-8964539; Glutamate and glutamine metabolism.
DR SABIO-RK; P04181; -.
DR SignaLink; P04181; -.
DR SIGNOR; P04181; -.
DR UniPathway; UPA00098; UER00358.
DR BioGRID-ORCS; 4942; 11 hits in 1084 CRISPR screens.
DR ChiTaRS; OAT; human.
DR EvolutionaryTrace; P04181; -.
DR GenomeRNAi; 4942; -.
DR Pharos; P04181; Tchem.
DR PRO; PR:P04181; -.
DR Proteomes; UP000005640; Chromosome 10.
DR RNAct; P04181; protein.
DR Bgee; ENSG00000065154; Expressed in jejunal mucosa and 206 other tissues.
DR ExpressionAtlas; P04181; baseline and differential.
DR Genevisible; P04181; HS.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005759; C:mitochondrial matrix; IDA:UniProtKB.
DR GO; GO:0005739; C:mitochondrion; IDA:HPA.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0042802; F:identical protein binding; IPI:UniProtKB.
DR GO; GO:0050155; F:ornithine(lysine) transaminase activity; IMP:UniProtKB.
DR GO; GO:0004587; F:ornithine-oxo-acid transaminase activity; IBA:GO_Central.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IBA:GO_Central.
DR GO; GO:0019544; P:arginine catabolic process to glutamate; IBA:GO_Central.
DR GO; GO:0010121; P:arginine catabolic process to proline via ornithine; IBA:GO_Central.
DR GO; GO:0055129; P:L-proline biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0007601; P:visual perception; TAS:ProtInc.
DR CDD; cd00610; OAT_like; 1.
DR Gene3D; 3.40.640.10; -; 1.
DR Gene3D; 3.90.1150.10; -; 1.
DR InterPro; IPR005814; Aminotrans_3.
DR InterPro; IPR010164; Orn_aminotrans.
DR InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR Pfam; PF00202; Aminotran_3; 1.
DR PIRSF; PIRSF000521; Transaminase_4ab_Lys_Orn; 1.
DR SUPFAM; SSF53383; SSF53383; 1.
DR TIGRFAMs; TIGR01885; Orn_aminotrans; 1.
DR PROSITE; PS00600; AA_TRANSFER_CLASS_3; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative splicing; Aminotransferase;
KW Direct protein sequencing; Disease variant; Mitochondrion;
KW Pyridoxal phosphate; Reference proteome; Transferase; Transit peptide.
FT TRANSIT 1..35
FT /note="Mitochondrion; in renal form"
FT /evidence="ECO:0000269|PubMed:2507357"
FT TRANSIT 1..25
FT /note="Mitochondrion; in hepatic form"
FT CHAIN 26..439
FT /note="Ornithine aminotransferase, hepatic form"
FT /id="PRO_0000001262"
FT CHAIN 36..439
FT /note="Ornithine aminotransferase, renal form"
FT /id="PRO_0000001263"
FT MOD_RES 49
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P29758"
FT MOD_RES 66
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P29758"
FT MOD_RES 102
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:P29758"
FT MOD_RES 107
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P29758"
FT MOD_RES 107
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P29758"
FT MOD_RES 292
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000269|PubMed:3754226"
FT MOD_RES 362
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P29758"
FT MOD_RES 362
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P29758"
FT MOD_RES 386
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P29758"
FT MOD_RES 392
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P29758"
FT MOD_RES 405
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P29758"
FT MOD_RES 405
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P29758"
FT MOD_RES 421
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P29758"
FT VAR_SEQ 1..138
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:17974005"
FT /id="VSP_043085"
FT VARIANT 51
FT /note="G -> D (in HOGA; loss of protein stability; loss of
FT ornithine aminotransferase activity; dbSNP:rs11553554)"
FT /evidence="ECO:0000269|PubMed:23076989"
FT /id="VAR_071924"
FT VARIANT 54
FT /note="N -> K (in HOGA; dbSNP:rs121965048)"
FT /evidence="ECO:0000269|PubMed:3375240"
FT /id="VAR_000565"
FT VARIANT 55
FT /note="Y -> H (in HOGA; decreased protein abundance;
FT dbSNP:rs121965037)"
FT /evidence="ECO:0000269|PubMed:1737786"
FT /id="VAR_000566"
FT VARIANT 89
FT /note="N -> K (in HOGA; no effect on protein abundance;
FT dbSNP:rs386833602)"
FT /evidence="ECO:0000269|PubMed:1737786"
FT /id="VAR_000567"
FT VARIANT 90
FT /note="Q -> E (in HOGA; mistargeted, accumulates in
FT cytoplasm; dbSNP:rs121965060)"
FT /evidence="ECO:0000269|PubMed:7668253"
FT /id="VAR_015648"
FT VARIANT 93
FT /note="C -> F (in HOGA; no effect on protein abundance;
FT dbSNP:rs121965038)"
FT /evidence="ECO:0000269|PubMed:1737786"
FT /id="VAR_000568"
FT VARIANT 104
FT /note="Q -> R (in HOGA; loss of protein stability; loss of
FT ornithine aminotransferase activity; dbSNP:rs386833604)"
FT /evidence="ECO:0000269|PubMed:23076989"
FT /id="VAR_071925"
FT VARIANT 154
FT /note="R -> L (in HOGA; no effect on protein abundance;
FT loss of ornithine aminotransferase activity;
FT dbSNP:rs121965039)"
FT /evidence="ECO:0000269|PubMed:1737786"
FT /id="VAR_000569"
FT VARIANT 180
FT /note="R -> T (in HOGA; no effect on protein abundance;
FT loss of ornithine aminotransferase activity;
FT dbSNP:rs121965040)"
FT /evidence="ECO:0000269|PubMed:1612597,
FT ECO:0000269|PubMed:1737786"
FT /id="VAR_000570"
FT VARIANT 184
FT /note="Missing (in HOGA; no effect on protein abundance;
FT loss of ornithine aminotransferase activity;
FT dbSNP:rs121965035)"
FT /evidence="ECO:0000269|PubMed:1737786"
FT /id="VAR_000571"
FT VARIANT 199
FT /note="P -> Q (in HOGA; loss of protein stability; loss of
FT ornithine aminotransferase activity; dbSNP:rs267606925)"
FT /evidence="ECO:0000269|PubMed:23076989"
FT /id="VAR_071926"
FT VARIANT 226
FT /note="A -> V (in HOGA; loss of protein stability; loss of
FT ornithine aminotransferase activity; dbSNP:rs121965059)"
FT /evidence="ECO:0000269|PubMed:23076989,
FT ECO:0000269|PubMed:7887415"
FT /id="VAR_000572"
FT VARIANT 241
FT /note="P -> L (in HOGA; no effect on protein abundance;
FT dbSNP:rs121965051)"
FT /evidence="ECO:0000269|PubMed:1612597,
FT ECO:0000269|PubMed:1737786"
FT /id="VAR_000573"
FT VARIANT 245
FT /note="Y -> C (in HOGA; no effect on protein abundance;
FT dbSNP:rs121965046)"
FT /evidence="ECO:0000269|PubMed:1737786"
FT /id="VAR_000574"
FT VARIANT 250
FT /note="R -> P (in HOGA; no effect on protein abundance;
FT dbSNP:rs121965052)"
FT /evidence="ECO:0000269|PubMed:1612597,
FT ECO:0000269|PubMed:1737786"
FT /id="VAR_000575"
FT VARIANT 267
FT /note="T -> I (in HOGA; decreased protein abundance;
FT dbSNP:rs386833618)"
FT /evidence="ECO:0000269|PubMed:1737786"
FT /id="VAR_000576"
FT VARIANT 270
FT /note="A -> P (decreased protein abundance;
FT dbSNP:rs121965041)"
FT /evidence="ECO:0000269|PubMed:1737786"
FT /id="VAR_000577"
FT VARIANT 271
FT /note="R -> K (in HOGA; no effect on protein abundance;
FT loss of ornithine aminotransferase activity;
FT dbSNP:rs121965042)"
FT /evidence="ECO:0000269|PubMed:1737786"
FT /id="VAR_000578"
FT VARIANT 318
FT /note="E -> K (in HOGA; loss of protein stability; loss of
FT ornithine aminotransferase activity; dbSNP:rs386833621)"
FT /evidence="ECO:0000269|PubMed:23076989"
FT /id="VAR_071927"
FT VARIANT 319
FT /note="H -> Y (in HOGA; dbSNP:rs121965049)"
FT /evidence="ECO:0000269|PubMed:2793865"
FT /id="VAR_000579"
FT VARIANT 332
FT /note="V -> M (in HOGA; loss of protein stability; loss of
FT ornithine aminotransferase activityx; dbSNP:rs121965047)"
FT /evidence="ECO:0000269|PubMed:23076989,
FT ECO:0000269|PubMed:3375240"
FT /id="VAR_000580"
FT VARIANT 353
FT /note="G -> D (in HOGA; decreased protein abundance;
FT dbSNP:rs121965053)"
FT /evidence="ECO:0000269|PubMed:1612597,
FT ECO:0000269|PubMed:1737786"
FT /id="VAR_000581"
FT VARIANT 375
FT /note="G -> A (in HOGA; decreased protein abundance;
FT dbSNP:rs121965045)"
FT /evidence="ECO:0000269|PubMed:1737786"
FT /id="VAR_000582"
FT VARIANT 394
FT /note="C -> R (in HOGA; no effect on protein abundance;
FT dbSNP:rs121965054)"
FT /evidence="ECO:0000269|PubMed:1612597,
FT ECO:0000269|PubMed:1737786"
FT /id="VAR_000583"
FT VARIANT 394
FT /note="C -> Y (in HOGA; loss of protein stability; loss of
FT ornithine aminotransferase activity; dbSNP:rs386833597)"
FT /evidence="ECO:0000269|PubMed:23076989"
FT /id="VAR_071928"
FT VARIANT 402
FT /note="L -> P (in HOGA; may affect protein stability; loss
FT of ornithine aminotransferase activity; dbSNP:rs121965043)"
FT /evidence="ECO:0000269|PubMed:1737786,
FT ECO:0000269|PubMed:23076989"
FT /id="VAR_000584"
FT VARIANT 417
FT /note="P -> L (in HOGA; loss of protein stability; loss of
FT ornithine aminotransferase activity; dbSNP:rs121965044)"
FT /evidence="ECO:0000269|PubMed:1737786,
FT ECO:0000269|PubMed:23076989"
FT /id="VAR_000585"
FT VARIANT 436
FT /note="I -> N (in HOGA; loss of protein stability; loss of
FT ornithine aminotransferase activity; dbSNP:rs386833598)"
FT /evidence="ECO:0000269|PubMed:23076989"
FT /id="VAR_071929"
FT VARIANT 437
FT /note="L -> F (in HOGA; no effect on protein stability;
FT increased ornithine aminotransferase activity;
FT dbSNP:rs1800456)"
FT /evidence="ECO:0000269|PubMed:1737786,
FT ECO:0000269|PubMed:23076989"
FT /id="VAR_000586"
FT HELIX 40..50
FT /evidence="ECO:0007829|PDB:5VWO"
FT STRAND 61..67
FT /evidence="ECO:0007829|PDB:5VWO"
FT STRAND 69..72
FT /evidence="ECO:0007829|PDB:5VWO"
FT STRAND 77..82
FT /evidence="ECO:0007829|PDB:5VWO"
FT HELIX 83..86
FT /evidence="ECO:0007829|PDB:5VWO"
FT TURN 87..90
FT /evidence="ECO:0007829|PDB:6OIA"
FT HELIX 95..104
FT /evidence="ECO:0007829|PDB:5VWO"
FT TURN 105..107
FT /evidence="ECO:0007829|PDB:5VWO"
FT STRAND 115..119
FT /evidence="ECO:0007829|PDB:5VWO"
FT HELIX 120..131
FT /evidence="ECO:0007829|PDB:5VWO"
FT STRAND 134..141
FT /evidence="ECO:0007829|PDB:5VWO"
FT HELIX 142..159
FT /evidence="ECO:0007829|PDB:5VWO"
FT STRAND 169..173
FT /evidence="ECO:0007829|PDB:5VWO"
FT HELIX 182..186
FT /evidence="ECO:0007829|PDB:5VWO"
FT HELIX 191..194
FT /evidence="ECO:0007829|PDB:5VWO"
FT STRAND 204..207
FT /evidence="ECO:0007829|PDB:5VWO"
FT HELIX 212..218
FT /evidence="ECO:0007829|PDB:5VWO"
FT STRAND 224..229
FT /evidence="ECO:0007829|PDB:5VWO"
FT STRAND 231..233
FT /evidence="ECO:0007829|PDB:5VWO"
FT TURN 234..237
FT /evidence="ECO:0007829|PDB:5VWO"
FT HELIX 245..255
FT /evidence="ECO:0007829|PDB:5VWO"
FT STRAND 259..263
FT /evidence="ECO:0007829|PDB:5VWO"
FT TURN 265..272
FT /evidence="ECO:0007829|PDB:5VWO"
FT STRAND 273..276
FT /evidence="ECO:0007829|PDB:5VWO"
FT HELIX 277..281
FT /evidence="ECO:0007829|PDB:5VWO"
FT STRAND 286..290
FT /evidence="ECO:0007829|PDB:5VWO"
FT HELIX 292..295
FT /evidence="ECO:0007829|PDB:5VWO"
FT STRAND 302..306
FT /evidence="ECO:0007829|PDB:5VWO"
FT HELIX 308..311
FT /evidence="ECO:0007829|PDB:5VWO"
FT HELIX 327..342
FT /evidence="ECO:0007829|PDB:5VWO"
FT HELIX 345..360
FT /evidence="ECO:0007829|PDB:5VWO"
FT TURN 365..367
FT /evidence="ECO:0007829|PDB:5VWO"
FT STRAND 368..374
FT /evidence="ECO:0007829|PDB:5VWO"
FT STRAND 377..382
FT /evidence="ECO:0007829|PDB:5VWO"
FT HELIX 390..399
FT /evidence="ECO:0007829|PDB:5VWO"
FT TURN 408..410
FT /evidence="ECO:0007829|PDB:5VWO"
FT STRAND 411..414
FT /evidence="ECO:0007829|PDB:5VWO"
FT HELIX 422..437
FT /evidence="ECO:0007829|PDB:5VWO"
SQ SEQUENCE 439 AA; 48535 MW; E9D0636824A83220 CRC64;
MFSKLAHLQR FAVLSRGVHS SVASATSVAT KKTVQGPPTS DDIFEREYKY GAHNYHPLPV
ALERGKGIYL WDVEGRKYFD FLSSYSAVNQ GHCHPKIVNA LKSQVDKLTL TSRAFYNNVL
GEYEEYITKL FNYHKVLPMN TGVEAGETAC KLARKWGYTV KGIQKYKAKI VFAAGNFWGR
TLSAISSSTD PTSYDGFGPF MPGFDIIPYN DLPALERALQ DPNVAAFMVE PIQGEAGVVV
PDPGYLMGVR ELCTRHQVLF IADEIQTGLA RTGRWLAVDY ENVRPDIVLL GKALSGGLYP
VSAVLCDDDI MLTIKPGEHG STYGGNPLGC RVAIAALEVL EEENLAENAD KLGIILRNEL
MKLPSDVVTA VRGKGLLNAI VIKETKDWDA WKVCLRLRDN GLLAKPTHGD IIRFAPPLVI
KEDELRESIE IINKTILSF
